Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P02091
|
HBB1_RAT
|
MVHLTDAEKAAVNGLWGKVNPDDVGGEALGRLLVVYPWTQRYFDSFGDLSSASAIMGNPKVKAHGKKVINAFNDGLKHLDNLKGTFAHLSELHCDKLHVDPENFRLLGNMIVIVLGHHLGKEFTPCAQAAFQKVVAGVASALAHKYH
| null | null |
carbon dioxide transport [GO:0015670]; erythrocyte development [GO:0048821]; glutathione metabolic process [GO:0006749]; hemopoiesis [GO:0030097]; hydrogen peroxide catabolic process [GO:0042744]; nitric oxide transport [GO:0030185]; oxygen transport [GO:0015671]; regulation of eIF2 alpha phosphorylation by heme [GO:0010999]; renal absorption [GO:0070293]; response to hydrogen peroxide [GO:0042542]
|
blood microparticle [GO:0072562]; extracellular space [GO:0005615]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; hemoglobin beta binding [GO:0031722]; hemoglobin binding [GO:0030492]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]; protein-containing complex binding [GO:0044877]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Rattus norvegicus (Rat)
|
P02094
|
HBB_MESAU
|
MVHLTDAEKALVTGLWGKVNADAVGAEALGRLLVVYPWTQRFFEHFGDLSSASAVMNNPQVKAHGKKVIHSFADGLKHLDNLKGAFSSLSELHCDKLHVDPENFKLLGNMIIIVLSHDLGKDFTPSAQSAFHKVVAGVANALAHKYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Mesocricetus auratus (Golden hamster)
|
P02100
|
HBE_HUMAN
|
MVHFTAEEKAAVTSLWSKMNVEEAGGEALGRLLVVYPWTQRFFDSFGNLSSPSAILGNPKVKAHGKKVLTSFGDAIKNMDNLKPAFAKLSELHCDKLHVDPENFKLLGNVMVIILATHFGKEFTPEVQAAWQKLVSAVAIALAHKYH
| null | null |
carbon dioxide transport [GO:0015670]; hydrogen peroxide catabolic process [GO:0042744]; oxygen transport [GO:0015671]; response to organic cyclic compound [GO:0014070]
|
blood microparticle [GO:0072562]; cytosol [GO:0005829]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]; protein-containing complex binding [GO:0044877]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: The epsilon chain is a beta-type chain of early mammalian embryonic hemoglobin.
|
Homo sapiens (Human)
|
P02104
|
HBE_MOUSE
|
MVNFTAEEKTLINGLWSKVNVEEVGGEALGRLLVVYPWTQRFFDSFGNLSSASAIMGNPRVKAHGKKVLTAFGESIKNLDNLKSALAKLSELHCDKLHVDPENFKLLGNVLVIVLASHFGNEFTAEMQAAWQKLVAGVATALSHKYH
| null | null |
carbon dioxide transport [GO:0015670]; hydrogen peroxide catabolic process [GO:0042744]; negative regulation of transcription by RNA polymerase II [GO:0000122]; oxygen transport [GO:0015671]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]; protein-containing complex binding [GO:0044877]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Hemoglobin epsilon chain is a beta-type chain found in early embryos.
|
Mus musculus (Mouse)
|
P02109
|
HBB_DIDVI
|
MVHLTSEEKNCITTIWSKVQVDQTGGEALGRMLVVYPWTTRFFGSFGDLSSPGAVMSNSKVQAHGAKVLTSFGEAVKHLDNLKGTYAKLSELHCDKLHVDPENFKMLGNIIVICLAEHFGKDFTPECQVAWQKLVAGVAHALAHKYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Didelphis virginiana (North American opossum) (Didelphis marsupialis virginiana)
|
P02110
|
HBB_TACAC
|
MVHLSGSEKTAVTNLWGHVNVNELGGEALGRLLVVYPWTQRFFESFGDLSSADAVMGNAKVKAHGAKVLTSFGDALKNLDNLKGTFAKLSELHCDKLHVDPENFNRLGNVLVVVLARHFSKEFTPEAQAAWQKLVSGVSHALAHKYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Tachyglossus aculeatus aculeatus (Southeast Australian short-beaked echidna)
|
P02112
|
HBB_CHICK
|
MVHWTAEEKQLITGLWGKVNVAECGAEALARLLIVYPWTQRFFASFGNLSSPTAILGNPMVRAHGKKVLTSFGDAVKNLDNIKNTFSQLSELHCDKLHVDPENFRLLGDILIIVLAAHFSKDFTPECQAAWQKLVRVVAHALARKYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; extracellular space [GO:0005615]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; hemoglobin binding [GO:0030492]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. The beta chain is a component of adult hemoglobin A and D.
|
Gallus gallus (Chicken)
|
P02114
|
HBB_ANAPL
|
MVHWTAEEKQLITGLWGKVNVADCGAEALARLLIVYPWTQRFFASFGNLSSPTAILGNPMVRAHGKKVLTSFGDAVKNLDNIKNTFAQLSELHCDKLHVDPENFRLLGDILIIVLAAHFTKDFTPECQAAWQKLVRVVAHALARKYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Anas platyrhynchos (Mallard) (Anas boschas)
|
P02129
|
HBB_CRONI
|
ASFDPHEKQLIGDLWHKVDVAHCGGEALSRMLIVYPWKRRYFENFGDISNAQAIMHNEKVQAHGKKVLASFGEAVCHLDGIRAHFANLSKLHCEKLHVDPENFKLLGDIIIIVLAAHYPKDFGLECHAAYQKLVRQVAAALAAEYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Crocodylus niloticus (Nile crocodile) (African crocodile)
|
P02130
|
HBB_ALLMI
|
ASFDAHERKFIVDLWAKVDVAQCGADALSRMLIVYPWKRRYFEHFGKMCNAHDILHNSKVQEHGKKVLASFGEAVKHLDNIKGHFANLSKLHCEKFHVDPENFKLLGDIIIIVLAAHHPEDFSVECHAAFQKLVRQVAAALAAEYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Alligator mississippiensis (American alligator)
|
P02132
|
HBB1_XENLA
|
MGLTAHDRQLINSTWGKLCAKTIGQEALGRLLWTYPWTQRYFSSFGNLNSADAVFHNEAVAAHGEKVVTSIGEAIKHMDDIKGYYAQLSKYHSETLHVDPLNFKRFGGCLSIALARHFHEEYTPELHAAYEHLFDAIADALGKGYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Xenopus laevis (African clawed frog)
|
P02133
|
HBB2_XENLA
|
MVHWTAEEKAAITSVWQKVNVEHDGHDALGRLLIVYPWTQRYFSNFGNLSNSAAVAGNAKVQAHGKKVLSAVGNAISHIDSVKSSLQQLSKIHATELFVDPENFKRFGGVLVIVLGAKLGTAFTPKVQAAWEKFIAVLVDGLSQGYN
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues.
|
Xenopus laevis (African clawed frog)
|
P02137
|
HBBL_XENLA
|
MVHLSADEKSAINAVWSKVNIENDGHDALTRLLVVFPWTQRYFSSFGNLSNVAAISGNAKVRAHGKKVLSAVDESIHHLDDIKNFLSVLSTKHAEELHVDPENFKRLADVLVIVLAGKLGAAFTPQVQAAWEKFSAGLVAALSHGYF
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: This is a larval (tadpole) beta-globin.
|
Xenopus laevis (African clawed frog)
|
P02139
|
HBB_CYPCA
|
VEWTDAERSAIIALWGKLNPDELGPEALARCLIVYPWTQRFFASYGNLSSPAAIMGNPKVAAHGRTVEGGLMRAIKDMDNIKATYAPLSVMHSEKLHVDPDNFRLLADCITVCAAMKFGPSGFSPNVQEAWQKFLSVVVNALKRQYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from gills to the various peripheral tissues.
|
Cyprinus carpio (Common carp)
|
P02141
|
HBB4_ONCMY
|
MVDWTDPERSAIVGLWGKISVDEIGPQALARLLIVSPWTQRHFSTFGNLSTPAAIMGNPAVAKHGKTVMHGLDRAVQNLDDIKNTYTALSVMHSEKLHVDPDNFRLLADCITVCVAAKLGPAVFSADTQEAFQKFLAVVVSALGRQYH
| null | null |
hydrogen peroxide catabolic process [GO:0042744]
|
blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833]
|
haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
1.10.490.10;
|
Globin family
| null | null | null | null | null | null | null |
FUNCTION: Involved in oxygen transport from gills to the various peripheral tissues.
|
Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
|
P02144
|
MYG_HUMAN
|
MGLSDGEWQLVLNVWGKVEADIPGHGQEVLIRLFKGHPETLEKFDKFKHLKSEDEMKASEDLKKHGATVLTALGGILKKKGHHEAEIKPLAQSHATKHKIPVKYLEFISECIIQVLQSKHPGDFGADAQGAMNKALELFRKDMASNYKELGFQG
|
1.11.1.-; 1.7.-.-
| null |
brown fat cell differentiation [GO:0050873]; enucleate erythrocyte differentiation [GO:0043353]; heart development [GO:0007507]; oxygen transport [GO:0015671]; removal of superoxide radicals [GO:0019430]; response to hypoxia [GO:0001666]
|
cytosol [GO:0005829]; extracellular exosome [GO:0070062]; sarcoplasm [GO:0016528]
|
heme binding [GO:0020037]; metal ion binding [GO:0046872]; nitrite reductase activity [GO:0098809]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
6.10.140.2100;6.10.140.2110;
|
Globin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, sarcoplasm {ECO:0000269|PubMed:30918256}.
|
CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:32891753}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:77713; Evidence={ECO:0000305|PubMed:32891753}; CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; Evidence={ECO:0000269|PubMed:34679218};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=163 uM for H2O2 {ECO:0000269|PubMed:34679218};
| null | null | null |
FUNCTION: Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand (PubMed:30918256, PubMed:34679218). Depending on the oxidative conditions of tissues and cells, and in addition to its ability to bind oxygen, it also has a nitrite reductase activity whereby it regulates the production of bioactive nitric oxide (PubMed:32891753). Under stress conditions, like hypoxia and anoxia, it also protects cells against reactive oxygen species thanks to its pseudoperoxidase activity (PubMed:34679218). {ECO:0000269|PubMed:30918256, ECO:0000269|PubMed:32891753, ECO:0000269|PubMed:34679218}.
|
Homo sapiens (Human)
|
P02185
|
MYG_PHYMC
|
MVLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASEDLKKHGVTVLTALGAILKKKGHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPGDFGADAQGAMNKALELFRKDIAAKYKELGYQG
|
1.11.1.-; 1.7.-.-
| null |
removal of superoxide radicals [GO:0019430]
|
extracellular exosome [GO:0070062]; sarcoplasm [GO:0016528]
|
heme binding [GO:0020037]; metal ion binding [GO:0046872]; nitrite reductase activity [GO:0098809]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
6.10.140.2100;6.10.140.2110;
|
Globin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:P02144}.
|
CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P02144}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:77713; Evidence={ECO:0000250|UniProtKB:P02144}; CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; Evidence={ECO:0000250|UniProtKB:P02144};
| null | null | null | null |
FUNCTION: Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand. Depending on the oxidative conditions of tissues and cells, and in addition to its ability to bind oxygen, it also has a nitrite reductase activity whereby it regulates the production of bioactive nitric oxide. Under stress conditions, like hypoxia and anoxia, it also protects cells against reactive oxygen species thanks to its pseudoperoxidase activity. {ECO:0000250|UniProtKB:P02144}.
|
Physeter macrocephalus (Sperm whale) (Physeter catodon)
|
P02189
|
MYG_PIG
|
MGLSDGEWQLVLNVWGKVEADVAGHGQEVLIRLFKGHPETLEKFDKFKHLKSEDEMKASEDLKKHGNTVLTALGGILKKKGHHEAELTPLAQSHATKHKIPVKYLEFISEAIIQVLQSKHPGDFGADAQGAMSKALELFRNDMAAKYKELGFQG
|
1.11.1.-; 1.7.-.-
| null |
oxygen transport [GO:0015671]; removal of superoxide radicals [GO:0019430]
|
extracellular exosome [GO:0070062]; sarcoplasm [GO:0016528]
|
heme binding [GO:0020037]; metal ion binding [GO:0046872]; nitrite reductase activity [GO:0098809]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
6.10.140.2100;6.10.140.2110;
|
Globin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:P02144}.
|
CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P02144}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:77713; Evidence={ECO:0000250|UniProtKB:P02144}; CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; Evidence={ECO:0000250|UniProtKB:P02144};
| null | null | null | null |
FUNCTION: Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand. Depending on the oxidative conditions of tissues and cells, and in addition to its ability to bind oxygen, it also has a nitrite reductase activity whereby it regulates the production of bioactive nitric oxide. Under stress conditions, like hypoxia and anoxia, it also protects cells against reactive oxygen species thanks to its pseudoperoxidase activity. {ECO:0000250|UniProtKB:P02144}.
|
Sus scrofa (Pig)
|
P02192
|
MYG_BOVIN
|
MGLSDGEWQLVLNAWGKVEADVAGHGQEVLIRLFTGHPETLEKFDKFKHLKTEAEMKASEDLKKHGNTVLTALGGILKKKGHHEAEVKHLAESHANKHKIPVKYLEFISDAIIHVLHAKHPSDFGADAQAAMSKALELFRNDMAAQYKVLGFHG
|
1.11.1.-; 1.7.-.-
| null |
oxygen transport [GO:0015671]; removal of superoxide radicals [GO:0019430]
|
extracellular exosome [GO:0070062]; sarcoplasm [GO:0016528]
|
heme binding [GO:0020037]; metal ion binding [GO:0046872]; nitrite reductase activity [GO:0098809]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601]
|
PF00042;
|
6.10.140.2100;6.10.140.2110;
|
Globin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:P02144}.
|
CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:0000250|UniProtKB:P02144}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:77713; Evidence={ECO:0000250|UniProtKB:P02144}; CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; Evidence={ECO:0000250|UniProtKB:P02144};
| null | null | null | null |
FUNCTION: Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand. Depending on the oxidative conditions of tissues and cells, and in addition to its ability to bind oxygen, it also has a nitrite reductase activity whereby it regulates the production of bioactive nitric oxide. Under stress conditions, like hypoxia and anoxia, it also protects cells against reactive oxygen species thanks to its pseudoperoxidase activity. {ECO:0000250|UniProtKB:P02144}.
|
Bos taurus (Bovine)
|
P02235
|
LGB2_SOYBN
|
MGAFTEKQEALVSSSFEAFKANIPQYSVVFYNSILEKAPAAKDLFSFLANGVDPTNPKLTGHAEKLFALVRDSAGQLKTNGTVVADAALVSIHAQKAVTDPQFVVVKEALLKTIKEAVGGNWSDELSSAWEVAYDELAAAIKKA
| null | null |
nodulation [GO:0009877]; response to cobalt ion [GO:0032025]; response to nitrogen compound [GO:1901698]
| null |
heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]
|
PF00042;
|
1.10.490.10;
|
Plant globin family
|
PTM: Nitrated mainly at Tyr-31 and, to a lower extent, at Tyr-26 and Tyr-134, in effective nodules and particularly in hypoxic conditions; this mechanism may play a protective role in the symbiosis by buffering toxic peroxynitrite NO(2)(-) (PubMed:17259612, PubMed:22308405, PubMed:25603991). Nitration level decrease during nodule senescence (PubMed:17259612, PubMed:25603991). {ECO:0000269|PubMed:17259612, ECO:0000269|PubMed:22308405, ECO:0000269|PubMed:25603991}.; PTM: Phosphorylation at Ser-46 disrupts the molecular environment of its porphyrin ring oxygen binding pocket, thus leading to a reduced oxygen consumption and to the delivery of oxygen O(2) to symbiosomes. {ECO:0000250|UniProtKB:Q3C1F7}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P02240}. Nucleus {ECO:0000250|UniProtKB:P02240}.
| null | null | null | null | null |
FUNCTION: Leghemoglobin that reversibly binds oxygen O(2) through a pentacoordinated heme iron (By similarity). In root nodules, facilitates the diffusion of oxygen to the bacteroids while preventing the bacterial nitrogenase from being inactivated by buffering dioxygen, nitric oxide and carbon monoxide, and promoting the formation of reactive oxygen species (ROS, e.g. H(2)O(2)) (PubMed:17540516, PubMed:22308405, PubMed:32297921). This role is essential for symbiotic nitrogen fixation (SNF) (PubMed:17540516, PubMed:32297921). {ECO:0000250|UniProtKB:Q43296, ECO:0000269|PubMed:22308405, ECO:0000269|PubMed:32297921, ECO:0000303|PubMed:17540516}.
|
Glycine max (Soybean) (Glycine hispida)
|
P02236
|
LGB4_SOYBN
|
MGAFTEKQEALVSSSFEAFKANIPQYSVVFYTSILEKAPAAKDLFSFLSNGVDPSNPKLTGHAEKLFGLVRDSAGQLKANGTVVADAALGSIHAQKAITDPQFVVVKEALLKTIKEAVGDKWSDELSSAWEVAYDELAAAIKKAF
| null | null |
nodulation [GO:0009877]; response to cobalt ion [GO:0032025]; response to nitrogen compound [GO:1901698]
| null |
heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]
|
PF00042;
|
1.10.490.10;
|
Plant globin family
|
PTM: Nitrated mainly at Tyr-31 and, to a lower extent, at Tyr-26 and Tyr-134, in effective nodules and particularly in hypoxic conditions; this mechanism may play a protective role in the symbiosis by buffering toxic peroxynitrite NO(2)(-) (PubMed:22308405). Nitration level decrease during nodule senescence (By similarity). {ECO:0000250|UniProtKB:P02235, ECO:0000269|PubMed:22308405}.; PTM: Phosphorylation at Ser-46 disrupts the molecular environment of its porphyrin ring oxygen binding pocket, thus leading to a reduced oxygen consumption and to the delivery of oxygen O(2) to symbiosomes. {ECO:0000250|UniProtKB:Q3C1F7}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P02240}. Nucleus {ECO:0000250|UniProtKB:P02240}.
| null | null | null | null | null |
FUNCTION: Leghemoglobin that reversibly binds oxygen O(2) through a pentacoordinated heme iron (By similarity). In root nodules, facilitates the diffusion of oxygen to the bacteroids while preventing the bacterial nitrogenase from being inactivated by buffering dioxygen, nitric oxide and carbon monoxide, and promoting the formation of reactive oxygen species (ROS, e.g. H(2)O(2)) (PubMed:17540516, PubMed:22308405, PubMed:32297921). This role is essential for symbiotic nitrogen fixation (SNF) (PubMed:17540516, PubMed:32297921). {ECO:0000250|UniProtKB:Q43296, ECO:0000269|PubMed:22308405, ECO:0000269|PubMed:32297921, ECO:0000303|PubMed:17540516}.
|
Glycine max (Soybean) (Glycine hispida)
|
P02237
|
LGB1_SOYBN
|
MGAFTDKQEALVSSSFEAFKTNIPQYSVVFYTSILEKAPVAKDLFSFLANGVDPTNPKLTGHAEKLFGLVRDSAGQLKASGTVVIDAALGSIHAQKAITDPQFVVVKEALLKTIKEAVGDKWSDELSSAWEVAYDELAAAIKKAF
| null | null |
nodulation [GO:0009877]; response to cobalt ion [GO:0032025]; response to nitrogen compound [GO:1901698]
| null |
heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]
|
PF00042;
|
1.10.490.10;
|
Plant globin family
|
PTM: Nitrated mainly at Tyr-31 and, to a lower extent, at Tyr-26 and Tyr-134, in effective nodules and particularly in hypoxic conditions; this mechanism may play a protective role in the symbiosis by buffering toxic peroxynitrite NO(2)(-) (PubMed:22308405). Nitration level decrease during nodule senescence (By similarity). {ECO:0000250|UniProtKB:P02235, ECO:0000269|PubMed:22308405}.; PTM: Phosphorylation at Ser-46 disrupts the molecular environment of its porphyrin ring oxygen binding pocket, thus leading to a reduced oxygen consumption and to the delivery of oxygen O(2) to symbiosomes. {ECO:0000250|UniProtKB:Q3C1F7}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P02240}. Nucleus {ECO:0000250|UniProtKB:P02240}.
| null | null | null | null | null |
FUNCTION: Leghemoglobin that reversibly binds oxygen O(2) through a pentacoordinated heme iron (By similarity). In root nodules, facilitates the diffusion of oxygen to the bacteroids while preventing the bacterial nitrogenase from being inactivated by buffering dioxygen, nitric oxide and carbon monoxide, and promoting the formation of reactive oxygen species (ROS, e.g. H(2)O(2)) (PubMed:17540516, PubMed:22308405, PubMed:32297921). This role is essential for symbiotic nitrogen fixation (SNF) (PubMed:17540516, PubMed:32297921). {ECO:0000250|UniProtKB:Q43296, ECO:0000269|PubMed:22308405, ECO:0000269|PubMed:32297921, ECO:0000303|PubMed:17540516}.
|
Glycine max (Soybean) (Glycine hispida)
|
P02238
|
LGB3_SOYBN
|
MVAFTEKQDALVSSSFEAFKANIPQYSVVFYTSILEKAPAAKDLFSFLANGVDPTNPKLTGHAEKLFALVRDSAGQLKASGTVVADAALGSVHAQKAVTDPQFVVVKEALLKTIKAAVGDKWSDELSRAWEVAYDELAAAIKKA
| null | null |
nodulation [GO:0009877]; response to cobalt ion [GO:0032025]; response to hydrogen sulfide [GO:1904880]; response to nitrogen compound [GO:1901698]
| null |
heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]
|
PF00042;
|
1.10.490.10;
|
Plant globin family
|
PTM: Nitrated mainly at Tyr-31 and, to a lower extent, at Tyr-26 and Tyr-134, in effective nodules and particularly in hypoxic conditions; this mechanism may play a protective role in the symbiosis by buffering toxic peroxynitrite NO(2)(-) (PubMed:17259612, PubMed:22308405, PubMed:25603991). Nitration level decrease during nodule senescence (PubMed:17259612, PubMed:22308405, PubMed:25603991). {ECO:0000269|PubMed:17259612, ECO:0000269|PubMed:22308405, ECO:0000269|PubMed:25603991}.; PTM: Phosphorylation at Ser-46 disrupts the molecular environment of its porphyrin ring oxygen binding pocket, thus leading to a reduced oxygen consumption and to the delivery of oxygen O(2) to symbiosomes. {ECO:0000250|UniProtKB:Q3C1F7}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P02240}. Nucleus {ECO:0000250|UniProtKB:P02240}.
| null | null | null | null | null |
FUNCTION: Leghemoglobin that reversibly binds oxygen O(2) through a pentacoordinated heme iron (PubMed:29100196). In root nodules, facilitates the diffusion of oxygen to the bacteroids while preventing the bacterial nitrogenase from being inactivated by buffering dioxygen, nitric oxide and carbon monoxide, and promoting the formation of reactive oxygen species (ROS, e.g. H(2)O(2)) (PubMed:17540516, PubMed:22308405, PubMed:29701804, PubMed:32297921). This role is essential for symbiotic nitrogen fixation (SNF) (PubMed:17540516, PubMed:32297921). {ECO:0000269|PubMed:22308405, ECO:0000269|PubMed:29100196, ECO:0000269|PubMed:29701804, ECO:0000269|PubMed:32297921, ECO:0000303|PubMed:17540516}.
|
Glycine max (Soybean) (Glycine hispida)
|
P02240
|
LGB2_LUPLU
|
MGALTESQAALVKSSWEEFNANIPKHTHRFFILVLEIAPAAKDLFSFLKGTSEVPQNNPELQAHAGKVFKLVYEAAIQLQVTGVVVTDATLKNLGSVHVSKGVADAHFPVVKEAILKTIKEVVGAKWSEELNSAWTIAYDELAIVIKKEMNDAA
| null | null |
response to nitrate [GO:0010167]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
heme binding [GO:0020037]; metal ion binding [GO:0046872]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]
|
PF00042;
|
1.10.490.10;
|
Plant globin family
|
PTM: Nitrated in effective nodules and particularly in hypoxic conditions; this mechanism may play a protective role in the symbiosis by buffering toxic peroxynitrite NO(2)(-). Nitration level decrease during nodule senescence. {ECO:0000250|UniProtKB:P02234}.; PTM: Phosphorylation at Ser-46 disrupts the molecular environment of its porphyrin ring oxygen binding pocket, thus leading to a reduced oxygen consumption and to the delivery of oxygen O(2) to symbiosomes. {ECO:0000250|UniProtKB:Q3C1F7}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16666792}. Nucleus {ECO:0000269|PubMed:16666792}.
| null | null | null | null | null |
FUNCTION: Leghemoglobin that reversibly binds oxygen O(2) through a pentacoordinated heme iron (PubMed:7643380, PubMed:8950274, Ref.5). In root nodules, facilitates the diffusion of oxygen to the bacteroids while preventing the bacterial nitrogenase from being inactivated by buffering dioxygen, nitric oxide and carbon monoxide, and promoting the formation of reactive oxygen species (ROS, e.g. H(2)O(2)) (By similarity). This role is essential for symbiotic nitrogen fixation (SNF) (By similarity). {ECO:0000250|UniProtKB:P02237, ECO:0000269|PubMed:7643380, ECO:0000269|PubMed:8950274, ECO:0000269|Ref.5}.
|
Lupinus luteus (European yellow lupine)
|
P02253
|
H12_BOVIN
|
MSETAPAAPAAAPPAEKTPVKKKAAKKPAGARRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAATGEAKPKAKKAGAAKPKKAAGAAKKTKKATGAATPKKTAKKTPKKAKKPAAAAVTKKVAKSPKKAKAAKPKKAAKSAAKAVKPKAAKPKVAKPKKAAPKKK
| null | null |
chromosome condensation [GO:0030261]; negative regulation of DNA recombination [GO:0045910]; nucleosome assembly [GO:0006334]
|
nucleosome [GO:0000786]; nucleus [GO:0005634]
|
double-stranded DNA binding [GO:0003690]; nucleosomal DNA binding [GO:0031492]; structural constituent of chromatin [GO:0030527]
|
PF00538;
|
1.10.10.10;
|
Histone H1/H5 family
|
PTM: H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter. {ECO:0000250}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes. {ECO:0000250|UniProtKB:P15864}.; PTM: ADP-ribosylated on Ser-188 in response to DNA damage. {ECO:0000250|UniProtKB:P16403}.; PTM: Citrullination at Arg-54 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance. {ECO:0000250|UniProtKB:P15864}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in euchromatin. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity). {ECO:0000250}.
|
Bos taurus (Bovine)
|
P02255
|
H1_DROME
|
MSDSAVATSASPVAAPPATVEKKVVQKKASGSAGTKAKKASATPSHPPTQQMVDASIKNLKERGGSSLLAIKKYITATYKCDAQKLAPFIKKYLKSAVVNGKLIQTKGKGASGSFKLSASAKKEKDPKAKSKVLSAEKKVQSKKVASKKIGVSSKKTAVGAADKKPKAKKAVATKKTAENKKTEKAKAKDAKKTGIIKSKPAATKAKVTAAKPKAVVAKASKAKPAVSAKPKKTVKKASVSATAKKPKAKTTAAKK
| null | null |
chromosome condensation [GO:0030261]; chromosome organization [GO:0051276]; heterochromatin formation [GO:0031507]; negative regulation of DNA recombination [GO:0045910]; nucleosome assembly [GO:0006334]
|
chromatin [GO:0000785]; nucleosome [GO:0000786]; nucleus [GO:0005634]
|
chromatin DNA binding [GO:0031490]; double-stranded DNA binding [GO:0003690]; nucleosomal DNA binding [GO:0031492]; structural constituent of chromatin [GO:0030527]
|
PF00538;
|
1.10.10.10;
|
Histone H1/H5 family
|
PTM: Phosphorylated in oocytes during prophase I of meiosis. {ECO:0000269|PubMed:16230526, ECO:0000269|PubMed:17372656}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome.
| null | null | null | null | null |
FUNCTION: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures.
|
Drosophila melanogaster (Fruit fly)
|
P02259
|
H5_CHICK
|
MTESLVLSPAPAKPKRVKASRRSASHPTYSEMIAAAIRAEKSRGGSSRQSIQKYIKSHYKVGHNADLQIKLSIRRLLAAGVLKQTKGVGASGSFRLAKSDKAKRSPGKKKKAVRRSTSPKKAARPRKARSPAKKPKATARKARKKSRASPKKAKKPKTVKAKSRKASKAKKVKRSKPRAKSGARKSPKKK
| null | null |
chromatin organization [GO:0006325]; chromosome condensation [GO:0030261]; negative regulation of DNA recombination [GO:0045910]; nucleosome assembly [GO:0006334]
|
nucleosome [GO:0000786]; nucleus [GO:0005634]
|
double-stranded DNA binding [GO:0003690]; nucleosomal DNA binding [GO:0031492]; structural constituent of chromatin [GO:0030527]
|
PF00538;
|
1.10.10.10;
|
Histone H1/H5 family
| null |
SUBCELLULAR LOCATION: Nucleus. Chromosome.
