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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P14424 | PA2BB_VIPAA | MRTLWIVAVCLIGVEGSLLEFGMMILGETGKNPLTSYSFYGCYCGVGGKGTPKDATDRCCFVHDCCYGNLPDCSPKTDRYKYHRENGAIVCGKGTSCENRICECDRAAAICFRKNLKTYNHIYMYYPDFLCKKESEKC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:16156665}; Note=Binds 1 Ca(2+) ion. {ECO:0000269|PubMed:16156665}; | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. Host cytoplasm, host cytosol {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that acts as a presynaptic neurotoxin, an inhibitor of blood coagulation, and has been found to bind with high affinity to intracellular proteins. The response of indirectly stimulated neuromuscular preparations to ammodytoxin (Atx) is triphasic. The first phase, the transi... | Vipera ammodytes ammodytes (Western sand viper) |
P14426 | HA13_MOUSE | MGAMVPRTLLLLLAAALAPAQTRAGPHSLRYFETVVSRPGLGEPRFISVGYVDNTEFVRFDSDAENPRDEPRVRWMEQEGPEYWERETQIAKGNEQSFRVDLRTLLRYYNQSEGGSHTIQRLSGCDVGSDWRLLRGYEQFAYDGCDYIALNEDLKTWTAADMAALITKHKWEQAGAAERDRAYLEGTCVEWLRRYLELGNATLLHTDSPKAHVTHHPRSKVEVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCHVYHEGLPEPLTLRWEPPPSTDSYMVIVAVLGVLGAV... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent [GO:0002485]; antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen ... | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886] | beta-2-microglobulin binding [GO:0030881]; peptide antigen binding [GO:0042605]; peptide binding [GO:0042277]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102] | PF07654;PF00129; | 2.60.40.10;3.30.500.10; | MHC class I family | PTM: Polyubiquitinated in case of infection by murid herpesvirus 4, by the viral E3 ligase K3 (mK3), leading to target the protein for rapid degradation by the endoplasmic reticulum-associated degradation (ERAD) system. Ubiquitination takes place on lysine, as well as serine and threonine residues present in the cytopl... | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Mus musculus (Mouse) |
P14427 | HA14_MOUSE | MAPRTLLLLLAAALAPTQTRAGPHSLRYFVTAVSRPGLGKPRYMEVGYVDNTEFVRFDSDAENPRMKPRVRWMEQEGPEYWEQETQNAKDHEQSFRVSLRNLLGYYNQSKGGSHTIQGMRGCDVGSDWRLLRGYEQFAYDGPDYIALNEDLKTWTAADMAAQITRRKWEQAGAAETLRAYLEGACVEWLRRYLELGNATLLCTDPPKAHVTHHPRSEGKVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWAALVVPLGKEQNYTCHVEHEGLPEPLTLRWEPPPSTDSYMVIVAVLVVLGAVFII... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent [GO:0002485]; antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen ... | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886] | beta-2-microglobulin binding [GO:0030881]; peptide antigen binding [GO:0042605]; peptide binding [GO:0042277]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102] | PF07654;PF00129;PF06623; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Mus musculus (Mouse) |
P14428 | HA1Q_MOUSE | PRFISVGYVDDTELVRFDSDAENPRYEPRARWMEQVEPEYWERNTQIAKDNEQSSRVDLRTLLRYYNQSAGGSHTIQRMYGCDVGSDGRLLRGYEQVAYDGCDYIALNEDLKTWTAADMAALITKHKWEQAGAAERRRAYLEGACVEWLSRHLKNGNATLLRTDSPKAHVTHHSRPEDKVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVYHQGLPKPLTLRWEPPPSAVSNTVIIAVLVVLGAAIVTGAVVAFVMMRRRNTGGKGGDYALAPGSQTSDLSLPDCKVM... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent [GO:0002485]; antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen ... | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670] | beta-2-microglobulin binding [GO:0030881]; peptide antigen binding [GO:0042605]; peptide binding [GO:0042277]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102] | PF07654;PF00129;PF06623; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Mus musculus (Mouse) |
P14429 | HA17_MOUSE | MALTMLLLLVAAALTLIETRAGQHSLQYFHTAVSRPGLGEPWFISVGYVDDTQFVRFDSDAENPRMEPRARWMEQEGPEYWERETQIAKGHEQSFRGSLRTAQSYYNQSKGGSHTLQWMYGCDMGSDGRLLRGYLQFAYEGRDYIALNEDLKTWTAVDMAAQITRRKWEQAGIAEKDQAYLEGTCMQSLRRYLQLGKETLLRTDPPKAHVTHHPRSYGAVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCHVNHEGLPEPLTLRWGRWEPPPYTVSNMATIAVVVDLGAV... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; cellular response to type II interferon [GO:0071346]; embryo implantation [GO:0007566]; immune ... | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670] | peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102] | PF07654;PF00129; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Mus musculus (Mouse) |
P14430 | HA18_MOUSE | MALTMLLLLVAAALTLIETRAGPHSLRYFHTAVSWPGLVEPRFIIVGYVDDTQFVRFDSDAENPRMEPRARWMEQEGPEYWERETQKAKGHEESFRVSLRTAQRYYNQSKGGSHTLQWMYGCDVGSDERLLRGYLQFAYEGRDYIALNEDLKTWTAADMAAQITLHKWEQAGIAERDRAYLEGACVQSLRRYLQLRKETLLCTDPPKAHVTHHPRSYGAVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCHVNHEGLPEPLTLRWEPPPSTVSNMANVAILVVLVAWPSL... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916] | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670] | beta-2-microglobulin binding [GO:0030881]; peptide antigen binding [GO:0042605]; peptide binding [GO:0042277]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102] | PF07654;PF00129; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Mus musculus (Mouse) |
P14431 | HA19_MOUSE | MALTMLLLLVAAALTLIETRAGQHSLQYFHTAVSRPGLGEPWFISVGYVDDTQFVRFDSDAENPRMEPRARWMEQEGPEYWERETQIAKGHEQSFRGSLRTAQSYYNQSKGGSHTLQWMYGCDMGSDGRLLRGYLQFAYEGRDYIALNEDLKTWTAVDMAAQITRRKWEQAGIAEKDQAYLEGTCMQSLRRYLELGKETL | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; cellular response to type II interferon [GO:0071346]; defense response to virus [GO:0051607]; i... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; MHC class Ib protein complex [GO:0032398]; phagocytic vesicle membrane [GO:0030670] | peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102] | PF00129; | 3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Mus musculus (Mouse) |
P14432 | HA1T_MOUSE | MRMGTPVPGTLLILLAASQGQTQTCPGSHSLRYFYTALSRPAISEPWYIAVGYLDDTQFVRFNSSGETATYKLSAPWVEQEGPEYWARETEIVTSNAQFFRENLQTMLDYYNLSQNGSHTIQVMYGCEVEFFGSLFRAYEQHGYDGPDYIALNEDLKTWTAADTAAEITRSKWEQAGYTELRRTYLEGPCKDSLLRYLENRKKTQECTDPPKTHVTHHPRPEGYVTLRCWALRFYPADITLTWQLNGEELIQDTELVETRPAGDGTFQKWAAVVVPLGKEQKYTCHVYHEGLPEPLTLRWEPPQTSMPNRTTVRALLGAM... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916] | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670] | peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102] | PF07654;PF00129; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Mus musculus (Mouse) |
P14434 | HA2B_MOUSE | MPRSRALILGVLALTTMLSLCGGEDDIEADHVGTYGISVYQSPGDIGQYTFEFDGDELFYVDLDKKETVWMLPEFGQLASFDPQGGLQNIAVVKHNLGVLTKRSNSTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINITWLRNSKSVADGVYETSFFVNRDYSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLKHWEPEIPAPMSELTETVVCALGLSVGLVGIVVGTIFIIQGLRSGGTSRHPGPL | null | null | adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; negative regulation of T cell proliferation [GO:0042130]; peptide ... | external side of plasma membrane [GO:0009897]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; MHC class II protein complex [GO:0042613]; plasma membrane [GO:0005886] | MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein-containing complex binding [GO:0044877] | PF07654;PF00993; | 2.60.40.10; | MHC class II family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | null | Mus musculus (Mouse) |
P14435 | HA2F_MOUSE | EDDIEADHVGFYGISVYQSPGDIGQYTFEFDGDEWFYVDLDKKETVWRLPEFGQLTSFDPQGGLQEIATGKHNLGILTKRSNFTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINITWLRNSKSVTDGVYETSFLVNRDHSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLKHWEPEIPAPMSELTETVVCALGLSVGLVGIVVGTIFIIQGLRSGGTSRHPGPL | null | null | adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; negative regulation of T cell proliferation [GO:0042130]; peptide ... | external side of plasma membrane [GO:0009897]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; MHC class II protein complex [GO:0042613]; plasma membrane [GO:0005886] | MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein-containing complex binding [GO:0044877] | PF07654;PF00993; | 2.60.40.10; | MHC class II family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | null | Mus musculus (Mouse) |
P14436 | HA2R_MOUSE | EDDIEADHVGVYGTTVYQSPGDIGQFTHEFDGDEWFYVDLDKKETVWMLPEFGQLTSFDPQGGLQNIAVVKHNLEILTKRSNFTPAANEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINITWLRNSKSVTDGVYETSFLVNRDHSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLKHWEPEIPAPMSELTETVVCALGLSVGLVGIVVGTIFIIQGLRSGGTSRHPGPL | null | null | adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; negative regulation of T cell proliferation [GO:0042130]; peptide ... | external side of plasma membrane [GO:0009897]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; MHC class II protein complex [GO:0042613]; plasma membrane [GO:0005886] | MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein-containing complex binding [GO:0044877] | PF07654;PF00993; | 2.60.40.10; | MHC class II family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | null | Mus musculus (Mouse) |
P14437 | HA2S_MOUSE | EDDIEADHVGVYGTTVYQSPGDIGQYTHEFDGDEWFYVDLDKKETIWMLPEFGQLTSFDPQGGLQNIATGKYTLGILTKRSNSTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINITWLRNSKSVTDGVYETSFLVNRDHSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLKHWEPEIPAPMSELTETVVCALGLSVGLVGIVVGTIFIIQGLRSGGTSRHPGPL | null | null | adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; negative regulation of T cell proliferation [GO:0042130]; peptide ... | external side of plasma membrane [GO:0009897]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; MHC class II protein complex [GO:0042613]; plasma membrane [GO:0005886] | MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein-containing complex binding [GO:0044877] | PF07654;PF00993; | 2.60.40.10; | MHC class II family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | null | Mus musculus (Mouse) |
P14438 | HA2U_MOUSE | DHVGSYGIVVYQSPGDIGQYTFEFDGDELFYVDLDKKETIWMLPEFAQLRSFDPQGGLQNIATGKHNLGVLTKRSNSTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINITWLRNSKSVADGVYETSFFVNRDYSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLKHWEPEIPAPMSELTETVVCALGLSVGLVGIVVGTIFIIQGLRSGGTSRHPGPL | null | null | adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; negative regulation of T cell proliferation [GO:0042130]; peptide ... | external side of plasma membrane [GO:0009897]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; MHC class II protein complex [GO:0042613]; plasma membrane [GO:0005886] | MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein-containing complex binding [GO:0044877] | PF07654;PF00993; | 2.60.40.10; | MHC class II family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | null | Mus musculus (Mouse) |
P14439 | HA23_MOUSE | MATIGALLLRFFFIAVLMSSQKSWAIKEEHTIIQAEFYLLPDKRGEYMFDFDGDEIFHVDIEKSETIWRLEEFAKFASFEAQGALANIAVDKANLDVMKKRSNNTPDANVAPEVTVLSRSPVNLGEPNILVCFIDKFSPPVVNVTWLRNGQPVTEGVSETVFLPRDDHLFRKFHYLTFLPSTDDFYDCEVDHWGLEEPLRKHWEFEEKTLLPETKENVVCALGLFVGLVGIVVGIILIMKGIKKRNVVERRQGAL | null | null | antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; immunoglobulin mediated immune response [GO:0016064]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of immune response [GO:0050778]; positive regulation of T cell activation [GO... | external side of plasma membrane [GO:0009897]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; MHC class II protein complex [GO:0042613]; plasma membrane [GO:0005886] | MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605] | PF07654;PF00993; | 2.60.40.10; | MHC class II family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | null | Mus musculus (Mouse) |
P14448 | FIBA_CHICK | MIPVTILCVLLCLNLAWAQDGKTTFEKEGGGGRGPRILENMHESSCKYEKNWPICVDDDWGTKCPSCCRMQGIIDDTDQNYSQRIDNIRQQLADSQNKYKTSNRVIVETINILKPGLEGAQQLDENYGHVSTELRRRIVTLKQRVATQVNRIKALQNSIQEQVVEMKRLEVDIDIKIRACKGSCARSFDYQVDKEGYDNIQKHLTQASSIDMHPDFQTTTLSTLKMRPLKDSNVPEHFKLKPSPEMQAMSAFNNIKQMQVVLERPETDHVAEARGDSSPSHTGKLITSSHRRESPSLVDKTSSASSVHRCTRTVTKKVIS... | null | null | blood coagulation, common pathway [GO:0072377]; fibrinolysis [GO:0042730]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of extrinsic apoptotic signaling pathway via death domain receptors [GO:1902042]; platelet aggregation [GO:0070527]; positive regulation of ERK1 and ERK2... | fibrinogen complex [GO:0005577] | extracellular matrix structural constituent [GO:0005201]; metal ion binding [GO:0046872]; protein-macromolecule adaptor activity [GO:0030674]; signaling receptor binding [GO:0005102] | PF08702;PF12160;PF00147; | 1.20.5.50;3.90.215.10;4.10.530.10; | null | PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsil... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10737772, ECO:0000269|PubMed:11601975}. | null | null | null | null | null | FUNCTION: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. {ECO:0000250|UniProtKB:E9PV24}. | Gallus gallus (Chicken) |
P14480 | FIBB_RAT | MRHLWLLLLSVSLVQTQAATTDSDKVDLSIARGHRPVDRRKEEPPSLRPAPPPISGGGYRARPAKVDAGQKKVERKPPDAGGCVHGDGDMGVLCPTGCELRQTLLNHERPIKNSIAELNSNINSVSETSSVTFQYLTLLKDMWKKKQAQVKDNENVINEYSSILEDQKLYIDETVNDNIPLNLRVLRSILEDLRSKIQKLESDISAQTEYCHTPCTVNCNIPVVSGKECEEIIRKGGETSEMYLIQPDTSSKPYRVYCDMKTENGGWTVIQNRQDGSVDFGRKWDPYKKGFGNIATNEDTKKYCGLPGEYWLGNDKISQL... | null | null | adaptive immune response [GO:0002250]; blood coagulation, fibrin clot formation [GO:0072378]; cell-matrix adhesion [GO:0007160]; cellular response to interleukin-1 [GO:0071347]; cellular response to leptin stimulus [GO:0044320]; fibrinolysis [GO:0042730]; induction of bacterial agglutination [GO:0043152]; innate immune... | blood microparticle [GO:0072562]; cell cortex [GO:0005938]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum [GO:0005783]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; fibrinogen complex [GO:0005577]; platelet alpha granule [GO:0... | cell adhesion molecule binding [GO:0050839]; protein-folding chaperone binding [GO:0051087]; signaling receptor binding [GO:0005102]; structural molecule activity [GO:0005198] | PF08702;PF00147; | 1.20.5.50;3.90.215.10; | null | PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of... | Rattus norvegicus (Rat) |
