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:00... | 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 acti... | 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:00002... | 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). Depen... | 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:00002... | 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... | 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:00002... | 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... | 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:00002... | 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... | 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 du... | 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 ... | 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 similar... | 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 ... | 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 similar... | 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 ... | 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 du... | 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 promotin... | 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 envir... | 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 ... | 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 ... | 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 rem... | 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 radia... | 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 r... | 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 r... | 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 c... | 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 r... | 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... | 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 r... | 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-damag... | 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 r... | 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-damag... | 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 r... | 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). Phosp... | 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 r... | 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: local... | 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 r... | 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 r... | 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 concentratio... | 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 | MTAMEESQSDISLELPLSQETFSGLWKLLPPEDILPSPHCMDDLLLPQDVEEFFEGPSEALRVSGAPAAQDPVTETPGPVAPAPATPWPLSSFVPSQKTYQGNYGFHLGFLQSGTAKSVMCTYSPPLNKLFCQLAKTCPVQLWVSATPPAGSRVRAMAIYKKSQHMTEVVRRCPHHERCSDGDGLAPPQHLIRVEGNLYPEYLEDRQTFRHSVVVPYEPPEAGSEYTTIHYKYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENFRKKEVLCPELPPGSAKRALPTCTSASPPQKKKPL... | 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 actinomy... | 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:000... | 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-spe... | 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 ... | 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, cen... | 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 t... | 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 tRN... | 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 t... | 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 t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P02452 | CO1A1_HUMAN | MFSFVDLRLLLLLAATALLTHGQEEGQVEGQDEDIPPITCVQNGLRYHDRDVWKPEPCRICVCDNGKVLCDDVICDETKNCPGAEVPEGECCPVCPDGSESPTDQETTGVEGPKGDTGPRGPRGPAGPPGRDGIPGQPGLPGPPGPPGPPGPPGLGGNFAPQLSYGYDEKSTGGISVPGPMGPSGPRGLPGPPGAPGPQGFQGPPGEPGEPGASGPMGPRGPPGPPGKNGDDGEAGKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDAGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGAPGPAG... | 