| null | null | null | null | null |
FUNCTION: Histone H5 performs the same function as H1, being necessary for the condensation of nucleosome chains into higher order structures, and replaces histone H1 in certain cells.
|
Gallus gallus (Chicken)
|
P02264
|
H2A_ONCMY
|
MSGRGKTGGKARAKAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKTEKAVKAK
| null | null |
defense response to fungus [GO:0050832]; defense response to Gram-positive bacterium [GO:0050830]; disruption of plasma membrane integrity in another organism [GO:0051673]; innate immune response [GO:0045087]; killing of cells of another organism [GO:0031640]
|
extracellular space [GO:0005615]; nucleosome [GO:0000786]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
|
PF00125;PF16211;
|
1.10.20.10;
|
Histone H2A family
|
PTM: Monoubiquitination of Lys-120 (H2AK119Ub) gives a specific tag for epigenetic transcriptional repression. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties, leading to the recruitment of repair proteins to sites of DNA damage. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination are distinct events (By similarity). {ECO:0000250}.; PTM: Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 directly represses transcription (By similarity). {ECO:0000250}.; PTM: Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=A secreted form has been detected in skin secretions.
| null | null | null | null | null |
FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:12164782}.; FUNCTION: The secreted form has antibacterial activity against Gram-positive bacteria and antifungal activity against S.cerevisiae. {ECO:0000269|PubMed:12164782}.
|
Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
|
P02273
|
H2AX_TETPY
|
MSTTGKGGKAKGKTASSKQVSRSARAGLQFPVGRISRFLKHGRYSERIGTGAPVYLAAVLEYLAAEVLELAGNAAKDNKKTRIVPRHILLAIRNDEELNKLMANTTIADGGVLPNINPMLLPSKSKKTESRGQASQDI
| null | null | null |
nucleosome [GO:0000786]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
|
PF00125;PF16211;
|
1.10.20.10;
|
Histone H2A family
|
PTM: Monoubiquitination of Lys-124 gives a specific tag for epigenetic transcriptional repression. {ECO:0000250}.; PTM: Acetylation occurs almost exclusively in the MAC. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Localizes to both the large, transcriptionally active, somatic macronucleus (MAC) and the small, transcriptionally inert, germ line micronucleus (MIC). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
|
Tetrahymena pyriformis
|
P02281
|
H2B11_XENLA
|
MPEPAKSAPAPKKGSKKAVTKTQKKDGKKRRKSRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSAK
| null | null | null |
nucleosome [GO:0000786]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
|
PF00125;
|
1.10.20.10;
|
Histone H2B family
|
PTM: Monoubiquitination of Lys-121 by BRE1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. {ECO:0000250|UniProtKB:P33778}.; PTM: Phosphorylated on Ser-15 during developmentally programmed apoptosis; which may facilitate apoptotic chromatin condensation. {ECO:0000269|PubMed:12757711}.; PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity). {ECO:0000250|UniProtKB:P62807}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome.
| null | null | null | null | null |
FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
|
Xenopus laevis (African clawed frog)
|
P02283
|
H2B_DROME
|
MPPKTSGKAAKKAGKAQKNITKTDKKKKRKRKESYAIYIYKVLKQVHPDTGISSKAMSIMNSFVNDIFERIAAEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK
| null | null |
chromatin organization [GO:0006325]
|
nucleosome [GO:0000786]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; protein-containing complex binding [GO:0044877]; structural constituent of chromatin [GO:0030527]
|
PF00125;
|
1.10.20.10;
|
Histone H2B family
|
PTM: Monoubiquitination of Lys-118 by Bre1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. {ECO:0000305|PubMed:3127388}.; PTM: Methylation at Pro-2 increases upon heat shock. {ECO:0000269|PubMed:3127388}.; PTM: GlcNAcylation at Ser-110 promotes monoubiquitination of Lys-118. It fluctuates in response to extracellular glucose, and associates with transcribed genes (Probable). {ECO:0000305}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome.
| null | null | null | null | null |
FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
|
Drosophila melanogaster (Fruit fly)
|
P02293
|
H2B1_YEAST
|
MSAKAEKKPASKAPAEKKPAAKKTSTSTDGKKRSKARKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERIATEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSEGTRAVTKYSSSTQA
| null | null |
chromatin organization [GO:0006325]; negative regulation of transcription by RNA polymerase II [GO:0000122]; postreplication repair [GO:0006301]; regulation of DNA-templated transcription [GO:0006355]
|
nucleosome [GO:0000786]; nucleus [GO:0005634]; replication fork protection complex [GO:0031298]
|
DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
|
PF00125;
|
1.10.20.10;
|
Histone H2B family
|
PTM: Monoubiquitinated by the RAD6/UBC2-BRE1 complex to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and H3K79me formation. H2BK123ub1 also modulates the formation of double-strand breaks during meiosis and is a prerequisite for DNA-damage checkpoint activation. Deubiquitination is performed by UBP8 in presence of SGF11.; PTM: Phosphorylated by STE20 to form H2BS10ph during progression through meiotic prophase. May be correlated with chromosome condensation. H2BS10ph is also formed after H(2)O(2) treatment, and is a step leading to apoptosis. {ECO:0000269|PubMed:15652479, ECO:0000269|PubMed:15970663}.; PTM: Acetylated by GCN5, a component of the SAGA complex, to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription. {ECO:0000269|PubMed:10777603, ECO:0000269|PubMed:11545749, ECO:0000269|PubMed:15186774, ECO:0000269|PubMed:16598039}.; PTM: Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su or H2BK17su, occurs preferentially near the telomeres and represses gene transcription. {ECO:0000269|PubMed:15166219, ECO:0000269|PubMed:16598039}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome.
| null | null | null | null | null |
FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:11973294, ECO:0000269|PubMed:12152067, ECO:0000269|PubMed:14752010, ECO:0000269|PubMed:15280549, ECO:0000269|PubMed:15632065, ECO:0000269|PubMed:15632126, ECO:0000269|PubMed:15652479, ECO:0000269|PubMed:15970663, ECO:0000269|PubMed:16598039}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P02294
|
H2B2_YEAST
|
MSSAAEKKPASKAPAEKKPAAKKTSTSVDGKKRSKVRKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERIATEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSEGTRAVTKYSSSTQA
| null | null |
chromatin organization [GO:0006325]; regulation of DNA-templated transcription [GO:0006355]
|
nucleosome [GO:0000786]; nucleus [GO:0005634]; replication fork protection complex [GO:0031298]
|
DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
|
PF00125;
|
1.10.20.10;
|
Histone H2B family
|
PTM: Monoubiquitinated by the RAD6/UBC2-BRE1 complex to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and H3K79me formation. H2BK123ub1 also modulates the formation of double-strand breaks during meiosis and is a prerequisite for DNA-damage checkpoint activation. Deubiquitination is performed by UBP8 in presence of SGF11.; PTM: Phosphorylated by STE20 to form H2BS10ph during progression through meiotic prophase. May be correlated with chromosome condensation. H2BS10ph is also formed after H(2)O(2) treatment, and is a step leading to apoptosis. {ECO:0000269|PubMed:15652479, ECO:0000269|PubMed:15970663}.; PTM: Acetylated by GCN5, a component of the SAGA complex, to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription. {ECO:0000269|PubMed:10777603, ECO:0000269|PubMed:11545749, ECO:0000269|PubMed:15186774, ECO:0000269|PubMed:16598039}.; PTM: Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su or H2BK17su, occurs preferentially near the telomeres and represses gene transcription. {ECO:0000269|PubMed:15166219, ECO:0000269|PubMed:16598039}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome.
| null | null | null | null | null |
FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. {ECO:0000269|PubMed:12152067, ECO:0000269|PubMed:14752010, ECO:0000269|PubMed:15280549, ECO:0000269|PubMed:15632065, ECO:0000269|PubMed:15652479, ECO:0000269|PubMed:15970663, ECO:0000269|PubMed:16598039}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P02299
|
H3_DROME
|
MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
| null | null |
nucleosome assembly [GO:0006334]
|
chromatin [GO:0000785]; nucleosome [GO:0000786]; polytene chromosome [GO:0005700]; RCAF complex [GO:0035059]
|
nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
|
PF00125;
|
1.10.20.10;
|
Histone H3 family
|
PTM: Phosphorylated at Thr-4 (H3T3ph) by Haspin during mitosis and interphase (PubMed:32750047). Phosphorylation at Ser-11 by aurB/ial during mitosis and meiosis is crucial for chromosome condensation and cell-cycle progression (PubMed:11114889, PubMed:11266459, PubMed:11371341, PubMed:12514098, PubMed:15175259). Phosphorylation at Ser-11 by JIL-1 during interphase is linked to gene activation and restricts the formation of heterochromatin at inappropriate sites. Phosphorylation at Ser-11 is enriched on male X chromosome compared to the autosome (PubMed:11114889, PubMed:11266459, PubMed:11371341, PubMed:12514098, PubMed:15175259). {ECO:0000269|PubMed:11114889, ECO:0000269|PubMed:11266459, ECO:0000269|PubMed:11371341, ECO:0000269|PubMed:12514098, ECO:0000269|PubMed:15175259, ECO:0000269|PubMed:32750047}.; PTM: Acetylation is generally linked to gene activation. Acetylated on Lys-15 during prophase I of meiosis. Phosphorylation of H2A 'Thr-119' is a prerequisite for H3 Lys-15 acetylation. Acetylation on Lys-15 is enriched on male X chromosome compared to the autosome. {ECO:0000269|PubMed:11114889, ECO:0000269|PubMed:11371341, ECO:0000269|PubMed:11859155, ECO:0000269|PubMed:14732680, ECO:0000269|PubMed:16230526}.; PTM: Methylation at Lys-5 or Lys-80 is generally associated with active chromatin. Methylation at Lys-80 by gpp occurs at low levels in specific developmental stages and tissues undergoing active cell division, and at highest levels in epidermal cells undergoing differentiation (PubMed:14732680, PubMed:15175259, PubMed:15371351). Tri-methylation at Lys-10 (H3K9me3) is generally associated with transcriptional repression (Probable). Tri-methylation at Lys-10 (H3K9me3) is partly stimulated at specific chromatin loci by homologous piRNAs (PubMed:25085419). Tri-methylation at Lys-10 (H3K9me3) stimulates recruitment of the Rhino-Deadlock-Cutoff (RDC) complex to promote piRNA biogenesis (PubMed:24906153, PubMed:25085419). {ECO:0000269|PubMed:14732680, ECO:0000269|PubMed:15175259, ECO:0000269|PubMed:15371351, ECO:0000269|PubMed:24906153, ECO:0000269|PubMed:25085419, ECO:0000305}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
|
Drosophila melanogaster (Fruit fly)
|
P02301
|
H3C_MOUSE
|
MALTKQTARKSTGGKAPRKQLATKATRKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
| null | null | null |
nucleosome [GO:0000786]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
|
PF00125;
|
1.10.20.10;
|
Histone H3 family
|
PTM: Acetylation is generally linked to gene activation. Acetylation on Lys-10 (H3K9ac) impairs methylation at Arg-9 (H3R8me2s). Acetylation on Lys-19 (H3K18ac) and Lys-24 (H3K24ac) favors methylation at Arg-18 (H3R17me). Acetylation at Lys-123 (H3K122ac) by EP300/p300 plays a central role in chromatin structure: localizes at the surface of the histone octamer and stimulates transcription, possibly by promoting nucleosome instability (By similarity). {ECO:0000250|UniProtKB:P84243}.; PTM: Citrullination at Arg-9 (H3R8ci) and/or Arg-18 (H3R17ci) by PADI4 impairs methylation and represses transcription. {ECO:0000250|UniProtKB:P84243}.; PTM: Butyrylation of histones marks active promoters and competes with histone acetylation. It is present during late spermatogenesis. {ECO:0000250|UniProtKB:P68433}.; PTM: Asymmetric dimethylation at Arg-18 (H3R17me2a) by CARM1 is linked to gene activation. Symmetric dimethylation at Arg-9 (H3R8me2s) by PRMT5 is linked to gene repression (By similarity). {ECO:0000250|UniProtKB:P84243}.; PTM: Methylation at Lys-5 (H3K4me), Lys-37 and Lys-80 are linked to gene activation. Methylation at Lys-5 (H3K4me) facilitates subsequent acetylation of H3 and H4. Methylation at Lys-80 is associated with DNA double-strand break (DSB) responses and is a specific target for TP53BP1. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are linked to gene repression. Methylation at Lys-10 (H3K9me) is a specific target for HP1 proteins (CBX1, CBX3 and CBX5) and prevents subsequent phosphorylation at Ser-11 (H3S10ph) and acetylation of H3 and H4. Methylation at Lys-5 (H3K4me) and Lys-80 require preliminary monoubiquitination of H2B at 'Lys-120'. Methylation at Lys-10 (H3K9me) and Lys-28 (H3K27me) are enriched in inactive X chromosome chromatin. Monomethylation at Lys-57 (H3K56me1) by EHMT2/G9A in G1 phase promotes interaction with PCNA and is required for DNA replication (By similarity). {ECO:0000250|UniProtKB:P84243}.; PTM: Phosphorylated at Thr-4 (H3T3ph) by HASPIN during prophase and dephosphorylated during anaphase. Phosphorylation at Ser-11 (H3S10ph) by AURKB is crucial for chromosome condensation and cell-cycle progression during mitosis and meiosis. In addition phosphorylation at Ser-11 (H3S10ph) by RPS6KA4 and RPS6KA5 is important during interphase because it enables the transcription of genes following external stimulation, like mitogens, stress, growth factors or UV irradiation and result in the activation of genes, such as c-fos and c-jun. Phosphorylation at Ser-11 (H3S10ph), which is linked to gene activation, prevents methylation at Lys-10 (H3K9me) but facilitates acetylation of H3 and H4. Phosphorylation at Ser-11 (H3S10ph) by AURKB mediates the dissociation of HP1 proteins (CBX1, CBX3 and CBX5) from heterochromatin. Phosphorylation at Ser-11 (H3S10ph) is also an essential regulatory mechanism for neoplastic cell transformation. Phosphorylated at Ser-29 (H3S28ph) by MAP3K20 isoform 1, RPS6KA5 or AURKB during mitosis or upon ultraviolet B irradiation. Phosphorylation at Thr-7 (H3T6ph) by PRKCB is a specific tag for epigenetic transcriptional activation that prevents demethylation of Lys-5 (H3K4me) by LSD1/KDM1A. At centromeres, specifically phosphorylated at Thr-12 (H3T11ph) from prophase to early anaphase, by DAPK3 and PKN1. Phosphorylation at Thr-12 (H3T11ph) by PKN1 or isoform M2 of PKM (PKM2) is a specific tag for epigenetic transcriptional activation that promotes demethylation of Lys-10 (H3K9me) by KDM4C/JMJD2C. Phosphorylation at Tyr-42 (H3Y41ph) by JAK2 promotes exclusion of CBX5 (HP1 alpha) from chromatin (By similarity). {ECO:0000250|UniProtKB:P84243}.; PTM: Lysine deamination at Lys-5 (H3K4all) to form allysine is mediated by LOXL2. Allysine formation by LOXL2 only takes place on H3K4me3 and results in gene repression (By similarity). {ECO:0000250|UniProtKB:P84243}.; PTM: Succinylation at Lys-80 (H3K79succ) by KAT2A takes place with a maximum frequency around the transcription start sites of genes. It gives a specific tag for epigenetic transcription activation. Desuccinylation at Lys-123 (H3K122succ) by SIRT7 in response to DNA damage promotes chromatin condensation and double-strand breaks (DSBs) repair. {ECO:0000250|UniProtKB:P68431}.; PTM: Serine ADP-ribosylation constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Serine ADP-ribosylation at Ser-11 (H3S10ADPr) is mutually exclusive with phosphorylation at Ser-11 (H3S10ph) and impairs acetylation at Lys-10 (H3K9ac). {ECO:0000250|UniProtKB:P68431}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome.
| null | null | null | null | null |
FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
|
Mus musculus (Mouse)
|
P02309
|
H4_YEAST
|
MSGRGKGGKGLGKGGAKRHRKILRDNIQGITKPAIRRLARRGGVKRISGLIYEEVRAVLKSFLESVIRDSVTYTEHAKRKTVTSLDVVYALKRQGRTLYGFGG
| null | null |
chromatin organization [GO:0006325]; nucleolar large rRNA transcription by RNA polymerase I [GO:0042790]; nucleosome assembly [GO:0006334]; positive regulation of transcription by RNA polymerase I [GO:0045943]; regulation of DNA-templated transcription [GO:0006355]
|
nucleosome [GO:0000786]; nucleus [GO:0005634]; replication fork protection complex [GO:0031298]; RNA polymerase I upstream activating factor complex [GO:0000500]
|
DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527]
|
PF15511;
|
1.10.20.10;
|
Histone H4 family
|
PTM: Glutarylation at Lys-92 (H4K91glu) destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes. {ECO:0000269|PubMed:31542297}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome.
| null | null | null | null | null |
FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Component of the UAF (upstream activation factor) complex which interacts with the upstream element of the RNA polymerase I promoter and forms a stable preinitiation complex. Together with SPT15/TBP UAF seems to stimulate basal transcription to a fully activated level.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P02315
|
H6_ONCMY
|
MPKRKSATKGDEPARRSARLSARPVPKPAAKPKKAAAPKKAVKGKKAAENGDAKAEAKVQAAGDGAGNAK
| null | null |
defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]
|
chromatin [GO:0000785]; extracellular region [GO:0005576]; nucleus [GO:0005634]
|
double-stranded DNA binding [GO:0003690]; nucleic acid binding [GO:0003676]; nucleosomal DNA binding [GO:0031492]
|
PF01101;
| null |
HMGN family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Oncorhyncin-3]: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Non-histone protein that probably binds to the inner side of nucleosomal DNA, altering the association between the DNA and the nucleosome octamer. {ECO:0000269|PubMed:12713443}.; FUNCTION: Oncorhyncin III has antibacterial activity against Gram-positive and Gram-negative bacteria at submicromolar concentrations. {ECO:0000269|PubMed:12713443}.
|
Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
|
P02319
|
HSP1_MOUSE
|
MARYRCCRSKSRSRCRRRRRRCRRRRRRCCRRRRRRCCRRRRSYTIRCKKY
| null | null |
chromosome condensation [GO:0030261]; nucleus organization [GO:0006997]; sperm DNA condensation [GO:0035092]; spermatid development [GO:0007286]
|
male germ cell nucleus [GO:0001673]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]
|
PF00260;
| null |
Protamine P1 family
|
PTM: Phosphorylated by SRPK1. {ECO:0000269|PubMed:10390541}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome.
| null | null | null | null | null |
FUNCTION: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex.
|
Mus musculus (Mouse)
|
P02340
|
P53_MOUSE
|
MTAMEESQSDISLELPLSQETFSGLWKLLPPEDILPSPHCMDDLLLPQDVEEFFEGPSEALRVSGAPAAQDPVTETPGPVAPAPATPWPLSSFVPSQKTYQGNYGFHLGFLQSGTAKSVMCTYSPPLNKLFCQLAKTCPVQLWVSATPPAGSRVRAMAIYKKSQHMTEVVRRCPHHERCSDGDGLAPPQHLIRVEGNLYPEYLEDRQTFRHSVVVPYEPPEAGSEYTTIHYKYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENFRKKEVLCPELPPGSAKRALPTCTSASPPQKKKPLDGEYFTLKIRGRKRFEMFRELNEALELKDAHATEESGDSRAHSSYLKTKKGQSTSRHKKTMVKKVGPDSD
| null |
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16717092}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:16717092};
|
apoptotic process [GO:0006915]; apoptotic signaling pathway [GO:0097190]; B cell lineage commitment [GO:0002326]; bone marrow development [GO:0048539]; cardiac muscle cell apoptotic process [GO:0010659]; cardiac septum morphogenesis [GO:0060411]; cell population proliferation [GO:0008283]; cellular response to actinomycin D [GO:0072717]; cellular response to gamma radiation [GO:0071480]; cellular response to glucose starvation [GO:0042149]; cellular response to ionizing radiation [GO:0071479]; cellular response to reactive oxygen species [GO:0034614]; cellular response to UV [GO:0034644]; cellular response to UV-C [GO:0071494]; cellular response to xenobiotic stimulus [GO:0071466]; cellular senescence [GO:0090398]; central nervous system development [GO:0007417]; cerebellum development [GO:0021549]; chromosome organization [GO:0051276]; circadian behavior [GO:0048512]; circadian rhythm [GO:0007623]; determination of adult lifespan [GO:0008340]; DNA damage response [GO:0006974]; DNA damage response, signal transduction by p53 class mediator [GO:0030330]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator [GO:0006978]; double-strand break repair [GO:0006302]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic organ development [GO:0048568]; entrainment of circadian clock by photoperiod [GO:0043153]; ER overload response [GO:0006983]; fibroblast proliferation [GO:0048144]; gastrulation [GO:0007369]; glial cell proliferation [GO:0014009]; glucose catabolic process to lactate via pyruvate [GO:0019661]; heart development [GO:0007507]; hematopoietic stem cell differentiation [GO:0060218]; in utero embryonic development [GO:0001701]; intrinsic apoptotic signaling pathway by p53 class mediator [GO:0072332]; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [GO:0042771]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; intrinsic apoptotic signaling pathway in response to hypoxia [GO:1990144]; mitochondrial DNA repair [GO:0043504]; mitophagy [GO:0000423]; mitotic G1 DNA damage checkpoint signaling [GO:0031571]; mRNA transcription [GO:0009299]; multicellular organism growth [GO:0035264]; necroptotic process [GO:0070266]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell growth [GO:0030308]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA biosynthetic process [GO:2000279]; negative regulation of DNA replication [GO:0008156]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of fibroblast proliferation [GO:0048147]; negative regulation of G1 to G0 transition [GO:1903451]; negative regulation of gene expression [GO:0010629]; negative regulation of glial cell proliferation [GO:0060253]; negative regulation of glucose catabolic process to lactate via pyruvate [GO:1904024]; negative regulation of miRNA processing [GO:1903799]; negative regulation of mitophagy [GO:1901525]; negative regulation of mitotic cell cycle [GO:0045930]; negative regulation of neuroblast proliferation [GO:0007406]; negative regulation of pentose-phosphate shunt [GO:1905856]; negative regulation of proteolysis [GO:0045861]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; negative regulation of smooth muscle cell proliferation [GO:0048662]; negative regulation of stem cell proliferation [GO:2000647]; negative regulation of telomere maintenance via telomerase [GO:0032211]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; neuroblast proliferation [GO:0007405]; neuron apoptotic process [GO:0051402]; nucleotide-excision repair [GO:0006289]; oligodendrocyte apoptotic process [GO:0097252]; oxidative stress-induced premature senescence [GO:0090403]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cardiac muscle cell apoptotic process [GO:0010666]; positive regulation of cell cycle [GO:0045787]; positive regulation of cellular senescence [GO:2000774]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of execution phase of apoptosis [GO:1900119]; positive regulation of gene expression [GO:0010628]; positive regulation of intrinsic apoptotic signaling pathway [GO:2001244]; positive regulation of leukocyte migration [GO:0002687]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of mitochondrial membrane permeability [GO:0035794]; positive regulation of neuron apoptotic process [GO:0043525]; positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731]; positive regulation of programmed necrotic cell death [GO:0062100]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; positive regulation of release of cytochrome c from mitochondria [GO:0090200]; positive regulation of RNA polymerase II transcription preinitiation complex assembly [GO:0045899]; positive regulation of thymocyte apoptotic process [GO:0070245]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein import into nucleus [GO:0006606]; protein stabilization [GO:0050821]; protein tetramerization [GO:0051262]; Ras protein signal transduction [GO:0007265]; reactive oxygen species metabolic process [GO:0072593]; regulation of apoptotic process [GO:0042981]; regulation of cell cycle [GO:0051726]; regulation of cell cycle G2/M phase transition [GO:1902749]; regulation of cell population proliferation [GO:0042127]; regulation of cellular senescence [GO:2000772]; regulation of DNA damage response, signal transduction by p53 class mediator [GO:0043516]; regulation of DNA-templated transcription [GO:0006355]; regulation of fibroblast apoptotic process [GO:2000269]; regulation of intracellular pH [GO:0051453]; regulation of intrinsic apoptotic signaling pathway by p53 class mediator [GO:1902253]; regulation of mitochondrial membrane permeability involved in apoptotic process [GO:1902108]; regulation of mitotic cell cycle [GO:0007346]; regulation of neuron apoptotic process [GO:0043523]; regulation of thymocyte apoptotic process [GO:0070243]; regulation of tissue remodeling [GO:0034103]; regulation of transcription by RNA polymerase II [GO:0006357]; release of cytochrome c from mitochondria [GO:0001836]; replicative senescence [GO:0090399]; response to gamma radiation [GO:0010332]; response to inorganic substance [GO:0010035]; response to ischemia [GO:0002931]; response to oxidative stress [GO:0006979]; response to salt stress [GO:0009651]; response to UV [GO:0009411]; response to X-ray [GO:0010165]; response to xenobiotic stimulus [GO:0009410]; rRNA transcription [GO:0009303]; signal transduction by p53 class mediator [GO:0072331]; somitogenesis [GO:0001756]; spermatogenesis [GO:0007283]; stem cell proliferation [GO:0072089]; T cell differentiation in thymus [GO:0033077]; T cell lineage commitment [GO:0002360]; T cell proliferation involved in immune response [GO:0002309]; thymocyte apoptotic process [GO:0070242]; transcription initiation-coupled chromatin remodeling [GO:0045815]; transforming growth factor beta receptor signaling pathway [GO:0007179]; tumor necrosis factor-mediated signaling pathway [GO:0033209]; type II interferon-mediated signaling pathway [GO:0060333]; viral process [GO:0016032]
|
centrosome [GO:0005813]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; germ cell nucleus [GO:0043073]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]; replication fork [GO:0005657]; RNA polymerase II transcription regulator complex [GO:0090575]; site of double-strand break [GO:0035861]; transcription regulator complex [GO:0005667]; transcription repressor complex [GO:0017053]
|
ATP-dependent DNA/DNA annealing activity [GO:0036310]; chromatin binding [GO:0003682]; copper ion binding [GO:0005507]; core promoter sequence-specific DNA binding [GO:0001046]; disordered domain specific binding [GO:0097718]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; histone deacetylase binding [GO:0042826]; histone deacetylase regulator activity [GO:0035033]; identical protein binding [GO:0042802]; MDM2/MDM4 family protein binding [GO:0097371]; molecular function activator activity [GO:0140677]; mRNA 3'-UTR binding [GO:0003730]; p53 binding [GO:0002039]; promoter-specific chromatin binding [GO:1990841]; protease binding [GO:0002020]; protein heterodimerization activity [GO:0046982]; protein phosphatase 2A binding [GO:0051721]; protein self-association [GO:0043621]; protein-folding chaperone binding [GO:0051087]; receptor tyrosine kinase binding [GO:0030971]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific DNA binding [GO:0043565]; TFIID-class transcription factor complex binding [GO:0001094]; transcription coregulator binding [GO:0001221]; transmembrane transporter binding [GO:0044325]; ubiquitin protein ligase binding [GO:0031625]
|
PF00870;PF08563;PF07710;
|
2.60.40.720;6.10.50.20;4.10.170.10;
|
P53 family
|
PTM: Phosphorylation on Ser residues mediates transcriptional activation. Phosphorylation at Ser-12 by HIPK4 increases repression activity on BIRC5 promoter. Phosphorylated on Thr-21 by VRK1. Phosphorylated on Ser-23 by CHEK2 in response to DNA damage, which prevents ubiquitination by MDM2. Phosphorylated on Ser-23 by PLK3 in response to reactive oxygen species (ROS), promoting p53/TP53-mediated apoptosis. Probably phosphorylated on by CDK7 in a CAK complex in response to DNA damage. Stabilized by CDK5-mediated phosphorylation in response to genotoxic and oxidative stresses at Ser-18 leading to accumulation of p53/TP53, particularly in the nucleus, thus inducing the transactivation of p53/TP53 target genes (By similarity). Phosphorylated on Ser-389 following UV but not gamma irradiation. Phosphorylated by HIPK1. Phosphorylation at Ser-18 is required for interaction with DDX3X and gamma-tubulin (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P04637, ECO:0000269|PubMed:12702766, ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:17254968, ECO:0000269|PubMed:18022393, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:2145148, ECO:0000269|PubMed:3006031}.; PTM: Ubiquitinated by MDM2 and SYVN1, which leads to proteasomal degradation. Ubiquitinated by RFWD3, which works in cooperation with MDM2 and may catalyze the formation of short polyubiquitin chains on p53/TP53 that are not targeted to the proteasome. Ubiquitinated by MKRN1 at Lys-288 and Lys-289, which leads to proteasomal degradation. Deubiquitinated by USP10, leading to stabilize it. Ubiquitinated by TRIM24, RFFL, RNF34 and RNF125, which leads to proteasomal degradation. Ubiquitination by TOPORS induces degradation. Deubiquitination by USP7, leading to stabilize it. Ubiquitinated by COP1, which leads to proteasomal degradation (By similarity). Ubiquitination and subsequent proteasomal degradation is negatively regulated by CCAR2 (PubMed:25732823). Polyubiquitinated by C10orf90/FATS, polyubiquitination is 'Lys-48'-linkage independent and non-proteolytic, leading to TP53 stabilization (PubMed:24240685). {ECO:0000250|UniProtKB:P04637, ECO:0000269|PubMed:24240685, ECO:0000269|PubMed:25732823}.; PTM: Monomethylated at Lys-369 by SETD7, leading to stabilization and increased transcriptional activation. Monomethylated at Lys-367 by SMYD2, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity. Lys-369 monomethylation prevents interaction with SMYD2 and subsequent monomethylation at Lys-367. Dimethylated at Lys-370 by EHMT1 and EHMT2. Monomethylated at Lys-379 by KMT5A, promoting interaction with L3MBTL1 and leading to repress transcriptional activity. Demethylation of dimethylated Lys-367 by KDM1A prevents interaction with TP53BP1 and represses TP53-mediated transcriptional activation (By similarity). Monomethylated at Arg-330 and dimethylated at Arg-332 and Arg-334 by PRMT5; methylation is increased after DNA damage and might possibly affect TP53 target gene specificity (By similarity). Polyubiquitinated by MUL1 at Lys-27 which leads to proteasomal degradation (By similarity). Deubiquitinated by USP3, leading to stabilization (By similarity). Ubiquitinated by MSL2, promoting its cytoplasmic localization (By similarity). {ECO:0000250|UniProtKB:P04637}.; PTM: Sumoylated with SUMO1. Sumoylated at Lys-383 by UBC9 (By similarity). {ECO:0000250}.; PTM: Acetylation of Lys-379 by CREBBP enhances transcriptional activity. Acetylation of Lys-379 by EP300. Deacetylation of Lys-379 by SIRT1 impairs its ability to induce proapoptotic program and modulate cell senescence. Deacetylation by SIRT2 impairs its ability to induce transcription activation in a AKT-dependent manner. Acetylation at Lys-378 increases stability. Deacetylation at Lys-378 by SIRT6 decreases its stability, thereby regulating cell senescence. Acetylated at Lys-117 by KAT5, KAT6A and KAT8; regulating its ability to induce proapoptotic program. {ECO:0000250|UniProtKB:P04637}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04637}. Nucleus {ECO:0000250|UniProtKB:P04637}. Nucleus, PML body {ECO:0000250|UniProtKB:P04637}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P04637}. Mitochondrion matrix {ECO:0000250|UniProtKB:P04637}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P04637}. Note=Interaction with BANP promotes nuclear localization. Recruited into PML bodies together with CHEK2. Translocates to mitochondria upon oxidative stress. Translocates to mitochondria in response to mitomycin C treatment (By similarity). Competitive inhibition of TP53 interaction with HSPA9/MOT-2 by UBXN2A results in increased protein abundance and subsequent translocation of TP53 to the nucleus (By similarity). {ECO:0000250|UniProtKB:P04637}.