P14483 | HB2A_MOUSE | MALQIPSLLLSAAVVVLMVLSSPGTEGGDSERHFVYQFMGECYFTNGTQRIRYVTRYIYNREEYVRYDSDVGEHRAVTELGRPDAEYWNSQPEILERTRAELDTVCRHNYEGPETHTSLRRLEQPNVVISLSRTEALNHHNTLVCSVTDFYPAKIKVRWFRNGQEETVGVSSTQLIRNGDWTFQVLVMLEMTPRRGEVYTCHVEHPSLKSPITVEWRAQSESAWSKMLSGIGGCVLGVIFLGLGLFIRHRSQKGPRGPPPAGLLQ | null | null | antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; B cell affinity maturation [GO:0002344]; cellular response to type II interferon [GO:0071346]; immune res... | cell surface [GO:0009986]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; MHC class II protein complex [GO:0042613]; multivesicular body [GO:0005771]; plasma membrane [... | MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein antigen binding [GO:1990405]; protein-containing complex binding [GO:0044877]; toxic substance binding [GO:0015643]; ubiquitin protein ligase binding [GO:0031625] | PF07654;PF00969; | 2.60.40.10; | MHC class II family | PTM: Ubiquitinated in immature dendritic cells leading to down-regulation of MHC class II. {ECO:0000269|PubMed:17051151, ECO:0000269|PubMed:17174123}. | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | null | Mus musculus (Mouse) |
P14488 | BLAB_BACCE | MKNTLLKLGVCVSLLGITPFVSTISSVQAERTVEHKVIKNETGTISISQLNKNVWVHTELGYFSGEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFKKRVTDVIITHAHADRIGGMKTLKERGIKAHSTALTAELAKKNGYEEPLGDLQSVTNLKFGNMKVETFYPGKGHTEDNIVVWLPQYQILAGGCLVKSASSKDLGNVADAYVNEWSTSIENVLKRYGNINLVVPGHGEVGDRGLLLHTLDLLK | 3.5.2.6 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P04190}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P04190}; | antibiotic catabolic process [GO:0017001]; response to antibiotic [GO:0046677] | periplasmic space [GO:0042597] | beta-lactamase activity [GO:0008800]; zinc ion binding [GO:0008270] | PF00753; | 3.60.15.10; | Metallo-beta-lactamase superfamily, Class-B beta-lactamase family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000250|UniProtKB:P25910}; | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. {ECO:0000269|PubMed:3131315}; | FUNCTION: Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Benzylpenicillin is a better substrate than cephalosporin C and ampicillin (PubMed:2501295, PubMed:3131315). {ECO:0000269|PubMed:1904717, ECO:0000269|PubMed:25012... | Bacillus cereus |
P14519 | GLYM_RABIT | MLPFSLLWAVRPLQRCGPLVRTAVRAQHGKAAQTQTGEASRGWTGQESLSDTDPEMWELLQREKDRQCRGLELIASENFCIRAALEALGSCLNNKYSEGYPGKRYYGGAEVVDEIELLCQRRALEAFDLDPAQWGVNVQPYSGSPANLAAYTALLQPHDRIMGLDLPDGGHLTHGYMSDVKRVSATSIFFESMPYKLNPQTGLIDYEQLALTARLFRPRLIIAGTSAYARLIDYARMREVCDEVKAHLLADMAHISGLVAAKVIPSPFKHADVVTTTTHKTLRGARSGLIFYRKGVRTVDPKTGQEIPYTFEDRINFAVF... | 2.1.2.1 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P34897}; | folic acid metabolic process [GO:0046655]; glycine biosynthetic process from serine [GO:0019264]; glycine metabolic process [GO:0006544]; L-serine catabolic process [GO:0006565]; L-serine metabolic process [GO:0006563]; one-carbon metabolic process [GO:0006730]; protein homotetramerization [GO:0051289]; protein K63-lin... | BRISC complex [GO:0070552]; cytoplasm [GO:0005737]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; cobalt ion binding [GO:0050897]; glycine hydroxymethyltransferase activity [GO:0004372]; pyridoxal phosphate binding [GO:0030170]; serine binding [GO:0070905]; zinc ion binding [GO:0008270] | PF00464; | 3.90.1150.10;3.40.640.10; | SHMT family | PTM: Succinylation at Lys-280 inhibits the hydroxymethyltransferase activity. Desuccinylation by SIRT5 restores the activity, leading to promote cell proliferation. {ECO:0000250|UniProtKB:P34897}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P34897}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:P34897}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P34897}. Cytoplasm {ECO:0000250|UniProtKB:P34897}. Nucleus {ECO:0000250|UniProtKB:P34897}. Note=Mainly localizes in the mit... | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine; Xref=Rhea:RHEA:15481, ChEBI:CHEBI:15377, ChEBI:CHEBI:15636, ChEBI:CHEBI:33384, ChEBI:CHEBI:57305, ChEBI:CHEBI:57453; EC=2.1.2.1; Evidence={ECO:0000250|UniProtKB:P34897}; PhysiologicalDir... | null | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. {ECO:0000250|UniProtKB:P34897}. | null | null | FUNCTION: Catalyzes the cleavage of serine to glycine accompanied with the production of 5,10-methylenetetrahydrofolate, an essential intermediate for purine biosynthesis. Serine provides the major source of folate one-carbon in cells by catalyzing the transfer of one carbon from serine to tetrahydrofolate. Contributes... | Oryctolagus cuniculus (Rabbit) |
P14526 | HBB_BRATR | MVHLADDEKAAVSALWHKVHVEEFGGEALGRLLVVYPWTSRFFESFGDLSSADAVFSNAKVKAHGKKVLTSFGEGLKHLDDLKGTYAHLSELHCDKLHVDPENFKLLGNVLVIVLARHFGKEFTPQLQAAYQKVTTGVSTALAHKYH | 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. | Bradypus tridactylus (Pale-throated three-toed sloth) |
P14530 | VM2HA_PROFL | MIEVLLVTICLAVFPYPGSSIILESGNVDDYEVVYPQKLTALPKGAVQPKYEDAMQYEFKVNGEPVVLHLEKNKGLFSEDYSETHYSPDGREITTYPSVEDHCYYHGRIQNDADSTASISACDGLKGYFKLQGETYLIEPLELSDSEAHAVFKYENVEKEDEAPKMCGVTQNWESDESIKKASQLYLTPEQQRFPQRYIELAIVVDHGMYTKYSSNFKKIRKRVHQMVNNINEMYRPLNIAITLSLLDVWSEKDLITMQAVAPTTARLFGDWRETVLLKQKDHDHAQLLTDINFTGNTIGWAYMGGMCNAKNSVGIVKDH... | 3.4.24.53 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | proteolysis [GO:0006508] | extracellular region [GO:0005576]; plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222]; toxin activity [GO:0090729] | PF00200;PF01562;PF01421; | 3.40.390.10;4.10.70.10; | Venom metalloproteinase (M12B) family, P-II subfamily, P-IIa sub-subfamily | PTM: Not N-glycosylated. {ECO:0000269|PubMed:2753880}. | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Cleavage of 3-Asn-|-Gln-4, 10-His-|-Leu-11 and 14-Ala-|-Leu-15 in the insulin B chain, and the bond Z-Gly-Pro-|-Leu-Gly-Pro in a small molecule substrate of microbial collagenase.; EC=3.4.24.53; | null | null | null | null | FUNCTION: [Snake venom metalloproteinase HR2a]: Zinc protease that induces hemorrhage. {ECO:0000269|PubMed:9114455}.; FUNCTION: [Disintegrin flavostatin]: Inhibits platelet aggregation induced by ADP, thrombin, and collagen. Acts by inhibiting fibrinogen interaction with platelet receptors GPIIb/GPIIIa (ITGA2B/ITGB3). ... | Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis) |
P14532 | CCPR_PSEAE | MQSSQLLPLGSLLLSFATPLAQADALHDQASALFKPIPEQVTELRGQPISEQQRELGKKLFFDPRLSRSHVLSCNTCHNVGTGGADNVPTSVGHGWQKGPRNSPTVFNAVFNAAQFWDGRAKDLGEQAKGPIQNSVEMHSTPQLVEQTLGSIPEYVDAFRKAFPKAGKPVSFDNMALAIEAYEATLVTPDSPFDLYLKGDDKALDAQQKKGLKAFMDSGCSACHNGINLGGQAYFPFGLVKKPDASVLPSGDKGRFAVTKTQSDEYVFRAAPLRNVALTAPYFHSGQVWELKDAVAIMGNAQLGKQLAPDDVENIVAFLH... | 1.11.1.5 | COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000269|PubMed:3030432}; Note=Binds 2 heme c groups covalently. Heme 1 is low-potential (-330 mV) with 2 His axial ligands and functions in the peroxidase reaction, while heme 2 is high potential (+320 mV) with His and Met axial ligands and functions to feed ... | null | periplasmic space [GO:0042597] | cytochrome-c peroxidase activity [GO:0004130]; electron transfer activity [GO:0009055]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF03150;PF00034; | 1.10.760.10; | null | PTM: Binds 2 heme groups per subunit (PubMed:8591033). Sequencing of the whole protein indicates about 20% starts on Val-247 (PubMed:8543038). {ECO:0000269|PubMed:8543038, ECO:0000269|PubMed:8591033}. | SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome c] + 2 H(+) + H2O2 = 2 Fe(III)-[cytochrome c] + 2 H2O; Xref=Rhea:RHEA:16581, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.11.1.5; Evidence={ECO:0000305|PubMed:1657179}; | null | null | null | null | FUNCTION: Catalyzes the peroxidative oxidation of azurin and cytochrome c551. Likely to provide protection against toxic peroxides. | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
P14540 | ALF_YEAST | MGVEQILKRKTGVIVGEDVHNLFTYAKEHKFAIPAINVTSSSTAVAALEAARDSKSPIILQTSNGGAAYFAGKGISNEGQNASIKGAIAAAHYIRSIAPAYGIPVVLHSDHCAKKLLPWFDGMLEADEAYFKEHGEPLFSSHMLDLSEETDEENISTCVKYFKRMAAMDQWLEMEIGITGGEEDGVNNENADKEDLYTKPEQVYNVYKALHPISPNFSIAAAFGNCHGLYAGDIALRPEILAEHQKYTREQVGCKEEKPLFLVFHGGSGSTVQEFHTGIDNGVVKVNLDTDCQYAYLTGIRDYVLNKKDYIMSPVGNPEG... | 4.1.2.13 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution. {ECO:0000250}; | canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739] | fructose-bisphosphate aldolase activity [GO:0004332]; melatonin binding [GO:1904408]; zinc ion binding [GO:0008270] | PF01116; | 3.20.20.70; | Class II fructose-bisphosphate aldolase family | null | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence={ECO:0000269|PubMed:2647491}; | null | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. | null | null | FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. {ECO:0000250}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14543 | NID1_HUMAN | MLASSSRIRAAWTRALLLPLLLAGPVGCLSRQELFPFGPGQGDLELEDGDDFVSPALELSGALRFYDRSDIDAVYVTTNGIIATSEPPAKESHPGLFPPTFGAVAPFLADLDTTDGLGKVYYREDLSPSITQRAAECVHRGFPEISFQPSSAVVVTWESVAPYQGPSRDPDQKGKRNTFQAVLASSDSSSYAIFLYPEDGLQFHTTFSKKENNQVPAVVAFSQGSVGFLWKSNGAYNIFANDRESVENLAKSSNSGQQGVWVFEIGSPATTNGVVPADVILGTEDGAEYDDEDEDYDLATTRLGLEDVGTTPFSYKALRR... | null | null | basement membrane organization [GO:0071711]; canonical Wnt signaling pathway [GO:0060070]; cell-matrix adhesion [GO:0007160]; glomerular basement membrane development [GO:0032836]; positive regulation of cell adhesion [GO:0045785]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of inte... | basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; protein complex involved in cell-matrix adhesion [GO:0098637] | calcium ion binding [GO:0005509]; collagen binding [GO:0005518]; extracellular matrix structural constituent [GO:0005201]; laminin binding [GO:0043236]; laminin-1 binding [GO:0043237]; proteoglycan binding [GO:0043394]; Wnt receptor activity [GO:0042813]; Wnt-protein binding [GO:0017147] | PF12662;PF12947;PF07645;PF14670;PF07474;PF00058;PF06119;PF00086; | 2.40.155.10;2.10.25.10;4.10.800.10;2.120.10.30; | null | PTM: N- and O-glycosylated. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. | null | null | null | null | null | FUNCTION: Sulfated glycoprotein widely distributed in basement membranes and tightly associated with laminin. Also binds to collagen IV and perlecan. It probably has a role in cell-extracellular matrix interactions. | Homo sapiens (Human) |
P14550 | AK1A1_HUMAN | MAASCVLLHTGQKMPLIGLGTWKSEPGQVKAAVKYALSVGYRHIDCAAIYGNEPEIGEALKEDVGPGKAVPREELFVTSKLWNTKHHPEDVEPALRKTLADLQLEYLDLYLMHWPYAFERGDNPFPKNADGTICYDSTHYKETWKALEALVAKGLVQALGLSNFNSRQIDDILSVASVRPAVLQVECHPYLAQNELIAHCQARGLEVTAYSPLGSSDRAWRDPDEPVLLEEPVVLALAEKYGRSPAQILLRWQVQRKVICIPKSITPSRILQNIKVFDFTFSPEEMKQLNALNKNWRYIVPMLTVDGKRVPRDAGHPLYP... | 1.1.1.19; 1.1.1.2; 1.1.1.20; 1.1.1.372; 1.1.1.54; 1.6.-.- | null | aldehyde catabolic process [GO:0046185]; cellular detoxification of aldehyde [GO:0110095]; D-glucuronate catabolic process [GO:0042840]; daunorubicin metabolic process [GO:0044597]; doxorubicin metabolic process [GO:0044598]; glucuronate catabolic process to xylulose 5-phosphate [GO:0019640]; glutathione derivative bio... | apical plasma membrane [GO:0016324]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; synapse [GO:0045202] | alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; aldo-keto reductase (NADP) activity [GO:0004033]; allyl-alcohol dehydrogenase activity [GO:0047655]; glucuronolactone reductase activity [GO:0047941]; glycerol dehydrogenase [NADP+] activity [GO:0047956]; L-glucuronate reductase activity [GO:0047939]; methylglyoxal ... | PF00248; | 3.20.20.100; | Aldo/keto reductase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JII6}. Apical cell membrane {ECO:0000250|UniProtKB:Q9JII6}. | CATALYTIC ACTIVITY: Reaction=a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH; Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.2; Evidence={ECO:0000269|PubMed:10510318}; CATALYTIC ACTIVITY: Reaction=allyl alcohol + NADP(+) = acrolein ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=58 uM for S-nitroso-CoA {ECO:0000269|PubMed:30538128}; KM=4555 uM for D-glucuronate {ECO:0000269|PubMed:30538128}; KM=2554 uM for D,L-glyceraldehyde {ECO:0000269|PubMed:30538128}; KM=184 uM for S-nitroso-glutathione {ECO:0000269|PubMed:31649033}; Vmax=1426 nmol/min... | null | null | null | FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols (PubMed:10510318, PubMed:30538128). Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides and bile acids, with a pr... | Homo sapiens (Human) |