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 ... | 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 ... | 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 | MFSFVDLRLLLLLAATALLTHGQEEGQEEGQEEDIPPVTCVQNGLRYHDRDVWKPVPCQICVCDNGNVLCDDVICDELKDCPNAKVPTDECCPVCPEGQESPTDQETTGVEGPKGDTGPRGPRGPAGPPGRDGIPGQPGLPGPPGPPGPPGPPGLGGNFAPQLSYGYDEKSTGISVPGPMGPSGPRGLPGPPGAPGPQGFQGPPGEPGEPGASGPMGPRGPPGPPGKNGDDGEAGKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDAGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGAPGPAGA... | 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 r... | 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 | MFSFVDLRLLLLLGATALLTHGQEDIPEVSCIHNGLRVPNGETWKPDVCLICICHNGTAVCDGVLCKEDLDCPNPQKREGECCPFCPEEYVSPDAEVIGVEGPKGDPGPQGPRGPVGPPGQDGIPGQPGLPGPPGPPGPPGPPGLGGNFASQMSYGYDEKSAGVSVPGPMGPSGPRGLPGPPGAPGPQGFQGPPGEPGEPGASGPMGPRGPPGPPGKNGDDGEAGKPGRPGERGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGDTGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGPPGSAGARGNDGAVGAA... | 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 ... | 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 ... | 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 | MFSFVDSRLLLLIAATVLLTRGEGEEDIQTGSCVQDGLTYNDKDVWKPEPCQICVCDSGNILCDEVICEDTSDCPNAEIPFGECCPICPDVDASPVYPESAGVEGPKGDTGPRGDRGLPGPPGRDGIPGQPGLPGPPGPPGPPGLGGNFAPQMSYGYDEKSAGVAVPGPMGPAGPRGLPGPPGAPGPQGFQGPPGEPGEPGASGPMGPRGPAGPPGKNGDDGEAGKPGRPGQRGPPGPQGARGLPGTAGLPGMKGHRGFSGLDGAKGQPGPAGPKGEPGSPGENGAPGQMGPRGLPGERGRPGPSGPAGARGNDGAPGAA... | 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: Contai... | 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 | MIRLGAPQTLVLLTLLVAAVLRCQGQDVQEAGSCVQDGQRYNDKDVWKPEPCRICVCDTGTVLCDDIICEDVKDCLSPEIPFGECCPICPTDLATASGQPGPKGQKGEPGDIKDIVGPKGPPGPQGPAGEQGPRGDRGDKGEKGAPGPRGRDGEPGTPGNPGPPGPPGPPGPPGLGGNFAAQMAGGFDEKAGGAQLGVMQGPMGPMGPRGPPGPAGAPGPQGFQGNPGEPGEPGVSGPMGPRGPPGPPGKPGDDGEAGKPGKAGERGPPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSP... | 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 [G... | 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 repeatin... | 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 | MIRLGAPQTLVLLTLLVAAVLRCHGQDVQKAGSCVQDGQRYNDKDVWKPEPCRICVCDTGTVLCDDIICEDMKDCLSPETPFGECCPICSADLPTASGQPGPKGQKGEPGDIKDIVGPKGPPGPQGPAGEQGPRGDRGDKGEKGAPGPRGRDGEPGTPGNPGPPGPPGPPGPPGLGGNFAAQMAGGFDEKAGGAQMGVMQGPMGPMGPRGPPGPAGAPGPQGFQGNPGEPGEPGVSGPMGPRGPPGPPGKPGDDGEAGKPGKSGERGPPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSP... | 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. {EC... | 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 | LQGLPGKDGETGAAGPLDPGPVGERGEQGAPGPSGFQGLPGPPGPPGESGKPGDQGVPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKGATGPAGPNGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKDGARGLTGPIGPPGPAGPNGEKGESGPPGPSGAAGARGAPGERGEPGAPGPAGFAGPPGADGQPGAKGEQGEPGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGPNGNPGPPGPPGSAGKDGPKGVRGDAGPPGRAGDPGLQG... | 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-... | 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 | MMSFVQKGSWLLLALLHPTIILAQQEAVEGGCSHLGQSYADRDVWKPEPCQICVCDSGSVLCDDIICDDQELDCPNPEIPFGECCAVCPQPPTAPTRPPNGQGPQGPKGDPGPPGIPGRNGDPGIPGQPGSPGSPGPPGICESCPTGPQNYSPQYDSYDVKSGVAVGGLAGYPGPAGPPGPPGPPGTSGHPGSPGSPGYQGPPGEPGQAGPSGPPGPPGAIGPSGPAGKDGESGRPGRPGERGLPGPPGIKGPAGIPGFPGMKGHRGFDGRNGEKGETGAPGLKGENGLPGENGAPGPMGPRGAPGERGRPGLPGAAGAR... | 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]; dig... | 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 G... | Homo sapiens (Human) |