| null | null | null | null | null |
FUNCTION: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Its pro-apoptotic activity is activated via its interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 (By similarity). However, this activity is inhibited when the interaction with PPP1R13B/ASPP1 or TP53BP2/ASPP2 is displaced by PPP1R13L/iASPP (By similarity). In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression (By similarity). Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis, but seems to have to effect on cell-cycle regulation. Regulates the circadian clock by repressing CLOCK-BMAL1-mediated transcriptional activation of PER2 (PubMed:24051492). {ECO:0000250|UniProtKB:P04637, ECO:0000269|PubMed:19556538, ECO:0000269|PubMed:20673990, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:24051492}.
|
Mus musculus (Mouse)
|
P02358
|
RS6_ECOLI
|
MRHYEIVFMVHPDQSEQVPGMIERYTAAITGAEGKIHRLEDWGRRQLAYPINKLHKAHYVLMNVEAPQEVIDELETTFRFNDAVIRSMVMRTKHAVTEASPMVKAKDERRERRDDFANETADDAEAGDSEEEEEE
| null | null |
cytoplasmic translation [GO:0002181]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]
|
mRNA 5'-UTR binding [GO:0048027]; small ribosomal subunit rRNA binding [GO:0070181]; structural constituent of ribosome [GO:0003735]
|
PF01250;
|
3.30.70.60;
|
Bacterial ribosomal protein bS6 family
|
PTM: 5 different forms of the protein, varying only in the number of C-terminal glutamate residues, were isolated. The sequence shown is form bS6-6, which is the longest. The first two Glu are encoded by the rpsF gene, the other Glu are added post-translationally by the RimK enzyme. {ECO:0000269|PubMed:328274}.
| null | null | null | null | null | null |
FUNCTION: Binds together with bS18 to 16S ribosomal RNA.
|
Escherichia coli (strain K12)
|
P02359
|
RS7_ECOLI
|
MPRRRVIGQRKILPDPKFGSELLAKFVNILMVDGKKSTAESIVYSALETLAQRSGKSELEAFEVALENVRPTVEVKSRRVGGSTYQVPVEVRPVRRNALAMRWIVEAARKRGDKSMALRLANELSDAAENKGTAVKKREDVHRMAEANKAFAHYRWLSLRSFSHQAGASSKQPALGYLN
| null | null |
cytoplasmic translation [GO:0002181]; negative regulation of translation [GO:0017148]; ribosomal small subunit assembly [GO:0000028]; translation [GO:0006412]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; membrane [GO:0016020]; ribosome [GO:0005840]
|
mRNA binding [GO:0003729]; rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735]; tRNA binding [GO:0000049]
|
PF00177;
|
1.10.455.10;
|
Universal ribosomal protein uS7 family
| null | null | null | null | null | null | null |
FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit (PubMed:2461734). Is located at the subunit interface close to the decoding center, where it has been shown to contact mRNA (PubMed:10606263). Has been shown to contact tRNA in both the P and E sites; it probably blocks exit of the E site tRNA (PubMed:8524654). {ECO:0000269|PubMed:10606263, ECO:0000269|PubMed:2461734, ECO:0000269|PubMed:8524654}.; FUNCTION: Protein S7 is also a translational repressor protein; it regulates the expression of the str operon members to different degrees by binding to its mRNA. {ECO:0000269|PubMed:7507167}.
|
Escherichia coli (strain K12)
|
P02400
|
RLA4_YEAST
|
MKYLAAYLLLVQGGNAAPSAADIKAVVESVGAEVDEARINELLSSLEGKGSLEEIIAEGQKKFATVPTGGASSAAAGAAGAAAGGDAAEEEKEEEAKEESDDDMGFGLFD
| null | null |
cytoplasmic translation [GO:0002181]; cytoplasmic translational elongation [GO:0002182]
|
cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; fungal-type vacuole [GO:0000324]
|
molecular function inhibitor activity [GO:0140678]; protein kinase activator activity [GO:0030295]; structural constituent of ribosome [GO:0003735]
|
PF00428;
|
1.10.10.1410;
|
Eukaryotic ribosomal protein P1/P2 family
|
PTM: The N-terminus is not modified. {ECO:0000269|PubMed:8476850}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
| null | null | null | null | null |
FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. {ECO:0000305|PubMed:22096102}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P02402
|
RLA1_ARTSA
|
MASKDELACVYAALILLDDDVDITTEKVNTILRAAGVSVEPYWPGLFTKALEGLDLKSMITNVGSGVGAAPAAGGAAAATEAPAAKEEKKEEKKEESEEEDEDMGFGLFD
| null | null |
cytoplasmic translation [GO:0002181]; translational elongation [GO:0006414]
|
cytosolic large ribosomal subunit [GO:0022625]
|
protein kinase activator activity [GO:0030295]; ribonucleoprotein complex binding [GO:0043021]; structural constituent of ribosome [GO:0003735]
|
PF00428;
|
1.10.10.1410;
|
Eukaryotic ribosomal protein P1/P2 family
|
PTM: Phosphorylation of Ser-97 converts eL12' to eL12'-P.
| null | null | null | null | null | null |
FUNCTION: Plays an important role in the elongation step of protein synthesis.
|
Artemia salina (Brine shrimp)
|
P02406
|
RL28_YEAST
|
MPSRFTKTRKHRGHVSAGKGRIGKHRKHPGGRGMAGGQHHHRINMDKYHPGYFGKVGMRYFHKQQAHFWKPVLNLDKLWTLIPEDKRDQYLKSASKETAPVIDTLAAGYGKILGKGRIPNVPVIVKARFVSKLAEEKIRAAGGVVELIA
| null | null |
cytoplasmic translation [GO:0002181]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; nucleus [GO:0005634]
|
RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]
|
PF00828;
|
3.100.10.10;
|
Universal ribosomal protein uL15 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}.
| null | null | null | null | null |
FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. {ECO:0000305|PubMed:22096102}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P02452
|
CO1A1_HUMAN
|
MFSFVDLRLLLLLAATALLTHGQEEGQVEGQDEDIPPITCVQNGLRYHDRDVWKPEPCRICVCDNGKVLCDDVICDETKNCPGAEVPEGECCPVCPDGSESPTDQETTGVEGPKGDTGPRGPRGPAGPPGRDGIPGQPGLPGPPGPPGPPGPPGLGGNFAPQLSYGYDEKSTGGISVPGPMGPSGPRGLPGPPGAPGPQGFQGPPGEPGEPGASGPMGPRGPPGPPGKNGDDGEAGKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDAGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGAPGPAGARGNDGATGAAGPPGPTGPAGPPGFPGAVGAKGEAGPQGPRGSEGPQGVRGEPGPPGPAGAAGPAGNPGADGQPGAKGANGAPGIAGAPGFPGARGPSGPQGPGGPPGPKGNSGEPGAPGSKGDTGAKGEPGPVGVQGPPGPAGEEGKRGARGEPGPTGLPGPPGERGGPGSRGFPGADGVAGPKGPAGERGSPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQDGRPGPPGPPGARGQAGVMGFPGPKGAAGEPGKAGERGVPGPPGAVGPAGKDGEAGAQGPPGPAGPAGERGEQGPAGSPGFQGLPGPAGPPGEAGKPGEQGVPGDLGAPGPSGARGERGFPGERGVQGPPGPAGPRGANGAPGNDGAKGDAGAPGAPGSQGAPGLQGMPGERGAAGLPGPKGDRGDAGPKGADGSPGKDGVRGLTGPIGPPGPAGAPGDKGESGPSGPAGPTGARGAPGDRGEPGPPGPAGFAGPPGADGQPGAKGEPGDAGAKGDAGPPGPAGPAGPPGPIGNVGAPGAKGARGSAGPPGATGFPGAAGRVGPPGPSGNAGPPGPPGPAGKEGGKGPRGETGPAGRPGEVGPPGPPGPAGEKGSPGADGPAGAPGTPGPQGIAGQRGVVGLPGQRGERGFPGLPGPSGEPGKQGPSGASGERGPPGPMGPPGLAGPPGESGREGAPGAEGSPGRDGSPGAKGDRGETGPAGPPGAPGAPGAPGPVGPAGKSGDRGETGPAGPAGPVGPVGARGPAGPQGPRGDKGETGEQGDRGIKGHRGFSGLQGPPGPPGSPGEQGPSGASGPAGPRGPPGSAGAPGKDGLNGLPGPIGPPGPRGRTGDAGPVGPPGPPGPPGPPGPPSAGFDFSFLPQPPQEKAHDGGRYYRADDANVVRDRDLEVDTTLKSLSQQIENIRSPEGSRKNPARTCRDLKMCHSDWKSGEYWIDPNQGCNLDAIKVFCNMETGETCVYPTQPSVAQKNWYISKNPKDKRHVWFGESMTDGFQFEYGGQGSDPADVAIQLTFLRLMSTEASQNITYHCKNSVAYMDQQTGNLKKALLLQGSNEIEIRAEGNSRFTYSVTVDGCTSHTGAWGKTVIEYKTTKTSRLPIIDVAPLDVGAPDQEFGFDVGPVCFL
| null | null |
blood vessel development [GO:0001568]; bone trabecula formation [GO:0060346]; cartilage development involved in endochondral bone morphogenesis [GO:0060351]; cellular response to amino acid stimulus [GO:0071230]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to fluoride [GO:1902618]; cellular response to glucose stimulus [GO:0071333]; cellular response to mechanical stimulus [GO:0071260]; cellular response to retinoic acid [GO:0071300]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to vitamin E [GO:0071306]; collagen biosynthetic process [GO:0032964]; collagen fibril organization [GO:0030199]; collagen-activated tyrosine kinase receptor signaling pathway [GO:0038063]; embryonic skeletal system development [GO:0048706]; endochondral ossification [GO:0001958]; extracellular matrix organization [GO:0030198]; face morphogenesis [GO:0060325]; intramembranous ossification [GO:0001957]; negative regulation of cell-substrate adhesion [GO:0010812]; ossification [GO:0001503]; osteoblast differentiation [GO:0001649]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell migration [GO:0030335]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; protein localization to nucleus [GO:0034504]; protein transport [GO:0015031]; response to cAMP [GO:0051591]; response to estradiol [GO:0032355]; response to hydrogen peroxide [GO:0042542]; response to hyperoxia [GO:0055093]; response to insulin [GO:0032868]; response to mechanical stimulus [GO:0009612]; response to steroid hormone [GO:0048545]; response to xenobiotic stimulus [GO:0009410]; sensory perception of sound [GO:0007605]; skeletal system development [GO:0001501]; skin development [GO:0043588]; skin morphogenesis [GO:0043589]; tooth mineralization [GO:0034505]; visual perception [GO:0007601]
|
collagen type I trimer [GO:0005584]; collagen type IV trimer [GO:0005587]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; secretory granule [GO:0030141]
|
extracellular matrix structural constituent conferring tensile strength [GO:0030020]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; platelet-derived growth factor binding [GO:0048407]; protease binding [GO:0002020]
|
PF01410;PF01391;PF00093;
|
2.60.120.1000;1.20.5.320;2.10.70.10;
|
Fibrillar collagen family
|
PTM: Contains mostly 4-hydroxyproline. Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000269|PubMed:4319110}.; PTM: Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline. {ECO:0000250|UniProtKB:P11087}.; PTM: Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains. {ECO:0000269|PubMed:4319110}.; PTM: O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide. {ECO:0000269|PubMed:4319110}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
| null | null | null | null | null |
FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen).
|
Homo sapiens (Human)
|
P02453
|
CO1A1_BOVIN
|
MFSFVDLRLLLLLAATALLTHGQEEGQEEGQEEDIPPVTCVQNGLRYHDRDVWKPVPCQICVCDNGNVLCDDVICDELKDCPNAKVPTDECCPVCPEGQESPTDQETTGVEGPKGDTGPRGPRGPAGPPGRDGIPGQPGLPGPPGPPGPPGPPGLGGNFAPQLSYGYDEKSTGISVPGPMGPSGPRGLPGPPGAPGPQGFQGPPGEPGEPGASGPMGPRGPPGPPGKNGDDGEAGKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDAGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGAPGPAGARGNDGATGAAGPPGPTGPAGPPGFPGAVGAKGEGGPQGPRGSEGPQGVRGEPGPPGPAGAAGPAGNPGADGQPGAKGANGAPGIAGAPGFPGARGPSGPQGPSGPPGPKGNSGEPGAPGSKGDTGAKGEPGPTGIQGPPGPAGEEGKRGARGEPGPAGLPGPPGERGGPGSRGFPGADGVAGPKGPAGERGAPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQDGRPGPPGPPGARGQAGVMGFPGPKGAAGEPGKAGERGVPGPPGAVGPAGKDGEAGAQGPPGPAGPAGERGEQGPAGSPGFQGLPGPAGPPGEAGKPGEQGVPGDLGAPGPSGARGERGFPGERGVQGPPGPAGPRGANGAPGNDGAKGDAGAPGAPGSQGAPGLQGMPGERGAAGLPGPKGDRGDAGPKGADGAPGKDGVRGLTGPIGPPGPAGAPGDKGEAGPSGPAGPTGARGAPGDRGEPGPPGPAGFAGPPGADGQPGAKGEPGDAGAKGDAGPPGPAGPAGPPGPIGNVGAPGPKGARGSAGPPGATGFPGAAGRVGPPGPSGNAGPPGPPGPAGKEGSKGPRGETGPAGRPGEVGPPGPPGPAGEKGAPGADGPAGAPGTPGPQGIAGQRGVVGLPGQRGERGFPGLPGPSGEPGKQGPSGASGERGPPGPMGPPGLAGPPGESGREGAPGAEGSPGRDGSPGAKGDRGETGPAGPPGAPGAPGAPGPVGPAGKSGDRGETGPAGPAGPIGPVGARGPAGPQGPRGDKGETGEQGDRGIKGHRGFSGLQGPPGPPGSPGEQGPSGASGPAGPRGPPGSAGSPGKDGLNGLPGPIGPPGPRGRTGDAGPAGPPGPPGPPGPPGPPSGGYDLSFLPQPPQEKAHDGGRYYRADDANVVRDRDLEVDTTLKSLSQQIENIRSPEGSRKNPARTCRDLKMCHSDWKSGEYWIDPNQGCNLDAIKVFCNMETGETCVYPTQPSVAQKNWYISKNPKEKRHVWYGESMTGGFQFEYGGQGSDPADVAIQLTFLRLMSTEASQNITYHCKNSVAYMDQQTGNLKKALLLQGSNEIEIRAEGNSRFTYSVTYDGCTSHTGAWGKTVIEYKTTKTSRLPIIDVAPLDVGAPDQEFGFDVGPACFL
| null | null |
blood vessel development [GO:0001568]; extracellular matrix organization [GO:0030198]; ossification [GO:0001503]; response to mechanical stimulus [GO:0009612]; skeletal system development [GO:0001501]; skin development [GO:0043588]
|
collagen type I trimer [GO:0005584]; collagen type IV trimer [GO:0005587]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]
|
extracellular matrix structural constituent conferring tensile strength [GO:0030020]; metal ion binding [GO:0046872]
|
PF01410;PF01391;PF00093;
|
2.60.120.1000;2.10.70.10;
|
Fibrillar collagen family
|
PTM: Contains mostly 4-hydroxyproline. Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000269|PubMed:1164916, ECO:0000269|PubMed:11946479}.; PTM: Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline. {ECO:0000269|PubMed:11946479}.; PTM: Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains. {ECO:0000250|UniProtKB:P02457}.; PTM: O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide. {ECO:0000250|UniProtKB:P11087}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
| null | null | null | null | null |
FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen).
|
Bos taurus (Bovine)
|
P02454
|
CO1A1_RAT
|
MFSFVDLRLLLLLGATALLTHGQEDIPEVSCIHNGLRVPNGETWKPDVCLICICHNGTAVCDGVLCKEDLDCPNPQKREGECCPFCPEEYVSPDAEVIGVEGPKGDPGPQGPRGPVGPPGQDGIPGQPGLPGPPGPPGPPGPPGLGGNFASQMSYGYDEKSAGVSVPGPMGPSGPRGLPGPPGAPGPQGFQGPPGEPGEPGASGPMGPRGPPGPPGKNGDDGEAGKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDTGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGPPGSAGARGNDGAVGAAGPPGPTGPTGPPGFPGAAGAKGEAGPQGARGSEGPQGVRGEPGPPGPAGAAGPAGNPGADGQPGAKGANGAPGIAGAPGFPGARGPSGPQGPSGAPGPKGNSGEPGAPGNKGDTGAKGEPGPAGVQGPPGPAGEEGKRGARGEPGPSGLPGPPGERGGPGSRGFPGADGVAGPKGPAGERGSPGPAGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQDGRPGPAGPPGARGQAGVMGFPGPKGTAGEPGKAGERGVPGPPGAVGPAGKDGEAGAQGAPGPAGPAGERGEQGPAGSPGFQGLPGPAGPPGEAGKPGEQGVPGDLGAPGPSGARGERGFPGERGVQGPPGPAGPRGNNGAPGNDGAKGDTGAPGAPGSQGAPGLQGMPGERGAAGLPGPKGDRGDAGPKGADGSPGKDGVRGLTGPIGPPGPAGAPGDKGETGPSGPAGPTGARGAPGDRGEPGPPGPAGFAGPPGADGQPGAKGEPGDTGVKGDAGPPGPAGPAGPPGPIGNVGAPGPKGSRGAAGPPGATGFPGAAGRVGPPGPSGNAGPPGPPGPVGKEGGKGPRGETGPAGRPGEVGPPGPPGPAGEKGSPGADGPAGSPGTPGPQGIAGQRGVVGLPGQRGERGFPGLPGPSGEPGKQGPSGASGERGPPGPMGPPGLAGPPGESGREGSPGAEGSPGRDGAPGAKGDRGETGPAGPPGAPGAPGAPGPVGPAGKNGDRGETGPAGPAGPIGPAGARGPAGPQGPRGDKGETGEQGDRGIKGHRGFSGLQGPPGSPGSPGEQGPSGASGPAGPRGPPGSAGSPGKDGLNGLPGPIGPPGPRGRTGDSGPAGPPGPPGPPGPPGPPSGGYDFSFLPQPPQEKSQDGGRYYRADDANVVRDRDLEVDTTLKSLSQQIENIRSPEGSRKNPARTCRDLKMCHSDWKSGEYWIDPNQGCNLDAIKVYCNMETGQTCVFPTQPSVPQKNWYISPNPKEKKHVWFGESMTDGFQFEYGSEGSDPADVAIQLTFLRLMSTEASQNITYHCKNSVAYMDQQTGNLKKSLLLQGSNEIELRGEGNSRFTYSTLVDGCTSHTGTWGKTVIEYKTTKTSRLPIIDVAPLDIGAPDQEFGMDIGPACFV
| null | null |
blood vessel development [GO:0001568]; bone trabecula formation [GO:0060346]; cartilage development involved in endochondral bone morphogenesis [GO:0060351]; cellular response to amino acid stimulus [GO:0071230]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to fluoride [GO:1902618]; cellular response to glucose stimulus [GO:0071333]; cellular response to mechanical stimulus [GO:0071260]; cellular response to retinoic acid [GO:0071300]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to vitamin E [GO:0071306]; collagen biosynthetic process [GO:0032964]; collagen fibril organization [GO:0030199]; collagen-activated tyrosine kinase receptor signaling pathway [GO:0038063]; embryonic skeletal system development [GO:0048706]; endochondral ossification [GO:0001958]; extracellular matrix organization [GO:0030198]; face morphogenesis [GO:0060325]; intramembranous ossification [GO:0001957]; negative regulation of cell-substrate adhesion [GO:0010812]; ossification [GO:0001503]; osteoblast differentiation [GO:0001649]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of cell migration [GO:0030335]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of epithelial to mesenchymal transition [GO:0010718]; protein localization to nucleus [GO:0034504]; protein transport [GO:0015031]; response to cAMP [GO:0051591]; response to estradiol [GO:0032355]; response to fluoride [GO:1902617]; response to hydrogen peroxide [GO:0042542]; response to hyperoxia [GO:0055093]; response to insulin [GO:0032868]; response to mechanical stimulus [GO:0009612]; response to nutrient [GO:0007584]; response to nutrient levels [GO:0031667]; response to organic cyclic compound [GO:0014070]; response to peptide hormone [GO:0043434]; response to steroid hormone [GO:0048545]; response to xenobiotic stimulus [GO:0009410]; sensory perception of sound [GO:0007605]; skeletal system development [GO:0001501]; skeletal system morphogenesis [GO:0048705]; skin development [GO:0043588]; skin morphogenesis [GO:0043589]; tooth mineralization [GO:0034505]; visual perception [GO:0007601]
|
collagen trimer [GO:0005581]; collagen type I trimer [GO:0005584]; collagen type IV trimer [GO:0005587]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; secretory granule [GO:0030141]
|
extracellular matrix structural constituent [GO:0005201]; extracellular matrix structural constituent conferring tensile strength [GO:0030020]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; platelet-derived growth factor binding [GO:0048407]; protease binding [GO:0002020]
|
PF01410;PF01391;PF00093;
|
2.60.120.1000;2.10.70.10;
|
Fibrillar collagen family
|
PTM: Contains mostly 4-hydroxyproline. Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000269|PubMed:5411206}.; PTM: Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline. {ECO:0000250|UniProtKB:P11087}.; PTM: Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains. {ECO:0000250|UniProtKB:P02457}.; PTM: O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide. {ECO:0000269|PubMed:5411206}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
| null | null | null | null | null |
FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen).
|
Rattus norvegicus (Rat)
|
P02457
|
CO1A1_CHICK
|
MFSFVDSRLLLLIAATVLLTRGEGEEDIQTGSCVQDGLTYNDKDVWKPEPCQICVCDSGNILCDEVICEDTSDCPNAEIPFGECCPICPDVDASPVYPESAGVEGPKGDTGPRGDRGLPGPPGRDGIPGQPGLPGPPGPPGPPGLGGNFAPQMSYGYDEKSAGVAVPGPMGPAGPRGLPGPPGAPGPQGFQGPPGEPGEPGASGPMGPRGPAGPPGKNGDDGEAGKPGRPGQRGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGQPGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGPSGPAGARGNDGAPGAAGPPGPTGPAGPPGFPGAAGAKGETGPQGARGSEGPQGSRGEPGPPGPAGAAGPAGNPGADGQPGAKGATGAPGIAGAPGFPGARGPSGPQGPSGAPGPKGNSGEPGAPGNKGDTGAKGEPGPAGVQGPPGPAGEEGKRGARGEPGPAGLPGPAGERGAPGSRGFPGADGIAGPKGPPGERGSPGAVGPKGSPGEAGRPGEAGLPGAKGLTGSPGSPGPDGKTGPPGPAGQDGRPGPAGPPGARGQAGVMGFPGPKGAAGEPGKPGERGAPGPPGAVGAAGKDGEAGAQGPPGPTGPAGERGEQGPAGAPGFQGLPGPAGPPGEAGKPGEQGVPGNAGAPGPAGARGERGFPGERGVQGPPGPQGPRGANGAPGNDGAKGDAGAPGAPGNEGPPGLEGMPGERGAAGLPGAKGDRGDPGPKGADGAPGKDGLRGLTGPIGPPGPAGAPGDKGEAGPPGPAGPTGARGAPGDRGEPGPPGPAGFAGPPGADGQPGAKGETGDAGAKGDAGPPGPAGPTGAPGPAGZVGAPGPKGARGSAGPPGATGFPGAAGRVGPPGPSGNIGLPGPPGPAGKZGSKGPRGETGPAGRPGEPGPAGPPGPPGEKGSPGADGPIGAPGTPGPQGIAGQRGVVGLPGQRGERGFPGLPGPSGEPGKQGPSGASGERGPPGPMGPPGLAGPPGEAGREGAPGAEGAPGRDGAAGPKGDRGETGPAGPPGAPGAPGAPGPVGPAGKNGDRGETGPAGPAGPPGPAGARGPAGPQGPRGDKGETGEQGDRGMKGHRGFSGLQGPPGPPGAPGEQGPSGASGPAGPRGPPGSAGAAGKDGLNGLPGPIGPPGPRGRTGEVGPVGPPGPPGPPGPPGPPSGGFDLSFLPQPPQEKAHDGGRYYRADDANVMRDRDLEVDTTLKSLSQQIENIRSPEGTRKNPARTCRDLKMCHGDWKSGEYWIDPNQGCNLDAIKVYCNMETGETCVYPTQATIAQKNWYLSKNPKEKKHVWFGETMSDGFQFEYGGEGSNPADVAIQLTFLRLMSTEATQNVTYHCKNSVAYMDHDTGNLKKALLLQGANEIEIRAEGNSRFTYGVTEDGCTSHTGAWGKTVIEYKTTKTSRLPIIDLAPMDVGAPDQEFGIDIGPVCFL
| null | null |
blood vessel development [GO:0001568]; extracellular matrix organization [GO:0030198]; ossification [GO:0001503]; response to mechanical stimulus [GO:0009612]; skeletal system development [GO:0001501]; skin development [GO:0043588]
|
collagen type I trimer [GO:0005584]; collagen type IV trimer [GO:0005587]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]
|
extracellular matrix structural constituent conferring tensile strength [GO:0030020]; metal ion binding [GO:0046872]
|
PF01410;PF01391;PF00093;
|
2.60.120.1000;2.10.70.10;
|
Fibrillar collagen family
|
PTM: Contains mostly 4-hydroxyproline. Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are 4-hydroxylated in some or all of the chains. {ECO:0000269|PubMed:1125203, ECO:0000269|PubMed:167810, ECO:0000269|PubMed:4313735, ECO:0000269|PubMed:7093229, ECO:0000269|PubMed:728430}.; PTM: Contains 3-hydroxyproline. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline. {ECO:0000269|PubMed:728430}.; PTM: Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains. {ECO:0000269|PubMed:1125204, ECO:0000269|PubMed:1165248, ECO:0000269|PubMed:728430}.; PTM: O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide. {ECO:0000269|PubMed:1165248, ECO:0000269|PubMed:728430}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
| null | null | null | null | null |
FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen).