P14553 | POLG_HAVS2 | MFMMMNMSKQGIFQTVGSGLDHILSLADVEEEQMIQSVDRTAVTGASYFTSVDQSSVHTAEVGAHQTEPLKTSVDKPGSKKTQGEKFFLIHSADWLTTHALFHEVAKLDVVSLLYNEQFAVQGLLRYHTYARFGIEIQVQINPTPFQQGGLICAMVPGDQGYGSIASLTVYPHGLLNCNINNVVRIKVPFIYTRGAYHFKDPQYPVWELTIRVWSELNIGTGTSAYTSLNVLARFTDLELHGLTPLSTQMMRNEFRVSTTENVVNLSNYEDARAKMSFALDQEDWKTDPSQGGGIKITHFTTWTSIPTLAAQFAFNASAS... | 2.7.7.48; 3.4.22.28; 3.6.1.15 | null | DNA-templated transcription [GO:0006351]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity [GO:0039545]; viral RNA genome re... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell mitochondrial outer membrane [GO:0044193]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule ... | PF20758;PF12944;PF00548;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;2.40.10.10; | Picornaviridae polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages by viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates are produced, such as P1-2A which is a functional precursor of the structural proteins, VP0 which is a VP4-VP2 precursor, VP1-2A precursor, 3ABC precu... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P08617}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P08617}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multivesicular bodies. {ECO:000025... | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000250|UniProtKB:P08617, ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYT... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Together they form an icosahedral capsid (T=3) composed of 60 copies of each VP1, VP2, and VP3, with a d... | Simian hepatitis A virus genotype V (isolate AGM-27) (SHAV) (Simian hepatitis A virus (isolate Cercopithecus/Kenya/AGM-27/1985)) |
P14555 | PA2GA_HUMAN | MKTLLLLAVIMIFGLLQAHGNLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDATDRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFARNKTTYNKKYQYYSNKHCRGSTPRC | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:2925633}; Note=Binds 1 Ca(2+) ion per subunit.; | arachidonic acid secretion [GO:0050482]; defense response to Gram-positive bacterium [GO:0050830]; inflammatory response [GO:0006954]; intestinal stem cell homeostasis [GO:0036335]; killing of cells of another organism [GO:0031640]; lipid catabolic process [GO:0016042]; low-density lipoprotein particle remodeling [GO:0... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; mitochondrial outer membrane [GO:0005741]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; secretory granu... | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipase A2 activity [GO:0004623]; phospholipid binding [GO:0005543] | PF00068; | 1.20.90.10; | Phospholipase A2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2925608, ECO:0000269|PubMed:2925633}. Cell membrane {ECO:0000269|PubMed:2775276}; Peripheral membrane protein {ECO:0000305}. Mitochondrion outer membrane {ECO:0000269|PubMed:25082876}; Peripheral membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+); Xref=Rhea:RHEA:44604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:64381, ChEBI:CHEBI:64612; Evidence={ECO:0000269|PubMed:10455175, ECO:0000269|PubM... | null | null | null | null | FUNCTION: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular phospholipids with implications in host antimicrobial defense, inflammatory response and tissue regeneration (PubMed:10455175, PubMed:10681567, PubMed:2925633). Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 ... | Homo sapiens (Human) |
P14562 | LAMP1_RAT | MAAPGARRPLLLLLLAGLAHSAPALFEVKDNNGTACIMASFSASFLTTYDAGHVSKVSNMTLPASAEVLKNSSSCGEKNASEPTLAITFGEGYLLKLTFTKNTTRYSVQHMYFTYNLSDTQFFPNASSKGPDTVDSTTDIKADINKTYRCVSDIRVYMKNVTIVLWDATIQAYLPSSNFSKEETRCPQDQPSPTTGPPSPSPPLVPTNPSVSKYNVTGDNGTCLLASMALQLNITYMKKDNTTVTRAFNINPSDKYSGTCGAQLVTLKVGNKSRVLELQFGMNATSSLFFLQGVQLNMTLPDAIEPTFSTSNYSLKALQA... | null | null | autophagic cell death [GO:0048102]; establishment of protein localization to organelle [GO:0072594]; Golgi to lysosome transport [GO:0090160]; granzyme-mediated programmed cell death signaling pathway [GO:0140507]; lysosomal lumen acidification [GO:0007042]; positive regulation of natural killer cell degranulation [GO:... | alveolar lamellar body [GO:0097208]; autolysosome [GO:0044754]; autophagosome membrane [GO:0000421]; cell surface [GO:0009986]; cytolytic granule [GO:0044194]; cytolytic granule membrane [GO:0101004]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; endosome [GO:0005768]; endosome membrane [GO:00100... | enzyme binding [GO:0019899]; ion channel inhibitor activity [GO:0008200]; protein domain specific binding [GO:0019904] | PF01299;PF21222; | 2.40.160.110; | LAMP family | PTM: O- and N-glycosylated; some of the N-glycans attached to LAMP-1 are polylactosaminoglycans. {ECO:0000250|UniProtKB:P11279}. | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein {ECO:0000255}. Endosome membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:P11279}; Single-pass type I membrane protein {ECO:... | null | null | null | null | null | FUNCTION: Lysosomal membrane glycoprotein which plays an important role in lysosome biogenesis, lysosomal pH regulation, autophagy and cholesterol homeostasis. Acts as an important regulator of lysosomal lumen pH regulation by acting as a direct inhibitor of the proton channel TMEM175, facilitating lysosomal acidificat... | Rattus norvegicus (Rat) |
P14565 | TRAI1_ECOLI | MMSIAQVRSAGSAGNYYTDKDNYYVLGSMGERWAGRGAEQLGLQGSVDKDVFTRLLEGRLPDGADLSRMQDGSNRHRPGYDLTFSAPKSVSMMAMLGGDKRLIDAHNQAVDFAVRQVEALASTRVMTDGQSETVLTGNLVMALFNHDTSRDQEPQLHTHAVVANVTQHNGEWKTLSSDKVGKTGFIENVYANQIAFGRLYREKLKEQVEALGYETEVVGKHGMWEMPGVPVEAFSGRSQTIREAVGEDASLKSRDVAALDTRKSKQHVDPEIKMAEWMQTLKETGFDIRAYRDAADQRADLRTLTPGPASQDGPDVQQAV... | 3.6.4.12; 5.6.2.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | metabolic process [GO:0008152] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917]; metal ion binding [GO:0046872] | PF13604;PF18272;PF18340;PF07057;PF08751; | 6.10.140.290;6.10.250.110;3.40.50.300; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; 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; EC=3.6.4.12... | null | null | null | null | FUNCTION: Conjugative DNA transfer (CDT) is the unidirectional transfer of ssDNA plasmid from a donor to a recipient cell. It is the central mechanism by which antibiotic resistance and virulence factors are propagated in bacterial populations. Part of the relaxosome, which facilitates a site- and strand-specific cut i... | Escherichia coli (strain K12) |
P14580 | CP4A6_RABIT | MSVSALNPTRLPGSLSGLLQVAGLLGLLLLLLKAAQLYLHRQWLLRALQQFPCPPFHWLLGHSREFQNGHELQVMLKWVEKFPSACPRWLWGSRAHLLIYDPDYMKVILGRSDPKAQGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVQIMLDKWEQLVSQDSSLEVFQDISLMTLDTIMKCAFSHQGSVQLDRNSQSYIQAVGDLNNLFFSRVRNVFHQSDTIYRLSPEGRLSHRACQLAHEHTDRVIQQRKAQLQQEGELEKVRRKRRLDFLDVLLFAKMENGSSLSDQDLRAEVDTFMF... | 1.14.14.80 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P51869}; | arachidonic acid metabolic process [GO:0019369]; icosanoid biosynthetic process [GO:0046456]; kidney development [GO:0001822]; lauric acid metabolic process [GO:0048252]; linoleic acid metabolic process [GO:0043651] | endoplasmic reticulum membrane [GO:0005789] | alkane 1-monooxygenase activity [GO:0018685]; arachidonic acid monooxygenase activity [GO:0008391]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; long-chain fatty acid omega-hydroxylase activity [GO:0102033] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an omega-methyl-long-chain fatty acid + O2 + reduced [NADPH--hemoprotein reductase] = an omega-hydroxy-long-chain fatty acid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:56748, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:... | null | null | null | null | FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.; FUNCTION: The kidney P-450 system is rather... | Oryctolagus cuniculus (Rabbit) |
P14581 | CP4A7_RABIT | MSVSALSSTRLPGSFSGFLQAAALLGLLLLLLKAAQLYLRRQWLLRALQQFPCPPSHWLLGHSREFPIDSELQQVLKRVEKFPSACPRWLWGSELFLICYDPDYMKTILGRSDPKARVSYSFLAPWIGYGLLLLEGQTWFQHRRMLTPAFHYDILKPYVGLMVDSVQVMLDKLEKLARKDAPLEIYEHVSLMTLETIMKCAFSHQGSVQLESRTSKSYIQAVRELSDLALQRVRNVFHQSDFLYRLSPEGRLSHRACQLAHEHTDRVIQQRKAQLQQEGELEKVRRKRRLDFLDVLLFAKMENGSSLSDQDLRAEVDTFM... | 1.14.14.80 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P51869}; | arachidonic acid metabolic process [GO:0019369]; icosanoid biosynthetic process [GO:0046456]; kidney development [GO:0001822]; lauric acid metabolic process [GO:0048252]; linoleic acid metabolic process [GO:0043651] | endoplasmic reticulum membrane [GO:0005789] | alkane 1-monooxygenase activity [GO:0018685]; arachidonic acid monooxygenase activity [GO:0008391]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; long-chain fatty acid omega-hydroxylase activity [GO:0102033] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an omega-methyl-long-chain fatty acid + O2 + reduced [NADPH--hemoprotein reductase] = an omega-hydroxy-long-chain fatty acid + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:56748, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:... | null | null | null | null | FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.; FUNCTION: The kidney P-450 system is rather... | Oryctolagus cuniculus (Rabbit) |
P14585 | LIN12_CAEEL | MRIPTICFLFLLISLSKSLHIGSCLGLICGRNGHCHAGPVNGTQTSYWCRCDEGFGGEYCEQQCDVSKCGADEKCVFDKDYRMETCVCKDCDINGNSLLKPSCPSGYGGDDCKTQGWCYPSVCMNGGQCIGAGNRAKCACPDGFKGERCELDVNECEENKNACGNRSTCMNTLGTYICVCPQGFLPPDCLKPGNTSTVEFKQPVCFLEISADHPDGRSMYCQNGGFCDKASSKCQCPPGYHGSTCELLEKEDSCASNPCSHGVCISFSGGFQCICDDGYSGSYCQEGKDNCVNNKCEAGSKCINGVNSYFCDCPPERTGP... | null | null | cell fate specification [GO:0001708]; cell projection morphogenesis [GO:0048858]; dauer exit [GO:0043054]; egg-laying behavior [GO:0018991]; nematode larval development [GO:0002119]; Notch signaling pathway [GO:0007219]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of mesodermal ... | apical plasma membrane [GO:0016324]; CSL-Notch-Mastermind transcription factor complex [GO:1990433]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; RNA polymerase II transcription regulator complex [GO:0090575] | calcium ion binding [GO:0005509]; DNA-binding transcription factor binding [GO:0140297]; Notch binding [GO:0005112]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transmembrane signaling receptor activity [GO:0004888] | PF12796;PF00008;PF07974;PF07645;PF12661;PF06816;PF07684;PF00066; | 3.30.300.320;3.30.70.3310;1.25.40.20;2.10.25.10; | NOTCH family | PTM: Upon binding its ligands, it is cleaved (S2 cleavage) in its extracellular domain, close to the transmembrane domain (By similarity). S2 cleavage is probably mediated by the metalloproteases adm-4 and sup-17 (PubMed:16197940). It is then cleaved (S3 cleavage) downstream of its transmembrane domain, releasing it fr... | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:32053105}; Single-pass type I membrane protein {ECO:0000255}. Note=Localizes to the apical cell membrane of vulval precursor cells. {ECO:0000269|PubMed:32053105}.; SUBCELLULAR LOCATION: [lin-12/Notch intracellular domain]: Nucleus {ECO:0000305|PubMed:165300... | null | null | null | null | null | FUNCTION: Essential signaling protein which has a major role in many developmental processes; involved in cell fate decisions that require cell-cell interactions (PubMed:3000611, PubMed:3419531). Probable membrane-bound receptor for putative ligands lag-2, apx-1, dsl-1 and osm-11 (PubMed:18036582, PubMed:18700817, PubM... | Caenorhabditis elegans |
P14598 | NCF1_HUMAN | MGDTFIRHIALLGFEKRFVPSQHYVYMFLVKWQDLSEKVVYRRFTEIYEFHKTLKEMFPIEAGAINPENRIIPHLPAPKWFDGQRAAENRQGTLTEYCSTLMSLPTKISRCPHLLDFFKVRPDDLKLPTDNQTKKPETYLMPKDGKSTATDITGPIILQTYRAIANYEKTSGSEMALSTGDVVEVVEKSESGWWFCQMKAKRGWIPASFLEPLDSPDETEDPEPNYAGEPYVAIKAYTAVEGDEVSLLEGEAVEVIHKLLDGWWVIRKDDVTGYFPSMYLQKSGQDVSQAQRQIKRGAPPRRSSIRNAHSIHQRSRKRLS... | null | null | cellular defense response [GO:0006968]; cellular response to cadmium ion [GO:0071276]; cellular response to glucose stimulus [GO:0071333]; cellular response to reactive oxygen species [GO:0034614]; cellular response to testosterone stimulus [GO:0071394]; innate immune response [GO:0045087]; positive regulation of DNA-t... | cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; dendrite [GO:0030425]; membrane [GO:0016020]; NADPH oxidase complex [GO:0043020]; neuronal cell body [GO:0043025]; phagolysosome [GO:0032010]; plasma membrane [GO:0005886] | electron transfer activity [GO:0009055]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; SH3 domain binding [GO:0017124]; superoxide-generating NAD(P)H oxidase activity [GO:0016175]; superoxide-generating NADPH oxidase activator activity [GO:0016176] | PF16621;PF08944;PF00787;PF00018; | 3.30.1520.10;2.30.30.40; | null | PTM: Phosphorylated by PRKCD; phosphorylation induces activation of NCF1 and NADPH oxidase activity. {ECO:0000269|PubMed:19801500, ECO:0000269|PubMed:8089108}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:2550933}. Membrane {ECO:0000269|PubMed:12356722}; Peripheral membrane protein {ECO:0000269|PubMed:12356722}; Cytoplasmic side {ECO:0000269|PubMed:12356722}. | null | null | null | null | null | FUNCTION: NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production). {ECO:0000269|PubMed:19801500, ECO:0000269|PubMed:2547247, ECO:0000269|PubMed:2550933}. | Homo sapiens (Human) |
P14599 | A4_DROME | MCAALRRNLLLRSLWVVLAIGTAQVQAASPRWEPQIAVLCEAGQIYQPQYLSEEGRWVTDLSKKTTGPTCLRDKMDLLDYCKKAYPNRDITNIVESSHYQKIGGWCRQGALNAAKCKGSHRWIKPFRCLGPFQSDALLVPEGCLFDHIHNASRCWPFVRWNQTGAAACQERGMQMRSFAMLLPCGISVFSGVEFVCCPKHFKTDEIHVKKTDLPVMPAAQINSANDELVMNDEDDSNDSNYSKDANEDDLDDEDDLMGDDEEDDMVADEAATAGGSPNTGSSGDSNSGSLDDINAEYDSGEEGDNYEEDGAGSESEAEVE... | null | null | axonogenesis [GO:0007409]; central nervous system development [GO:0007417]; learning or memory [GO:0007611]; long-term memory [GO:0007616]; mushroom body development [GO:0016319]; neuron projection morphogenesis [GO:0048812]; peripheral nervous system development [GO:0007422]; response to axon injury [GO:0048678]; resp... | axon [GO:0030424]; extracellular region [GO:0005576]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886] | heparin binding [GO:0008201]; transition metal ion binding [GO:0046914] | PF10515;PF12924;PF12925;PF02177; | 1.20.120.770;3.30.1490.140;3.90.570.10; | APP family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: During development, plays a role in the regulation of the neddylation pathway. Appl and APP-BP1 interact antagonistically during development. {ECO:0000269|PubMed:16628230}. | Drosophila melanogaster (Fruit fly) |