P02462 | CO4A1_HUMAN | MGPRLSVWLLLLPAALLLHEEHSRAAAKGGCAGSGCGKCDCHGVKGQKGERGLPGLQGVIGFPGMQGPEGPQGPPGQKGDTGEPGLPGTKGTRGPPGASGYPGNPGLPGIPGQDGPPGPPGIPGCNGTKGERGPLGPPGLPGFAGNPGPPGLPGMKGDPGEILGHVPGMLLKGERGFPGIPGTPGPPGLPGLQGPVGPPGFTGPPGPPGPPGPPGEKGQMGLSFQGPKGDKGDQGVSGPPGVPGQAQVQEKGDFATKGEKGQKGEPGFQGMPGVGEKGEPGKPGPRGKPGKDGDKGEKGSPGFPGEPGYPGLIGRQGPQG... | 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]; epitheli... | 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 t... | 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 fo... | Homo sapiens (Human) |
P02463 | CO4A1_MOUSE | MGPRLSVWLLLLFAALLLHEERSRAAAKGDCGGSGCGKCDCHGVKGQKGERGLPGLQGVIGFPGMQGPEGPHGPPGQKGDAGEPGLPGTKGTRGPPGAAGYPGNPGLPGIPGQDGPPGPPGIPGCNGTKGERGPLGPPGLPGFSGNPGPPGLPGMKGDPGEILGHVPGTLLKGERGFPGIPGMPGSPGLPGLQGPVGPPGFTGPPGPPGPPGPPGEKGQMGSSFQGPKGDKGEQGVSGPPGVPGQAQVKEKGDFAPTGEKGQKGEPGFPGVPGYGEKGEPGKQGPRGKPGKDGEKGERGSPGIPGDSGYPGLPGRQGPQG... | 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]; ext... | 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.... | 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 for... | Mus musculus (Mouse) |
P02465 | CO1A2_BOVIN | MLSFVDTRTLLLLAVTSCLATCQSLQEATARKGPSGDRGPRGERGPPGPPGRDGDDGIPGPPGPPGPPGPPGLGGNFAAQFDAKGGGPGPMGLMGPRGPPGASGAPGPQGFQGPPGEPGEPGQTGPAGARGPPGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAPGVKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGELGPVGNPGPAGPAGPRGEVGLPGLSGPVGPPGNPGANGLPGAKGAAGLPGVAGAPG... | 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 | MLSFVDTRTLLLLAVTSCLATCQSLQMGSVRKGPTGDRGPRGQRGPAGPRGRDGVDGPVGPPGPPGAPGPPGPPGPPGLTGNFAAQYSDKGVSAGPGPMGLMGPRGPPGAVGAPGPQGFQGPAGEPGEPGQTGPAGSRGPAGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAQGVKGEPGAPGENGTPGQAGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGELGPVGNPGPAGPAGPRGEAGLPGLSGPVGPPGNPGANGLTGAKGATGL... | 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 [... | 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 | MLSFVDTRILLLLAVTSYLATSQHLFQASAGRKGPRGDKGPQGERGPPGPPGRDGEDGPPGPPGPPGPPGLGGNFAAQYDPSKAADFGPGPMGLMGPRGPPGASGPPGPPGFQGVPGEPGEPGQTGPQGPRGPPGPPGKAGEDGHPGKPGRPGERGVAGPQGARGFPGTPGLPGFKGIRGHNGLDGQKGQPGTPGTKGEPGAPGENGTPGQPGARGLPGERGRIGAPGPAGARGSDGSAGPTGPAGPIGAAGPPGFPGAPGAKGEIGPAGNVGPTGPAGPRGEIGLPGSSGPVGPPGNPGANGLPGAKGAAGLPGVAGAP... | 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 | MTGGGRAALALQPRGRLWPLLAVLAAVAGCVRAAMDECADEGGRPQRCMPEFVNAAFNVTVVATNTCGTPPEEYCVQTGVTGVTKSCHLCDAGQQHLQHGAAFLTDYNNQADTTWWQSQTMLAGVQYPNSINLTLHLGKAFDITYVRLKFHTSRPESFAIYKRTREDGPWIPYQYYSGSCENTYSKANRGFIRTGGDEQQALCTDEFSDISPLTGGNVAFSTLEGRPSAYNFDNSPVLQEWVTATDIRVTLNRLNTFGDEVFNEPKVLKSYYYAISDFAVGGRCKCNGHASECVKNEFDKLMCNCKHNTYGVDCEKCLPF... | 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:007... | 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 | MGLLQVFAFGVLALWGTRVCAQEPEFSYGCAEGSCYPATGDLLIGRAQKLSVTSTCGLHKPEPYCIVSHLQEDKKCFICDSRDPYHETLNPDSHLIENVVTTFAPNRLKIWWQSENGVENVTIQLDLEAEFHFTHLIMTFKTFRPAAMLIERSSDFGKAWGVYRYFAYDCESSFPGISTGPMKKVDDIICDSRYSDIEPSTEGEVIFRALDPAFKIEDPYSPRIQNLLKITNLRIKFVKLHTLGDNLLDSRMEIREKYYYAVYDMVVRGNCFCYGHASECAPVDGVNEEVEGMVHGHCMCRHNTKGLNCELCMDFYHDLP... | 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:0... | 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]; nucl... | 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 ... | 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,... | 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 duri... | 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... | 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, PubMe... | 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 sp... | 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:000... | 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 