|
Gallus gallus (Chicken)
|
P02458
|
CO2A1_HUMAN
|
MIRLGAPQTLVLLTLLVAAVLRCQGQDVQEAGSCVQDGQRYNDKDVWKPEPCRICVCDTGTVLCDDIICEDVKDCLSPEIPFGECCPICPTDLATASGQPGPKGQKGEPGDIKDIVGPKGPPGPQGPAGEQGPRGDRGDKGEKGAPGPRGRDGEPGTPGNPGPPGPPGPPGPPGLGGNFAAQMAGGFDEKAGGAQLGVMQGPMGPMGPRGPPGPAGAPGPQGFQGNPGEPGEPGVSGPMGPRGPPGPPGKPGDDGEAGKPGKAGERGPPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPGAKGEAGPTGARGPEGAQGPRGEPGTPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRGARGEPGGVGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPGVMGFPGPKGANGEPGKAGEKGLPGAPGLRGLPGKDGETGAAGPPGPAGPAGERGEQGAPGPSGFQGLPGPPGPPGEGGKPGDQGVPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKGASGPAGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGSNGNPGPPGPPGPSGKDGPKGARGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRGETGAVGAPGAPGPPGSPGPAGPTGKQGDRGEAGAQGPMGPSGPAGARGIQGPQGPRGDKGEAGEPGERGLKGHRGFTGLQGLPGPPGPSGDQGASGPAGPSGPRGPPGPVGPSGKDGANGIPGPIGPPGPRGRSGETGPAGPPGNPGPPGPPGPPGPGIDMSAFAGLGPREKGPDPLQYMRADQAAGGLRQHDAEVDATLKSLNNQIESIRSPEGSRKNPARTCRDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPANVPKKNWWSSKSKEKKHIWFGETINGGFHFSYGDDNLAPNTANVQMTFLRLLSTEGSQNITYHCKNSIAYLDEAAGNLKKALLIQGSNDVEIRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGPEQEFGVDIGPVCFL
| null | null |
anterior head development [GO:0097065]; cartilage condensation [GO:0001502]; cartilage development [GO:0051216]; cartilage development involved in endochondral bone morphogenesis [GO:0060351]; cellular response to BMP stimulus [GO:0071773]; central nervous system development [GO:0007417]; chondrocyte differentiation [GO:0002062]; collagen fibril organization [GO:0030199]; embryonic skeletal joint morphogenesis [GO:0060272]; endochondral ossification [GO:0001958]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; heart morphogenesis [GO:0003007]; inner ear morphogenesis [GO:0042472]; limb bud formation [GO:0060174]; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [GO:2001240]; notochord development [GO:0030903]; otic vesicle development [GO:0071599]; proteoglycan metabolic process [GO:0006029]; regulation of gene expression [GO:0010468]; roof of mouth development [GO:0060021]; sensory perception of sound [GO:0007605]; skeletal system development [GO:0001501]; tissue homeostasis [GO:0001894]; visual perception [GO:0007601]
|
basement membrane [GO:0005604]; collagen type II trimer [GO:0005585]; collagen type XI trimer [GO:0005592]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
extracellular matrix structural constituent conferring tensile strength [GO:0030020]; metal ion binding [GO:0046872]; MHC class II protein binding [GO:0042289]; platelet-derived growth factor binding [GO:0048407]; protein homodimerization activity [GO:0042803]; proteoglycan binding [GO:0043394]
|
PF01410;PF01391;PF00093;
|
2.60.120.1000;2.10.70.10;
|
Fibrillar collagen family
|
PTM: The N-telopeptide is covalently linked to the helical COL2 region of alpha 1(IX), alpha 2(IX) and alpha 3(IX) chain. The C-telopeptide is covalently linked to an another site in the helical region of alpha 3(IX) COL2.; PTM: Contains mostly 4-hydroxyproline. Prolines at the third position of the tripeptide repeating unit (G-X-P) are 4-hydroxylated in some or all of the chains. {ECO:0000250|UniProtKB:P05539}.; PTM: Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline. {ECO:0000250|UniProtKB:P05539}.; PTM: Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains. {ECO:0000250|UniProtKB:P05539}.; PTM: O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide. {ECO:0000250|UniProtKB:P05539}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
| null | null | null | null | null |
FUNCTION: Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.
|
Homo sapiens (Human)
|
P02459
|
CO2A1_BOVIN
|
MIRLGAPQTLVLLTLLVAAVLRCHGQDVQKAGSCVQDGQRYNDKDVWKPEPCRICVCDTGTVLCDDIICEDMKDCLSPETPFGECCPICSADLPTASGQPGPKGQKGEPGDIKDIVGPKGPPGPQGPAGEQGPRGDRGDKGEKGAPGPRGRDGEPGTPGNPGPPGPPGPPGPPGLGGNFAAQMAGGFDEKAGGAQMGVMQGPMGPMGPRGPPGPAGAPGPQGFQGNPGEPGEPGVSGPMGPRGPPGPPGKPGDDGEAGKPGKSGERGPPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPGAKGEAGPTGARGPEGAQGPRGEPGTPGSPGPAGAAGNPGTDGIPGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRGARGEPGGAGPAGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPGVMGFPGPKGANGEPGKAGEKGLPGAPGLRGLPGKDGETGAAGPPGPAGPAGERGEQGAPGPSGFQGLPGPPGPPGEGGKPGDQGVPGEAGAPGLVGPRGERGFPGERGSPGSQGLQGARGLPGTPGTDGPKGAAGPAGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPAGTAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGSNGNPGPPGPPGPSGKDGPKGARGDSGPPGRAGDPGLQGPAGPPGEKGEPGDDGPSGPDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRGETGAVGAPGAPGPPGSPGPAGPIGKQGDRGEAGAQGPMGPAGPAGARGMPGPQGPRGDKGETGEAGERGLKGHRGFTGLQGLPGPPGPSGDQGASGPAGPSGPRGPPGPVGPSGKDGANGIPGPIGPPGPRGRSGETGPAGPPGNPGPPGPPGPPGPGIDMSAFAGLGQREKGPDPLQYMRADEAAGNLRQHDAEVDATLKSLNNQIESLRSPEGSRKNPARTCRDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPASVPKKNWWSSKSKDKKHIWFGETINGGFHFSYGDDNLAPNTANVQMTFLRLLSTEGSQNITYHCKNSIAYLDEAAGNLKKALLIQGSNDVEIRAEGNSRFTYTVLKDGCTKHTGKWGKTMIEYRSQKTSRLPIIDIAPMDIGGPEQEFGVDIGPVCFL
| null | null |
collagen fibril organization [GO:0030199]; notochord development [GO:0030903]; skeletal system development [GO:0001501]
|
collagen type II trimer [GO:0005585]; collagen type XI trimer [GO:0005592]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
extracellular matrix structural constituent conferring tensile strength [GO:0030020]; metal ion binding [GO:0046872]
|
PF01410;PF01391;PF00093;
|
2.60.120.1000;2.10.70.10;
|
Fibrillar collagen family
|
PTM: Probably 3-hydroxylated on prolines by LEPREL1 (By similarity). Proline residues at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Proline residues at the second position of the tripeptide repeating unit (G-P-X) are hydroxylated in some of the chains. {ECO:0000250, ECO:0000269|PubMed:2714276, ECO:0000269|PubMed:4857180, ECO:0000269|PubMed:782511, ECO:0000269|PubMed:833147}.; PTM: O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups. {ECO:0000269|PubMed:2714276, ECO:0000269|PubMed:4857180, ECO:0000269|PubMed:782511}.; PTM: Contains mostly 4-hydroxyproline. Prolines at the third position of the tripeptide repeating unit (G-X-P) are 4-hydroxylated in some or all of the chains. {ECO:0000269|PubMed:2714276, ECO:0000269|PubMed:4857180, ECO:0000269|PubMed:782511, ECO:0000269|PubMed:833147}.; PTM: Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline. {ECO:0000250|UniProtKB:P05539}.; PTM: Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains. {ECO:0000250|UniProtKB:P05539}.; PTM: O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide. {ECO:0000269|PubMed:2714276, ECO:0000269|PubMed:4857180, ECO:0000269|PubMed:782511}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
| null | null | null | null | null |
FUNCTION: Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.
|
Bos taurus (Bovine)
|
P02460
|
CO2A1_CHICK
|
LQGLPGKDGETGAAGPLDPGPVGERGEQGAPGPSGFQGLPGPPGPPGESGKPGDQGVPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKGATGPAGPNGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKDGARGLTGPIGPPGPAGPNGEKGESGPPGPSGAAGARGAPGERGEPGAPGPAGFAGPPGADGQPGAKGEQGEPGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGPNGNPGPPGPPGSAGKDGPKGVRGDAGPPGRAGDPGLQGPAGPPGEKGEPGEDGPAGPDGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGSAGDRGPPGPVGPPGLTGPAGEPGREGNPGADGPPGRDGAAGVKGDRGETGPVGAPGAPGAPGAPGPVGPTGKQGDRGETGAQGPMGPSGPAGARGMPGPQGPRGDKGETGEAGERGLKGHRGFTGLQGLPGPPGPSGDQGAAGPAGPSGPRGPPGPVGPSGKDGSNGMPGPIGPPGPRGRSGEPGPAGPPGNPGPPGPPGPPGTGIDMSAFAGLGQTEKGPDPIRYMRADEAAGGLRQHDVEVDATLKSLNNQIESIRSPEGSKKNPARTCRDIKLCHPEWKSGDYWIDPNQGCTLDAIKVFCNMETGETCVYPTPSSIPRKNWWTSKTKDKKHVWFAETINGGFHFSYGDENLSPNTASIQMTFLRLLSTEGSQNVTYHCKNSIAYMDEETGNLKKAILIQGSNDVEIRAEGNSRFTYSVLEDGCTKHTGKWGKTVIEYRSQKTSRLPIVDIAPMDIGGADQEFGVDIGPVCFL
| null | null |
collagen fibril organization [GO:0030199]; notochord development [GO:0030903]; skeletal system development [GO:0001501]
|
collagen type II trimer [GO:0005585]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
|
extracellular matrix structural constituent conferring tensile strength [GO:0030020]; metal ion binding [GO:0046872]
|
PF01410;PF01391;
|
2.60.120.1000;
|
Fibrillar collagen family
|
PTM: Contains mostly 4-hydroxyproline. Prolines at the third position of the tripeptide repeating unit (G-X-P) are 4-hydroxylated in some or all of the chains. {ECO:0000250|UniProtKB:P05539}.; PTM: Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline. {ECO:0000250|UniProtKB:P05539}.; PTM: Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains. {ECO:0000250|UniProtKB:P05539}.; PTM: O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide. {ECO:0000250|UniProtKB:P05539}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
| null | null | null | null | null |
FUNCTION: Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.
|
Gallus gallus (Chicken)
|
P02461
|
CO3A1_HUMAN
|
MMSFVQKGSWLLLALLHPTIILAQQEAVEGGCSHLGQSYADRDVWKPEPCQICVCDSGSVLCDDIICDDQELDCPNPEIPFGECCAVCPQPPTAPTRPPNGQGPQGPKGDPGPPGIPGRNGDPGIPGQPGSPGSPGPPGICESCPTGPQNYSPQYDSYDVKSGVAVGGLAGYPGPAGPPGPPGPPGTSGHPGSPGSPGYQGPPGEPGQAGPSGPPGPPGAIGPSGPAGKDGESGRPGRPGERGLPGPPGIKGPAGIPGFPGMKGHRGFDGRNGEKGETGAPGLKGENGLPGENGAPGPMGPRGAPGERGRPGLPGAAGARGNDGARGSDGQPGPPGPPGTAGFPGSPGAKGEVGPAGSPGSNGAPGQRGEPGPQGHAGAQGPPGPPGINGSPGGKGEMGPAGIPGAPGLMGARGPPGPAGANGAPGLRGGAGEPGKNGAKGEPGPRGERGEAGIPGVPGAKGEDGKDGSPGEPGANGLPGAAGERGAPGFRGPAGPNGIPGEKGPAGERGAPGPAGPRGAAGEPGRDGVPGGPGMRGMPGSPGGPGSDGKPGPPGSQGESGRPGPPGPSGPRGQPGVMGFPGPKGNDGAPGKNGERGGPGGPGPQGPPGKNGETGPQGPPGPTGPGGDKGDTGPPGPQGLQGLPGTGGPPGENGKPGEPGPKGDAGAPGAPGGKGDAGAPGERGPPGLAGAPGLRGGAGPPGPEGGKGAAGPPGPPGAAGTPGLQGMPGERGGLGSPGPKGDKGEPGGPGADGVPGKDGPRGPTGPIGPPGPAGQPGDKGEGGAPGLPGIAGPRGSPGERGETGPPGPAGFPGAPGQNGEPGGKGERGAPGEKGEGGPPGVAGPPGGSGPAGPPGPQGVKGERGSPGGPGAAGFPGARGLPGPPGSNGNPGPPGPSGSPGKDGPPGPAGNTGAPGSPGVSGPKGDAGQPGEKGSPGAQGPPGAPGPLGIAGITGARGLAGPPGMPGPRGSPGPQGVKGESGKPGANGLSGERGPPGPQGLPGLAGTAGEPGRDGNPGSDGLPGRDGSPGGKGDRGENGSPGAPGAPGHPGPPGPVGPAGKSGDRGESGPAGPAGAPGPAGSRGAPGPQGPRGDKGETGERGAAGIKGHRGFPGNPGAPGSPGPAGQQGAIGSPGPAGPRGPVGPSGPPGKDGTSGHPGPIGPPGPRGNRGERGSEGSPGHPGQPGPPGPPGAPGPCCGGVGAAAIAGIGGEKAGGFAPYYGDEPMDFKINTDEIMTSLKSVNGQIESLISPDGSRKNPARNCRDLKFCHPELKSGEYWVDPNQGCKLDAIKVFCNMETGETCISANPLNVPRKHWWTDSSAEKKHVWFGESMDGGFQFSYGNPELPEDVLDVHLAFLRLLSSRASQNITYHCKNSIAYMDQASGNVKKALKLMGSNEGEFKAEGNSKFTYTVLEDGCTKHTGEWSKTVFEYRTRKAVRLPIVDIAPYDIGGPDQEFGVDVGPVCFL
| null | null |
aorta smooth muscle tissue morphogenesis [GO:0060414]; basement membrane organization [GO:0071711]; cell-matrix adhesion [GO:0007160]; cellular response to amino acid stimulus [GO:0071230]; cerebral cortex development [GO:0021987]; chondrocyte differentiation [GO:0002062]; collagen fibril organization [GO:0030199]; digestive tract development [GO:0048565]; elastic fiber assembly [GO:0048251]; endochondral bone morphogenesis [GO:0060350]; extracellular matrix organization [GO:0030198]; fibroblast proliferation [GO:0048144]; heart development [GO:0007507]; in utero embryonic development [GO:0001701]; integrin-mediated signaling pathway [GO:0007229]; layer formation in cerebral cortex [GO:0021819]; limb joint morphogenesis [GO:0036022]; lung development [GO:0030324]; multicellular organism growth [GO:0035264]; negative regulation of immune response [GO:0050777]; negative regulation of neuron migration [GO:2001223]; neuron migration [GO:0001764]; peptide cross-linking [GO:0018149]; platelet activation [GO:0030168]; positive regulation of Rho protein signal transduction [GO:0035025]; response to angiotensin [GO:1990776]; response to cytokine [GO:0034097]; response to radiation [GO:0009314]; skin development [GO:0043588]; supramolecular fiber organization [GO:0097435]; tissue homeostasis [GO:0001894]; transforming growth factor beta receptor signaling pathway [GO:0007179]; transforming growth factor beta1 production [GO:0032905]; wound healing [GO:0042060]
|
collagen type III trimer [GO:0005586]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
extracellular matrix structural constituent [GO:0005201]; extracellular matrix structural constituent conferring tensile strength [GO:0030020]; integrin binding [GO:0005178]; metal ion binding [GO:0046872]; platelet-derived growth factor binding [GO:0048407]; protease binding [GO:0002020]; SMAD binding [GO:0046332]
|
PF01410;PF01391;PF00093;
|
2.60.120.1000;2.10.70.10;
|
Fibrillar collagen family
|
PTM: Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000269|PubMed:557335, ECO:0000269|PubMed:7016180}.; PTM: O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
| null | null | null | null | null |
FUNCTION: Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly GNA12.
|
Homo sapiens (Human)
|
P02462
|
CO4A1_HUMAN
|
MGPRLSVWLLLLPAALLLHEEHSRAAAKGGCAGSGCGKCDCHGVKGQKGERGLPGLQGVIGFPGMQGPEGPQGPPGQKGDTGEPGLPGTKGTRGPPGASGYPGNPGLPGIPGQDGPPGPPGIPGCNGTKGERGPLGPPGLPGFAGNPGPPGLPGMKGDPGEILGHVPGMLLKGERGFPGIPGTPGPPGLPGLQGPVGPPGFTGPPGPPGPPGPPGEKGQMGLSFQGPKGDKGDQGVSGPPGVPGQAQVQEKGDFATKGEKGQKGEPGFQGMPGVGEKGEPGKPGPRGKPGKDGDKGEKGSPGFPGEPGYPGLIGRQGPQGEKGEAGPPGPPGIVIGTGPLGEKGERGYPGTPGPRGEPGPKGFPGLPGQPGPPGLPVPGQAGAPGFPGERGEKGDRGFPGTSLPGPSGRDGLPGPPGSPGPPGQPGYTNGIVECQPGPPGDQGPPGIPGQPGFIGEIGEKGQKGESCLICDIDGYRGPPGPQGPPGEIGFPGQPGAKGDRGLPGRDGVAGVPGPQGTPGLIGQPGAKGEPGEFYFDLRLKGDKGDPGFPGQPGMPGRAGSPGRDGHPGLPGPKGSPGSVGLKGERGPPGGVGFPGSRGDTGPPGPPGYGPAGPIGDKGQAGFPGGPGSPGLPGPKGEPGKIVPLPGPPGAEGLPGSPGFPGPQGDRGFPGTPGRPGLPGEKGAVGQPGIGFPGPPGPKGVDGLPGDMGPPGTPGRPGFNGLPGNPGVQGQKGEPGVGLPGLKGLPGLPGIPGTPGEKGSIGVPGVPGEHGAIGPPGLQGIRGEPGPPGLPGSVGSPGVPGIGPPGARGPPGGQGPPGLSGPPGIKGEKGFPGFPGLDMPGPKGDKGAQGLPGITGQSGLPGLPGQQGAPGIPGFPGSKGEMGVMGTPGQPGSPGPVGAPGLPGEKGDHGFPGSSGPRGDPGLKGDKGDVGLPGKPGSMDKVDMGSMKGQKGDQGEKGQIGPIGEKGSRGDPGTPGVPGKDGQAGQPGQPGPKGDPGISGTPGAPGLPGPKGSVGGMGLPGTPGEKGVPGIPGPQGSPGLPGDKGAKGEKGQAGPPGIGIPGLRGEKGDQGIAGFPGSPGEKGEKGSIGIPGMPGSPGLKGSPGSVGYPGSPGLPGEKGDKGLPGLDGIPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEPGLPGRGFPGFPGAKGDKGSKGEVGFPGLAGSPGIPGSKGEQGFMGPPGPQGQPGLPGSPGHATEGPKGDRGPQGQPGLPGLPGPMGPPGLPGIDGVKGDKGNPGWPGAPGVPGPKGDPGFQGMPGIGGSPGITGSKGDMGPPGVPGFQGPKGLPGLQGIKGDQGDQGVPGAKGLPGPPGPPGPYDIIKGEPGLPGPEGPPGLKGLQGLPGPKGQQGVTGLVGIPGPPGIPGFDGAPGQKGEMGPAGPTGPRGFPGPPGPDGLPGSMGPPGTPSVDHGFLVTRHSQTIDDPQCPSGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASRNDYSYWLSTPEPMPMSMAPITGENIRPFISRCAVCEAPAMVMAVHSQTIQIPPCPSGWSSLWIGYSFVMHTSAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYANAYSFWLATIERSEMFKKPTPSTLKAGELRTHVSRCQVCMRRT
| null | null |
basement membrane organization [GO:0071711]; blood vessel morphogenesis [GO:0048514]; brain development [GO:0007420]; branching involved in blood vessel morphogenesis [GO:0001569]; cellular response to amino acid stimulus [GO:0071230]; collagen-activated tyrosine kinase receptor signaling pathway [GO:0038063]; epithelial cell differentiation [GO:0030855]; extracellular matrix organization [GO:0030198]; neuromuscular junction development [GO:0007528]; renal tubule morphogenesis [GO:0061333]; retinal blood vessel morphogenesis [GO:0061304]
|
basement membrane [GO:0005604]; collagen type IV trimer [GO:0005587]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
extracellular matrix structural constituent [GO:0005201]; extracellular matrix structural constituent conferring tensile strength [GO:0030020]; platelet-derived growth factor binding [GO:0048407]
|
PF01413;PF01391;
|
2.170.240.10;
|
Type IV collagen family
|
PTM: Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated. The modified lysines can be O-glycosylated. {ECO:0000269|PubMed:6434307}.; PTM: Contains 4-hydroxyproline (Probable). Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains (By similarity). {ECO:0000250|UniProtKB:P02463, ECO:0000305|PubMed:6434307}.; PTM: Contains 3-hydroxyproline. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline. {ECO:0000250|UniProtKB:P02463, ECO:0000250|UniProtKB:Q7SIB2}.; PTM: Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding (PubMed:2844531). 12 of these, located in the NC1 domain, are conserved in all known type IV collagens. {ECO:0000269|PubMed:2844531, ECO:0000305}.; PTM: The trimeric structure of the NC1 domains is stabilized by covalent bonds (sulfilimine cross-links) between Lys and Met residues (PubMed:12011424). These cross-links are important for the mechanical stability of the basement membrane (By similarity). Sulfilimine cross-link is catalyzed by PXDN (By similarity). {ECO:0000250|UniProtKB:P02463, ECO:0000269|PubMed:12011424}.; PTM: Proteolytic processing produces the C-terminal NC1 peptide, arresten. {ECO:0000269|PubMed:10811134}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000250|UniProtKB:P02463}.
| null | null | null | null | null |
FUNCTION: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. {ECO:0000250|UniProtKB:P02463}.; FUNCTION: Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. {ECO:0000269|PubMed:10811134, ECO:0000269|PubMed:18775695}.
|
Homo sapiens (Human)
|
P02463
|
CO4A1_MOUSE
|
MGPRLSVWLLLLFAALLLHEERSRAAAKGDCGGSGCGKCDCHGVKGQKGERGLPGLQGVIGFPGMQGPEGPHGPPGQKGDAGEPGLPGTKGTRGPPGAAGYPGNPGLPGIPGQDGPPGPPGIPGCNGTKGERGPLGPPGLPGFSGNPGPPGLPGMKGDPGEILGHVPGTLLKGERGFPGIPGMPGSPGLPGLQGPVGPPGFTGPPGPPGPPGPPGEKGQMGSSFQGPKGDKGEQGVSGPPGVPGQAQVKEKGDFAPTGEKGQKGEPGFPGVPGYGEKGEPGKQGPRGKPGKDGEKGERGSPGIPGDSGYPGLPGRQGPQGEKGEAGLPGPPGTVIGTMPLGEKGDRGYPGAPGLRGEPGPKGFPGTPGQPGPPGFPTPGQAGAPGFPGERGEKGDQGFPGVSLPGPSGRDGAPGPPGPPGPPGQPGHTNGIVECQPGPPGDQGPPGTPGQPGLTGEVGQKGQKGESCLACDTEGLRGPPGPQGPPGEIGFPGQPGAKGDRGLPGRDGLEGLPGPQGSPGLIGQPGAKGEPGEIFFDMRLKGDKGDPGFPGQPGMPGRAGTPGRDGHPGLPGPKGSPGSIGLKGERGPPGGVGFPGSRGDIGPPGPPGVGPIGPVGEKGQAGFPGGPGSPGLPGPKGEAGKVVPLPGPPGAAGLPGSPGFPGPQGDRGFPGTPGRPGIPGEKGAVGQPGIGFPGLPGPKGVDGLPGEIGRPGSPGRPGFNGLPGNPGPQGQKGEPGIGLPGLKGQPGLPGIPGTPGEKGSIGGPGVPGEQGLTGPPGLQGIRGDPGPPGVQGPAGPPGVPGIGPPGAMGPPGGQGPPGSSGPPGIKGEKGFPGFPGLDMPGPKGDKGSQGLPGLTGQSGLPGLPGQQGTPGVPGFPGSKGEMGVMGTPGQPGSPGPAGTPGLPGEKGDHGLPGSSGPRGDPGFKGDKGDVGLPGMPGSMEHVDMGSMKGQKGDQGEKGQIGPTGDKGSRGDPGTPGVPGKDGQAGHPGQPGPKGDPGLSGTPGSPGLPGPKGSVGGMGLPGSPGEKGVPGIPGSQGVPGSPGEKGAKGEKGQSGLPGIGIPGRPGDKGDQGLAGFPGSPGEKGEKGSAGTPGMPGSPGPRGSPGNIGHPGSPGLPGEKGDKGLPGLDGVPGVKGEAGLPGTPGPTGPAGQKGEPGSDGIPGSAGEKGEQGVPGRGFPGFPGSKGDKGSKGEVGFPGLAGSPGIPGVKGEQGFMGPPGPQGQPGLPGTPGHPVEGPKGDRGPQGQPGLPGHPGPMGPPGFPGINGPKGDKGNQGWPGAPGVPGPKGDPGFQGMPGIGGSPGITGSKGDMGLPGVPGFQGQKGLPGLQGVKGDQGDQGVPGPKGLQGPPGPPGPYDVIKGEPGLPGPEGPPGLKGLQGPPGPKGQQGVTGSVGLPGPPGVPGFDGAPGQKGETGPFGPPGPRGFPGPPGPDGLPGSMGPPGTPSVDHGFLVTRHSQTTDDPLCPPGTKILYHGYSLLYVQGNERAHGQDLGTAGSCLRKFSTMPFLFCNINNVCNFASRNDYSYWLSTPEPMPMSMAPISGDNIRPFISRCAVCEAPAMVMAVHSQTIQIPQCPNGWSSLWIGYSFVMHTSAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYANAYSFWLATIERSEMFKKPTPSTLKAGELRTHVSRCQVCMRRT
| null | null |
basement membrane organization [GO:0071711]; brain development [GO:0007420]; branching involved in blood vessel morphogenesis [GO:0001569]; cellular response to amino acid stimulus [GO:0071230]; collagen-activated tyrosine kinase receptor signaling pathway [GO:0038063]; epithelial cell differentiation [GO:0030855]; extracellular matrix organization [GO:0030198]; neuromuscular junction development [GO:0007528]; renal tubule morphogenesis [GO:0061333]; retinal blood vessel morphogenesis [GO:0061304]
|
basement membrane [GO:0005604]; collagen type IV trimer [GO:0005587]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
extracellular matrix structural constituent conferring tensile strength [GO:0030020]; platelet-derived growth factor binding [GO:0048407]
|
PF01413;PF01391;
|
2.170.240.10;
|
Type IV collagen family
|
PTM: Lysines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated. The modified lysines can be O-glycosylated. {ECO:0000269|PubMed:25645914}.; PTM: Contains 4-hydroxyproline. Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000269|PubMed:25645914}.; PTM: Contains 3-hydroxyproline. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline. {ECO:0000269|PubMed:24368846, ECO:0000269|PubMed:25645914}.; PTM: Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known type IV collagens. {ECO:0000250|UniProtKB:P02462}.; PTM: The trimeric structure of the NC1 domains is stabilized by covalent bonds (sulfilimine cross-links) between Lys and Met residues. These cross-links are important for the mechanical stability of the basement membrane (PubMed:22842973, PubMed:28424209). Sulfilimine cross-link is catalyzed by PXDN (PubMed:22842973). {ECO:0000269|PubMed:22842973, ECO:0000269|PubMed:28424209}.; PTM: Proteolytic processing produces the C-terminal NC1 peptide, arresten. {ECO:0000250|UniProtKB:P02462}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:24368846}.
| null | null | null | null | null |
FUNCTION: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen. {ECO:0000305|PubMed:28424209}.; FUNCTION: Arresten, comprising the C-terminal NC1 domain, inhibits angiogenesis and tumor formation. The C-terminal half is found to possess the anti-angiogenic activity. Specifically inhibits endothelial cell proliferation, migration and tube formation. {ECO:0000250|UniProtKB:P02462}.