P14600 | NK1R_RAT | MDNVLPMDSDLFPNISTNTSESNQFVQPTWQIVLWAAAYTVIVVTSVVGNVVVIWIILAHKRMRTVTNYFLVNLAFAEACMAAFNTVVNFTYAVHNVWYYGLFYCKFHNFFPIAALFASIYSMTAVAFDRYMAIIHPLQPRLSATATKVVIFVIWVLALLLAFPQGYYSTTETMPSRVVCMIEWPEHPNRTYEKAYHICVTVLIYFLPLLVIGYAYTVVGITLWASEIPGDSSDRYHEQVSAKRKVVKMMIVVVCTFAICWLPFHVFFLLPYINPDLYLKKFIQQVYLASMWLAMSSTMYNPIIYCCLNDRFRLGFKHAF... | null | null | aggressive behavior [GO:0002118]; angiotensin-mediated drinking behavior [GO:0003051]; associative learning [GO:0008306]; behavioral response to pain [GO:0048266]; eating behavior [GO:0042755]; learning or memory [GO:0007611]; long-term memory [GO:0007616]; neuropeptide signaling pathway [GO:0007218]; operant condition... | cell body [GO:0044297]; cell periphery [GO:0071944]; cell surface [GO:0009986]; dendrite [GO:0030425]; plasma membrane [GO:0005886]; sperm flagellum [GO:0036126]; sperm head [GO:0061827]; sperm midpiece [GO:0097225] | substance P receptor activity [GO:0016496] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: This is a receptor for the tachykinin neuropeptide substance P. It is probably associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of affinity of this receptor to tachykinins is: substance P > substance K > neuromedin-K. | Rattus norvegicus (Rat) |
P14602 | HSPB1_MOUSE | MTERRVPFSLLRSPSWEPFRDWYPAHSRLFDQAFGVPRLPDEWSQWFSAAGWPGYVRPLPAATAEGPAAVTLAAPAFSRALNRQLSSGVSEIRQTADRWRVSLDVNHFAPEELTVKTKEGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTLVSSSLSPEGTLTVEAPLPKAVTQSAEITIPVTFEARAQIGGPEAGKSEQSGAK | null | null | anterograde axonal protein transport [GO:0099641]; chaperone-mediated protein folding [GO:0061077]; intracellular signal transduction [GO:0035556]; negative regulation of apoptotic process [GO:0043066]; negative regulation of apoptotic signaling pathway [GO:2001234]; negative regulation of cellular response to oxidativ... | axon [GO:0030424]; axon cytoplasm [GO:1904115]; cardiac myofibril [GO:0097512]; contractile fiber [GO:0043292]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; I band [GO:0031674]; M band [GO:0031430]; nucleus [GO:0005634]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynap... | identical protein binding [GO:0042802]; protein folding chaperone [GO:0044183]; protein homodimerization activity [GO:0042803]; protein kinase C binding [GO:0005080]; protein kinase C inhibitor activity [GO:0008426]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; ubiquitin binding [GO... | PF00011; | 2.60.40.790; | Small heat shock protein (HSP20) family | PTM: Phosphorylated upon exposure to protein kinase C activators and heat shock (By similarity). Phosphorylation by MAPKAPK2 and MAPKAPK3 in response to stress dissociates HSPB1 from large small heat-shock protein (sHsps) oligomers and impairs its chaperone activity and ability to protect against oxidative stress effec... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04792}. Nucleus {ECO:0000250|UniProtKB:P04792}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P04792}. Note=Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells. Translocates to the nucleus during heat shock and resides in ... | null | null | null | null | null | FUNCTION: Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Plays a role in stress resistance and actin organization (PubMed:17661394). Through its molecular chaperone activity may regulate numerous biological processes including the ... | Mus musculus (Mouse) |
P14604 | ECHM_RAT | MAALRALLPRACNSLLSPVRCPEFRRFASGANFQYIITEKKGKNSSVGLIQLNRPKALNALCNGLIEELNQALETFEEDPAVGAIVLTGGEKAFAAGADIKEMQNRTFQDCYSGKFLSHWDHITRIKKPVIAAVNGYALGGGCELAMMCDIIYAGEKAQFGQPEILLGTIPGAGGTQRLTRAVGKSLAMEMVLTGDRISAQDAKQAGLVSKIFPVETLVEEAIQCAEKIANNSKIIVAMAKESVNAAFEMTLTEGNKLEKKLFYSTFATDDRREGMSAFVEKRKANFKDH | 4.2.1.17; 5.3.3.8 | null | fatty acid beta-oxidation [GO:0006635] | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | 3-hydroxypropionyl-CoA dehydratase activity [GO:0043956]; crotonyl-CoA hydratase activity [GO:0120092]; delta(3)-delta(2)-enoyl-CoA isomerase activity [GO:0004165]; enoyl-CoA hydratase activity [GO:0004300] | PF00378; | 1.10.12.10; | Enoyl-CoA hydratase/isomerase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:9480773}. | CATALYTIC ACTIVITY: Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O; Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318, ChEBI:CHEBI:58856; EC=4.2.1.17; Evidence={ECO:0000269|PubMed:10074351, ECO:0000269|PubMed:7883013}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16107; Evidence={ECO:000030... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25 uM for (2E)-hexenoyl-CoA {ECO:0000269|PubMed:10074351}; KM=4.9 uM for (2E)-decenoyl-CoA {ECO:0000269|PubMed:10074351}; KM=65.5 uM for (3E)-hexenoyl-CoA {ECO:0000269|PubMed:10074351}; KM=49.9 uM for crotonyl-CoA ((2E)-butenoyl-CoA) {ECO:0000269|PubMed:10074351}; ... | PATHWAY: Lipid metabolism; fatty acid beta-oxidation. {ECO:0000250|UniProtKB:P30084}. | null | null | FUNCTION: Converts unsaturated trans-2-enoyl-CoA species ((2E)-enoyl-CoA) to the corresponding 3(S)-3-hydroxyacyl-CoA species through addition of a water molecule to the double bond (PubMed:10074351, PubMed:7883013). Catalyzes the hydration of medium- and short-chained fatty enoyl-CoA thioesters from 4 carbons long (C4... | Rattus norvegicus (Rat) |
P14605 | CYAA_SCHPO | MDQSKRLLKSAVPNPPEHFKTGISWLDDLDEKDDDSATSVNYDIPEITEANLCNDSHEALSPCTQPVGNSGRPVEAFKTYPSTPAVPSKSVLFHFYEPDENFSLSDTGRTKSDTALAARESSEKSEVPRDTRSAGIKPYKENNSSNCAISKEAGLRRLIDKDRESFDKNLNQSFTNLTFPEPISDDSDSVEFQRDSLNNNWPASLEGSIHELPRNSDDDGIPASAAHILDLDYHRDSYDSPWKKFLPYPSILSDDSWKAPESWGTSLPTEAIPKQVFTTRFFARPSLGNRKKEFFLRVYRDDRTSVSFICPIGIQTHEVI... | 4.6.1.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; | adenylate cyclase-activating glucose-activated G protein-coupled receptor signaling pathway [GO:0010619]; cAMP biosynthetic process [GO:0006171]; intracellular signal transduction [GO:0035556]; negative regulation of induction of conjugation with cellular fusion [GO:0010515]; negative regulation of transcription by RNA... | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145] | PF00211;PF13855;PF00481; | 3.30.70.1230;3.60.40.10;3.80.10.10; | Adenylyl cyclase class-3 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16489217}. | CATALYTIC ACTIVITY: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; | null | null | null | null | FUNCTION: Plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP. | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P14607 | DDIT3_CRIGR | MAAESLPFTLETVSSWELEAWYEDLQEVLSSDENGGPYSSSLGNEEGESKTFTTLDPASLAWLTEEPGPAEVTSSSQSPRSPDSSQSCMAQEEEEDQGRTRKRKQSGQCPARGTGKQRMKEKEQENERKVAQLAEENERLKQEIERLTREVEATRPGSDRPHVNLQQV | null | null | apoptotic process [GO:0006915]; blood vessel maturation [GO:0001955]; cell cycle [GO:0007049]; endoplasmic reticulum unfolded protein response [GO:0030968]; ER overload response [GO:0006983]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; negative regulation of DNA-templ... | CHOP-ATF3 complex [GO:1990622]; CHOP-ATF4 complex [GO:1990617]; CHOP-C/EBP complex [GO:0036488]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | cAMP response element binding protein binding [GO:0008140]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region s... | null | 1.20.5.170; | BZIP family | PTM: Ubiquitinated, leading to its degradation by the proteasome. {ECO:0000250}.; PTM: Phosphorylation at serine residues by MAPK14 enhances its transcriptional activation activity while phosphorylation at serine residues by CK2 inhibits its transcriptional activation activity. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}. Note=Present in the cytoplasm under non-stressed conditions and ER stress leads to its nuclear accumulation. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Multifunctional transcription factor in ER stress response. Plays an essential role in the response to a wide variety of cell stresses and induces cell cycle arrest and apoptosis in response to ER stress. Plays a dual role both as an inhibitor of CCAAT/enhancer-binding protein (C/EBP) function and as an activ... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
P14611 | THIL_CUPNH | MTDVVIVSAARTAVGKFGGSLAKIPAPELGAVVIKAALERAGVKPEQVSEVIMGQVLTAGSGQNPARQAAIKAGLPAMVPAMTINKVCGSGLKAVMLAANAIMAGDAEIVVAGGQENMSAAPHVLPGSRDGFRMGDAKLVDTMIVDGLWDVYNQYHMGITAENVAKEYGITREAQDEFAVGSQNKAEAAQKAGKFDEEIVPVLIPQRKGDPVAFKTDEFVRQGATLDSMSGLKPAFDKAGTVTAANASGLNDGAAAVVVMSAAKAKELGLTPLATIKSYANAGVDPKVMGMGPVPASKRALSRAEWTPQDLDLMEINEAF... | 2.3.1.9 | null | fatty acid beta-oxidation [GO:0006635]; poly-hydroxybutyrate biosynthetic process [GO:0042619] | cytosol [GO:0005829] | acetyl-CoA C-acetyltransferase activity [GO:0003985] | PF02803;PF00108; | 3.40.47.10; | Thiolase-like superfamily, Thiolase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9; Evidence={ECO:0000255|PROSITE-ProRule:PRU10020, ECO:0000269|PubMed:25152395, ECO:0000269|PubMed:4198758}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=390 uM for acetyl-CoA {ECO:0000269|PubMed:4198758}; | PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate biosynthesis. {ECO:0000269|PubMed:2670936, ECO:0000269|PubMed:4198758}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.8 for the condensation reaction and 8.1 for the reverse cleavage reaction. {ECO:0000269|PubMed:4198758}; | null | FUNCTION: Catalyzes the condensation of two acetyl-coA units to form acetoacetyl-CoA (PubMed:4198758). Is involved in the biosynthesis of polyhydroxybutyrate (PHB), which is accumulated as an intracellular energy reserve material when cells grow under conditions of nutrient limitation (PubMed:2670936, PubMed:4198758). ... | Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha) |
P14615 | PA2N3_BUNFA | NLFQFKNMIQCAGTRSWTDYVSYGCYCGKGGSGTPVDQLDRCCKVHDDCYGDAEKIPKCKPYYKTYSYDCSEGKLTCKADNDECAAFICNCDRVAAICFAGAPYNDNNFMIDSKTRCNDI | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion. {ECO:0000250}; | arachidonic acid secretion [GO:0050482]; fatty acid biosynthetic process [GO:0006633]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]; positive regulation of fibroblast proliferation [GO:0048146] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | Bungarus fasciatus (Banded krait) (Pseudoboa fasciata) |
P14616 | INSRR_HUMAN | MAVPSLWPWGACLPVIFLSLGFGLDTVEVCPSLDIRSEVAELRQLENCSVVEGHLQILLMFTATGEDFRGLSFPRLTQVTDYLLLFRVYGLESLRDLFPNLAVIRGTRLFLGYALVIFEMPHLRDVALPALGAVLRGAVRVEKNQELCHLSTIDWGLLQPAPGANHIVGNKLGEECADVCPGVLGAAGEPCAKTTFSGHTDYRCWTSSHCQRVCPCPHGMACTARGECCHTECLGGCSQPEDPRACVACRHLYFQGACLWACPPGTYQYESWRCVTAERCASLHSVPGRASTFGIHQGSCLAQCPSGFTRNSSSIFCHKC... | 2.7.10.1 | null | actin cytoskeleton organization [GO:0030036]; cellular response to alkaline pH [GO:0071469]; male sex determination [GO:0030238]; protein autophosphorylation [GO:0046777]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | axon [GO:0030424]; insulin receptor complex [GO:0005899]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; insulin receptor activity [GO:0005009]; insulin receptor substrate binding [GO:0043560]; phosphatidylinositol 3-kinase binding [GO:0043548]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF00757;PF07714;PF01030; | 2.60.40.10;3.80.20.20;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily | PTM: Autophosphorylated on tyrosine residues between pH 7.9 and pH 10.5. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Receptor with tyrosine-protein kinase activity. Functions as a pH sensing receptor which is activated by increased extracellular pH. Activates an intracellular signaling pathway that involves IRS1 and AKT1/PKB. {ECO:0000269|PubMed:21641549}. | Homo sapiens (Human) |
P14617 | INSRR_CAVPO | MARPKLWPWGILLLVSLLSAGFNLDTMNVCPSLDIRSEVAELRRLENCSVVEGHLQILLMFTATGEDFRSLSFPHLTQVTDYLLLFRVYGLESLRDLFPNLAVIRGAHLFLGYALVIFEMPHLRDVGLPALGAVLHGSVRVEKNQELCHLSTIDWGLLQPTPSTNYIVGNKLGEECADVCPGTLGAAGEPCARTTFNGHTDYRCWTSSHCQRVCPCPQGLACTISGECCHTECLGGCSQPEDPRACVACRHFYYQSACHRACPLGTYEHESWRCVTAESCANLRSVPGRASTFGIHQGKCLAQCPPGFTRNGSSIFCHKC... | 2.7.10.1 | null | actin cytoskeleton organization [GO:0030036]; cellular response to alkaline pH [GO:0071469]; male sex determination [GO:0030238]; protein autophosphorylation [GO:0046777] | axon [GO:0030424]; insulin receptor complex [GO:0005899] | ATP binding [GO:0005524]; insulin receptor activity [GO:0005009]; insulin receptor substrate binding [GO:0043560]; phosphatidylinositol 3-kinase binding [GO:0043548]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF00757;PF07714;PF01030; | 2.60.40.10;3.80.20.20;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily | PTM: Autophosphorylated on tyrosine residues between pH 7.9 and pH 10.5. {ECO:0000250}. | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Receptor with tyrosine-protein kinase activity. Functions as a pH sensing receptor which is activated by increased extracellular pH. Activates an intracellular signaling pathway that involves IRS1 and AKT1/PKB (By similarity). {ECO:0000250}. | Cavia porcellus (Guinea pig) |