amylo... | 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:000565... | 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:... | 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 speck... | 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:000... | 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]; respo... | 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 | MTTCSRQFTSSSSMKGSCGIGGGIGGGSSRISSVLAGGSCRAPSTYGGGLSVSSSRFSSGGACGLGGGYGGGFSSSSSSFGSGFGGGYGGGLGAGLGGGFGGGFAGGDGLLVGSEKVTMQNLNDRLASYLDKVRALEEANADLEVKIRDWYQRQRPAEIKDYSPYFKTIEDLRNKILTATVDNANVLLQIDNARLAADDFRTKYETELNLRMSVEADINGLRRVLDELTLARADLEMQIESLKEELAYLKKNHEEEMNALRGQVGGDVNVEMDAAPGVDLSRILNEMRDQYEKMAEKNRKDAEEWFFTKTEELNREVATN... | 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 | MSVLYSSSSKQFSSSRSGGGGGGGSVRVSSTRGSLGGGYSSGGFSGGSFSRGSSGGGCFGGSSGGYGGFGGGGSFGGGYGGSSFGGGYGGSSFGGGYGGSSFGGAGFGGGGSFGGGSFGGGSYGGGFGGGGFGGDGGSLLSGNGRVTMQNLNDRLASYMDKVRALEESNYELEGKIKEWYEKHGNSSQREPRDYSKYYKTIEDLKGQILTLTTDNANVLLQIDNARLAADDFRLKYENEVTLRQSVEADINGLRRVLDELTLSKSDLEMQIESLNEELAYLKKNHEEEMRDLQNVSTGDVNVEMNAAPGVDLTQLLNNMR... | 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]; p... | 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: (Micr... | Mus musculus (Mouse) |
P02538 | K2C6A_HUMAN | MASTSTTIRSHSSSRRGFSANSARLPGVSRSGFSSVSVSRSRGSGGLGGACGGAGFGSRSLYGLGGSKRISIGGGSCAISGGYGSRAGGSYGFGGAGSGFGFGGGAGIGFGLGGGAGLAGGFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPTIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLETKWTLLQEQGTKTVRQNLEPLFEQYINNLRRQLDSIVGERGRLDSELRGMQDLVEDFKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDTSVVL... | 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]; morphogenesi... | 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 wo... | Homo sapiens (Human) |
P02540 | DESM_PIG | MSQAYSSSQRVSSYRRTFGGAPSFPLGSPLSSPVFPRAGFGTKGSSSSVTSRVYQVSRTSGGAGGLGPLRASRLGATRVPSSSYGAGELLDFSLADAVNQEFLTTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAEIYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQ... | 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... | 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:P3100... | 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 mito... | Sus scrofa (Pig) |
P02541 | DESM_MESAU | MSQAYSSSQRVSSYRRTFGGAPSFSLGSPLSSPVFPRAGFGTKGSSSSVTSRVYQVSRTSGGAGGLGSLRASRLGSTRAPSYGAGELLDFSLADAVNQEFLATRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAELYEEEMRELRRQVEVLTNQRARVDVERDNLIDDLQRLKAKLQEEIQLREEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEM... | 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... | 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:P3100... | 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 mito... | Mesocricetus auratus (Golden hamster) |
P02542 | DESM_CHICK | MSQSYSSSQRVSSYRRTFGGGTSPVFPRASFGSRGSGSSVTSRVYQVSRTSAVPTLSTFRTTRVTPLRTYQSAYQGAGELLDFSLADAMNQEFLQTRTNEKVELQELNDRFANYIEKVRFLEQQNALMVAEVNRLRGKEPTRVAEMYEEELRELRRQVDALTGQRARVEVERDNLLDDLQKLKQRLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLQEEIAFLKKVHEEEIRELQAQLQEQHIQVEMDISKPDLTAALRDIRAQYESIAAKNIAEAEEWYKSKVSDLTQAANKNNDALRQAKQEMLEYRHQI... | 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 mito... | Gallus gallus (Chicken) |
P02543 | VIME_PIG | MSTRTVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYTSSPGGVYATRSSAVRLRSSVPGVRLLQDAVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEETLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQAQIQEQHVQIDMDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYR... | 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 phospho... | 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 ... | Sus scrofa (Pig) |