|
Mus musculus (Mouse)
|
P02465
|
CO1A2_BOVIN
|
MLSFVDTRTLLLLAVTSCLATCQSLQEATARKGPSGDRGPRGERGPPGPPGRDGDDGIPGPPGPPGPPGPPGLGGNFAAQFDAKGGGPGPMGLMGPRGPPGASGAPGPQGFQGPPGEPGEPGQTGPAGARGPPGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAPGVKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGELGPVGNPGPAGPAGPRGEVGLPGLSGPVGPPGNPGANGLPGAKGAAGLPGVAGAPGLPGPRGIPGPVGAAGATGARGLVGEPGPAGSKGESGNKGEPGAVGQPGPPGPSGEEGKRGSTGEIGPAGPPGPPGLRGNPGSRGLPGADGRAGVMGPAGSRGATGPAGVRGPNGDSGRPGEPGLMGPRGFPGSPGNIGPAGKEGPVGLPGIDGRPGPIGPAGARGEPGNIGFPGPKGPSGDPGKAGEKGHAGLAGARGAPGPDGNNGAQGPPGLQGVQGGKGEQGPAGPPGFQGLPGPAGTAGEAGKPGERGIPGEFGLPGPAGARGERGPPGESGAAGPTGPIGSRGPSGPPGPDGNKGEPGVVGAPGTAGPSGPSGLPGERGAAGIPGGKGEKGETGLRGDIGSPGRDGARGAPGAIGAPGPAGANGDRGEAGPAGPAGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGTKGPKGENGPVGPTGPVGAAGPSGPNGPPGPAGSRGDGGPPGATGFPGAAGRTGPPGPSGISGPPGPPGPAGKEGLRGPRGDQGPVGRSGETGASGPPGFVGEKGPSGEPGTAGPPGTPGPQGLLGAPGFLGLPGSRGERGLPGVAGSVGEPGPLGIAGPPGARGPPGNVGNPGVNGAPGEAGRDGNPGNDGPPGRDGQPGHKGERGYPGNAGPVGAAGAPGPQGPVGPVGKHGNRGEPGPAGAVGPAGAVGPRGPSGPQGIRGDKGEPGDKGPRGLPGLKGHNGLQGLPGLAGHHGDQGAPGAVGPAGPRGPAGPSGPAGKDGRIGQPGAVGPAGIRGSQGSQGPAGPPGPPGPPGPPGPSGGGYEFGFDGDFYRADQPRSPTSLRPKDYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWSSGYYWIDPNQGCTMDAIKVYCDFSTGETCIRAQPEDIPVKNWYRNSKAKKHVWVGETINGGTQFEYNVEGVTTKEMATQLAFMRLLANHASQNITYHCKNSIAYMDEETGNLKKAVILQGSNDVELVAEGNSRFTYTVLVDGCSKKTNEWQKTIIEYKTNKPSRLPILDIAPLDIGGADQEIRLNIGPVCFK
| null | null |
extracellular matrix organization [GO:0030198]
|
collagen type I trimer [GO:0005584]; collagen type IV trimer [GO:0005587]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]
|
extracellular matrix structural constituent conferring tensile strength [GO:0030020]; metal ion binding [GO:0046872]
|
PF01410;PF01391;
|
2.60.120.1000;
|
Fibrillar collagen family
|
PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
| null | null | null | null | null |
FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen).
|
Bos taurus (Bovine)
|
P02466
|
CO1A2_RAT
|
MLSFVDTRTLLLLAVTSCLATCQSLQMGSVRKGPTGDRGPRGQRGPAGPRGRDGVDGPVGPPGPPGAPGPPGPPGPPGLTGNFAAQYSDKGVSAGPGPMGLMGPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPAGSRGPAGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAQGVKGEPGAPGENGTPGQAGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGELGPVGNPGPAGPAGPRGEAGLPGLSGPVGPPGNPGANGLTGAKGATGLPGVAGAPGLPGPRGIPGPVGAAGATGPRGLVGEPGPAGSKGETGNKGEPGSAGAQGPPGPSGEEGKRGSPGEPGSAGPAGPPGLRGSPGSRGLPGADGRAGVMGPPGNRGSTGPAGVRGPNGDAGRPGEPGLMGPRGLPGSPGNVGPAGKEGPVGLPGIDGRPGPIGPAGPRGEAGNIGFPGPKGPSGDPGKPGEKGHPGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPAGPPGFQGLPGPSGTAGEVGKPGERGLPGEFGLPGPAGPRGERGPPGESGAAGPSGPIGIRGPSGAPGPDGNKGEAGAVGAPGSAGASGPGGLPGERGAAGIPGGKGEKGETGLRGEIGNPGRDGARGAPGAIGAPGPAGASGDRGEAGAAGPSGPAGPRGSPGERGEVGPAGPNGFAGPAGSAGQPGAKGEKGTKGPKGENGIVGPTGPVGAAGPSGPNGPPGPAGSRGDGGPPGMTGFPGAAGRTGPPGPSGITGPPGPPGAAGKEGIRGPRGDQGPVGRTGEIGASGPPGFAGEKGPSGEPGTTGPPGTAGPQGLLGAPGILGLPGSRGERGQPGIAGALGEPGPLGIAGPPGARGPPGAVGSPGVNGAPGEAGRDGNPGSDGPPGRDGQPGHKGERGYPGNIGPTGAAGAPGPHGSVGPAGKHGNRGEPGPAGSVGPVGAVGPRGPSGPQGIRGDKGEPGDKGARGLPGLKGHNGLQGLPGLAGLHGDQGAPGPVGPAGPRGPAGPSGPIGKDGRSGHPGPVGPAGVRGSQGSQGPAGPPGPPGPPGPPGVSGGGYDFGFEGGFYRADQPRSQPSLRPKDYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWKSDYYWIDPNQGCTMDAIKVYCDFSTGETCIQAQPVNTPAKNAYSRAQANKHVWLGETINGGSQFEYNAEGVSSKEMATQLAFMRLLANRASQNITYHCKNSIAYLDEETGRLNKAVILQGSNDVELVAEGNSRFTYTVLVDGCSKKTNEWDKTVIEYKTNKPSRLPFLDIAPLDIGGTNQEFRVEVGPVCFK
| null | null |
blood vessel development [GO:0001568]; bone mineralization [GO:0030282]; cellular response to amino acid stimulus [GO:0071230]; cellular response to organic substance [GO:0071310]; cellular response to retinoic acid [GO:0071300]; cellular response to thyroid hormone stimulus [GO:0097067]; collagen fibril organization [GO:0030199]; collagen metabolic process [GO:0032963]; extracellular matrix assembly [GO:0085029]; extracellular matrix organization [GO:0030198]; protein heterotrimerization [GO:0070208]; regulation of blood pressure [GO:0008217]; response to norepinephrine [GO:0071873]; Rho protein signal transduction [GO:0007266]; skeletal system development [GO:0001501]; skin morphogenesis [GO:0043589]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
collagen trimer [GO:0005581]; collagen type I trimer [GO:0005584]; collagen type IV trimer [GO:0005587]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
extracellular matrix structural constituent conferring tensile strength [GO:0030020]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; platelet-derived growth factor binding [GO:0048407]; protease binding [GO:0002020]; protein-macromolecule adaptor activity [GO:0030674]; SMAD binding [GO:0046332]
|
PF01410;PF01391;
|
2.60.120.1000;
|
Fibrillar collagen family
|
PTM: Proline residues at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Proline residues at the second position of the tripeptide repeating unit (G-P-X) are hydroxylated in some of the chains.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
| null | null | null | null | null |
FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen).
|
Rattus norvegicus (Rat)
|
P02467
|
CO1A2_CHICK
|
MLSFVDTRILLLLAVTSYLATSQHLFQASAGRKGPRGDKGPQGERGPPGPPGRDGEDGPPGPPGPPGPPGLGGNFAAQYDPSKAADFGPGPMGLMGPRGPPGASGPPGPPGFQGVPGEPGEPGQTGPQGPRGPPGPPGKAGEDGHPGKPGRPGERGVAGPQGARGFPGTPGLPGFKGIRGHNGLDGQKGQPGTPGTKGEPGAPGENGTPGQPGARGLPGERGRIGAPGPAGARGSDGSAGPTGPAGPIGAAGPPGFPGAPGAKGEIGPAGNVGPTGPAGPRGEIGLPGSSGPVGPPGNPGANGLPGAKGAAGLPGVAGAPGLPGPRGIPGPPGPAGPSGARGLVGEPGPAGAKGESGNKGEPGAAGPPGPPGPSGEEGKRGSNGEPGSAGPPGPAGLRGVPGSRGLPGADGRAGVMGPAGNRGASGPVGAKGPNGDAGRPGEPGLMGPRGLPGQPGSPGPAGKEGPVGFPGADGRVGPIGPAGNRGEPGNIGFPGPKGPTGEPGKPGEKGNVGLAGPRGAPGPEGNNGAQGPPGVTGNQGAKGETGPAGPPGFQGLPGPSGPAGEAGKPGERGLHGEFGVPGPAGPRGERGLPGESGAVGPAGPIGSRGPSGPPGPDGNKGEPGNVGPAGAPGPAGPGGIPGERGVAGVPGGKGEKGAPGLRGDTGATGRDGARGLPGAIGAPGPAGGAGDRGEGGPAGPAGPAGARGIPGERGEPGPVGPSGFAGPPGAAGQPGAKGERGPKGPKGETGPTGAIGPIGASGPPGPVGAAGPAGPRGDAGPPGMTGFPGAAGRVGPPGPAGITGPPGPPGPAGKDGPRGLRGDVGPVGRTGEQGIAGPPGFAGEKGPSGEAGAAGPPGTPGPQGILGAPGILGLPGSRGERGLPGIAGATGEPGPLGVSGPPGARGPSGPVGSPGPNGAPGEAGRDGNPGNDGPPGRDGAPGFKGERGAPGNPGPSGALGAPGPHGQVGPSGKPGNRGDPGPVGPVGPAGAFGPRGLAGPQGPRGEKGEPGDKGHRGLPGLKGHNGLQGLPGLAGQHGDQGPPGNNGPAGPRGPPGPSGPPGKDGRNGLPGPIGPAGVRGSHGSQGPAGPPGPPGPPGPPGPNGGGYEVGFDAEYYRADQPSLRPKDYEVDATLKTLNNQIETLLTPEGSKKNPARTCRDLRLSHPEWSSGFYWIDPNQGCTADAIRAYCDFATGETCIHASLEDIPTKTWYVSKNPKDKKHIWFGETINGGTQFEYNGEGVTTKDMATQLAFMRLLANHASQNITYHCKNSIAYMDEETGNLKKAVILQGSNDVELRAEGNSRFTFSVLVDGCSKKNNKWGKTIIEYRTNKPSRLPILDIAPLDIGGADQEFGLHIGPVCFK
| null | null |
extracellular matrix organization [GO:0030198]
|
collagen type I trimer [GO:0005584]; collagen type IV trimer [GO:0005587]; collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615]; fibrillar collagen trimer [GO:0005583]
|
extracellular matrix structural constituent conferring tensile strength [GO:0030020]; metal ion binding [GO:0046872]
|
PF01410;PF01391;
|
2.60.120.1000;
|
Fibrillar collagen family
|
PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000269|PubMed:5544653}.; PTM: The N-terminus of the mature protein is blocked.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
| null | null | null | null | null |
FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen).
|
Gallus gallus (Chicken)
|
P02468
|
LAMC1_MOUSE
|
MTGGGRAALALQPRGRLWPLLAVLAAVAGCVRAAMDECADEGGRPQRCMPEFVNAAFNVTVVATNTCGTPPEEYCVQTGVTGVTKSCHLCDAGQQHLQHGAAFLTDYNNQADTTWWQSQTMLAGVQYPNSINLTLHLGKAFDITYVRLKFHTSRPESFAIYKRTREDGPWIPYQYYSGSCENTYSKANRGFIRTGGDEQQALCTDEFSDISPLTGGNVAFSTLEGRPSAYNFDNSPVLQEWVTATDIRVTLNRLNTFGDEVFNEPKVLKSYYYAISDFAVGGRCKCNGHASECVKNEFDKLMCNCKHNTYGVDCEKCLPFFNDRPWRRATAESASESLPCDCNGRSQECYFDPELYRSTGHGGHCTNCRDNTDGAKCERCRENFFRLGNTEACSPCHCSPVGSLSTQCDSYGRCSCKPGVMGDKCDRCQPGFHSLTEAGCRPCSCDLRGSTDECNVETGRCVCKDNVEGFNCERCKPGFFNLESSNPKGCTPCFCFGHSSVCTNAVGYSVYDISSTFQIDEDGWRVEQRDGSEASLEWSSDRQDIAVISDSYFPRYFIAPVKFLGNQVLSYGQNLSFSFRVDRRDTRLSAEDLVLEGAGLRVSVPLIAQGNSYPSETTVKYIFRLHEATDYPWRPALSPFEFQKLLNNLTSIKIRGTYSERTAGYLDDVTLQSARPGPGVPATWVESCTCPVGYGGQFCETCLPGYRRETPSLGPYSPCVLCTCNGHSETCDPETGVCDCRDNTAGPHCEKCSDGYYGDSTLGTSSDCQPCPCPGGSSCAIVPKTKEVVCTHCPTGTAGKRCELCDDGYFGDPLGSNGPVRLCRPCQCNDNIDPNAVGNCNRLTGECLKCIYNTAGFYCDRCKEGFFGNPLAPNPADKCKACACNPYGTVQQQSSCNPVTGQCQCLPHVSGRDCGTCDPGYYNLQSGQGCERCDCHALGSTNGQCDIRTGQCECQPGITGQHCERCETNHFGFGPEGCKPCDCHHEGSLSLQCKDDGRCECREGFVGNRCDQCEENYFYNRSWPGCQECPACYRLVKDKAAEHRVKLQELESLIANLGTGDDMVTDQAFEDRLKEAEREVTDLLREAQEVKDVDQNLMDRLQRVNSSLHSQISRLQNIRNTIEETGILAERARSRVESTEQLIEIASRELEKAKMAAANVSITQPESTGEPNNMTLLAEEARRLAERHKQEADDIVRVAKTANETSAEAYNLLLRTLAGENQTALEIEELNRKYEQAKNISQDLEKQAARVHEEAKRAGDKAVEIYASVAQLTPVDSEALENEANKIKKEAADLDRLIDQKLKDYEDLREDMRGKEHEVKNLLEKGKAEQQTADQLLARADAAKALAEEAAKKGRSTLQEANDILNNLKDFDRRVNDNKTAAEEALRRIPAINRTIAEANEKTREAQLALGNAAADATEAKNKAHEAERIASAVQKNATSTKADAERTFGEVTDLDNEVNGMLRQLEEAENELKRKQDDADQDMMMAGMASQAAQEAELNARKAKNSVSSLLSQLNNLLDQLGQLDTVDLNKLNEIEGSLNKAKDEMKASDLDRKVSDLESEARKQEAAIMDYNRDIAEIIKDIHNLEDIKKTLPTGCFNTPSIEKP
| null | null |
animal organ morphogenesis [GO:0009887]; axon guidance [GO:0007411]; cell adhesion [GO:0007155]; cell migration [GO:0016477]; chromatin organization [GO:0006325]; extracellular matrix disassembly [GO:0022617]; gene expression [GO:0010467]; hair cell differentiation [GO:0035315]; hair follicle cell proliferation [GO:0071335]; hair follicle morphogenesis [GO:0031069]; hemidesmosome assembly [GO:0031581]; neuron projection development [GO:0031175]; positive regulation of cell adhesion [GO:0045785]; positive regulation of integrin-mediated signaling pathway [GO:2001046]; positive regulation of muscle cell differentiation [GO:0051149]; protein-containing complex assembly [GO:0065003]; regulation of basement membrane organization [GO:0110011]; substrate adhesion-dependent cell spreading [GO:0034446]; tissue development [GO:0009888]; tissue morphogenesis [GO:0048729]
|
basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; laminin-1 complex [GO:0005606]; laminin-10 complex [GO:0043259]; neuromuscular junction [GO:0031594]; protein complex involved in cell-matrix adhesion [GO:0098637]; synaptic cleft [GO:0043083]
|
extracellular matrix structural constituent [GO:0005201]; glycosphingolipid binding [GO:0043208]
|
PF00052;PF00053;PF00055;
|
2.60.120.260;2.10.25.10;
| null | null |
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane.
| null | null | null | null | null |
FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
|
Mus musculus (Mouse)
|
P02469
|
LAMB1_MOUSE
|
MGLLQVFAFGVLALWGTRVCAQEPEFSYGCAEGSCYPATGDLLIGRAQKLSVTSTCGLHKPEPYCIVSHLQEDKKCFICDSRDPYHETLNPDSHLIENVVTTFAPNRLKIWWQSENGVENVTIQLDLEAEFHFTHLIMTFKTFRPAAMLIERSSDFGKAWGVYRYFAYDCESSFPGISTGPMKKVDDIICDSRYSDIEPSTEGEVIFRALDPAFKIEDPYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIREKYYYAVYDMVVRGNCFCYGHASECAPVDGVNEEVEGMVHGHCMCRHNTKGLNCELCMDFYHDLPWRPAEGRNSNACKKCNCNEHSSSCHFDMAVFLATGNVSGGVCDNCQHNTMGRNCEQCKPFYFQHPERDIRDPNLCEPCTCDPAGSENGGICDGYTDFSVGLIAGQCRCKLHVEGERCDVCKEGFYDLSAEDPYGCKSCACNPLGTIPGGNPCDSETGYCYCKRLVTGQRCDQCLPQHWGLSNDLDGCRPCDCDLGGALNNSCSEDSGQCSCLPHMIGRQCNEVESGYYFTTLDHYIYEAEEANLGPGVIVVERQYIQDRIPSWTGPGFVRVPEGAYLEFFIDNIPYSMEYEILIRYEPQLPDHWEKAVITVQRPGKIPASSRCGNTVPDDDNQVVSLSPGSRYVVLPRPVCFEKGMNYTVRLELPQYTASGSDVESPYTFIDSLVLMPYCKSLDIFTVGGSGDGEVTNSAWETFQRYRCLENSRSVVKTPMTDVCRNIIFSISALIHQTGLACECDPQGSLSSVCDPNGGQCQCRPNVVGRTCNRCAPGTFGFGPNGCKPCDCHLQGSASAFCDAITGQCHCFQGIYARQCDRCLPGYWGFPSCQPCQCNGHALDCDTVTGECLSCQDYTTGHNCERCLAGYYGDPIIGSGDHCRPCPCPDGPDSGRQFARSCYQDPVTLQLACVCDPGYIGSRCDDCASGFFGNPSDFGGSCQPCQCHHNIDTTDPEACDKETGRCLKCLYHTEGDHCQLCQYGYYGDALRQDCRKCVCNYLGTVKEHCNGSDCHCDKATGQCSCLPNVIGQNCDRCAPNTWQLASGTGCGPCNCNAAHSFGPSCNEFTGQCQCMPGFGGRTCSECQELFWGDPDVECRACDCDPRGIETPQCDQSTGQCVCVEGVEGPRCDKCTRGYSGVFPDCTPCHQCFALWDAIIGELTNRTHKFLEKAKALKISGVIGPYRETVDSVEKKVNEIKDILAQSPAAEPLKNIGILFEEAEKLTKDVTEKMAQVEVKLTDTASQSNSTAGELGALQAEAESLDKTVKELAEQLEFIKNSDIQGALDSITKYFQMSLEAEKRVNASTTDPNSTVEQSALTRDRVEDLMLERESPFKEQQEEQARLLDELAGKLQSLDLSAVAQMTCGTPPGADCSESECGGPNCRTDEGEKKCGGPGCGGLVTVAHSAWQKAMDFDRDVLSALAEVEQLSKMVSEAKVRADEAKQNAQDVLLKTNATKEKVDKSNEDLRNLIKQIRNFLTEDSADLDSIEAVANEVLKMEMPSTPQQLQNLTEDIRERVETLSQVEVILQQSAADIARAELLLEEAKRASKSATDVKVTADMVKEALEEAEKAQVAAEKAIKQADEDIQGTQNLLTSIESETAASEETLTNASQRISKLERNVEELKRKAAQNSGEAEYIEKVVYSVKQNADDVKKTLDGELDEKYKKVESLIAQKTEESADARRKAELLQNEAKTLLAQANSKLQLLEDLERKYEDNQKYLEDKAQELVRLEGEVRSLLKDISEKVAVYSTCL
| null | null |
animal organ morphogenesis [GO:0009887]; axon guidance [GO:0007411]; basement membrane assembly [GO:0070831]; cell migration [GO:0016477]; embryo implantation [GO:0007566]; learning or memory [GO:0007611]; negative regulation of cell adhesion [GO:0007162]; neuron projection development [GO:0031175]; odontogenesis [GO:0042476]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell migration [GO:0030335]; positive regulation of integrin-mediated signaling pathway [GO:2001046]; positive regulation of muscle cell differentiation [GO:0051149]; regulation of basement membrane organization [GO:0110011]; substrate adhesion-dependent cell spreading [GO:0034446]; tissue development [GO:0009888]
|
basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; laminin complex [GO:0043256]; laminin-1 complex [GO:0005606]; laminin-10 complex [GO:0043259]; laminin-2 complex [GO:0005607]; laminin-8 complex [GO:0043257]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; protein complex involved in cell-matrix adhesion [GO:0098637]
|
enzyme binding [GO:0019899]; extracellular matrix structural constituent [GO:0005201]; glycosphingolipid binding [GO:0043208]; integrin binding [GO:0005178]; structural constituent of synapse-associated extracellular matrix [GO:0150043]
|
PF00053;PF21199;PF00055;
|
2.60.120.260;2.10.25.10;2.170.300.10;
| null | null |
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component.
| null | null | null | null | null |
FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Involved in the organization of the laminar architecture of the cerebral cortex (By similarity). It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons (By similarity). Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface (By similarity). {ECO:0000250}.
|
Mus musculus (Mouse)
|
P02470
|
CRYAA_BOVIN
|
MDIAIQHPWFKRTLGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQEDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFSGPKIPSGVDAGHSERAIPVSREEKPSSAPSS
| null | null |
lens development in camera-type eye [GO:0002088]; negative regulation of apoptotic process [GO:0043066]; response to heat [GO:0009408]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; structural constituent of eye lens [GO:0005212]; unfolded protein binding [GO:0051082]
|
PF00525;PF00011;
|
2.60.40.790;
|
Small heat shock protein (HSP20) family
|
PTM: Acetylation at Lys-70 may increase chaperone activity. {ECO:0000250|UniProtKB:P02489}.; PTM: Undergoes age-dependent proteolytical cleavage at the C-terminus. {ECO:0000269|PubMed:8529423}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P02489}. Nucleus {ECO:0000250|UniProtKB:P02489}. Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. {ECO:0000250|UniProtKB:P02489}.
| null | null | null | null | null |
FUNCTION: Contributes to the transparency and refractive index of the lens (By similarity). Acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions (PubMed:20440841). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (By similarity). {ECO:0000250|UniProtKB:P02489, ECO:0000269|PubMed:20440841}.
|
Bos taurus (Bovine)
|
P02489
|
CRYAA_HUMAN
|
MDVTIQHPWFKRTLGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVRSDRDKFVIFLDVKHFSPEDLTVKVQDDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALSCSLSADGMLTFCGPKIQTGLDATHAERAIPVSREEKPTSAPSS
| null | null |
lens development in camera-type eye [GO:0002088]; negative regulation of apoptotic process [GO:0043066]; negative regulation of intracellular transport [GO:0032387]; protein refolding [GO:0042026]; protein stabilization [GO:0050821]; response to heat [GO:0009408]; visual perception [GO:0007601]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; structural constituent of eye lens [GO:0005212]; structural molecule activity [GO:0005198]; unfolded protein binding [GO:0051082]
|
PF00525;PF00011;
|
2.60.40.790;
|
Small heat shock protein (HSP20) family
|
PTM: O-glycosylated; contains N-acetylglucosamine side chains.; PTM: Deamidation of Asn-101 in lens occurs mostly during the first 30 years of age, followed by a small additional amount of deamidation (approximately 5%) during the next approximately 38 years, resulting in a maximum of approximately 50% deamidation during the lifetime of the individual. {ECO:0000269|PubMed:18754677, ECO:0000269|PubMed:8175657, ECO:0000269|PubMed:9068373, ECO:0000269|PubMed:9543632, ECO:0000269|PubMed:9655350}.; PTM: Phosphorylation on Ser-122 seems to be developmentally regulated. Absent in the first months of life, it appears during the first 12 years of human lifetime. The relative amount of phosphorylated form versus unphosphorylated form does not change over the lifetime of the individual. {ECO:0000269|PubMed:10930324, ECO:0000269|PubMed:8175657, ECO:0000269|PubMed:8759518, ECO:0000269|PubMed:9068373, ECO:0000269|PubMed:9655350}.; PTM: Acetylation at Lys-70 may increase chaperone activity. {ECO:0000269|PubMed:22120592, ECO:0000269|PubMed:817940, ECO:0000269|PubMed:9655350}.; PTM: Undergoes age-dependent proteolytical cleavage at the C-terminus. Alpha-crystallin A(1-172) is the most predominant form produced most rapidly during the first 12 years of age and after this age is present in approximately 50% of the lens molecules. {ECO:0000269|PubMed:10930324, ECO:0000269|PubMed:12356833, ECO:0000269|PubMed:8175657, ECO:0000269|PubMed:9068373, ECO:0000269|PubMed:9655350}.; PTM: In young individuals and during the first approximately 30 years of life, less than half molecules contain an intramolecular disulfide bond (oxidized form), while in the remaining fraction the cysteines are in the free sulfhydryl form (reduced form). With aging, the amount of oxidized form increases up to 90% and it becomes a major constituent of high molecular weight aggregates, concomitant with an age-dependent loss of its chaperone activity. The reduced form is undetectable in cataractous lenses. {ECO:0000305|PubMed:31792453}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14512969, ECO:0000269|PubMed:19464326, ECO:0000269|PubMed:19503744, ECO:0000269|PubMed:26004348, ECO:0000269|PubMed:30340470}. Nucleus {ECO:0000269|PubMed:19464326}. Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.
| null | null | null | null | null |
FUNCTION: Contributes to the transparency and refractive index of the lens (PubMed:18302245). In its oxidized form (absence of intramolecular disulfide bond), acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions (PubMed:18199971, PubMed:19595763, PubMed:22120592, PubMed:31792453). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (PubMed:28935373). {ECO:0000269|PubMed:18199971, ECO:0000269|PubMed:19595763, ECO:0000269|PubMed:22120592, ECO:0000269|PubMed:28935373, ECO:0000269|PubMed:31792453, ECO:0000303|PubMed:18302245}.
|
Homo sapiens (Human)
|
P02510
|
CRYAB_BOVIN
|
MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPASTSLSPFYLRPPSFLRAPSWIDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLAITSSLSSDGVLTVNGPRKQASGPERTIPITREEKPAVTAAPKK
| null | null |
negative regulation of apoptotic process [GO:0043066]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of intracellular transport [GO:0032387]; protein refolding [GO:0042026]; response to heat [GO:0009408]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; lysosome [GO:0005764]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; structural constituent of eye lens [GO:0005212]; unfolded protein binding [GO:0051082]
|
PF00525;PF00011;
|
2.60.40.790;
|
Small heat shock protein (HSP20) family
|
PTM: It is not known whether either Lys-90, or Lys-92, or both are glycated.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P02511}. Nucleus {ECO:0000250|UniProtKB:P02511}. Secreted {ECO:0000250|UniProtKB:P02511}. Lysosome {ECO:0000250|UniProtKB:P23927}. Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. Localizes at the Z-bands and the intercalated disk in cardiomyocytes. Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion. {ECO:0000250|UniProtKB:P02511}.
| null | null | null | null | null |
FUNCTION: May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. In lens epithelial cells, stabilizes the ATP6V1A protein, preventing its degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:P23927}.
|
Bos taurus (Bovine)
|
P02511
|
CRYAB_HUMAN
|
MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFPTSTSLSPFYLRPPSFLRAPSWFDTGLSEMRLEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQVSGPERTIPITREEKPAVTAAPKK
| null | null |
apoptotic process involved in morphogenesis [GO:0060561]; cellular response to gamma radiation [GO:0071480]; lens development in camera-type eye [GO:0002088]; microtubule polymerization or depolymerization [GO:0031109]; muscle contraction [GO:0006936]; muscle organ development [GO:0007517]; negative regulation of amyloid fibril formation [GO:1905907]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell growth [GO:0030308]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of gene expression [GO:0010629]; negative regulation of intracellular transport [GO:0032387]; negative regulation of protein-containing complex assembly [GO:0031333]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; protein folding [GO:0006457]; protein refolding [GO:0042026]; protein stabilization [GO:0050821]; regulation of programmed cell death [GO:0043067]; response to estradiol [GO:0032355]; response to heat [GO:0009408]; response to hydrogen peroxide [GO:0042542]; response to hypoxia [GO:0001666]; stress-activated MAPK cascade [GO:0051403]; tubulin complex assembly [GO:0007021]
|
actin filament bundle [GO:0032432]; axon [GO:0030424]; cardiac myofibril [GO:0097512]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; lysosome [GO:0005764]; M band [GO:0031430]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perikaryon [GO:0043204]; protein-containing complex [GO:0032991]; synaptic membrane [GO:0097060]; Z disc [GO:0030018]
|
amyloid-beta binding [GO:0001540]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; microtubule binding [GO:0008017]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; structural constituent of eye lens [GO:0005212]; structural molecule activity [GO:0005198]; unfolded protein binding [GO:0051082]
|
PF00525;PF00011;
|
2.60.40.790;
|
Small heat shock protein (HSP20) family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19464326, ECO:0000269|PubMed:28493373}. Nucleus {ECO:0000269|PubMed:19464326}. Secreted {ECO:0000269|PubMed:32272059}. Lysosome {ECO:0000250|UniProtKB:P23927}. Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles (PubMed:19464326). Localizes at the Z-bands and the intercalated disk in cardiomyocytes (PubMed:28493373). Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059). {ECO:0000269|PubMed:19464326, ECO:0000269|PubMed:28493373, ECO:0000269|PubMed:32272059}.