P14618 | KPYM_HUMAN | MSKPHSEAGTAFIQTQQLHAAMADTFLEHMCRLDIDSPPITARNTGIICTIGPASRSVETLKEMIKSGMNVARLNFSHGTHEYHAETIKNVRTATESFASDPILYRPVAVALDTKGPEIRTGLIKGSGTAEVELKKGATLKITLDNAYMEKCDENILWLDYKNICKVVEVGSKIYVDDGLISLQVKQKGADFLVTEVENGGSLGSKKGVNLPGAAVDLPAVSEKDIQDLKFGVEQDVDMVFASFIRKASDVHEVRKVLGEKGKNIKIISKIENHEGVRRFDEILEASDGIMVARGDLGIEIPAEKVFLAQKMMIGRCNRA... | 2.7.1.40; 2.7.10.2; 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:23530218}; COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000305|PubMed:23530218}; | canonical glycolysis [GO:0061621]; cellular response to insulin stimulus [GO:0032869]; glycolytic process [GO:0006096]; phosphorylation [GO:0016310]; positive regulation of cytoplasmic translation [GO:2000767]; positive regulation of sprouting angiogenesis [GO:1903672]; positive regulation of transcription by RNA polym... | cilium [GO:0005929]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular vesicle [GO:1903561]; ficolin-1-rich granule lumen [GO:1904813]; mitochondrion [GO:0005739]; nucleus [GO:0005634]... | ATP binding [GO:0005524]; cadherin binding [GO:0045296]; histone H3T11 kinase activity [GO:0035402]; magnesium ion binding [GO:0000287]; MHC class II protein complex binding [GO:0023026]; mRNA binding [GO:0003729]; potassium ion binding [GO:0030955]; protein homodimerization activity [GO:0042803]; protein tyrosine kina... | PF00224;PF02887; | 3.20.20.60;2.40.33.10;3.40.1380.20; | Pyruvate kinase family | PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: Under hypoxia, hydroxylated by EGLN3. {ECO:0000269|PubMed:21620138}.; PTM: Acetylation at Lys-305 is stimulated by high glucose concentration, it decreases enzyme activity and promotes its lysosomal-dependent degradation via chaperone-mediated autophagy. {ECO:0000269... | SUBCELLULAR LOCATION: [Isoform M2]: Cytoplasm {ECO:0000269|PubMed:25263439, ECO:0000269|PubMed:26787900, ECO:0000269|PubMed:27573352, ECO:0000269|PubMed:32268273}. Nucleus {ECO:0000269|PubMed:17308100, ECO:0000269|PubMed:18191611, ECO:0000269|PubMed:22056988, ECO:0000269|PubMed:22901803, ECO:0000269|PubMed:24120661, EC... | CATALYTIC ACTIVITY: [Isoform M2]: Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate; Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216; EC=2.7.1.40; Evidence={ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:1854723, ECO:0000269|PubMed:20847263}... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.7 mM for phosphoenolpyruvate (at 32 degrees Celsius, pH 8.0) {ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:1854723}; KM=0.17 mM for phosphoenolpyruvate (in the presence of 2 mM D-fructose 1,6-bisphosphate (FBP), at 32 degrees Celsius, pH 8.0) {ECO:0000269|PubM... | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5. {ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:1854723}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH for T3 binding is 6.0-6.5. Increase in pH causes T3 binding to drop, does not bind T3 above pH 9.0 or below pH 5.0. {ECO:0000269|PubMed:15996096, ECO:0000269|PubMed:1854723}; | null | FUNCTION: Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP (PubMed:15996096, PubMed:1854723, PubMed:20847263). The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether... | Homo sapiens (Human) |
P14625 | ENPL_HUMAN | MRALWVLGLCCVLLTFGSVRADDEVDVDGTVEEDLGKSREGSRTDDEVVQREEEAIQLDGLNASQIRELREKSEKFAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALSGNEELTVKIKCDKEKNLLHVTDTGVGMTREELVKNLGTIAKSGTSEFLNKMTEAQEDGQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHIWESDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIKNLVKKYSQFINFPIYVWSSKTETVEEPMEEEEAAKEEKEESDDEAAVEEEEEEKK... | null | null | actin rod assembly [GO:0031247]; cellular response to ATP [GO:0071318]; cellular response to manganese ion [GO:0071287]; DNA damage response [GO:0006974]; ERAD pathway [GO:0036503]; negative regulation of apoptotic process [GO:0043066]; protein folding [GO:0006457]; protein folding in endoplasmic reticulum [GO:0034975]... | collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; endocytic vesicle lumen [GO:0071682]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:00... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; calcium ion binding [GO:0005509]; low-density lipoprotein particle receptor binding [GO:0050750]; protein phosphatase binding [GO:0019903]; RNA binding [GO:0003723]; unfolded protein binding [GO:0051082... | PF13589;PF00183; | 3.30.230.80;3.40.50.11260;1.20.120.790;3.30.565.10; | Heat shock protein 90 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000305|PubMed:12475965}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P41148}. Melanosome {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000269|PubMed:... | null | null | null | null | null | FUNCTION: Molecular chaperone that functions in the processing and transport of secreted proteins (By similarity). When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD) (PubMed:18264092). Has ATPase activity (By s... | Homo sapiens (Human) |
P14630 | APOM_RAT | MFHQVWAALLYLYGLLFNSMNQCPEHSQLMTLGMDDKETPEPHLGLWYFIAGAAPTMEELATFDQVDNIVFNMAAGSAPRQLQLRATIRTKNGVCVPRKWTYHLTEGKGNTELRTEGRPDMKTDLFSISCPGGIMLKETGQGYQRFLLYNRSPHPPEECVEEFQSLTSCLDFKAFLVTPRNQEACPLSSK | null | null | cholesterol efflux [GO:0033344]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein particle clearance [GO:0034384]; high-density lipoprotein particle remodeling [GO:0034375]; lipoprotein metabolic process [GO:0042157]; negative regulation of plasma lipoprotein oxidation [GO:0034445]; res... | discoidal high-density lipoprotein particle [GO:0034365]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; low-density lipoprotein particle [GO:0034362]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [G... | antioxidant activity [GO:0016209]; lipid transporter activity [GO:0005319]; phospholipid binding [GO:0005543] | PF11032; | 2.40.128.20; | Calycin superfamily, Lipocalin family | null | SUBCELLULAR LOCATION: Secreted. Note=Associated with HDL. | null | null | null | null | null | FUNCTION: Probably involved in lipid transport. Can bind sphingosine-1-phosphate, myristic acid, palmitic acid and stearic acid, retinol, all-trans-retinoic acid and 9-cis-retinoic acid (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
P14632 | TRFL_PIG | MKLFIPALLFLGTLGLCLAAPKKGVRWCVISTAEYSKCRQWQSKIRRTNPMFCIRRASPTDCIRAIAAKRADAVTLDGGLVFEADQYKLRPVAAEIYGTEENPQTYYYAVAVVKKGFNFQLNQLQGRKSCHTGLGRSAGWNIPIGLLRRFLDWAGPPEPLQKAVAKFFSQSCVPCADGNAYPNLCQLCIGKGKDKCACSSQEPYFGYSGAFNCLHKGIGDVAFVKESTVFENLPQKADRDKYELLCPDNTRKPVEAFRECHLARVPSHAVVARSVNGKENSIWELLYQSQKKFGKSNPQEFQLFGSPGQQKDLLFRDATI... | 3.4.21.- | null | antibacterial humoral response [GO:0019731]; antifungal humoral response [GO:0019732]; bone morphogenesis [GO:0060349]; innate immune response in mucosa [GO:0002227]; iron ion transport [GO:0006826]; negative regulation of apoptotic process [GO:0043066]; negative regulation of lipopolysaccharide-mediated signaling path... | early endosome [GO:0005769]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; specific granule [GO:0042581] | iron ion binding [GO:0005506]; serine-type endopeptidase activity [GO:0004252] | PF00405; | 3.40.190.10; | Transferrin family | PTM: Poly-N-acetyllactosaminic carbohydrate moiety seems to be needed for TLR4 activation. {ECO:0000250|UniProtKB:P02788}. | SUBCELLULAR LOCATION: Secreted. Cytoplasmic granule {ECO:0000250}. Note=Secreted into most exocrine fluids by various endothelial cells. Stored in the secondary granules of neutrophils (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. {ECO:0000250|UniProtKB:P02788}.; FUNCTION: [Lactotransferrin]: Major iron-binding and multifunctional protein found in exocrine fluids such as breast milk and mucos... | Sus scrofa (Pig) |
P14635 | CCNB1_HUMAN | MALRVTRNSKINAENKAKINMAGAKRVPTAPAATSKPGLRPRTALGDIGNKVSEQLQAKMPMKKEAKPSATGKVIDKKLPKPLEKVPMLVPVPVSEPVPEPEPEPEPEPVKEEKLSPEPILVDTASPSPMETSGCAPAEEDLCQAFSDVILAVNDVDAEDGADPNLCSEYVKDIYAYLRQLEEEQAVRPKYLLGREVTGNMRAILIDWLVQVQMKFRLLQETMYMTVSIIDRFMQNNCVPKKMLQLVGVTAMFIASKYEEMYPPEIGDFAFVTDNTYTKHQIRQMEMKILRALNFGLGRPLPLHFLRRASKIGEVDVEQH... | null | null | cell division [GO:0051301]; G2/M transition of mitotic cell cycle [GO:0000086]; in utero embryonic development [GO:0001701]; mitotic cell cycle phase transition [GO:0044772]; mitotic metaphase chromosome alignment [GO:0007080]; mitotic spindle organization [GO:0007052]; positive regulation of attachment of spindle micr... | centrosome [GO:0005813]; cyclin B1-CDK1 complex [GO:0097125]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; mitochondrial matrix [GO:0005759]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; outer kinetochore [GO:0000940]; spindle pole [GO:0000922] | cyclin-dependent protein serine/threonine kinase activator activity [GO:0061575]; cyclin-dependent protein serine/threonine kinase regulator activity [GO:0016538]; patched binding [GO:0005113]; protein kinase binding [GO:0019901]; ubiquitin-like protein ligase binding [GO:0044389] | PF02984;PF00134; | 1.10.472.10; | Cyclin family, Cyclin AB subfamily | PTM: Ubiquitinated by the SCF(NIPA) complex during interphase, leading to its destruction (PubMed:16009132). Deubiquitinated by USP22 during G2/M phase (PubMed:27030811). {ECO:0000269|PubMed:16009132, ECO:0000269|PubMed:27030811}.; PTM: Phosphorylated by PLK1 at Ser-133 on centrosomes during prophase: phosphorylation b... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. | null | null | null | null | null | FUNCTION: Essential for the control of the cell cycle at the G2/M (mitosis) transition. {ECO:0000269|PubMed:17495531, ECO:0000269|PubMed:17495533, ECO:0000269|PubMed:27030811}. | Homo sapiens (Human) |
P14640 | TBA1_MAIZE | MRECISIHIGQAGIQVGNACWELYCLEHGIQADGQMPGDKTIGGGDDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQVSTSVVEPYNSVLSTHSLLEHTDVAILLDNEAIYDICRRSLDIERPTYTNLNRLVSQVISSLTASLRFDGALNVDVNEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAFEPSSMMAKCDPRHGKYMACCLMYR... | 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: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000250}.; PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects ... | 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... | Zea mays (Maize) |
P14641 | TBA2_MAIZE | MRECISIHIGQAGIQVGNACWELYCLEHGIQADGQMPGDKTIGGGDDAFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRIRKLADNCTGLQGFLVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTVYPSPQVSTSVVEPYNSVLSTHSLLEHTDVAILLDNEAIYDICRRSLDIERPTYTNLNRLVSQVISSLTASLRFDGALNVDVNEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQLSVAEITNSAFEPSSMMAKCDPRHGKYMACCLMYR... | 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: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000250}.; PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects ... | 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... | Zea mays (Maize) |
P14646 | PDE4B_RAT | MKKSRSVMAVTADDNLKDYFECSLSKSYSSSSYTLGIDLWRGRRCCSGNLQLPPLSQRQSERARTPEGDGISRPTTLPLTTLPSIAITTVSQECFDVENGPSPGRSPLDPQASSSSGLVLHAAFPGHSQRRESFLYRSDSDYDLSPKAMSRNSSLPSEQHGDDLIVTPFAQVLASLRIVRNNFTLLTNLHGAPNKRSPAASQAPVTRVSLQEESYQKLAMETLEELDWCLDQLETIQTYRSVSEMASNKFKRMLNRELTHLSEMSRSGNQVSEYISNTFLDKQNDVEIPSPTQKDREKKKKQQLMTQISGVKKLMHSSSL... | 3.1.4.53 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q07343}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions. {ECO:0000250|UniProtKB:Q07343}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q07343}; Name=Mn(2+); Xref=ChE... | cAMP catabolic process [GO:0006198]; cAMP-mediated signaling [GO:0019933]; cellular response to epinephrine stimulus [GO:0071872]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to xenobiotic stimulus [GO:0071466]; leukocyte migration [GO:0050900]; negative regulation of adenylate cyclase-activ... | cell periphery [GO:0071944]; centrosome [GO:0005813]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; excitatory synapse [GO:0060076]; gamma-tubulin complex [GO:0000930]; membrane [GO:0016020]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; postsynaptic density [GO:0014069]; synaptic vesicle [G... | 3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; calcium channel regulator activity [GO:0005246]; cAMP binding [GO:0030552]; gamma-tubulin binding [GO:0043015]; metal ion binding [GO:0046872]; transmembrane transporter binding [GO:0044325] | PF18100;PF00233; | 1.10.1300.10; | Cyclic nucleotide phosphodiesterase family, PDE4 subfamily | null | SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm {ECO:0000250|UniProtKB:Q07343}. Cell membrane {ECO:0000250|UniProtKB:Q07343}. | CATALYTIC ACTIVITY: Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165, ChEBI:CHEBI:456215; EC=3.1.4.53; Evidence={ECO:0000269|PubMed:12441002}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25278; Evidence={ECO:0000305|PubMed:12441002}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.4 uM for cAMP {ECO:0000269|PubMed:12441002}; Note=Vmax values for isoforms 2, 3 and 4 relative to isoform 1 are 3.8, 1.6 and 2.1. {ECO:0000269|PubMed:12441002}; | PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1. {ECO:0000305|PubMed:12441002}. | null | null | FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. {ECO:0000269|PubMed:12441002}. | Rattus norvegicus (Rat) |
P14647 | RDRP_BPQBE | MSKTASSRNSLSAQLRRAANTRIEVEGNLALSIANDLLLAYGQSPFNSEAECISFSPRFDGTPDDFRINYLKAEIMSKYDDFSLGIDTEAVAWEKFLAAEAECALTNARLYRPDYSEDFNFSLGESCIHMARRKIAKLIGDVPSVEGMLRHCRFSGGATTTNNRSYGHPSFKFALPQACTPRALKYVLALRASTHFDIRISDISPFNKAVTVPKNSKTDRCIAIEPGWNMFFQLGIGGILRDRLRCWGIDLNDQTINQRRAHEGSVTNNLATVDLSAASDSISLALCELLLPPGWFEVLMDLRSPKGRLPDGSVVTYEKI... | 2.7.7.48 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418}; Note=Binds 2 Mg(2+) per subunit, Ca(2+) is used in crystallization to prevent RNA polymerase activity. {ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970, ECO:0000269|P... | viral RNA genome replication [GO:0039694] | null | metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968] | PF03431; | null | null | null | null | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539, ECO:0000269|PubMed:22245970}; | null | null | null | null | FUNCTION: This is the catalytic subunit of the viral RNA-dependent RNA polymerase complex. This complex is involved in viral RNA replication that produces (+)-stranded genomes via a complementary, (-)-stranded intermediate. Binds RNA cooperatively with the host ribosomal protein S1. {ECO:0000269|PubMed:20534494, ECO:00... | Escherichia virus Qbeta (Bacteriophage Q-beta) |