P02544 | VIME_MESAU | MSTRSVSSSSYRRMFGGPGTSNRQSSNRSYVTTSTRTYSLGSLRPSTSRSLYSSSPGGAYVTRSSAVRLRSSMPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAESTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHDEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESNEYRR... | 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 ... | 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 ... | Mesocricetus auratus (Golden hamster) |
P02545 | LMNA_HUMAN | METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVRSLETENAGLRLRITESEEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQARLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRLQTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKELEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKL... | 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 regula... | 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:0... | 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 ac... | 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}. Nuc... | 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... | Homo sapiens (Human) |
P02547 | NFL_PIG | MSSFYSEPYYSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGLMPSLENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAQLLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIE... | 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|UniP... | Sus scrofa (Pig) |
P02548 | NFL_BOVIN | MSSFSYEPYYSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGSLMPSLESLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEI... | 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 p... | 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:... | 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|UniP... | Bos taurus (Bovine) |
P02549 | SPTA1_HUMAN | MEQFPKETVVESSGPKVLETAEEIQERRQEVLTRYQSFKERVAERGQKLEDSYHLQVFKRDADDLGKWIMEKVNILTDKSYEDPTNIQGKYQKHQSLEAEVQTKSRLMSELEKTREERFTMGHSAHEETKAHIEELRHLWDLLLELTLEKGDQLLRALKFQQYVQECADILEWIGDKEAIATSVELGEDWERTEVLHKKFEDFQVELVAKEGRVVEVNQYANECAEENHPDLPLIQSKQNEVNAAWERLRGLALQRQKALSNAANLQRFKRDVTEAIQWIKEKEPVLTSEDYGKDLVASEGLFHSHKGLERNLAVMSDKV... | 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 p... | 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 [G... | 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 | MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFSVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRAHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR... | 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. Bo... | 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:P6836... | 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... | Sus scrofa (Pig) |
P02552 | TBA1A_CHICK | MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR... | 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. Bo... | 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:P6836... | 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 a... | Gallus gallus (Chicken) |
P02554 | TBB_PIG | MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR... | 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. Bo... | 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... | Sus scrofa (Pig) |