| null | null | null | null | null |
FUNCTION: May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. In lens epithelial cells, stabilizes the ATP6V1A protein, preventing its degradation by the proteasome (By similarity). {ECO:0000250|UniProtKB:P23927}.
|
Homo sapiens (Human)
|
P02518
|
HSP27_DROME
|
MSIIPLLHLARELDHDYRTDWGHLLEDDFGFGVHAHDLFHPRRLLLPNTLGLGRRRYSPYERSHGHHNQMSRRASGGPNALLPAVGKDGFQVCMDVSQFKPNELTVKVVDNTVVVEGKHEEREDGHGMIQRHFVRKYTLPKGFDPNEVVSTVSSDGVLTLKAPPPPSKEQAKSERIVQIQQTGPAHLSVKAPAPEAGDGKAENGSGEKMETSK
| null | null |
behavioral response to starvation [GO:0042595]; chaperone-mediated protein folding [GO:0061077]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; determination of adult lifespan [GO:0008340]; negative regulation of apoptotic process [GO:0043066]; protein refolding [GO:0042026]; response to heat [GO:0009408]
|
cytoplasm [GO:0005737]; endoplasmic reticulum chaperone complex [GO:0034663]; nucleus [GO:0005634]
|
unfolded protein binding [GO:0051082]
|
PF00011;
|
2.60.40.790;
|
Small heat shock protein (HSP20) family
| null | null | null | null | null | null | null | null |
Drosophila melanogaster (Fruit fly)
|
P02522
|
CRBB2_BOVIN
|
MASDHQTQAGKPQPLNPKIIIFEQENFQGHSHELNGPCPNLKETGVEKAGSVLVQAGPWVGYEQANCKGEQFVFEKGEYPRWDSWTSSRRTDSLSSLRPIKVDSQEHKITLYENPNFTGKKMEVIDDDVPSFHAHGYQEKVSSVRVQSGTWVGYQYPGYRGLQYLLEKGDYKDSGDFGAPQPQVQSVRRIRDMQWHQRGAFHPSS
| null | null |
lens development in camera-type eye [GO:0002088]; visual perception [GO:0007601]
| null |
structural constituent of eye lens [GO:0005212]
|
PF00030;
|
2.60.20.10;
|
Beta/gamma-crystallin family
| null | null | null | null | null | null | null |
FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens.
|
Bos taurus (Bovine)
|
P02523
|
CRBB1_RAT
|
MSQVAKAAATTAVNPGPDGKGKGTPSTGTAPAPGPTPVPASVPRPAAKVGELPPGSYRLVVFEQENFQGRRVEFSGECLNLGDRGFDRVRSLIVLSGPWVAFEQSAFRGEMFVLEKGEYPRWDTWTSSYRSDRLMSFRPIRMDSQEHKICLFEGANFKGNTMEIQEDDVPSLWVYGFCDRVGSITVSSGTWVGYQYPGYRGYQYLLEPGDFRHWNEWGAFQPQMQAVRRLRDRQWHQEGCFPVLTAEPPK
| null | null |
lens development in camera-type eye [GO:0002088]; visual perception [GO:0007601]
| null |
structural constituent of eye lens [GO:0005212]
|
PF00030;
|
2.60.20.10;
|
Beta/gamma-crystallin family
|
PTM: Specific cleavages in the N-terminal arm occur during lens maturation and give rise to truncated forms, leading to impaired oligomerization and protein insolubilization. The protease responsible for this partial degradation could be calpain II.
| null | null | null | null | null | null |
FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens.
|
Rattus norvegicus (Rat)
|
P02533
|
K1C14_HUMAN
|
MTTCSRQFTSSSSMKGSCGIGGGIGGGSSRISSVLAGGSCRAPSTYGGGLSVSSSRFSSGGACGLGGGYGGGFSSSSSSFGSGFGGGYGGGLGAGLGGGFGGGFAGGDGLLVGSEKVTMQNLNDRLASYLDKVRALEEANADLEVKIRDWYQRQRPAEIKDYSPYFKTIEDLRNKILTATVDNANVLLQIDNARLAADDFRTKYETELNLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLKKNHEEEMNALRGQVGGDVNVEMDAAPGVDLSRILNEMRDQYEKMAEKNRKDAEEWFFTKTEELNREVATNSELVQSGKSEISELRRTMQNLEIELQSQLSMKASLENSLEETKGRYCMQLAQIQEMIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAHLSSSQFSSGSQSSRDVTSSSRQIRTKVMDVHDGKVVSTHEQVLRTKN
| null | null |
epidermis development [GO:0008544]; epithelial cell differentiation [GO:0030855]; hair cycle [GO:0042633]; intermediate filament bundle assembly [GO:0045110]; intermediate filament organization [GO:0045109]; keratinocyte differentiation [GO:0030216]; stem cell differentiation [GO:0048863]
|
basal part of cell [GO:0045178]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]; keratin filament [GO:0045095]; nucleus [GO:0005634]
|
keratin filament binding [GO:1990254]; structural constituent of cytoskeleton [GO:0005200]
|
PF00038;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
|
PTM: A disulfide bond is formed between rather than within filaments and promotes the formation of a keratin filament cage around the nucleus. {ECO:0000250|UniProtKB:Q61781}.; PTM: Ubiquitinated by the BCR(KLHL24) E3 ubiquitin ligase complex. {ECO:0000269|PubMed:27798626}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11724817, ECO:0000269|PubMed:31995743, ECO:0000269|PubMed:32179842}. Nucleus {ECO:0000269|PubMed:11724817}. Note=Expressed in both as a filamentous pattern. {ECO:0000269|PubMed:11724817}.
| null | null | null | null | null |
FUNCTION: The nonhelical tail domain is involved in promoting KRT5-KRT14 filaments to self-organize into large bundles and enhances the mechanical properties involved in resilience of keratin intermediate filaments in vitro. {ECO:0000269|PubMed:11724817}.
|
Homo sapiens (Human)
|
P02535
|
K1C10_MOUSE
|
MSVLYSSSSKQFSSSRSGGGGGGGSVRVSSTRGSLGGGYSSGGFSGGSFSRGSSGGGCFGGSSGGYGGFGGGGSFGGGYGGSSFGGGYGGSSFGGGYGGSSFGGAGFGGGGSFGGGSFGGGSYGGGFGGGGFGGDGGSLLSGNGRVTMQNLNDRLASYMDKVRALEESNYELEGKIKEWYEKHGNSSQREPRDYSKYYKTIEDLKGQILTLTTDNANVLLQIDNARLAADDFRLKYENEVTLRQSVEADINGLRRVLDELTLSKSDLEMQIESLNEELAYLKKNHEEEMRDLQNVSTGDVNVEMNAAPGVDLTQLLNNMRNQYEQLAEKNRKDAEEWFNQKSKELTTEIDSNIEQMSSHKSEITELRRTVQGLEIELQSQLALKQSLEASLAETEGRYCVQLSQIQSQISALEEQLQQIRAETECQNAEYQQLLDIKTRLENEIQTYRSLLEGEGSSSGGGGGRRGGSGGGSYGGSSGGGSYGGSSGGGGSYGGSSGGGGSYGGGSSGGGSHGGSSGGGYGGGSSSGGAGGHGGSSGGGYGGGSSSGGQGGSGGFKSSGGGDQSSKGPRY
| null | null |
cellular response to calcium ion [GO:0071277]; epidermis development [GO:0008544]; epithelial cell differentiation [GO:0030855]; intermediate filament organization [GO:0045109]; keratinocyte development [GO:0003334]; keratinocyte differentiation [GO:0030216]; positive regulation of epidermis development [GO:0045684]; protein heterotetramerization [GO:0051290]; stem cell differentiation [GO:0048863]
|
cell surface [GO:0009986]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular region [GO:0005576]; keratin filament [GO:0045095]
|
cytoskeletal protein binding [GO:0008092]; protein heterodimerization activity [GO:0046982]; structural constituent of skin epidermis [GO:0030280]
|
PF00038;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250|UniProtKB:P13645}. Cell surface {ECO:0000269|PubMed:19627498}. Cytoplasm {ECO:0000269|PubMed:24751727}.
| null | null | null | null | null |
FUNCTION: Plays a role in the establishment of the epidermal barrier on plantar skin (PubMed:26603179). Involved in the maintenance of cell layer development and keratin filament bundles in suprabasal cells of the epithelium (PubMed:24751727). {ECO:0000269|PubMed:24751727, ECO:0000269|PubMed:26603179}.; FUNCTION: (Microbial infection) Acts as a mediator of S.aureus adherence to desquamated nasal epithelial cells via clfB, and hence may play a role in nasal colonization. {ECO:0000269|PubMed:15385531}.; FUNCTION: (Microbial infection) Binds S.pneumoniae PsrP, mediating adherence of the bacteria to lung cell lines. {ECO:0000269|PubMed:19627498}.
|
Mus musculus (Mouse)
|
P02538
|
K2C6A_HUMAN
|
MASTSTTIRSHSSSRRGFSANSARLPGVSRSGFSSVSVSRSRGSGGLGGACGGAGFGSRSLYGLGGSKRISIGGGSCAISGGYGSRAGGSYGFGGAGSGFGFGGGAGIGFGLGGGAGLAGGFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPTIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQGTKTVRQNLEPLFEQYINNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIAQRSRAEAESWYQTKYEELQVTAGRHGDDLRNTKQEIAEINRMIQRLRSEIDHVKKQCANLQAAIADAEQRGEMALKDAKNKLEGLEDALQKAKQDLARLLKEYQELMNVKLALDVEIATYRKLLEGEECRLNGEGVGQVNISVVQSTVSSGYGGASGVGSGLGLGGGSSYSYGSGLGVGGGFSSSSGRAIGGGLSSVGGGSSTIKYTTTSSSSRKSYKH
| null | null |
antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cell differentiation [GO:0030154]; defense response to Gram-positive bacterium [GO:0050830]; intermediate filament organization [GO:0045109]; keratinization [GO:0031424]; killing of cells of another organism [GO:0031640]; morphogenesis of an epithelium [GO:0002009]; negative regulation of entry of bacterium into host cell [GO:2000536]; positive regulation of cell population proliferation [GO:0008284]; wound healing [GO:0042060]
|
cytosol [GO:0005829]; extracellular exosome [GO:0070062]; keratin filament [GO:0045095]; membrane [GO:0016020]; nucleus [GO:0005634]
|
structural constituent of cytoskeleton [GO:0005200]; structural constituent of skin epidermis [GO:0030280]
|
PF00038;PF16208;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
| null | null | null | null | null | null | null |
FUNCTION: Epidermis-specific type I keratin involved in wound healing. Involved in the activation of follicular keratinocytes after wounding, while it does not play a major role in keratinocyte proliferation or migration. Participates in the regulation of epithelial migration by inhibiting the activity of SRC during wound repair. {ECO:0000250|UniProtKB:P50446}.
|
Homo sapiens (Human)
|
P02540
|
DESM_PIG
|
MSQAYSSSQRVSSYRRTFGGAPSFPLGSPLSSPVFPRAGFGTKGSSSSVTSRVYQVSRTSGGAGGLGPLRASRLGATRVPSSSYGAGELLDFSLADAVNQEFLTTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAEIYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRINLPIQTFSALNFRETSPEQRGSEVHTKKTVMIKTIETRDGEVVSEATQQQHEVL
| null | null |
intermediate filament organization [GO:0045109]; nuclear envelope organization [GO:0006998]; skeletal muscle organ development [GO:0060538]
|
cell tip [GO:0051286]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; intercalated disc [GO:0014704]; intermediate filament [GO:0005882]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; sarcolemma [GO:0042383]; Z disc [GO:0030018]
|
structural constituent of cytoskeleton [GO:0005200]
|
PF00038;PF04732;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
|
PTM: ADP-ribosylation prevents ability to form intermediate filaments. {ECO:0000250|UniProtKB:P48675}.; PTM: Phosphorylation at Ser-7, Ser-28 and Ser-32 by CDK1 and phosphorylation at Ser-60 by AURKB contribute to efficient separation of desmin intermediate filaments during mitosis. {ECO:0000250|UniProtKB:P31001}.; PTM: Ubiquitination by a SCF-like complex containing ASB2 leads to proteasomal degradation. {ECO:0000250|UniProtKB:P31001}.
|
SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:P17661}. Cytoplasm {ECO:0000250|UniProtKB:P17661}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P17661}. Nucleus {ECO:0000250|UniProtKB:P31001}. Cell tip {ECO:0000250|UniProtKB:P31001}. Nucleus envelope {ECO:0000250|UniProtKB:P31001}. Note=Localizes in the intercalated disks which occur at the Z line of cardiomyocytes. Localizes in the nucleus exclusively in differentiating cardiac progenitor cells and premature cardiomyocytes. PKP2 is required for correct anchoring of DES at the cell tip and nuclear envelope (By similarity). {ECO:0000250|UniProtKB:P17661, ECO:0000250|UniProtKB:P31001}.
| null | null | null | null | null |
FUNCTION: Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity. In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures. May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction. Required for nuclear membrane integrity, via anchoring at the cell tip and nuclear envelope, resulting in maintenance of microtubule-derived intracellular mechanical forces (By similarity). Contributes to the transcriptional regulation of the NKX2-5 gene in cardiac progenitor cells during a short period of cardiomyogenesis and in cardiac side population stem cells in the adult. Plays a role in maintaining an optimal conformation of nebulette (NEB) on heart muscle sarcomeres to bind and recruit cardiac alpha-actin. {ECO:0000250|UniProtKB:P17661, ECO:0000250|UniProtKB:P31001}.
|
Sus scrofa (Pig)
|
P02541
|
DESM_MESAU
|
MSQAYSSSQRVSSYRRTFGGAPSFSLGSPLSSPVFPRAGFGTKGSSSSVTSRVYQVSRTSGGAGGLGSLRASRLGSTRAPSYGAGELLDFSLADAVNQEFLATRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAELYEEEMRELRRQVEVLTNQRARVDVERDNLIDDLQRLKAKLQEEIQLREEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRINLPIQTFSALNFRETSPEQRGSEVHTKKTVMIKTIETRDGEVVSEATQQQHEVL
| null | null |
intermediate filament organization [GO:0045109]; nuclear envelope organization [GO:0006998]; skeletal muscle organ development [GO:0060538]
|
cardiac myofibril [GO:0097512]; cell tip [GO:0051286]; cytoplasm [GO:0005737]; fascia adherens [GO:0005916]; intercalated disc [GO:0014704]; intermediate filament [GO:0005882]; neuromuscular junction [GO:0031594]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]; sarcolemma [GO:0042383]; Z disc [GO:0030018]
|
cytoskeletal protein binding [GO:0008092]; identical protein binding [GO:0042802]; structural constituent of cytoskeleton [GO:0005200]
|
PF00038;PF04732;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
|
PTM: ADP-ribosylation prevents ability to form intermediate filaments. {ECO:0000250|UniProtKB:P48675}.; PTM: Phosphorylation at Ser-7, Ser-28 and Ser-32 by CDK1 and phosphorylation at Ser-60 by AURKB contribute to efficient separation of desmin intermediate filaments during mitosis. {ECO:0000250|UniProtKB:P31001}.; PTM: Ubiquitination by a SCF-like complex containing ASB2 leads to proteasomal degradation. {ECO:0000250|UniProtKB:P31001}.
|
SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:P17661}. Cytoplasm {ECO:0000250|UniProtKB:P17661}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P17661}. Nucleus {ECO:0000250|UniProtKB:P31001}. Cell tip {ECO:0000250|UniProtKB:P31001}. Nucleus envelope {ECO:0000250|UniProtKB:P31001}. Note=Localizes in the intercalated disks which occur at the Z line of cardiomyocytes. Localizes in the nucleus exclusively in differentiating cardiac progenitor cells and premature cardiomyocytes. PKP2 is required for correct anchoring of DES at the cell tip and nuclear envelope (By similarity). {ECO:0000250|UniProtKB:P17661, ECO:0000250|UniProtKB:P31001}.
| null | null | null | null | null |
FUNCTION: Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity. In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures. May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction. Required for nuclear membrane integrity, via anchoring at the cell tip and nuclear envelope, resulting in maintenance of microtubule-derived intracellular mechanical forces (By similarity). Contributes to the transcriptional regulation of the NKX2-5 gene in cardiac progenitor cells during a short period of cardiomyogenesis and in cardiac side population stem cells in the adult. Plays a role in maintaining an optimal conformation of nebulette (NEB) on heart muscle sarcomeres to bind and recruit cardiac alpha-actin. {ECO:0000250|UniProtKB:P17661, ECO:0000250|UniProtKB:P31001}.
|
Mesocricetus auratus (Golden hamster)
|
P02542
|
DESM_CHICK
|
MSQSYSSSQRVSSYRRTFGGGTSPVFPRASFGSRGSGSSVTSRVYQVSRTSAVPTLSTFRTTRVTPLRTYQSAYQGAGELLDFSLADAMNQEFLQTRTNEKVELQELNDRFANYIEKVRFLEQQNALMVAEVNRLRGKEPTRVAEMYEEELRELRRQVDALTGQRARVEVERDNLLDDLQKLKQRLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLQEEIAFLKKVHEEEIRELQAQLQEQHIQVEMDISKPDLTAALRDIRAQYESIAAKNIAEAEEWYKSKVSDLTQAANKNNDALRQAKQEMLEYRHQIQSYTCEIDALKGTNDSLMRQMREMEERFAGEAGGYQDTIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEENRISIPMHQTFASALNFRETSPDQRGSEVHTKKTVMIKTIETRDGEVVSEATQQQHEVL
| null | null |
intermediate filament organization [GO:0045109]; intermediate filament polymerization [GO:0045107]; skeletal muscle organ development [GO:0060538]
|
cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; dense body [GO:0097433]; intercalated disc [GO:0014704]; intermediate filament [GO:0005882]; sarcolemma [GO:0042383]; type III intermediate filament [GO:0045098]; Z disc [GO:0030018]
|
structural constituent of cytoskeleton [GO:0005200]
|
PF00038;PF04732;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
| null |
SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:P17661}. Cytoplasm {ECO:0000250|UniProtKB:P17661}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P17661}.
| null | null | null | null | null |
FUNCTION: Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity. In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures. {ECO:0000250|UniProtKB:P17661, ECO:0000250|UniProtKB:P31001}.
|
Gallus gallus (Chicken)
|
P02543
|
VIME_PIG
|
MSTRTVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYTSSPGGVYATRSSAVRLRSSVPGVRLLQDAVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEETLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQAQIQEQHVQIDMDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFAVEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLESLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE
| null | null |
cellular response to lipopolysaccharide [GO:0071222]; cellular response to muramyl dipeptide [GO:0071225]; intermediate filament organization [GO:0045109]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; intermediate filament [GO:0005882]; nuclear matrix [GO:0016363]; plasma membrane [GO:0005886]
|
structural constituent of cytoskeleton [GO:0005200]
|
PF00038;PF04732;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
|
PTM: One of the most prominent phosphoproteins in various cells of mesenchymal origin. Phosphorylation is enhanced during cell division, at which time vimentin filaments are significantly reorganized. Phosphorylation by PKN1 inhibits the formation of filaments. Filament disassembly during mitosis is promoted by phosphorylation at Ser-55 as well as by nestin. Phosphorylated at Ser-56 by CDK5 during neutrophil secretion in the cytoplasm. Phosphorylated by STK33. Phosphorylated on tyrosine residues by SRMS. {ECO:0000250|UniProtKB:P08670, ECO:0000250|UniProtKB:P31000}.; PTM: S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex. {ECO:0000250|UniProtKB:P08670}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08670}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08670}. Nucleus matrix {ECO:0000250|UniProtKB:P31000}. Cell membrane {ECO:0000250|UniProtKB:P20152}.
| null | null | null | null | null |
FUNCTION: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. {ECO:0000250|UniProtKB:P31000}.; FUNCTION: Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. {ECO:0000250|UniProtKB:P08670}.
|
Sus scrofa (Pig)
|
P02544
|
VIME_MESAU
|
MSTRSVSSSSYRRMFGGPGTSNRQSSNRSYVTTSTRTYSLGSLRPSTSRSLYSSSPGGAYVTRSSAVRLRSSMPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRRQVQSLTCEVDALKGTNESLERQMREMEENFALEAANYQDTIGRLQDEIQNMKEEMARHLREYQDLLNVKMALDIEIATYRKLLEGEESRISLPLPNFSSLNLRETNLESLPLVDTHSKRTLLIKTVETRDGQVINETSQHHDDLE
| null | null |
cellular response to lipopolysaccharide [GO:0071222]; cellular response to muramyl dipeptide [GO:0071225]; intermediate filament organization [GO:0045109]; intermediate filament polymerization [GO:0045107]
|
axon [GO:0030424]; cytoplasm [GO:0005737]; intermediate filament [GO:0005882]; nuclear matrix [GO:0016363]; plasma membrane [GO:0005886]
|
structural constituent of cytoskeleton [GO:0005200]
|
PF00038;PF04732;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
|
PTM: Phosphorylation by PKN1 inhibits the formation of filaments. Filament disassembly during mitosis is promoted by phosphorylation at Ser-54 as well as by nestin. One of the most prominent phosphoproteins in various cells of mesenchymal origin. Phosphorylation is enhanced during cell division, at which time vimentin filaments are significantly reorganized. Phosphorylated at Ser-55 by CDK5 during neutrophil secretion in the cytoplasm. Phosphorylated by STK33. Phosphorylated on tyrosine residues by SRMS. {ECO:0000250|UniProtKB:P08670, ECO:0000250|UniProtKB:P31000}.; PTM: S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex. {ECO:0000250|UniProtKB:P08670}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08670}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08670}. Nucleus matrix {ECO:0000250|UniProtKB:P31000}. Cell membrane {ECO:0000250|UniProtKB:P20152}.
| null | null | null | null | null |
FUNCTION: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. {ECO:0000250|UniProtKB:P31000}.; FUNCTION: Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2. {ECO:0000250|UniProtKB:P08670}.
|
Mesocricetus auratus (Golden hamster)
|
P02545
|
LMNA_HUMAN
|
METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLARERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSPTSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRNKSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNTWGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRSRTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRSYLLGNSSPRTQSPQNCSIM
| null | null |
cellular response to hypoxia [GO:0071456]; cellular senescence [GO:0090398]; DNA double-strand break attachment to nuclear envelope [GO:1990683]; establishment or maintenance of microtubule cytoskeleton polarity [GO:0030951]; heterochromatin formation [GO:0031507]; muscle organ development [GO:0007517]; negative regulation of cardiac muscle hypertrophy in response to stress [GO:1903243]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of extrinsic apoptotic signaling pathway [GO:2001237]; negative regulation of mesenchymal cell proliferation [GO:0072201]; negative regulation of release of cytochrome c from mitochondria [GO:0090201]; nuclear envelope organization [GO:0006998]; nuclear migration [GO:0007097]; nuclear pore localization [GO:0051664]; positive regulation of gene expression [GO:0010628]; protein import into nucleus [GO:0006606]; protein localization [GO:0008104]; protein localization to nuclear envelope [GO:0090435]; protein localization to nucleus [GO:0034504]; regulation of cell migration [GO:0030334]; regulation of protein localization to nucleus [GO:1900180]; regulation of protein stability [GO:0031647]; regulation of telomere maintenance [GO:0032204]; ventricular cardiac muscle cell development [GO:0055015]
|
cytosol [GO:0005829]; intermediate filament [GO:0005882]; lamin filament [GO:0005638]; nuclear envelope [GO:0005635]; nuclear lamina [GO:0005652]; nuclear matrix [GO:0016363]; nuclear membrane [GO:0031965]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; site of double-strand break [GO:0035861]
|
identical protein binding [GO:0042802]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of nuclear lamina [GO:0160123]; structural molecule activity [GO:0005198]
|
PF00038;PF00932;
|
1.20.5.170;2.60.40.1260;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
|
PTM: Proteolytic cleavage of the C-terminal of 18 residues of prelamin-A/C results in the production of lamin-A/C (PubMed:20458013, PubMed:8175923, PubMed:9030603). The prelamin-A/C maturation pathway includes farnesylation of CAAX motif by protein farnesyltransferase (FNTA and FNTB), removal of the last three amino acids (-AAX) by RCE1/FACE2 and/or ZMPSTE24, methylation of the C-terminal cysteine by ICMT and endoproteolytic removal of the last 15 C-terminal amino acids by ZMPSTE24 (PubMed:20458013, PubMed:8175923, PubMed:9030603). Proteolytic cleavage requires prior farnesylation and methylation, and absence of these blocks cleavage (PubMed:20458013, PubMed:8175923, PubMed:9030603). {ECO:0000269|PubMed:20458013, ECO:0000269|PubMed:8175923, ECO:0000269|PubMed:9030603}.; PTM: Farnesylation of prelamin-A/C facilitates nuclear envelope targeting. {ECO:0000269|PubMed:15317753, ECO:0000269|PubMed:22355414}.; PTM: Phosphorylation plays a key role in lamin organization, subcellular localization and nuclear envelope disintegration (PubMed:2188730, PubMed:2344612, PubMed:24741066, PubMed:37788673, PubMed:37832547). Phosphorylation by CDK1 at Ser-22 and Ser-392 at the onset of mitosis drives lamin disassembly and nuclear envelope breakdown (PubMed:2188730, PubMed:2344612). Phosphorylation at Ser-22 and Ser-392 during interphase promotes localization to the nucleoplasm and regulates lamina assembly (PubMed:24741066). Phosphorylation at Ser-22, Ser-392 and Ser-628 during interphase causes redistribution between the nucleus and the cytoplasm (PubMed:24741066). Phosphorylation at Ser-22 by CDK1 regulates matrix stiffness (PubMed:25127216). Phosphorylation status of Ser-22 determines its localization between double-strand break (DSB) sites and the nuclear matrix (PubMed:31548606). Phosphorylated by ATR at Ser-282 in response to DNA damage, leading to lamin disassembly and nuclear envelope rupture (PubMed:37832547). Phosphorylation also regulates stability in micronuclei arising from genome instability: phosphorylation at Ser-395 by ATR in response to genome instability and double-stranded DNA breaks primes LMNA for subsequent phosphorylation at Ser-392 by CDK1 and micronuclei envelope rupture (PubMed:37788673). The rupture of micronuclear envelope triggers the cGAS-STING pathway thereby activating the type I interferon response and innate immunity (PubMed:37788673). {ECO:0000269|PubMed:2188730, ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066, ECO:0000269|PubMed:25127216, ECO:0000269|PubMed:31548606, ECO:0000269|PubMed:37788673, ECO:0000269|PubMed:37832547}.; PTM: Acetylation by KAT8 is required for nuclear architecture. {ECO:0000250|UniProtKB:P48678}.; PTM: Sumoylation is necessary for the localization to the nuclear envelope. {ECO:0000269|PubMed:18606848}.
|
SUBCELLULAR LOCATION: Nucleus lamina {ECO:0000269|PubMed:2188730, ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:24741066, ECO:0000269|PubMed:37788673, ECO:0000269|PubMed:37832547, ECO:0000305|PubMed:10080180}. Nucleus envelope {ECO:0000269|PubMed:29599122, ECO:0000269|PubMed:37788673, ECO:0000269|PubMed:37832547}. Nucleus, nucleoplasm {ECO:0000269|PubMed:15372542, ECO:0000269|PubMed:24741066, ECO:0000269|PubMed:31548606}. Nucleus matrix {ECO:0000269|PubMed:31548606}. Note=Farnesylation of prelamin-A/C facilitates nuclear envelope targeting and subsequent cleavage by ZMPSTE24/FACE1 to remove the farnesyl group produces mature lamin-A/C, which can then be inserted into the nuclear lamina (PubMed:15317753). EMD is required for proper localization of non-farnesylated prelamin-A/C (PubMed:19323649). Also localizes to the micronuclear envelope in response to response to genome instability (PubMed:37788673). {ECO:0000269|PubMed:15317753, ECO:0000269|PubMed:19323649, ECO:0000269|PubMed:37788673}.; SUBCELLULAR LOCATION: [Isoform C]: Nucleus speckle {ECO:0000269|PubMed:16061563}.