P14649 | MYL6B_HUMAN | MPPKKDVPVKKPAGPSISKPAAKPAAAGAPPAKTKAEPAVPQAPQKTQEPPVDLSKVVIEFNKDQLEEFKEAFELFDRVGDGKILYSQCGDVMRALGQNPTNAEVLKVLGNPKSDELKSRRVDFETFLPMLQAVAKNRGQGTYEDYLEGFRVFDKEGNGKVMGAELRHVLTTLGEKMTEEEVETVLAGHEDSNGCINYEAFLKHILSV | null | null | muscle contraction [GO:0006936]; muscle filament sliding [GO:0030049]; skeletal muscle tissue development [GO:0007519] | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; muscle myosin complex [GO:0005859]; myosin complex [GO:0016459]; myosin II complex [GO:0016460]; unconventional myosin complex [GO:0016461] | calcium ion binding [GO:0005509]; cytoskeletal motor activity [GO:0003774]; 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. | Homo sapiens (Human) |
P14650 | PERT_RAT | MRTLGAMAVMLVVMGTAIFLPFLLRSRDILGGKTMTSHVISVVETSQLLVDNAVYNTMKRNLKKRGVLSPAQLLSFSKLPESTSGAISRAAEIMETSIQVMKREQSQFSTDALSADILATIANLSGCLPFMLPPRCPDTCLANKYRPITGVCNNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNPNFLYHGFPLPPVREVTRHLIQVSNEAVTEDDQYSDFLPVWGQYIDHDIALTPQSTSTAAFWGGVDCQLTCENQNPCFPIQLPSNSSRTTACLPFYRSSAACGTGDQGALFGNLSAANPRQQMNGLTSFLDAST... | 1.11.1.8 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX... | cellular response to nitric oxide [GO:0071732]; embryonic hemopoiesis [GO:0035162]; hormone biosynthetic process [GO:0042446]; hydrogen peroxide catabolic process [GO:0042744]; response to lipid [GO:0033993]; response to oxidative stress [GO:0006979]; thyroid hormone generation [GO:0006590] | cell surface [GO:0009986]; extracellular space [GO:0005615]; membrane [GO:0016020] | calcium ion binding [GO:0005509]; heme binding [GO:0020037]; iodide peroxidase activity [GO:0004447]; peroxidase activity [GO:0004601] | PF03098;PF07645;PF00084; | 2.10.70.10;1.10.640.10;2.10.25.10; | Peroxidase family, XPO subfamily | PTM: Heme is covalently bound through a H(2)O(2)-dependent autocatalytic process. Heme insertion is important for the delivery of protein at the cell surface (By similarity). {ECO:0000250}.; PTM: Cleaved in its N-terminal part. {ECO:0000250}. | SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O2 + 2 iodide = diiodine + 2 H2O; Xref=Rhea:RHEA:23336, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:17606; EC=1.11.1.8; Evidence={ECO:0000250|UniProtKB:P09933}; CATALYTIC ACTIVITY: Reaction=[thyroglobulin]-L-tyrosine + H(+) + H2O2 + iod... | null | PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis. | null | null | FUNCTION: Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4). {ECO:0000250|UniProtKB:P09933}. | Rattus norvegicus (Rat) |
P14651 | HXB3_HUMAN | MQKATYYDNAAAALFGGYSSYPGSNGFGFDVPPQPPFQAATHLEGDYQRSACSLQSLGNAAPHAKSKELNGSCMRPGLAPEPLSAPPGSPPPSAAPTSATSNSSNGGGPSKSGPPKCGPGTNSTLTKQIFPWMKESRQTSKLKNNSPGTAEGCGGGGGGGGGGGSGGSGGGGGGGGGGDKSPPGSAASKRARTAYTSAQLVELEKEFHFNRYLCRPRRVEMANLLNLSERQIKIWFQNRRMKYKKDQKAKGLASSSGGPSPAGSPPQPMQSTAGFMNALHSMTPSYESPSPPAFGKAHQNAYALPSNYQPPLKGCGAPQK... | null | null | angiogenesis [GO:0001525]; anterior/posterior pattern specification [GO:0009952]; cartilage development [GO:0051216]; definitive hemopoiesis [GO:0060216]; embryonic skeletal system morphogenesis [GO:0048704]; face development [GO:0060324]; glossopharyngeal nerve morphogenesis [GO:0021615]; hematopoietic progenitor cell... | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF13293;PF00046; | 1.10.10.60; | Antp homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. | Homo sapiens (Human) |
P14652 | HXB2_HUMAN | MNFEFEREIGFINSQPSLAECLTSFPAVLETFQTSSIKESTLIPPPPPFEQTFPSLQPGASTLQRPRSQKRAEDGPALPPPPPPPLPAAPPAPEFPWMKEKKSAKKPSQSATSPSPAASAVPASGVGSPADGLGLPEAGGGGARRLRTAYTNTQLLELEKEFHFNKYLCRPRRVEIAALLDLTERQVKVWFQNRRMKHKRQTQHREPPDGEPACPGALEDICDPAEEPAASPGGPSASRAAWEACCHPPEVVPGALSADPRPLAVRLEGAGASSPGCALRGAGGLEPGPLPEDVFSGRQDSPFLPDLNFFAADSCLQLSG... | null | null | anterior/posterior pattern specification [GO:0009952]; dorsal/ventral pattern formation [GO:0009953]; embryonic skeletal system morphogenesis [GO:0048704]; facial nerve structural organization [GO:0021612]; morphogenesis of an epithelial sheet [GO:0002011]; nervous system development [GO:0007399]; neural nucleus develo... | chromatin [GO:0000785]; nucleoplasm [GO:0005654] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific dou... | PF00046; | 1.10.10.60; | Antp homeobox family, Proboscipedia subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. {ECO:0000269|PubMed:10595394}. | Homo sapiens (Human) |
P14653 | HXB1_HUMAN | MDYNRMNSFLEYPLCNRGPSAYSAHSAPTSFPPSSAQAVDSYASEGRYGGGLSSPAFQQNSGYPAQQPPSTLGVPFPSSAPSGYAPAACSPSYGPSQYYPLGQSEGDGGYFHPSSYGAQLGGLSDGYGAGGAGPGPYPPQHPPYGNEQTASFAPAYADLLSEDKETPCPSEPNTPTARTFDWMKVKRNPPKTAKVSEPGLGSPSGLRTNFTTRQLTELEKEFHFNKYLSRARRVEIAATLELNETQVKIWFQNRRMKQKKREREEGRVPPAPPGCPKEAAGDASDQSTCTSPEASPSSVTS | null | null | anatomical structure formation involved in morphogenesis [GO:0048646]; anterior/posterior pattern specification [GO:0009952]; embryonic skeletal system morphogenesis [GO:0048704]; facial nerve structural organization [GO:0021612]; facial nucleus development [GO:0021754]; pattern specification process [GO:0007389]; posi... | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein domain specific binding [GO:0019904]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:000... | PF00046; | 1.10.10.60; | Antp homeobox family, Labial subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis. Acts on the anterior body structures. | Homo sapiens (Human) |
P14654 | GLN12_ORYSJ | MANLTDLVNLNLSDCSDKIIAEYIWVGGSGIDLRSKARTVKGPITDVSQLPKWNYDGSSTGQAPGEDSEVILYPQAIFKDPFRRGDNILVMCDCYTPQGEPIPTNKRHSAAKIFSHPDVVAEVPWYGIEQEYTLLQKDVNWPLGWPVGGFPGPQGPYYCAAGAEKAFGRDIVDAHYKACIYAGINISGINGEVMPGQWEFQVGPSVGIAAADQVWVARYILERVTEVAGVVLSLDPKPIPGDWNGAGAHTNFSTKSMREPGGYEVIKKAIDKLALRHKEHIAAYGEGNERRLTGRHETADINTFKWGVANRGASIRVGRD... | 6.3.1.2 | null | glutamine biosynthetic process [GO:0006542] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; glutamine synthetase activity [GO:0004356] | PF00120;PF03951; | 3.10.20.70;3.30.590.10; | Glutamine synthetase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000269|PubMed:15574840}; PhysiologicalDir... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.1 mM for glutamate {ECO:0000269|PubMed:15574840}; KM=73 uM for ammonium {ECO:0000269|PubMed:15574840}; KM=530 uM for ATP {ECO:0000269|PubMed:15574840}; Vmax=94.7 nmol/sec/mg enzyme with glutamate as substrate {ECO:0000269|PubMed:15574840}; Vmax=98.1 nmol/sec/mg e... | null | null | null | FUNCTION: High-affinity glutamine synthetase involved in ammonium assimilation (Probable). Plays an important role in the primary assimilation of ammonium taken up by roots (PubMed:23509111). Plays a role in maintaining nitrogen metabolic balance during ammonium assimilation, thus controlling plant growth and developme... | Oryza sativa subsp. japonica (Rice) |
P14655 | GLNA2_ORYSJ | MAQAVVPAMQCQVGAVRARPAAAAAAAGGRVWGVRRTGRGTSGFRVMAVSTETTGVVTRMEQLLNMDTTPFTDKIIAEYIWVGGTGIDLRSKSRTISKPVEDPSELPKWNYDGSSTGQAPGEDSEVILYPQAIFKDPFRGGNNILVMCDTYTPAGEPIPTNKRNRAAQVFSDPKVVSQVPWFGIEQEYTLLQRDVNWPLGWPVGGYPGPQGPYYCAVGSDKSFGRDISDAHYKACLYAGINISGTNGEVMPGQWEYQVGPSVGIEAGDHIWISRYILERITEQAGVVLTLDPKPIQGDWNGAGCHTNYSTKSMREDGGFE... | 6.3.1.2 | null | glutamine biosynthetic process [GO:0006542]; response to cadmium ion [GO:0046686] | chloroplast [GO:0009507]; cytoplasm [GO:0005737]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; glutamine synthetase activity [GO:0004356]; mRNA binding [GO:0003729] | PF00120;PF03951; | 3.10.20.70;3.30.590.10; | Glutamine synthetase family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000250|UniProtKB:P14656}; PhysiologicalDi... | null | null | null | null | FUNCTION: Light-modulated chloroplastic glutamine synthetase, encoded by a nuclear gene and expressed primarily in leaves, and which is responsible for the reassimilation of the ammonia generated by photorespiration. {ECO:0000269|PubMed:10949377}. | Oryza sativa subsp. japonica (Rice) |
P14656 | GLN11_ORYSJ | MASLTDLVNLNLSDTTEKIIAEYIWIGGSGMDLRSKARTLSGPVTDPSKLPKWNYDGSSTGQAPGEDSEVILYPQAIFKDPFRKGNNILVMCDCYTPAGEPIPTNKRHNAAKIFSSPEVASEEPWYGIEQEYTLLQKDINWPLGWPVGGFPGPQGPYYCGIGADKSFGRDIVDSHYKACLYAGINISGINGEVMPGQWEFQVGPSVGISAGDQVWVARYILERITEIAGVVVSFDPKPIPGDWNGAGAHTNYSTKSMRNDGGYEIIKSAIEKLKLRHKEHISAYGEGNERRLTGRHETADINTFSWGVANRGASVRVGRE... | 6.3.1.2 | null | glutamine biosynthetic process [GO:0006542] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; glutamine synthetase activity [GO:0004356] | PF00120;PF03951; | 3.10.20.70;3.30.590.10; | Glutamine synthetase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine + phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2; Evidence={ECO:0000269|PubMed:15574840}; PhysiologicalDir... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.9 mM for glutamate {ECO:0000269|PubMed:15574840}; KM=27 uM for ammonium {ECO:0000269|PubMed:15574840}; KM=450 uM for ATP {ECO:0000269|PubMed:15574840}; Vmax=190 nmol/sec/mg enzyme with glutamate as substrate {ECO:0000269|PubMed:15574840}; Vmax=186.3 nmol/sec/mg e... | null | null | null | FUNCTION: High-affinity glutamine synthetase involved in ammonium assimilation (PubMed:15918879, PubMed:21255162). Seems to be a major component of the cytosolic glutamine synthetic pathway in leaf blades (PubMed:15918879, PubMed:21255162). Plays an important role in maintaining carbon and nitrogen metabolic balance du... | Oryza sativa subsp. japonica (Rice) |
P14659 | HSP72_RAT | MSARGPAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTIFDAKRLIGRKFEDATVQSDMKHWPFRVVSEGGKPKVQVEYKGEMKTFFPEEISSMVLTKMKEIAEAYLGGKVQSAVITVPAYFNDSQRQATKDAGTITGLNVLRIINEPTAAAIAYGLDKKGCAGGEKNVLIFDLGGGTFDVSILTIEDGIFEVKSTAGDTHLGGEDFDNRMVSHLAEEFKRKHKKDIGPNKRAVRRLRTACERAKRTLSSSTQASIEIDSLYEGVDFYTSITRARFEELNADLFRGTLEPV... | null | null | chaperone cofactor-dependent protein refolding [GO:0051085]; male meiosis I [GO:0007141]; male meiotic nuclear division [GO:0007140]; negative regulation of inclusion body assembly [GO:0090084]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; positive regulation of protein phosphorylation [GO... | CatSper complex [GO:0036128]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; male germ cell nucleus [GO:0001673]; meiotic spindle [GO:0072687]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; synaptonemal complex [GO:0000795] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein folding chaperone [GO:0140662]; disordered domain specific binding [GO:0097718]; enzyme binding [GO:0019899]; glycolipid binding [GO:0051861]; heat shock protein binding [GO:0031072]; protein folding chaperone [GO:0044183]; protein-fo... | PF00012; | 1.20.1270.10;3.30.30.30;3.30.420.40; | Heat shock protein 70 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P17156}. Note=Colocalizes with SHCBP1L at spindle during the meiosis process. {ECO:0000250|UniProtKB:P17156}. | null | null | null | null | null | FUNCTION: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in th... | Rattus norvegicus (Rat) |
P14660 | PSBA_SYNY4 | MTTTLQQRESASLWEQFCQWVTSTNNRIYVGWFGTLMIPTLLTATTCFIIAFIAAPPVDIDGIREPVAGSLLYGNNIISGAVVPSSNAIGLHFYPIWEAASLDEWLYNGGPYQLVVFQFLIGIFCYMGRQWELSYRLGMRPWICVAYSAPVSARTAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLVRETTEVESQNYGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLGAWPVIGIWFTAMGVSTMAFNLNGFNFNQSILDSQGRVIGTWADV... | 1.10.3.9 | COFACTOR: Note=The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster o... | photosynthetic electron transport in photosystem II [GO:0009772]; response to herbicide [GO:0009635] | photosystem II [GO:0009523]; plasma membrane-derived thylakoid membrane [GO:0031676] | chlorophyll binding [GO:0016168]; electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity [GO:0045156]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor [GO:0016682]; oxygen evolv... | PF00124; | 1.20.85.10; | Reaction center PufL/M/PsbA/D family | PTM: Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or Y-Z. {ECO:0000255|HAMAP-Rule:MF_01379}.; PTM: C-terminally processed by CtpA; processing is essential to allow assembly of the oxygen-evolving complex and thus photosynthetic growth. {ECO:0000255|HAMAP-Rule:MF_01379}. | SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01379}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01379}. | CATALYTIC ACTIVITY: Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2; Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757, ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01379}; | null | null | null | null | FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that conver... | Synechocystis sp. (strain PCC 6714) (Aphanocapsa sp. (strain PCC 6714)) |