P02557 | TBB_YEAST | MREIIHISTGQCGNQIGAAFWETICGEHGLDFNGTYHGHDDIQKERLNVYFNEASSGKWVPRSINVDLEPGTIDAVRNSAIGNLFRPDNYIFGQSSAGNVWAKGHYTEGAELVDSVMDVIRREAEGCDSLQGFQITHSLGGGTGSGMGTLLISKIREEFPDRMMATFSVLPSPKTSDTVVEPYNATLSVHQLVEHSDETFCIDNEALYDICQRTLKLNQPSYGDLNNLVSSVMSGVTTSLRYPGQLNSDLRKLAVNLVPFPRLHFFMVGYAPLTAIGSQSFRSLTVPELTQQMFDAKNMMAAADPRNGRYLTVAAFFRGK... | 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 i... | 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... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P02562 | MYSS_RABIT | SAETEKEMANMKEEFEKTKESLAKAEAKRKELEEKMVALMQEKNDLQLQVQAEADSLADAEERQDLIKTKIQLEAKIKEVTERAEDEEEINAELTAKKRKLEDECSELKKDIDDLELTLAKVEKEKHATENKVKNLTEEMAGLDETIAKLTKEKKALQEAHQQTLDDLQAEEDKVNTLTKAKTKLEQQVDDLEGSLEQEKKIRMDLERAKRKLEGDLKLAQETSMDIENDKQQLDEKLKKLEFMTNLQSKIEDEQALMTNLQRIEELEEEIEAERASRAKAEKQRSDLSRELEEISERLEEAGGATSAQIEMNKKREAEF... | 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 | MTDAQMADFGAARYLRKSEKERLEAQTRPFDIRTECFVPDDKEEYVKAKIVSREGGKVTAETENGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFASIAAIGDRSKKDNPNANKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERNYHIFYQILSNKKPELLDMLLVTNNPYDYAFVSQGEVSV... | 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:00148... | 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 | MADREMAAFGAGAPFLRKSEKERLEAQTRPFDLKKDVFVPDDKEEFVKAKIVSREGGKVTAETENGKTVTVKEDQVMQQNPPKFDKIEDMAMLTFLHEPAVLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAQVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQTPGKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFFSQGETTV... | 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 per... | 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 | MATDADMAIFGEAAPYLRKSEKERIEAQNKPFDAKSSVFVVHAKESYVKSTIQSKESGKVTVKTEGGETLTVKEDQIFSMNPPKYDKIEDMAMMTHLHEPAVLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVLAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGESGAGKTVNTKRVIQYFATIAASGDKKKEEQPAGKMQGTLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLASADIETYLLEKSRVTFQLKAERSYHIFYQIMSNKKPELIEMLLITTNPYDYQYVSQGE... | 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 | MEHEKDPGWQYLRRTREQVLEDQSKPYDSKKNVWIPDPEEGYLAGEITATKGDQVTIVTARGNEVTLKKELVQEMNPPKFEKTEDMSNLSFLNDASVLHNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSCARMFMGKRKTEMPPHLFAVSDEAYRNMLQDHENQSMLITGESGAGKTENTKKVICYFAAVGASQQEGGAEVDPNKKKVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHGRLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFRPELKKELLLDLPIKDYWFVAQAELIIDG... | 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 | MSLEHEKDPGWQYLKRSREQQLADQSRPYDSKKNVWIPDAEEGYIEGVIKGPGPKADTVIVTAGGKDVTLKKDIVQEVNPPKFEKTEDMSNLTFLNDASVLWNLRSRYAAMLIYTYSGLFCVVINPYKRLPIYTDSVARMFMGKRRTEMPPHLFAVSDQAYRYMLQDHENQSMLITGESGAGKTENTKKVICYFATVGASQKAALKEGEKEVTLEDQIVQTNPVLEAFGNAKTVRNNNSSRFGKFIRIHFNKHGTLASCDIEHYLLEKSRVIRQAPGERCYHIFYQIYSDFKPQLRDELLLNHPISNYWFVAQAELLIDG... | 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 | MCDEEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPESLFQPSFLGMEACGIHETTYNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITA... | 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 (... | 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 | MCDEEASALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDCYVGDEAQSKRGILSLKYPIEHGIITNWDDMEKVWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNSPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAAASTSLEKSYELPDGQVITIGNERFRTPEALFQPSFLGMESCGIHETVYQSIMKCDVDIRKDLYANNVLSGGTTMYPGIADRMQKEITA... | 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 (... | 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 | MEGEDVQALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHTGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLAYVALDFEQEMQTAASSSALEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESAGIHETTYNSIMKCDVDIRKDLYGNVVLSGGTTMFPGIADRMQKELTA... | 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. ... | 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 regul... | 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:001990... | 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 t... | 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... | Bos taurus (Bovine) |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.