| null | null | null | null | null |
FUNCTION: [Lamin-A/C]: Lamins are intermediate filament proteins that assemble into a filamentous meshwork, and which constitute the major components of the nuclear lamina, a fibrous layer on the nucleoplasmic side of the inner nuclear membrane (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:2188730, PubMed:22431096, PubMed:2344612, PubMed:23666920, PubMed:24741066, PubMed:31434876, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamins provide a framework for the nuclear envelope, bridging the nuclear envelope and chromatin, thereby playing an important role in nuclear assembly, chromatin organization, nuclear membrane and telomere dynamics (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:24741066, PubMed:31548606, PubMed:37788673, PubMed:37832547). Lamin A and C also regulate matrix stiffness by conferring nuclear mechanical properties (PubMed:23990565, PubMed:25127216). The structural integrity of the lamina is strictly controlled by the cell cycle, as seen by the disintegration and formation of the nuclear envelope in prophase and telophase, respectively (PubMed:2188730, PubMed:2344612). Lamin A and C are present in equal amounts in the lamina of mammals (PubMed:10080180, PubMed:10580070, PubMed:10587585, PubMed:10814726, PubMed:11799477, PubMed:12075506, PubMed:12927431, PubMed:15317753, PubMed:18551513, PubMed:18611980, PubMed:22431096, PubMed:23666920, PubMed:31548606). Also invoved in DNA repair: recruited by DNA repair proteins XRCC4 and IFFO1 to the DNA double-strand breaks (DSBs) to prevent chromosome translocation by immobilizing broken DNA ends (PubMed:31548606). Required for normal development of peripheral nervous system and skeletal muscle and for muscle satellite cell proliferation (PubMed:10080180, PubMed:10814726, PubMed:11799477, PubMed:18551513, PubMed:22431096). Required for osteoblastogenesis and bone formation (PubMed:12075506, PubMed:15317753, PubMed:18611980). Also prevents fat infiltration of muscle and bone marrow, helping to maintain the volume and strength of skeletal muscle and bone (PubMed:10587585). Required for cardiac homeostasis (PubMed:10580070, PubMed:12927431, PubMed:18611980, PubMed:23666920). {ECO:0000269|PubMed:10080180, ECO:0000269|PubMed:10580070, ECO:0000269|PubMed:10587585, ECO:0000269|PubMed:10814726, ECO:0000269|PubMed:11799477, ECO:0000269|PubMed:12075506, ECO:0000269|PubMed:12927431, ECO:0000269|PubMed:15317753, ECO:0000269|PubMed:18551513, ECO:0000269|PubMed:18611980, ECO:0000269|PubMed:2188730, ECO:0000269|PubMed:22431096, ECO:0000269|PubMed:2344612, ECO:0000269|PubMed:23666920, ECO:0000269|PubMed:23990565, ECO:0000269|PubMed:24741066, ECO:0000269|PubMed:25127216, ECO:0000269|PubMed:31434876, ECO:0000269|PubMed:31548606, ECO:0000269|PubMed:37788673, ECO:0000269|PubMed:37832547}.; FUNCTION: [Prelamin-A/C]: Prelamin-A/C can accelerate smooth muscle cell senescence (PubMed:20458013). It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence (PubMed:20458013). {ECO:0000269|PubMed:20458013}.
|
Homo sapiens (Human)
|
P02547
|
NFL_PIG
|
MSSFYSEPYYSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGLMPSLENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAQLLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGSLTTGYSQSSQVFGRSAYGGLQTSSYLMSTRSFPSYYTSHVQEEQIEVEETIEAAKAEEAKDEPPSEGEAEEEGKEKEEAEAEAEAEEEGAQEEEEAAEKEESEEAKEEEGGEGEQGEETKEAEEEEKKDEGAGEEQATKKKD
| null | null |
anterograde axonal transport [GO:0008089]; axonal transport of mitochondrion [GO:0019896]; intermediate filament organization [GO:0045109]; neurofilament bundle assembly [GO:0033693]; retrograde axonal transport [GO:0008090]
|
axon [GO:0030424]; axon cytoplasm [GO:1904115]; cytoplasm [GO:0005737]; intermediate filament [GO:0005882]; neurofilament [GO:0005883]; postsynaptic intermediate filament cytoskeleton [GO:0099160]
|
identical protein binding [GO:0042802]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of postsynaptic intermediate filament cytoskeleton [GO:0099184]
|
PF00038;PF04732;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
|
PTM: O-glycosylated. {ECO:0000250}.; PTM: Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization. {ECO:0000250}.; PTM: Ubiquitinated in the presence of TRIM2 and UBE2D1. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000250|UniProtKB:P08551}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08551}.
| null | null | null | null | null |
FUNCTION: Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (By similarity). {ECO:0000250|UniProtKB:P08551}.
|
Sus scrofa (Pig)
|
P02548
|
NFL_BOVIN
|
MSSFSYEPYYSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGSLMPSLESLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGSLTTGYTQSSQVFGRSAYGGLQTSSYLMSARSFPSYYTSHVQEEQIEVEETIEAAKAEEAKDEPPSEGEAEEEEKEKEEAEAEAEAEAEAEAEEEEGAQEEEAAKEDAEEAKEEEGGEGEEAEETKEAEEEEKKDEGAGEEQATKKKD
| null | null |
anterograde axonal transport [GO:0008089]; axonal transport of mitochondrion [GO:0019896]; axonogenesis [GO:0007409]; intermediate filament bundle assembly [GO:0045110]; intermediate filament organization [GO:0045109]; locomotion [GO:0040011]; microtubule cytoskeleton organization [GO:0000226]; motor neuron apoptotic process [GO:0097049]; negative regulation of motor neuron apoptotic process [GO:2000672]; negative regulation of neuron apoptotic process [GO:0043524]; neurofilament bundle assembly [GO:0033693]; neurofilament cytoskeleton organization [GO:0060052]; neuromuscular process controlling balance [GO:0050885]; neuron projection morphogenesis [GO:0048812]; peripheral nervous system axon regeneration [GO:0014012]; positive regulation of axonogenesis [GO:0050772]; postsynaptic modulation of chemical synaptic transmission [GO:0099170]; regulation of axon diameter [GO:0031133]; regulation of synapse maturation [GO:0090128]; retrograde axonal transport [GO:0008090]
|
axon [GO:0030424]; axon cytoplasm [GO:1904115]; cholinergic synapse [GO:0098981]; cytoplasm [GO:0005737]; intermediate filament [GO:0005882]; neurofilament [GO:0005883]; neuromuscular junction [GO:0031594]; postsynaptic intermediate filament cytoskeleton [GO:0099160]; presynaptic intermediate filament cytoskeleton [GO:0099182]; Schaffer collateral - CA1 synapse [GO:0098685]
|
identical protein binding [GO:0042802]; protein-macromolecule adaptor activity [GO:0030674]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of postsynaptic intermediate filament cytoskeleton [GO:0099184]
|
PF00038;PF04732;
|
1.20.5.170;1.20.5.500;1.20.5.1160;
|
Intermediate filament family
|
PTM: O-glycosylated. {ECO:0000250}.; PTM: Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization. {ECO:0000250}.; PTM: Ubiquitinated in the presence of TRIM2 and UBE2D1. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000250|UniProtKB:P08551}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08551}.
| null | null | null | null | null |
FUNCTION: Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (By similarity). {ECO:0000250|UniProtKB:P08551}.
|
Bos taurus (Bovine)
|
P02549
|
SPTA1_HUMAN
|
MEQFPKETVVESSGPKVLETAEEIQERRQEVLTRYQSFKERVAERGQKLEDSYHLQVFKRDADDLGKWIMEKVNILTDKSYEDPTNIQGKYQKHQSLEAEVQTKSRLMSELEKTREERFTMGHSAHEETKAHIEELRHLWDLLLELTLEKGDQLLRALKFQQYVQECADILEWIGDKEAIATSVELGEDWERTEVLHKKFEDFQVELVAKEGRVVEVNQYANECAEENHPDLPLIQSKQNEVNAAWERLRGLALQRQKALSNAANLQRFKRDVTEAIQWIKEKEPVLTSEDYGKDLVASEGLFHSHKGLERNLAVMSDKVKELCAKAEKLTLSHPSDAPQIQEMKEDLVSSWEHIRALATSRYEKLQATYWYHRFSSDFDELSGWMNEKTAAINADELPTDVAGGEVLLDRHQQHKHEIDSYDDRFQSADETGQDLVNANHEASDEVREKMEILDNNWTALLELWDERHRQYEQCLDFHLFYRDSEQVDSWMSRQEAFLENEDLGNSLGSAEALLQKHEDFEEAFTAQEEKIITVDKTATKLIGDDHYDSENIKAIRDGLLARRDALREKAATRRRLLKESLLLQKLYEDSDDLKNWINKKKKLADDEDYKDIQNLKSRVQKQQVFEKELAVNKTQLENIQKTGQEMIEGGHYASDNVTTRLSEVASLWEELLEATKQKGTQLHEANQQLQFENNAEDLQRWLEDVEWQVTSEDYGKGLAEVQNRLRKHGLLESAVAARQDQVDILTDLAAYFEEIGHPDSKDIRARQESLVCRFEALKEPLATRKKKLLDLLHLQLICRDTEDEEAWIQETEPSATSTYLGKDLIASKKLLNRHRVILENIASHEPRIQEITERGNKMVEEGHFAAEDVASRVKSLNQNMESLRARAARRQNDLEANVQFQQYLADLHEAETWIREKEPIVDNTNYGADEEAAGALLKKHEAFLLDLNSFGDSMKALRNQANACQQQQAAPVEGVAGEQRVMALYDFQARSPREVTMKKGDVLTLLSSINKDWWKVEAADHQGIVPAVYVRRLAHDEFPMLPQRRREEPGNITQRQEQIENQYRSLLDRAEERRRRLLQRYNEFLLAYEAGDMLEWIQEKKAENTGVELDDVWELQKKFDEFQKDLNTNEPRLRDINKVADDLLFEGLLTPEGAQIRQELNSRWGSLQRLADEQRQLLGSAHAVEVFHREADDTKEQIEKKCQALSAADPGSDLFSVQALQRRHEGFERDLVPLGDKVTILGETAERLSESHPDATEDLQRQKMELNEAWEDLQGRTKDRKESLNEAQKFYLFLSKARDLQNWISSIGGMVSSQELAEDLTGIEILLERHQEHRADMEAEAPTFQALEDFSAELIDSGHHASPEIEKKLQAVKLERDDLEKAWEKRKKILDQCLELQMFQGNCDQVESWMVARENSLRSDDKSSLDSLEALMKKRDDLDKAITAQEGKITDLEHFAESLIADEHYAKEEIATRLQRVLDRWKALKAQLIDERTKLGDYANLKQFYRDLEELEEWISEMLPTACDESYKDATNIQRKYLKHQTFAHEVDGRSEQVHGVINLGNSLIECSACDGNEEAMKEQLEQLKEHWDHLLERTNDKGKKLNEASRQQRFNTSIRDFEFWLSEAETLLAMKDQARDLASAGNLLKKHQLLEREMLAREDALKDLNTLAEDLLSSGTFNVDQIVKKKDNVNKRFLNVQELAAAHHEKLKEAYALFQFFQDLDDEESWIEEKLIRVSSQDYGRDLQGVQNLLKKHKRLEGELVAHEPAIQNVLDMAEKLKDKAAVGQEEIQLRLAQFVEHWEKLKELAKARGLKLEESLEYLQFMQNAEEEEAWINEKNALAVRGDCGDTLAATQSLLMKHEALENDFAVHETRVQNVCAQGEDILNKVLQEESQNKEISSKIEALNEKTPSLAKAIAAWKLQLEDDYAFQEFNWKADVVEAWIADKETSLKTNGNGADLGDFLTLLAKQDTLDASLQSFQQERLPEITDLKDKLISAQHNQSKAIEERYAALLKRWEQLLEASAVHRQKLLEKQLPLQKAEDLFVEFAHKASALNNWCEKMEENLSEPVHCVSLNEIRQLQKDHEDFLASLARAQADFKCLLELDQQIKALGVPSSPYTWLTVEVLERTWKHLSDIIEEREQELQKEEARQVKNFEMCQEFEQNASTFLQWILETRAYFLDGSLLKETGTLESQLEANKRKQKEIQAMKRQLTKIVDLGDNLEDALILDIKYSTIGLAQQWDQLYQLGLRMQHNLEQQIQAKDIKGVSEETLKEFSTIYKHFDENLTGRLTHKEFRSCLRGLNYYLPMVEEDEHEPKFEKFLDAVDPGRKGYVSLEDYTAFLIDKESENIKSSDEIENAFQALAEGKSYITKEDMKQALTPEQVSFCATHMQQYMDPRGRSHLSGYDYVGFTNSYFGN
| null | null |
actin cytoskeleton organization [GO:0030036]; actin filament bundle assembly [GO:0051017]; actin filament capping [GO:0051693]; actin filament organization [GO:0007015]; hemopoiesis [GO:0030097]; lymphocyte homeostasis [GO:0002260]; plasma membrane organization [GO:0007009]; porphyrin-containing compound biosynthetic process [GO:0006779]; positive regulation of T cell proliferation [GO:0042102]; regulation of cell shape [GO:0008360]
|
actin cytoskeleton [GO:0015629]; actin filament bundle [GO:0032432]; actomyosin contractile ring [GO:0005826]; axon [GO:0030424]; cell junction [GO:0030054]; cell projection [GO:0042995]; cortical actin cytoskeleton [GO:0030864]; cuticular plate [GO:0032437]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; plasma membrane [GO:0005886]; spectrin [GO:0008091]; spectrin-associated cytoskeleton [GO:0014731]
|
actin filament binding [GO:0051015]; actin lateral binding [GO:0003786]; calcium ion binding [GO:0005509]; structural constituent of cytoskeleton [GO:0005200]
|
PF08726;PF00018;PF00435;
|
1.20.5.170;1.20.58.60;1.10.238.10;2.30.30.40;
|
Spectrin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
| null | null | null | null | null |
FUNCTION: Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane.
|
Homo sapiens (Human)
|
P02550
|
TBA1A_PIG
|
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRAHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYEPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
|
3.6.5.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363};
|
microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]
|
cytoplasm [GO:0005737]; microtubule [GO:0005874]
|
GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200]
|
PF00091;PF03953;
|
1.10.287.600;3.30.1330.20;3.40.50.1440;
|
Tubulin family
|
PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. Cilia and flagella glycylation is required for their stability and maintenance. Flagella glycylation controls sperm motility. {ECO:0000250|UniProtKB:P68369}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (By similarity). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). Glutamylation is also involved in cilia motility (By similarity). {ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.; PTM: Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen. This modification has been correlated with increased microtubule stability, intracellular transport and ciliary assembly. {ECO:0000250|UniProtKB:Q71U36}.; PTM: Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability. {ECO:0000250|UniProtKB:P68363}.; PTM: Nitration of Tyr-451 is irreversible and interferes with normal dynein intracellular distribution. {ECO:0000250|UniProtKB:Q71U36}.; PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (MATCAP, VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.; PTM: [Tubulin alpha-1A chain]: Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1 (By similarity). Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules. In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (By similarity). {ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.; PTM: [Detyrosinated tubulin alpha-1A chain]: Detyrosination is involved in metaphase plate congression by guiding chromosomes during mitosis: detyrosination promotes interaction with CENPE, promoting pole-proximal transport of chromosomes toward the equator (By similarity). Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle. In cardiomyocytes, detyrosinated microtubules are required to resist to contractile compression during contraction: detyrosination promotes association with desmin (DES) at force-generating sarcomeres, leading to buckled microtubules and mechanical resistance to contraction (By similarity). {ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:7225365}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P68363};
| null | null | null | null |
FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers (PubMed:7225365). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms (PubMed:7225365). Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (PubMed:7225365). {ECO:0000269|PubMed:7225365}.
|
Sus scrofa (Pig)
|
P02552
|
TBA1A_CHICK
|
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
|
3.6.5.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363};
|
microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]
|
cytoplasm [GO:0005737]; microtubule [GO:0005874]
|
GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200]
|
PF00091;PF03953;
|
1.10.287.600;3.30.1330.20;3.40.50.1440;
|
Tubulin family
|
PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of polyglycylation is still unclear. {ECO:0000250|UniProtKB:P68369}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (By similarity). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). {ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.; PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.; PTM: [Tubulin alpha-1A chain]: Tyrosination promotes microtubule interaction with CAP-Gly microtubule plus-end tracking proteins. Tyrosinated tubulins regulate the initiation of dynein-driven motility. {ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.; PTM: [Detyrosinated tubulin alpha-1A chain]: Detyrosination is involved in metaphase plate congression by guiding chromosomes during mitosis (By similarity). Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle. In cardiomyocytes, detyrosinated microtubules are required to resist to contractile compression during contraction (By similarity). {ECO:0000250|UniProtKB:P68369, ECO:0000250|UniProtKB:Q71U36}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P68363};
| null | null | null | null |
FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
|
Gallus gallus (Chicken)
|
P02554
|
TBB_PIG
|
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEGEEDEA
| null |
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363};
|
microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]
|
cytoplasm [GO:0005737]; microtubule [GO:0005874]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200]
|
PF00091;PF03953;
|
1.10.287.600;3.30.1330.20;3.40.50.1440;
|
Tubulin family
|
PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. Cilia and flagella glycylation is required for their stability and maintenance. Flagella glycylation controls sperm motility. {ECO:0000250|UniProtKB:A2AQ07}.; PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (By similarity). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (By similarity). {ECO:0000250|UniProtKB:A2AQ07, ECO:0000250|UniProtKB:Q71U36}.; PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules. {ECO:0000250|UniProtKB:Q3ZCM7}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:7225365}.
| null | null | null | null | null |
FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers (PubMed:7225365). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms (PubMed:7225365). Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin (PubMed:7225365). {ECO:0000269|PubMed:7225365}.
|
Sus scrofa (Pig)
|
P02557
|
TBB_YEAST
|
MREIIHISTGQCGNQIGAAFWETICGEHGLDFNGTYHGHDDIQKERLNVYFNEASSGKWVPRSINVDLEPGTIDAVRNSAIGNLFRPDNYIFGQSSAGNVWAKGHYTEGAELVDSVMDVIRREAEGCDSLQGFQITHSLGGGTGSGMGTLLISKIREEFPDRMMATFSVLPSPKTSDTVVEPYNATLSVHQLVEHSDETFCIDNEALYDICQRTLKLNQPSYGDLNNLVSSVMSGVTTSLRYPGQLNSDLRKLAVNLVPFPRLHFFMVGYAPLTAIGSQSFRSLTVPELTQQMFDAKNMMAAADPRNGRYLTVAAFFRGKVSVKEVEDEMHKVQSKNSDYFVEWIPNNVQTAVCSVAPQGLDMAATFIANSTSIQELFKRVGDQFSAMFKRKAFLHWYTSEGMDELEFSEAESNMNDLVSEYQQYQEATVEDDEEVDENGDFGAPQNQDEPITENFE
| null |
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363};
|
cytoplasmic microtubule organization [GO:0031122]; cytoskeleton organization [GO:0007010]; microtubule cytoskeleton organization [GO:0000226]; microtubule-based process [GO:0007017]; mitotic cell cycle [GO:0000278]; mitotic spindle assembly [GO:0090307]; mitotic spindle elongation [GO:0000022]; positive regulation of intracellular protein transport [GO:0090316]; response to antibiotic [GO:0046677]
|
cytoplasm [GO:0005737]; microtubule [GO:0005874]; tubulin complex [GO:0045298]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200]
|
PF00091;PF03953;
|
1.10.287.600;3.30.1330.20;3.40.50.1440;
|
Tubulin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:23001566}. Note=Colocalizes with kinesin KIP3 at the plus ends of growing microtubules and along the microtubule lattice. {ECO:0000269|PubMed:23001566}.
| null | null | null | null | null |
FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers (PubMed:28013290). Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. {ECO:0000269|PubMed:28013290}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
P02562
|
MYSS_RABIT
|
SAETEKEMANMKEEFEKTKESLAKAEAKRKELEEKMVALMQEKNDLQLQVQAEADSLADAEERQDLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQETSMDIENDKQQLDEKLKKLEFMTNLQSKIEDEQALMTNLQRIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEFEKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSELKMEIDDLAGNMETVSKAKGNLEKMCRTLEDQLSEVKTKEEEHQRLINELSAQKARLHTESGEFSRQLDEKDAMVSQLSRGGQAFTQQIEGLKRQLEEETKAKSALAHALQSSRRDCDLLREQYEEEQEAKAELQRAMSKANSEVSQWRTKCETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEAEDLMIDVERSNATCARMDKKQRNFDKVLAEWKHKYEETQAELEASQKESRSLSTEVFKVKNAYEESLDHLETLKRENKNLQQEISDLTEQIAESAKHIHELEKVKKQIDQEKSELQAALEEAEGSLEHEEGKILRIQLELNQVKSEIDRKIAEKDEEIDQLKRNHLRVVESMQSTLDAEIRSRNDALRIKKKMEGDLNEMEIQLNHANRQAAEAIKNLRNTQGILKDTQLHLDDAVRGQDDHKEQLAMVERRANLMQAEIEELRASLEQTERSRRVADQDLLDASERVQLLHTQNTSLINTKKKLETDISQIQGEMEDIVQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTVKDLQQRLDEAEQLALKGGKKQIQKLEARVKELENEVESEQKRNVEAVKGLRKHERRVKELTYQTEEDRKNVLRLQDLVDKLQSKVKAYKRQAEEAEEQSNINLSKFRKLQHELEEAEERADIAESQVNKLRVKSRDVHSKVISEE
| null | null |
actin filament-based movement [GO:0030048]; muscle contraction [GO:0006936]
|
myofibril [GO:0030016]; myosin complex [GO:0016459]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]
|
actin filament binding [GO:0051015]; ATP binding [GO:0005524]; microfilament motor activity [GO:0000146]
|
PF01576;
|
1.20.5.340;1.20.5.370;6.10.250.2420;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
| null | null | null | null | null |
FUNCTION: Muscle contraction.
|
Oryctolagus cuniculus (Rabbit)
|
P02563
|
MYH6_RAT
|
MTDAQMADFGAARYLRKSEKERLEAQTRPFDIRTECFVPDDKEEYVKAKIVSREGGKVTAETENGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRSKKDNPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSVASIDDSEELLATDSAFDVLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQREEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQSVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNVKGKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQKSSLKLMATLFSTYASADTGDSGKGKGGKKKGSSFQTVSALHRENLNKLMTNLRTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSGKGAEKLLGSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRIQAQARGQLMRIEFKKMVERRDALLVIQWNIRAFMGVKNWPWMKLYFKIKPLLKSAETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKSKVKLEQQVDDLEGSLEQEKKVRMDLERAKRKLEGDLKLTQESIMDLENDKLQLEEKLKKKEFDISQQNSKIEDEQALALQLQKKLKENQARIEELEEELEAERTARAKVEKLRSDLTRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSHMEQIIKAKANLEKVSRTLEDQANEYRVKLEEAQRSLNDFTTQRAKLQTENGELARQLEEKEALIWQLTRGKLSYTQQMEDLKRQLEEEGKAKNALAHALQSARHDCDLLREQYEEEMEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILAEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGEGGKNVHELEKIRKQLEVEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSQANRIASEAQKHLKNAQAHLKDTQLQLDDAVRANDDLKENIAIVERRNTLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDKKNLVRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKQKMHDEE
| null | null |
actin filament-based movement [GO:0030048]; adult heart development [GO:0007512]; ATP metabolic process [GO:0046034]; atrial cardiac muscle tissue morphogenesis [GO:0055009]; cardiac muscle cell development [GO:0055013]; cardiac muscle contraction [GO:0060048]; cardiac muscle hypertrophy in response to stress [GO:0014898]; cellular response to 3,3',5-triiodo-L-thyronine [GO:1905243]; in utero embryonic development [GO:0001701]; muscle contraction [GO:0006936]; muscle filament sliding [GO:0030049]; myofibril assembly [GO:0030239]; regulation of blood pressure [GO:0008217]; regulation of heart contraction [GO:0008016]; regulation of heart growth [GO:0060420]; regulation of heart rate [GO:0002027]; regulation of the force of heart contraction [GO:0002026]; sarcomere organization [GO:0045214]; striated muscle contraction [GO:0006941]; ventricular cardiac muscle tissue morphogenesis [GO:0055010]; visceral muscle development [GO:0007522]
|
cytoplasm [GO:0005737]; muscle myosin complex [GO:0005859]; myofibril [GO:0030016]; myosin complex [GO:0016459]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]; stress fiber [GO:0001725]; Z disc [GO:0030018]
|
actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calcium-dependent ATPase activity [GO:0030899]; calmodulin binding [GO:0005516]; identical protein binding [GO:0042802]; microfilament motor activity [GO:0000146]; protein kinase binding [GO:0019901]; protein-containing complex binding [GO:0044877]
|
PF00063;PF02736;PF01576;
|
1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;6.10.250.2420;3.40.850.10;2.30.30.360;1.20.120.720;1.20.5.1160;
|
TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
| null | null | null | null | null |
FUNCTION: Muscle contraction.
|
Rattus norvegicus (Rat)
|
P02564
|
MYH7_RAT
|
MADREMAAFGAGAPFLRKSEKERLEAQTRPFDLKKDVFVPDDKEEFVKAKIVSREGGKVTAETENGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAQVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFFSQGETTVASIDDSEEHMATDSAFDVLGFTPEEKNSIYKLTGAIMHFGNMKFKQKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQNVQQVAYAIGALAKSVYEKMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLYDNHLGKSNNFQKPRNIKGKQEAHFSLIHYAGTVDYNILGWLQKNKDPLNETVVGLYQKSSLKLLSNLFANYAGADAPVDKGKGKAKKGSSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEGQFIDSRKGAEKLLGSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRIQAQSRGVLSRMEFKKLLERRDSLLIIQWNIRAFMGVKNWPWMKLYFKIKPLLKSAETEKEMANMKEEFGRVKDALEKSEARRKELEEKMVSLLQEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMTERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDEIIVKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLDQDKKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEELEAERTARAKVEKLRSDLSRELEEISERLEEAGGATSVQIEMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSVAELGEQIDNLQRVKQKLEKEKSEFKLELDDVTSNMEQIIKAKANLEKMCRTLEDQMNEHRSKAEETQRSVNDLTRQRAKLQTENGELSRQLDEKEALISQLTRGKLTYTQQLEDLKRQLEEEVKAKNALAHALQSARHDCDLLREQYEEETEAKAELQRVLSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEAVEAVNAKCSSLEKTKHRLQNEIEDLMVDVERSNAAAAALDKKQRNFDKILVEWKQKYEESQSELESSQKEARSLSTELFKLKNAYEESLEHLETFKRENKNLQEEISDLTEQLGSTGKSIHELEKIRKQLEAEKLELQSALEEAEASLEHEEGKILRAQLEFNQIKAEIERKLAEKDEEMEQAKRNHLRVVDSLQTSLDAETRSRNEALRVKKKMEGDLNEMEIQLSHANRMAAEAQKQVKSLQSLLKDTQIQLDDAVRANDDLKENIAIVERRNNLLQAELEELRAVVEQTERSRKLAEQELIETSERVQLLHSQNTSLINQKKKMDADLSQLQTEVEEAVQECRNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKNNMEQTIKDLQHRLDEAEQIALKGGKKQLQKLEARVRELENELEAEQKRNAESVKGMRKSERRIKELTYQTEEDRKNLLRLQDLVDKLQLKVKAYKRQAEEAEEQANTNLSKFRKVQHELDEAEERADIAESQVNKLRAKSRDIGAKGLNEE
| null | null |
adult heart development [GO:0007512]; ATP metabolic process [GO:0046034]; cardiac muscle contraction [GO:0060048]; cardiac muscle hypertrophy in response to stress [GO:0014898]; cellular response to 3,3',5-triiodo-L-thyronine [GO:1905243]; cellular response to angiotensin [GO:1904385]; cellular response to hydrogen peroxide [GO:0070301]; muscle contraction [GO:0006936]; muscle filament sliding [GO:0030049]; regulation of heart rate [GO:0002027]; regulation of slow-twitch skeletal muscle fiber contraction [GO:0031449]; regulation of the force of heart contraction [GO:0002026]; regulation of the force of skeletal muscle contraction [GO:0014728]; sarcomere organization [GO:0045214]; skeletal muscle contraction [GO:0003009]; striated muscle contraction [GO:0006941]; transition between fast and slow fiber [GO:0014883]; ventricular cardiac muscle tissue morphogenesis [GO:0055010]
|
cytoplasm [GO:0005737]; muscle myosin complex [GO:0005859]; myofibril [GO:0030016]; myosin complex [GO:0016459]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]; sarcomere [GO:0030017]; stress fiber [GO:0001725]; Z disc [GO:0030018]
|
actin filament binding [GO:0051015]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calmodulin binding [GO:0005516]; identical protein binding [GO:0042802]; microfilament motor activity [GO:0000146]; protein-containing complex binding [GO:0044877]
|
PF00063;PF02736;PF01576;
|
1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;6.10.250.2420;3.40.850.10;2.30.30.360;1.20.120.720;
|
TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, myofibril {ECO:0000269|PubMed:26150528}. Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:26150528}. Note=Thick filaments of the myofibrils. {ECO:0000269|PubMed:26150528}.