P14668 | ANXA5_RAT | MALRGTVTDFSGFDGRADAEVLRKAMKGLGTDEDSILNLLTARSNAQRQQIAEEFKTLFGRDLVNDMKSELTGKFEKLIVALMKPSRLYDAYELKHALKGAGTDEKVLTEIIASRTPEELRAIKQAYEEEYGSNLEDDVVGDTSGYYQRMLVVLLQANRDPDTAIDDAQVELDAQALFQAGELKWGTDEEKFITILGTRSVSHLRRVFDKYMTISGFQIEETIDRETSGNLENLLLAVVKSIRSIPAYLAETLYYAMKGAGTDDHTLIRVIVSRSEIDLFNIRKEFRKNFATSLYSMIKGDTSGDYKKALLLLCGGEDD | null | null | blood coagulation [GO:0007596]; cellular response to gonadotropin-releasing hormone [GO:0097211]; cellular response to lead ion [GO:0071284]; negative regulation of blood coagulation [GO:0030195]; negative regulation of prolactin secretion [GO:1902721]; positive regulation of apoptotic process [GO:0043065]; regulation ... | axon terminus [GO:0043679]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; endothelial microparticle [GO:0072563]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; intercalated disc [GO:0014704]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; sarc... | calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; identical protein binding [GO:0042802]; P-type calcium transporter activity [GO:0005388]; peptide hormone binding [GO:0017046]; phosphatidylserine binding [GO:0001786]; receptor tyrosine kinase binding [GO:0030971] | PF00191; | 1.10.220.10; | Annexin family | PTM: S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex. {ECO:0000250|UniProtKB:P08758}. | null | null | null | null | null | null | FUNCTION: This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. | Rattus norvegicus (Rat) |
P14669 | ANXA3_RAT | MAASLWVGPRGTINNYPGFNPSVDAEAIRKAIKGIGTDEKTLINILTERSNAQRQLIVKQYQEAYEQALKADLKGDLSGHFEHVMVALITAPAVFDAKQLKKSMRGMGTDEDTLIEILTTRTSRQMKEISQAYYTAYKKNLRDDISSETSGDFRKALLTLADGGRDESLKVDEHLAKKDAQTLYDAGEKKWGTDEDKFTEILCLRSFPQLKLTFDEYRNISQKDIEDSIKGELSGHFEDLLLAVVRCTRNTPAFLAGRLHQALKGAGTDEFTLNRIMVSRSEIDLLDIRREFKKHYGCSLYSAIQSDTSGDYRTVLLKIC... | null | null | animal organ regeneration [GO:0031100]; defense response to bacterium [GO:0042742]; hippocampus development [GO:0021766]; neutrophil degranulation [GO:0043312]; phagocytosis [GO:0006909]; positive regulation of angiogenesis [GO:0045766]; positive regulation of DNA metabolic process [GO:0051054]; positive regulation of ... | axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; phagocytic vesicle membrane [GO:0030670]; plasma membrane [GO:0005886]; specific granule [GO:0042581] | calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; phosphatidylserine binding [GO:0001786]; phospholipase A2 inhibitor activity [GO:0019834] | PF00191; | 1.10.220.10; | Annexin family | null | null | null | null | null | null | null | FUNCTION: Inhibitor of phospholipase A2, also possesses anti-coagulant properties. | Rattus norvegicus (Rat) |
P14672 | GLUT4_HUMAN | MPSGFQQIGSEDGEPPQQRVTGTLVLAVFSAVLGSLQFGYNIGVINAPQKVIEQSYNETWLGRQGPEGPSSIPPGTLTTLWALSVAIFSVGGMISSFLIGIISQWLGRKRAMLVNNVLAVLGGSLMGLANAAASYEMLILGRFLIGAYSGLTSGLVPMYVGEIAPTHLRGALGTLNQLAIVIGILIAQVLGLESLLGTASLWPLLLGLTVLPALLQLVLLPFCPESPRYLYIIQNLEGPARKSLKRLTGWADVSGVLAELKDEKRKLERERPLSLLQLLGSRTHRQPLIIAVVLQLSQQLSGINAVFYYSTSIFETAGVG... | null | null | amylopectin biosynthetic process [GO:0010021]; brown fat cell differentiation [GO:0050873]; carbohydrate metabolic process [GO:0005975]; cellular response to hypoxia [GO:0071456]; cellular response to insulin stimulus [GO:0032869]; cellular response to osmotic stress [GO:0071470]; cellular response to tumor necrosis fa... | clathrin-coated pit [GO:0005905]; clathrin-coated vesicle [GO:0030136]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; insulin-responsive compartment [GO:0032593]; membrane [GO:0016020]... | D-glucose transmembrane transporter activity [GO:0055056]; glucose transmembrane transporter activity [GO:0005355]; glucose uniporter activity [GO:0015304] | PF00083; | 1.20.1250.20; | Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family, Glucose transporter subfamily | PTM: Sumoylated. {ECO:0000269|PubMed:11842083}.; PTM: Palmitoylated (PubMed:28057756). Palmitoylation by ZDHHC7 controls the insulin-dependent translocation of GLUT4 to the plasma membrane (PubMed:28057756). {ECO:0000269|PubMed:28057756}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P14142}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P14142}. Endomembrane system {ECO:0000269|PubMed:8300557}; Multi-pass membrane protein {ECO:0000269|PubMed:8300557}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P14142}. Note=Localizes primari... | CATALYTIC ACTIVITY: Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376, ChEBI:CHEBI:4167; Evidence={ECO:0000250|UniProtKB:P19357}; | null | null | null | null | FUNCTION: Insulin-regulated facilitative glucose transporter, which plays a key role in removal of glucose from circulation. Response to insulin is regulated by its intracellular localization: in the absence of insulin, it is efficiently retained intracellularly within storage compartments in muscle and fat cells. Upon... | Homo sapiens (Human) |
P14678 | RSMB_HUMAN | MTVGKSSKMLQHIDYRMRCILQDGRIFIGTFKAFDKHMNLILCDCDEFRKIKPKNSKQAEREEKRVLGLVLLRGENLVSMTVEGPPPKDTGIARVPLAGAAGGPGIGRAAGRGIPAGVPMPQAPAGLAGPVRGVGGPSQQVMTPQGRGTVAAAAAAATASIAGAPTQYPPGRGGPPPPMGRGAPPPGMMGPPPGMRPPMGPPMGIPPGRGTPMGMPPPGMRPPPPGMRGPPPPGMRPPRP | null | null | 7-methylguanosine cap hypermethylation [GO:0036261]; mRNA splicing, via spliceosome [GO:0000398]; protein methylation [GO:0006479]; RNA splicing [GO:0008380]; spliceosomal snRNP assembly [GO:0000387]; U2-type prespliceosome assembly [GO:1903241] | catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; histone pre-mRNA 3'end processing complex [GO:0071204]; methylosome [GO:0034709]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; small nuclear ribonucleoprotein complex [GO:0030532]; SMN-Sm protein complex [GO:0034719]; spliceosom... | histone pre-mRNA DCP binding [GO:0071208]; RNA binding [GO:0003723]; telomerase RNA binding [GO:0070034]; U1 snRNP binding [GO:1990446]; U2 snRNP binding [GO:1990447] | PF01423; | 2.30.30.100; | SnRNP SmB/SmN family | PTM: Methylated by PRMT5 (By similarity). Arg-108 and Arg-112 are dimethylated, probably to asymmetric dimethylarginine (PubMed:16087681, Ref.10). {ECO:0000250|UniProtKB:P27048, ECO:0000269|PubMed:16087681, ECO:0000269|Ref.10}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18984161}. Nucleus {ECO:0000269|PubMed:11574479, ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166}. Note=SMN-mediated assembly into core snRNPs occurs in the cytoso... | null | null | null | null | null | FUNCTION: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (PubMed:11991638, PubMed:18984161, PubMed:19325628, PubMed:25555158, PubMed:26912367, PubMed:28076346, PubMed:28502770, PubMed:28781166,... | Homo sapiens (Human) |
P14679 | TYRO_HUMAN | MLLAVLYCLLWSFQTSAGHFPRACVSSKNLMEKECCPPWSGDRSPCGQLSGRGSCQNILLSNAPLGPQFPFTGVDDRESWPSVFYNRTCQCSGNFMGFNCGNCKFGFWGPNCTERRLLVRRNIFDLSAPEKDKFFAYLTLAKHTISSDYVIPIGTYGQMKNGSTPMFNDINIYDLFVWMHYYVSMDALLGGSEIWRDIDFAHEAPAFLPWHRLFLLRWEQEIQKLTGDENFTIPYWDWRDAEKCDICTDEYMGGQHPTNPNLLSPASFFSSWQIVCSRLEEYNSHQSLCNGTPEGPLRRNPGNHDKSRTPRLPSSADVEF... | 1.14.18.1 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:Q9ZP19}; Note=Binds 2 copper ions per subunit. {ECO:0000250|UniProtKB:Q9ZP19}; | cell population proliferation [GO:0008283]; eye pigment biosynthetic process [GO:0006726]; melanin biosynthetic process [GO:0042438]; melanin biosynthetic process from tyrosine [GO:0006583]; pigmentation [GO:0043473]; response to blue light [GO:0009637]; response to cAMP [GO:0051591]; response to UV [GO:0009411]; respo... | cytoplasm [GO:0005737]; Golgi-associated vesicle [GO:0005798]; intracellular membrane-bounded organelle [GO:0043231]; lysosome [GO:0005764]; melanosome [GO:0042470]; melanosome membrane [GO:0033162]; perinuclear region of cytoplasm [GO:0048471] | copper ion binding [GO:0005507]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; tyrosinase activity [GO:0004503] | PF00264; | 1.10.1280.10; | Tyrosinase family | PTM: Glycosylated. {ECO:0000250|UniProtKB:P11344}. | SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}; Single-pass type I membrane protein {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}. Melanosome {ECO:0000250|UniProtKB:P11344}. Note=Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RA... | CATALYTIC ACTIVITY: Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; Xref=Rhea:RHEA:34287, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504, ChEBI:CHEBI:57924; EC=1.14.18.1; Evidence={ECO:0000269|PubMed:28661582}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:34288; Evidence={ECO:0000305|PubMed:28661582}... | null | null | null | null | FUNCTION: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the initial and rate limiting step in the cascade of reactions leading to melanin production from tyrosine (By similarity). In addition to hydroxylating tyrosine to DOPA... | Homo sapiens (Human) |
P14680 | YAK1_YEAST | MNSSNNNDSSSSNSNMNNSLSPTLVTHSDASMGSGRASPDNSHMGRGIWNPSYVNQGSQRSPQQQHQNHHQQQQQQQQQQQQNSQFCFVNPWNEEKVTNSQQNLVYPPQYDDLNSNESLDAYRRRKSSLVVPPARAPAPNPFQYDSYPAYTSSNTSLAGNSSGQYPSGYQQQQQQVYQQGAIHPSQFGSRFVPSLYDRQDFQRRQSLAATNYSSNFSSLNSNTNQGTNSIPVMSPYRRLSAYPPSTSPPLQPPFKQLRRDEVQGQKLSIPQMQLCNSKNDLQPVLNATPKFRRASLNSKTISPLVSVTKSLITTYSLCSP... | 2.7.12.1 | null | phosphorylation [GO:0016310]; positive regulation of cell-substrate adhesion [GO:0010811]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of response to extracellular stimulus [GO:0032106]; protein kinase A signaling [GO:0010737] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MNB/DYRK subfamily | PTM: Phosphorylated; highly. {ECO:0000269|PubMed:10816418}. | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between both compartments in response to glucose. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.12.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Negative regulator of the cell cycle acting downstream of the cAMP-dependent protein kinase. Part of a glucose-sensing system involved in growth control in response to glucose availability. Phosphorylates POP2. {ECO:0000269|PubMed:11358866}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14681 | KSS1_YEAST | MARTITFDIPSQYKLVDLIGEGAYGTVCSAIHKPSGIKVAIKKIQPFSKKLFVTRTIREIKLLRYFHEHENIISILDKVRPVSIDKLNAVYLVEELMETDLQKVINNQNSGFSTLSDDHVQYFTYQILRALKSIHSAQVIHRDIKPSNLLLNSNCDLKVCDFGLARCLASSSDSRETLVGFMTEYVATRWYRAPEIMLTFQEYTTAMDIWSCGCILAEMVSGKPLFPGRDYHHQLWLILEVLGTPSFEDFNQIKSKRAKEYIANLPMRPPLPWETVWSKTDLNPDMIDLLDKMLQFNPDKRISAAEALRHPYLAMYHDPS... | 2.7.11.24 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | cell cycle [GO:0007049]; intracellular signal transduction [GO:0035556]; invasive growth in response to glucose limitation [GO:0001403]; pheromone-dependent signal transduction involved in conjugation with cellular fusion [GO:0000750]; phosphorylation [GO:0016310]; positive regulation of division septum assembly [GO:00... | cellular bud neck [GO:0005935]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; periplasmic space [GO:0042597] | ATP binding [GO:0005524]; MAP kinase activity [GO:0004707]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, MAP kinase subfamily. HOG1 sub-subfamily | PTM: Dually phosphorylated on Thr-183 and Tyr-185 by STE7 in response to pheromone or carbon/nitrogen limitation, which activates the enzyme. Activated FUS3 down-regulates KSS1 phosphorylation. {ECO:0000269|PubMed:1628831}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11781566}. Cytoplasm {ECO:0000269|PubMed:11781566}. Periplasm {ECO:0000269|PubMed:11781566}. Note=KSS1 shuttles rapidly between the cytoplasm and the nucleus independent of its activation state. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Together with closely related FUS3, KSS1 is the final kinase in the signal transduction cascade regulating activation/repression of the mating and filamentation pathways, induced by pheromone and nitrogen/carbon limitation, respectively. Phosphorylated KSS1 activates both pathways, whereas activated FUS3 acti... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14682 | UBC3_YEAST | MSSRKSTASSLLLRQYRELTDPKKAIPSFHIELEDDSNIFTWNIGVMVLNEDSIYHGGFFKAQMRFPEDFPFSPPQFRFTPAIYHPNVYRDGRLCISILHQSGDPMTDEPDAETWSPVQTVESVLISIVSLLEDPNINSPANVDAAVDYRKNPEQYKQRVKMEVERSKQDIPKGFIMPTSESAYISQSKLDEPESNKDMADNFWYDSDLDDDENGSVILQDDDYDDGNNHIPFEDDDVYNYNDNDDDDERIEFEDDDDDDDDSIDNDSVMDRKQPHKAEDESEDVEDVERVSKKI | 2.3.2.23 | null | cell division [GO:0051301]; cellular response to methylmercury [GO:0071406]; DNA replication [GO:0006260]; G1/S transition of mitotic cell cycle [GO:0000082]; G2/M transition of mitotic cell cycle [GO:0000086]; mitochondrial fusion [GO:0008053]; mitotic intra-S DNA damage checkpoint signaling [GO:0031573]; positive reg... | chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; SCF ubiquitin ligase complex [GO:0019005] | ATP binding [GO:0005524]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin-protein transferase activity [GO:0004842] | PF00179; | 3.10.110.10; | Ubiquitin-conjugating enzyme family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROS... | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388}. | null | null | FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Capable, in vitro, to ubiquitinate histone H2A.; FUNCTION: Mediates the initiation of DNA replication (transition of G1 to S phase in cell cycle). Essential component of the E3 ubiquitin ligase complex SCF (SKP1-CUL1-F-box protein), which media... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14683 | CLUS_MESAU | NRRPHFLYPKSRLIRSLLPPPHYGPLSFHDMFQPFLEMIHQAQQAMDVQFHSPAFQFPDMDLLREGEDDRAVCKEIRHNSTGCLKMKGQCEKCQEILSVDCSANNPAQAHLRQELNDSLQVAERLTQRYNELLHSLQTKMLNTSSLLEQLNEQFNWVSQLANLTQGEDQYYLRVSTVTTHSSDSEVPSRVT | null | null | cell differentiation [GO:0030154]; immune complex clearance [GO:0002434]; negative regulation of amyloid fibril formation [GO:1905907]; positive regulation of apoptotic process [GO:0043065]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of receptor-me... | chromaffin granule [GO:0042583]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear endoplasmic reticulum lumen [GO:0099020] | misfolded protein binding [GO:0051787]; unfolded protein binding [GO:0051082] | PF01093; | null | Clusterin family | PTM: Proteolytically cleaved on its way through the secretory system, probably within the Golgi lumen. Proteolytic cleavage is not necessary for its chaperone activity. All non-secreted forms are not proteolytically cleaved. Chaperone activity of uncleaved forms is dependent on a non-reducing environment. {ECO:0000250|... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P10909}. Nucleus {ECO:0000250|UniProtKB:P10909}. Cytoplasm {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10909}; Cytoplasmic side {ECO:0000250|UniProtKB:P10909}. Cytoplasm, ... | null | null | null | null | null | FUNCTION: Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partia... | Mesocricetus auratus (Golden hamster) |