| null | null | null | null | null |
FUNCTION: Myosins are actin-based motor molecules with ATPase activity essential for muscle contraction. Forms regular bipolar thick filaments that, together with actin thin filaments, constitute the fundamental contractile unit of skeletal and cardiac muscle. {ECO:0000305|PubMed:26150528}.
|
Rattus norvegicus (Rat)
|
P02565
|
MYH1B_CHICK
|
MATDADMAIFGEAAPYLRKSEKERIEAQNKPFDAKSSVFVVHAKESYVKSTIQSKESGKVTVKTEGGETLTVKEDQIFSMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVLAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAASGDKKKEEQPAGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDYQYVSQGEITVPSINDQEELMATDSAIDILGFTPDEKTAIYKLTGAVMHYGNLKFKQKQREEQAEPGGTEVADKAAYLMGLNSADLLKALCYPRVKVGNEYVTKGQTVQQVYNSVGALAKSVFEKMFLWMVVRINQQLDTKQPRQYFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNHHMFVLEQEEYKKEGIEWEFIDFGMDLAACIELIEKPMGIFSILEEECMFPKATDTSFKNKLYDQHLGKSNNFQKPKPGKGKAEAHFSLVHYAGTVDYNITGWLEKNKDPLNETVVGLYQKSSLKTLALLFASVGGAEAESGAGGKKGGKKKGSSFQTVSALFRENLNKLMSNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPIRILYADFKQRYKVLNASAIPEGQFIDSKKASEKLLGSIDVDHTQYKFGHTKVFFKAGLLGLLEEMRDEKLAQLITRTQARCRGFLMRVEFKKMMERRESIFCIQYNVRAFMNVKHWPWMKLFFKIKPLLKSAESEKEMANMKEEFEKTKEELAKSEAKRKELEEKMVSLLQEKNDLQLQVQAEADGLADAEERCDQLIKTKIQLEAKIKELTERAEDEEEMNAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAALDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKLRMDLERAKRKLEGDLKMTQESTMDLENDKQQLDEKLKKKDFEISQIQSKIEDEQALGMQLQKKIKELQARIEELEEEIEAERTSRAKAEKHRADLSRELEEISERLEEAGGATAAQIDMNKKREAEFQKMRRDLEEATLQHEATAAALRKKHADSTADVGEQIDNLQRVKQKLEKEKSELKMEIDDLASNMESVSKAKANLEKMCRSLEDQLSEIKTKEEEQQRTINDISAQKARLQTESGEYSRQVEEKDALISQLSRGKQAFTQQIEELKRHLEEEIKAKKCPAHALQSARHDCDLLREQYEEEQEAKGELQRALSKANSEVAQWRTKYETDAIQRTEELEEAKKKLAQRLQDAEEHVEAVNSKCASLEKTKQRLQNEVEDLMIDVERSNAACAALDKKQKNFDKILSEWKQKYEETQAELEASQKESRSLSTELFKMKNAYEESLDHLETLKRENKNLQQEISDLTEQIAEGGKAIHELEKVKKQIEQEKSELQTALEEAEASLEHEEGKILRVQLELNQVKSDIDRKIAEKDEEIDQLKRNHLRVVDSMQSTLDAEIRSRNEALRLKKKMEGDLNEIEIQLSHANRQAAEAQKNLRNTQGVLKDTQIHLDDALRSQEDLKEQVAMVERRANLLQAEIEELRAALEQTERSRKVAEQELLDASERVQLLHTQNTSLINTKKKLESDISQIQSEMEDTIQEARNAEEKAKKAITDAAMMAEELKKEQDTSAHLERMKKNLDQTVKDLQHRLDEAEQLALKGGKKQIQKLEARVRELEGEVDAEQKRSAEAVKGVRKYERRVKELTYQSEEDRKNVLRLQDLVDKLQMKVKSYKRQAEEAEELSNVNLSKFRKIQHELEEAEERADIAESQVNKLRAKSREIGKKAESEE
| null | null |
muscle contraction [GO:0006936]
|
cytoplasm [GO:0005737]; myofibril [GO:0030016]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]
|
actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]
|
PF00063;PF02736;PF01576;
|
1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;6.10.250.2420;3.40.850.10;2.30.30.360;1.20.120.720;
|
TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
| null | null | null | null | null |
FUNCTION: Muscle contraction.
|
Gallus gallus (Chicken)
|
P02566
|
MYO4_CAEEL
|
MEHEKDPGWQYLRRTREQVLEDQSKPYDSKKNVWIPDPEEGYLAGEITATKGDQVTIVTARGNEVTLKKELVQEMNPPKFEKTEDMSNLSFLNDASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITGESGAGKTENTKKVICYFAAVGASQQEGGAEVDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAELIIDGIDDVEEFQLTDEAFDILNFSAVEKQDCYRLMSAHMHMGNMKFKQRPREEQAEPDGTDEAEKASNMYGIGCEEFLKALTKPRVKVGTEWVSKGQNCEQVNWAVGAMAKGLYSRVFNWLVKKCNLTLDQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWVFIDFGLDLQACIELIEKPLGIISMLDEECIVPKATDLTLASKLVDQHLGKHPNFEKPKPPKGKQGEAHFAMRHYAGTVRYNCLNWLEKNKDPLNDTVVSAMKQSKGNDLLVEIWQDYTTQEEAAAKAKEGGGGGKKKGKSGSFMTVSMLYRESLNNLMTMLNKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTLHPDFVQRYAILAAKEAKSDDDKKKCAEAIMSKLVNDGSLSEEMFRIGLTKVFFKAGVLAHLEDIRDEKLATILTGFQSQIRWHLGLKDRKRRMEQRAGLLIVQRNVRSWCTLRTWEWFKLYGKVKPMLKAGKEAEELEKINDKVKALEDSLAKEEKLRKELEESSAKLVEEKTSLFTNLESTKTQLSDAEERLAKLEAQQKDASKQLSELNDQLADNEDRTADVQRAKKKIEAEVEALKKQIQDLEMSLRKAESEKQSKDHQIRSLQDEMQQQDEAIAKLNKEKKHQEEINRKLMEDLQSEEDKGNHQNKVKAKLEQTLDDLEDSLEREKRARADLDKQKRKVEGELKIAQENIDESGRQRHDLENNLKKKESELHSVSSRLEDEQALVSKLQRQIKDGQSRISELEEELENERQSRSKADRAKSDLQRELEELGEKLDEQGGATAAQVEVNKKREAELAKLRRDLEEANMNHENQLGGLRKKHTDAVAELTDQLDQLNKAKAKVEKDKAQAVRDAEDLAAQLDQETSGKLNNEKLAKQFELQLTELQSKADEQSRQLQDFTSLKGRLHSENGDLVRQLEDAESQVNQLTRLKSQLTSQLEEARRTADEEARERQTVAAQAKNYQHEAEQLQESLEEEIEGKNEILRQLSKANADIQQWKARFEGEGLLKADELEDAKRRQAQKINELQEALDAANSKNASLEKTKSRLVGDLDDAQVDVERANGVASALEKKQKGFDKIIDEWRKKTDDLAAELDGAQRDLRNTSTDLFKAKNAQEELAEVVEGLRRENKSLSQEIKDLTDQLGEGGRSVHEMQKIIRRLEIEKEELQHALDEAEAALEAEESKVLRAQVEVSQIRSEIEKRIQEKEEEFENTRKNHARALESMQASLETEAKGKAELLRIKKKLEGDINELEIALDHANKANADAQKNLKRYQEQVRELQLQVEEEQRNGADTREQFFNAEKRATLLQSEKEELLVANEAAERARKQAEYEAADARDQANEANAQVSSLTSAKRKLEGEIQAIHADLDETLNEYKAAEERSKKAIADATRLAEELRQEQEHSQHVDRLRKGLEQQLKEIQVRLDEAEAAALKGGKKVIAKLEQRVRELESELDGEQRRFQDANKNLGRADRRVRELQFQVDEDKKNFERLQDLIDKLQQKLKTQKKQVEEAEELANLNLQKYKQLTHQLEDAEERADQAENSLSKMRSKSRASASVAPGLQSSASAAVIRSPSRARASDF
| null | null |
egg-laying behavior [GO:0018991]; locomotion [GO:0040011]; muscle contraction [GO:0006936]; sarcomere organization [GO:0045214]; skeletal muscle myosin thick filament assembly [GO:0030241]
|
A band [GO:0031672]; cytoplasm [GO:0005737]; muscle myosin complex [GO:0005859]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]; striated muscle myosin thick filament [GO:0005863]
|
actin filament binding [GO:0051015]; ATP binding [GO:0005524]; microfilament motor activity [GO:0000146]; structural constituent of muscle [GO:0008307]
|
PF00063;PF02736;PF01576;
|
1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;3.40.850.10;2.30.30.360;1.20.120.720;
|
TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
|
PTM: Unfolded unc-54 is poly-ubiquitinated by ufd-2. {ECO:0000269|PubMed:29396393}.
|
SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
| null | null | null | null | null |
FUNCTION: Required for muscle contraction. {ECO:0000269|PubMed:27123983}.
|
Caenorhabditis elegans
|
P02567
|
MYO1_CAEEL
|
MSLEHEKDPGWQYLKRSREQQLADQSRPYDSKKNVWIPDAEEGYIEGVIKGPGPKADTVIVTAGGKDVTLKKDIVQEVNPPKFEKTEDMSNLTFLNDASVLWNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDQAYRYMLQDHENQSMLITGESGAGKTENTKKVICYFATVGASQKAALKEGEKEVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHGTLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFKPQLRDELLLNHPISNYWFVAQAELLIDGIDDTEEFQLTDEAFDVLKFSPTEKMDCYRLMSAHMHMGNMKFKQRPREEQAEPDGQDEAERACNMYGIDVDQFLKALVSPRVKVGTEWVSKGQNVDQVHWAIGAMAKGLYARVFHWLVKKCNLTLDQKGIDRDYFIGVLDIAGFEIFDFNSFEQLWINFVNEKLQQFFNHHMFVLEQEEYAREGIQWTFIDFGLDLQACIELIEKPLGIISMLDEECIVPKATDMTLAQKLTDQHLGKHPNFEKPKPPKGKQGEAHFAMRHYAGTVRYNVLNWLEKNKDPLNDTVVSVMKASKKNDLLVEIWQDYTTQEEAAAAAKAGGGRKGGKSGSFMTVSMMYRESLNKLMTMLHKTHPHFIRCIIPNEKKQSGMIDAALVLNQLTCNGVLEGIRICRKGFPNRTQHPDFVQRYAILAAKEAKSSDDMKTCAGAILQALINQKQLNDEQFRIGHTKVFFKAGVVAHIEDLRDDKLNQIITGFQSAIRWYTATADAGARRKQLNSYIILQRNIRSWCVLRTWDWFLLFGKLRPQLKCGKMAEEMIKMAEEQKVLEAEAKKAESARKSQEEAYAKLSAERSKLLEALELTQGGSAAIEEKLTRLNSARQEVEKSLNDANDRLSEHEEKNADLEKQRRKAQQEVENLKKSIEAVDGNLAKSLEEKAAKENQIHSLQDEMNSQDETIGKINKEKKLLEENNRQLVDDLQAEEAKQAQANRLRGKLEQTLDEMEEAVEREKRIRAETEKSKRKVEGELKGAQETIDELSAIKLETDASLKKKEADIHALGVRIEDEQALANRLTRQSKENAQRIIEIEDELEHERQSRSKADRARAELQRELDELNERLDEQNKQLEIQQDNNKKKDSEIIKFRRDLDEKNMANEDQMAMIRRKNNDQISALTNTLDALQKSKAKIEKEKGVLQKELDDINAQVDQETKSRVEQERLAKQYEIQVAELQQKVDEQSRQIGEYTSTKGRLSNDNSDLARQVEELEIHLATINRAKTAFSSQLVEAKKAAEDELHERQEFHAACKNLEHELDQCHELLEEQINGKDDIQRQLSRINSEISQWKARYEGEGLVGSEELEELKRKQMNRVMDLQEALSAAQNKVISLEKAKGKLLAETEDARSDVDRHLTVIASLEKKQRAFDKIVDDWKRKVDDIQKEIDATTRDSRNTSTEVFKLRSSMDNLSEQIETLRRENKIFSQEIRDINEQITQGGRTYQEVHKSVRRLEQEKDELQHALDEAEAALEAEESKVLRLQIEVQQIRSEIEKRIQEKEEEFENTRKNHQRALESIQASLETEAKSKAELARAKKKLETDINQLEIALDHANKANVDAQKNLKKLFDQVKELQGQVDDEQRRREEIRENYLAAEKRLAIALSESEDLAHRIEASDKHKKQLEIEQAELKSSNTELIGNNAALSAMKRKVENEVQIARNELDEYLNELKASEERARKAAADADRLAEEVRQEQEHAVHVDRQRKSLELNAKELQAKIDDAERAMIQFGAKALAKVEDRVRSLEAELHSEQRRHQESIKGYTKQERRARELQFQVEEDKKAFDRLQENVEKLQQKIRVQKRQIEEAEEVATQNLSKFRQIQLALENAEERAEVAENSLVRMRGQVVRSATNK
| null | null |
muscle contraction [GO:0006936]; nematode pharyngeal pumping [GO:0043050]; sarcomere organization [GO:0045214]
|
cytoplasm [GO:0005737]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]; striated muscle myosin thick filament [GO:0005863]
|
actin filament binding [GO:0051015]; ATP binding [GO:0005524]; microfilament motor activity [GO:0000146]; structural constituent of muscle [GO:0008307]
|
PF00063;PF02736;PF01576;
|
1.10.10.820;1.20.5.340;1.20.5.370;1.20.58.530;6.20.240.20;3.40.850.10;2.30.30.360;1.20.120.720;4.10.270.10;1.20.5.1160;
|
TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
| null |
SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
| null | null | null | null | null |
FUNCTION: Muscle contraction.
|
Caenorhabditis elegans
|
P02572
|
ACT2_DROME
|
MCDEEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPESLFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIVAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
|
3.6.4.-
| null |
anatomical structure morphogenesis [GO:0009653]; mitotic cytokinesis [GO:0000281]; regulation of transcription by RNA polymerase II [GO:0006357]
|
brahma complex [GO:0035060]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; RSC-type complex [GO:0016586]; SWI/SNF complex [GO:0016514]
|
ATP binding [GO:0005524]; hydrolase activity [GO:0016787]
|
PF00022;
|
3.30.420.40;
|
Actin family
|
PTM: N-terminal cleavage of acetylated cysteine of immature actin by ACTMAP. {ECO:0000250|UniProtKB:P68134}.; PTM: Oxidation of Met-45 by Mical to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not known whether the (S)-S-oxide or the (R)-S-oxide is produced. {ECO:0000269|PubMed:22116028}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P68137};
| null | null | null | null |
FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.; FUNCTION: Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction.
|
Drosophila melanogaster (Fruit fly)
|
P02574
|
ACT4_DROME
|
MCDEEASALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDCYVGDEAQSKRGILSLKYPIEHGIITNWDDMEKVWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNSPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAAASTSLEKSYELPDGQVITIGNERFRTPEALFQPSFLGMESCGIHETVYQSIMKCDVDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTIKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPGIVHRKCF
|
3.6.4.-
| null |
mitotic cytokinesis [GO:0000281]
|
cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]
|
ATP binding [GO:0005524]; hydrolase activity [GO:0016787]
|
PF00022;
|
3.30.420.40;
|
Actin family
|
PTM: N-terminal cleavage of acetylated cysteine of immature actin by ACTMAP. {ECO:0000250|UniProtKB:P68134}.; PTM: Oxidation of Met-45 by Mical to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not known whether the (S)-S-oxide or the (R)-S-oxide is produced. {ECO:0000269|PubMed:22116028}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P68137};
| null | null | null | null |
FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.; FUNCTION: Multiple isoforms are involved in various cellular functions such as cytoskeleton structure, cell mobility, chromosome movement and muscle contraction.
|
Drosophila melanogaster (Fruit fly)
|
P02576
|
ACTA_PHYPO
|
MEGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEQEMQTAASSSALEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMQKELTALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPSIVHRKCF
|
3.6.4.-
| null |
phagocytosis [GO:0006909]; response to chemical [GO:0042221]
|
actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]
|
ATP binding [GO:0005524]; hydrolase activity [GO:0016787]
|
PF00022;
|
3.30.420.40;
|
Actin family
|
PTM: Phosphorylated by actin-fragmin kinase (AFK). {ECO:0000269|PubMed:1315751, ECO:0000269|PubMed:1324166, ECO:0000269|PubMed:8896448}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P68137};
| null | null | null | null |
FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
|
Physarum polycephalum (Slime mold)
|
P02585
|
TNNC2_HUMAN
|
MTDQQAEARSYLSEEMIAEFKAAFDMFDADGGGDISVKELGTVMRMLGQTPTKEELDAIIEEVDEDGSGTIDFEEFLVMMVRQMKEDAKGKSEEELAECFRIFDRNADGYIDPEELAEIFRASGEHVTDEEIESLMKDGDKNNDGRIDFDEFLKMMEGVQ
| null | null |
regulation of muscle contraction [GO:0006937]; skeletal muscle contraction [GO:0003009]
|
cytosol [GO:0005829]; myosin II complex [GO:0016460]; troponin complex [GO:0005861]
|
calcium ion binding [GO:0005509]
|
PF13499;
|
1.10.238.10;
|
Troponin C family
| null | null | null | null | null | null | null |
FUNCTION: Troponin is the central regulatory protein of striated muscle contraction. Tn consists of three components: Tn-I which is the inhibitor of actomyosin ATPase, Tn-T which contains the binding site for tropomyosin and Tn-C. The binding of calcium to Tn-C abolishes the inhibitory action of Tn on actin filaments. {ECO:0000269|PubMed:33755597}.
|
Homo sapiens (Human)
|
P02592
|
AEQ2_AEQVI
|
MTSKQYSVKLTSDFDNPRWIGRHKHMFNFLDVNHNGKISLDEMVYKASDIVINNLGATPEQAKRHKDAVEAFFGGAGMKYGVETDWPAYIEGWKKLATDELEKYAKNEPTLIRIWGDALFDIVDKDQNGAITLDEWKAYTKAAGIIQSSEDCEETFRVCDIDESGQLDVDEMTRQHLGFWYTMDPACEKLYGGAVP
| null | null |
bioluminescence [GO:0008218]
| null |
calcium ion binding [GO:0005509]
|
PF13202;PF13499;
|
1.10.238.10;
|
Aequorin family
|
PTM: The reduction of the disulfide bond is necessary to regenerate aequorin from apoaequorin.
| null | null | null | null | null | null |
FUNCTION: Ca(2+)-dependent bioluminescence photoprotein. Displays an emission peak at 470 nm (blue light). Trace amounts of calcium ion trigger the intramolecular oxidation of the chromophore, coelenterazine into coelenteramide and CO(2) with the concomitant emission of light.
|
Aequorea victoria (Water jellyfish) (Mesonema victoria)
|
P02599
|
CALM_DICDI
|
MASQESLTEEQIAEFKEAFSLFDKDGDGSITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGNIDFPEFLTMMARKMQDTDTEEEIREAFKVFDKDGNGYISAAELRHVMTSLGEKLTNEEVDEMIREADLDGDGQVNYDEFVKMMIVRN
| null | null |
establishment of protein localization to vacuole [GO:0072666]; mitotic cytokinesis [GO:0000281]; negative regulation of asexual reproduction [GO:1903665]; negative regulation of proteolysis [GO:0045861]; plasma membrane repair [GO:0001778]; positive regulation of positive chemotaxis to cAMP [GO:0061122]; positive regulation of sequestering of calcium ion [GO:0051284]; protein export from nucleus [GO:0006611]; regulation of sorocarp stalk cell differentiation [GO:0031285]
|
contractile vacuole [GO:0000331]; cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; nucleus [GO:0005634]
|
calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; cell adhesion molecule binding [GO:0050839]; cyclic nucleotide phosphodiesterase activator activity [GO:0170005]; cyclic-nucleotide phosphodiesterase activity [GO:0004112]; enzyme regulator activity [GO:0030234]; kinase binding [GO:0019900]; myosin I binding [GO:0017024]; protein kinase binding [GO:0019901]; protein kinase regulator activity [GO:0019887]; troponin I binding [GO:0031013]
|
PF13499;
|
1.10.238.10;
|
Calmodulin family
|
PTM: The N-terminus is blocked.; PTM: Trimethylation of Lys-118 observed in other calmodulins is absent here.
|
SUBCELLULAR LOCATION: Contractile vacuole {ECO:0000269|PubMed:1629238}.
| null | null | null | null | null |
FUNCTION: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. {ECO:0000269|PubMed:1493336, ECO:0000269|PubMed:6087882, ECO:0000269|PubMed:6243626}.
|
Dictyostelium discoideum (Social amoeba)
|
P02607
|
MYL6_CHICK
|
MCDFSEEQTAEFKEAFQLFDRTGDGKILYSQCGDVMRALGQNPTNAEVMKVLGNPKSDEMNLKTLKFEQFLPMMQTIAKNKDQGCFEDYVEGLRVFDKEGNGTVMGAEIRHVLVTLGEKMTEEEVEQLVAGHEDSNGCINYEELVRMVLSG
| null | null |
actomyosin structure organization [GO:0031032]; myofibril assembly [GO:0030239]
|
actomyosin [GO:0042641]; cytosol [GO:0005829]; muscle myosin complex [GO:0005859]; myosin II complex [GO:0016460]; myosin II filament [GO:0097513]
|
ADP binding [GO:0043531]; calcium ion binding [GO:0005509]; magnesium ion binding [GO:0000287]; microfilament motor activity [GO:0000146]; myosin heavy chain binding [GO:0032036]; myosin II binding [GO:0045159]; structural constituent of muscle [GO:0008307]
| null |
1.10.238.10;
| null | null | null | null | null | null | null | null |
FUNCTION: Regulatory light chain of myosin. Does not bind calcium.
|
Gallus gallus (Chicken)
|
P02609
|
MYL11_CHICK
|
MAPKKAKRRAAEGSSNVFSMFDQTQIQEFKEAFTVIDQNRDGIIDKDDLRETFAAMGRLNVKNEELDAMIKEASGPINFTVFLTMFGEKLKGADPEDVIMGAFKVLDPDGKGSIKKSFLEELLTTQCDRFTPEEIKNMWAAFPPDVAGNVDYKNICYVITHGEDKEGE
| null | null |
muscle contraction [GO:0006936]; skeletal muscle tissue development [GO:0007519]
|
cytoplasm [GO:0005737]; myosin complex [GO:0016459]
|
calcium ion binding [GO:0005509]
|
PF13405;
|
1.10.238.10;
| null |
PTM: The N-terminus is blocked. N,N,N-trimethylalanine, found in other myosin light chains would not have been detected in the N-terminal tryptic peptide in PubMed:7358336 because it would remain trimethylated and ninhydrin negative after hydrolysis.
| null | null | null | null | null | null |
FUNCTION: Myosin regulatory subunit that plays an essential to maintain muscle integrity during early development (By similarity). Plays a role in muscle contraction (PubMed:15256600). {ECO:0000250|UniProtKB:O93409, ECO:0000269|PubMed:15256600}.
|
Gallus gallus (Chicken)
|
P02612
|
MLRM_CHICK
|
MSSKRAKAKTTKKRPQRATSNVFAMFDQSQIQEFKEAFNMIDQNRDGFIDKEDLHDMLASMGKNPTDEYLEGMMSEAPGPINFTMFLTMFGEKLNGTDPEDVIRNAFACFDEEASGFIHEDHLRELLTTMGDRFTDEEVDEMYREAPIDKKGNFNYVEFTRILKHGAKDKDD
| null | null |
myofibril assembly [GO:0030239]; platelet aggregation [GO:0070527]
|
cytoplasm [GO:0005737]; muscle myosin complex [GO:0005859]; myofibril [GO:0030016]; stress fiber [GO:0001725]
|
calcium ion binding [GO:0005509]; myosin II binding [GO:0045159]; structural constituent of muscle [GO:0008307]
|
PF13499;
|
1.10.238.10;
| null | null | null | null | null | null | null | null |
FUNCTION: Myosin regulatory subunit that plays an important role in regulation of both smooth muscle and nonmuscle cell contractile activity. Implicated in cytokinesis, receptor capping, and cell locomotion (By similarity). {ECO:0000250}.
|
Gallus gallus (Chicken)
|
P02625
|
PRVA_RAT
|
MSMTDLLSAEDIKKAIGAFTAADSFDHKKFFQMVGLKKKSADDVKKVFHILDKDKSGFIEEDELGSILKGFSSDARDLSAKETKTLMAAGDKDGDGKIGVEEFSTLVAES
| null | null |
cochlea development [GO:0090102]; excitatory chemical synaptic transmission [GO:0098976]; gene expression [GO:0010467]; inhibitory chemical synaptic transmission [GO:0098977]
|
axon [GO:0030424]; cuticular plate [GO:0032437]; cytoplasm [GO:0005737]; neuronal cell body [GO:0043025]; protein-containing complex [GO:0032991]; stereocilium [GO:0032420]; terminal bouton [GO:0043195]
|
calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; protein-containing complex binding [GO:0044877]
|
PF13499;
|
1.10.238.10;
|
Parvalbumin family
| null | null | null | null | null | null | null |
FUNCTION: In muscle, parvalbumin is thought to be involved in relaxation after contraction. It binds two calcium ions.
|
Rattus norvegicus (Rat)
|
P02631
|
ONCO_RAT
|
MSITDILSAEDIAAALQECQDPDTFEPQKFFQTSGLSKMSASQVKDIFRFIDNDQSGYLDGDELKYFLQKFQSDARELTESETKSLMDAADNDGDGKIGADEFQEMVHS
| null | null |
cochlea development [GO:0090102]; response to wounding [GO:0009611]
|
cuticular plate [GO:0032437]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; protein-containing complex [GO:0032991]; stereocilium [GO:0032420]; supramolecular fiber [GO:0099512]; vesicle [GO:0031982]
|
calcium ion binding [GO:0005509]; identical protein binding [GO:0042802]; ion binding [GO:0043167]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]
|
PF13499;
|
1.10.238.10;
|
Parvalbumin family
| null | null | null | null | null | null | null |
FUNCTION: Has some calmodulin-like activity with respect to enzyme activation and growth regulation. Binds two calcium ions.
|
Rattus norvegicus (Rat)
|
P02638
|
S100B_BOVIN
|
MSELEKAVVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDSDGDGECDFQEFMAFVAMITTACHEFFEHE
| null | null |
adaptive thermogenesis [GO:1990845]; astrocyte activation [GO:0048143]; axonogenesis [GO:0007409]; cell adhesion [GO:0007155]; learning or memory [GO:0007611]; negative regulation of monocyte chemotactic protein-1 production [GO:0071638]; phosphorylation [GO:0016310]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of complement activation [GO:0045917]; regulation of translation [GO:0006417]; sympathetic neuron projection extension [GO:0097490]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; sarcoplasmic reticulum [GO:0016529]
|
calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; kinase inhibitor activity [GO:0019210]; protein homodimerization activity [GO:0042803]; RAGE receptor binding [GO:0050786]; S100 protein binding [GO:0044548]; tau protein binding [GO:0048156]; zinc ion binding [GO:0008270]
|
PF00036;PF01023;
|
1.10.238.10;
|
S-100 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04271}. Nucleus {ECO:0000250|UniProtKB:P04271}. Secreted {ECO:0000250|UniProtKB:P50114}. Note=Secretion into the medium is promoted by interaction with isoform CLSTN3beta of CLSTN3. {ECO:0000250|UniProtKB:P50114}.
| null | null | null | null | null |
FUNCTION: Small zinc- and- and calcium-binding protein that is highly expressed in astrocytes and constitutes one of the most abundant soluble proteins in brain (PubMed:3722149, PubMed:6615778). Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer (PubMed:3722149, PubMed:6615778). Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites (PubMed:3722149). Acts as a neurotrophic factor that promotes astrocytosis and axonal proliferation (By similarity). Involved in innervation of thermogenic adipose tissue by acting as an adipocyte-derived neurotrophic factor that promotes sympathetic innervation of adipose tissue (By similarity). Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase (PubMed:14661952). Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling (By similarity). Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization (By similarity). May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity (By similarity). {ECO:0000250|UniProtKB:P04271, ECO:0000250|UniProtKB:P04631, ECO:0000250|UniProtKB:P50114, ECO:0000269|PubMed:14661952, ECO:0000269|PubMed:3722149, ECO:0000269|PubMed:6615778}.
|
Bos taurus (Bovine)
|
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