P14693 | SAM35_YEAST | MVSSFSVPMPVKRIFDTFPLQTYAAQTDKDEAVALEIQRRSYTFTERGGGSSELTVEGTYKLGVYNVFLEANTGAALATDPWCLFVQLALCQKNGLVLPTHSQEQTPSHTCNHEMLVLSRLSNPDEALPILVEGYKKRIIRSTVAISEIMRSRILDDAEQLMYYTLLDTVLYDCWITQIIFCASDAQFMELYSCQKLSGSIVTPLDVENSLLQKLSAKSLKISLTKRNKFQFRHREIVKSMQGVYHNHHNSVNQEQVLNVLFENSKQVLLGLKDMLKSDGQPTYLHLKIASYILCITNVKEPIKLKTFVENECKELVQFA... | null | null | mitochondrial outer membrane translocase complex assembly [GO:0070096]; protein import into mitochondrial matrix [GO:0030150]; protein insertion into mitochondrial outer membrane [GO:0045040] | mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; SAM complex [GO:0001401] | null | PF10806; | null | null | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:14699090, ECO:0000269|PubMed:15326197}. | null | null | null | null | null | FUNCTION: Essential component of the mitochondrial outer membrane sorting assembly machinery (SAM or TOB) complex, which is required for the sorting of proteins with complicated topology, such as beta-barrel proteins, to the mitochondrial outer membrane after import by the TOM complex. {ECO:0000269|PubMed:14699090, ECO... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14697 | PHAB_CUPNH | MTQRIAYVTGGMGGIGTAICQRLAKDGFRVVAGCGPNSPRREKWLEQQKALGFDFIASEGNVADWDSTKTAFDKVKSEVGEVDVLINNAGITRDVVFRKMTRADWDAVIDTNLTSLFNVTKQVIDGMADRGWGRIVNISSVNGQKGQFGQTNYSTAKAGLHGFTMALAQEVATKGVTVNTVSPGYIATDMVKAIRQDVLDKIVATIPVKRLGLPEEIASICAWLSSEESGFSTGADFSLNGGLHMG | 1.1.1.36 | null | poly-hydroxybutyrate biosynthetic process [GO:0042619] | cytoplasm [GO:0005737] | acetoacetyl-CoA reductase activity [GO:0018454] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=a (3R)-3-hydroxyacyl-CoA + NADP(+) = a 3-oxoacyl-CoA + H(+) + NADPH; Xref=Rhea:RHEA:22256, ChEBI:CHEBI:15378, ChEBI:CHEBI:57319, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:90726; EC=1.1.1.36; CATALYTIC ACTIVITY: Reaction=(3R)-3-hydroxybutanoyl-CoA + NADP(+) = acetoacetyl-CoA + H(+) +... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.7 uM for acetoacetyl-CoA {ECO:0000269|PubMed:23913421}; KM=149 uM for NADPH {ECO:0000269|PubMed:23913421}; Note=kcat is 102 sec(-1).; | PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate biosynthesis. {ECO:0000269|PubMed:23913421, ECO:0000269|PubMed:2670936}. | null | null | FUNCTION: Catalyzes the chiral reduction of acetoacetyl-CoA to (R)-3-hydroxybutyryl-CoA. Is involved in the biosynthesis of polyhydroxybutyrate (PHB), which is accumulated as an intracellular energy reserve material when cells grow under conditions of nutrient limitation. {ECO:0000269|PubMed:23913421, ECO:0000269|PubMe... | Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337) (Ralstonia eutropha) |
P14712 | PHYA_ARATH | MSGSRPTQSSEGSRRSRHSARIIAQTTVDAKLHADFEESGSSFDYSTSVRVTGPVVENQPPRSDKVTTTYLHHIQKGKLIQPFGCLLALDEKTFKVIAYSENASELLTMASHAVPSVGEHPVLGIGTDIRSLFTAPSASALQKALGFGDVSLLNPILVHCRTSAKPFYAIIHRVTGSIIIDFEPVKPYEVPMTAAGALQSYKLAAKAITRLQSLPSGSMERLCDTMVQEVFELTGYDRVMAYKFHEDDHGEVVSEVTKPGLEPYLGLHYPATDIPQAARFLFMKNKVRMIVDCNAKHARVLQDEKLSFDLTLCGSTLRAP... | null | null | detection of visible light [GO:0009584]; gravitropism [GO:0009630]; negative regulation of translation [GO:0017148]; photomorphogenesis [GO:0009640]; phototropism [GO:0009638]; red light signaling pathway [GO:0010161]; regulation of DNA-templated transcription [GO:0006355]; response to arsenic-containing substance [GO:... | cytoplasm [GO:0005737]; nuclear body [GO:0016604]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | far-red light photoreceptor activity [GO:0031516]; identical protein binding [GO:0042802]; mRNA binding [GO:0003729]; phosphorelay sensor kinase activity [GO:0000155]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; red or far-red light photoreceptor activity [GO:0009883] | PF01590;PF02518;PF00512;PF00989;PF08446;PF00360; | 1.10.287.130;3.30.450.270;3.30.450.40;3.30.565.10;3.30.450.20; | Phytochrome family | PTM: Phosphorylated.; PTM: Contains one covalently linked phytochromobilin chromophore. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15707897, ECO:0000269|PubMed:21969386}. Nucleus, nucleoplasm {ECO:0000269|PubMed:15707897, ECO:0000269|PubMed:21969386}. Nucleus speckle {ECO:0000269|PubMed:15707897}. Note=Cytoplasmic in darkness, but translocated to the nucleus upon illumination, when associated wit... | null | null | null | null | null | FUNCTION: Regulatory photoreceptor which exists in two forms that are reversibly interconvertible by light: the Pr form that absorbs maximally in the red region of the spectrum and the Pfr form that absorbs maximally in the far-red region. Photoconversion of Pr to Pfr induces an array of morphogenetic responses, wherea... | Arabidopsis thaliana (Mouse-ear cress) |
P14713 | PHYB_ARATH | MVSGVGGSGGGRGGGRGGEEEPSSSHTPNNRRGGEQAQSSGTKSLRPRSNTESMSKAIQQYTVDARLHAVFEQSGESGKSFDYSQSLKTTTYGSSVPEQQITAYLSRIQRGGYIQPFGCMIAVDESSFRIIGYSENAREMLGIMPQSVPTLEKPEILAMGTDVRSLFTSSSSILLERAFVAREITLLNPVWIHSKNTGKPFYAILHRIDVGVVIDLEPARTEDPALSIAGAVQSQKLAVRAISQLQALPGGDIKLLCDTVVESVRDLTGYDRVMVYKFHEDEHGEVVAESKRDDLEPYIGLHYPATDIPQASRFLFKQNR... | null | null | abscisic acid metabolic process [GO:0009687]; chromatin organization [GO:0006325]; circadian regulation of calcium ion oscillation [GO:0010617]; detection of visible light [GO:0009584]; entrainment of circadian clock [GO:0009649]; gravitropism [GO:0009630]; jasmonic acid mediated signaling pathway [GO:0009867]; negativ... | cytosol [GO:0005829]; nuclear body [GO:0016604]; nuclear speck [GO:0016607]; nucleus [GO:0005634] | far-red light photoreceptor activity [GO:0031516]; identical protein binding [GO:0042802]; phosphorelay sensor kinase activity [GO:0000155]; promoter-specific chromatin binding [GO:1990841]; protein homodimerization activity [GO:0042803]; red light photoreceptor activity [GO:0031517]; red or far-red light photoreceptor... | PF01590;PF02518;PF00512;PF00989;PF08446;PF00360; | 3.30.450.270;3.30.450.40;3.30.565.10;3.30.450.20; | Phytochrome family | PTM: Contains one covalently linked phytochromobilin chromophore. {ECO:0000269|PubMed:24982198, ECO:0000269|PubMed:28376244}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15707897}. Nucleus, nucleoplasm {ECO:0000269|PubMed:15707897}. Nucleus speckle {ECO:0000269|PubMed:15707897}. Nucleus {ECO:0000269|PubMed:24127609}. Note=Cytoplasmic in darkness, but translocated to the nucleus upon illumination, when associated with PAPP5 into speckl... | null | null | null | null | null | FUNCTION: Regulatory photoreceptor which exists in two forms that are reversibly interconvertible by light: the Pr form that absorbs maximally in the red region of the spectrum and the Pfr form that absorbs maximally in the far-red region. Photoconversion of Pr to Pfr induces an array of morphogenetic responses, wherea... | Arabidopsis thaliana (Mouse-ear cress) |
P14719 | ILRL1_MOUSE | MIDRQRMGLWALAILTLPMYLTVTEGSKSSWGLENEALIVRCPQRGRSTYPVEWYYSDTNESIPTQKRNRIFVSRDRLKFLPARVEDSGIYACVIRSPNLNKTGYLNVTIHKKPPSCNIPDYLMYSTVRGSDKNFKITCPTIDLYNWTAPVQWFKNCKALQEPRFRAHRSYLFIDNVTHDDEGDYTCQFTHAENGTNYIVTATRSFTVEEKGFSMFPVITNPPYNHTMEVEIGKPASIACSACFGKGSHFLADVLWQINKTVVGNFGEARIQEEEGRNESSSNDMDCLTSVLRITGVTEKDLSLEYDCLALNLHGMIRHT... | 3.2.2.6 | null | inflammatory response [GO:0006954]; macrophage differentiation [GO:0030225]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of T-helper 1 type immune response [GO:0002826]; negative regulation of type II interferon production [GO:0032689]; positive regulation of chemokine product... | cell surface [GO:0009986]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; focal adhesion [GO:0005925] | interleukin-1 receptor activity [GO:0004908]; interleukin-33 binding [GO:0002113]; interleukin-33 receptor activity [GO:0002114]; NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809] | PF00047;PF01582; | 2.60.40.10;3.40.50.10140; | Interleukin-1 receptor family | PTM: Phosphorylated by GSK3B at Ser-442; leading to proteasomal degradation. {ECO:0000269|PubMed:22660580}.; PTM: Ubiquitinated at Lys-326 in a FBXL19-mediated manner; leading to proteasomal degradation (PubMed:22660580). Ubiquitination by TRAF6 via 'Lys-27'-linked polyubiquitination and deubiquitination by USP38 serve... | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform B]: Secreted. | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU00204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Ev... | null | null | null | null | FUNCTION: Receptor for interleukin-33 (IL-33) which plays crucial roles in innate and adaptive immunity, contributing to tissue homeostasis and responses to environmental stresses together with coreceptor IL1RAP (PubMed:17675517, PubMed:18450470, PubMed:22660580, PubMed:29045903). Its stimulation recruits MYD88, IRAK1,... | Mus musculus (Mouse) |
P14724 | CDC26_YEAST | MIRRAPTTLQLSHDDVTSLIDDLNEQKLKQQLNIEKTKYFQGKNGGSLHSNTDFQDTSQNIEDNNNDNDNDIDEDDDMSSYNDKAASVAHTRVLNSLHLSTDSNTAHETSNANDNHNPFYIREE | null | null | anaphase-promoting complex-dependent catabolic process [GO:0031145]; cell cycle [GO:0007049]; cell division [GO:0051301]; chromatin organization [GO:0006325]; protein ubiquitination [GO:0016567]; regulation of meiotic cell cycle [GO:0051445]; regulation of mitotic cell cycle [GO:0007346] | anaphase-promoting complex [GO:0005680]; cytosol [GO:0005829]; nucleus [GO:0005634] | null | PF10471; | null | CDC26 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes,... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14727 | AVRB3_XANEU | MDPIRSRTPSPARELLPGPQPDGVQPTADRGVSPPAGGPLDGLPARRTMSRTRLPSPPAPSPAFSAGSFSDLLRQFDPSLFNTSLFDSLPPFGAHHTEAATGEWDEVQSGLRAADAPPPTMRVAVTAARPPRAKPAPRRRAAQPSDASPAAQVDLRTLGYSQQQQEKIKPKVRSTVAQHHEALVGHGFTHAHIVALSQHPAALGTVAVKYQDMIAALPEATHEAIVGVGKQWSGARALEALLTVAGELRGPPLQLDTGQLLKIAKRGGVTAVEAVHAWRNALTGAPLNLTPEQVVAIASHDGGKQALETVQRLLPVLCQA... | null | null | symbiont-mediated perturbation of host defense-related programmed cell death [GO:0034053]; symbiont-mediated perturbation of host transcription [GO:0052026] | extracellular region [GO:0005576]; host cell nucleus [GO:0042025] | sequence-specific DNA binding [GO:0043565] | PF03377; | 6.10.140.500; | Transcription activator-like effector (TALE) family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10430949, ECO:0000269|PubMed:11439138, ECO:0000269|PubMed:12366827, ECO:0000269|PubMed:15807781, ECO:0000269|PubMed:8980236}. Host nucleus {ECO:0000269|PubMed:12366827}. Note=Secreted via type III secretion system (T3SS) (PubMed:10430949, PubMed:12366827). Localizes to... | null | null | null | null | null | FUNCTION: Avirulence protein. Acts as a transcription factor in C.annuum plants. In susceptible plants lacking the Bs3 resistance gene induces expression of a number of genes, including genes homologous to a family of auxin-induced genes, alpha-expansin genes, pectate lyase, anthocyanidin glucoside rhamnosyl transferas... | Xanthomonas euvesicatoria |
P14731 | LMNB1_CHICK | MAAAVAPLSPQPRGAAASAALSPTRISRLQEKEELRQLNDRLAVYIDKVRSLETENSALQRRVSEREQVCGREISGLKELFETELADARKTLDDTARERAKLQIELGKLRAEHEQVLSSYAKKDSDLNAAQVKLREFEAALNAKEAALATALGDKRSQEEELEDLRDQIAQLEVSLAAAKKELADETLQKVDLENRCQSLIEDLEFRKNVYEEEIKETRRKHETRLVEVDSGRQIEYEYKLAQALKEIREQHDAQVKLYKEELEQTYSSKLENIRQSSEMHSCTANTVREELHESRMRIETLSSHIADIQKESRAWQDRV... | null | null | heterochromatin formation [GO:0031507]; nuclear envelope organization [GO:0006998]; nuclear migration [GO:0007097]; nuclear pore localization [GO:0051664]; protein localization to nuclear envelope [GO:0090435] | intermediate filament [GO:0005882]; nuclear envelope [GO:0005635]; nuclear lamina [GO:0005652]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654] | structural constituent of cytoskeleton [GO:0005200] | PF00038;PF00932; | 1.20.5.170;2.60.40.1260;1.20.5.1160; | Intermediate filament family | PTM: Phosphorylation plays a key role in lamin organization, subcellular localization and nuclear envelope disintegration (PubMed:2188731). Phosphorylation by CDK1 at Ser-22 at the onset of mitosis drives lamin disassembly and nuclear envelope breakdown (By similarity). {ECO:0000250|UniProtKB:P14732, ECO:0000269|PubMed... | SUBCELLULAR LOCATION: Nucleus lamina {ECO:0000269|PubMed:2188731}. Nucleus envelope {ECO:0000250|UniProtKB:P02545}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P02545}. Nucleus matrix {ECO:0000250|UniProtKB:P02545}. | null | null | null | null | null | FUNCTION: 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:2188731). Lamins provide a framework for the nuclear envelope, bridging the nucl... | Gallus gallus (Chicken) |
P14732 | LMNB2_CHICK | MSGTPIRGTPGGTPLSPTRISRLQEKEELRQLNDRLAVYIDRVRALELENDRLLVKISEKEEVTTREVSGIKNLYESELADARRVLDETAKERARLQIEIGKLRAELEEFNKSYKKKDADLSVAQGRIKDLEVLFHRSEAELNTVLNEKRSLEAEVADLRAQLAKAEDGHAVAKKQLEKETLMRVDLENRCQSLQEDLDFRKNVFEEEIRETRKRHEHRLVEVDTSRQQEYENKMAQALEDLRNQHDEQVKLYKMELEQTYQAKLENAILASDQNDKAAGAAREELKEARMRIESLSHQLSGLQKQASATEDRIRELKET... | null | null | heterochromatin formation [GO:0031507]; nuclear envelope organization [GO:0006998]; nuclear migration [GO:0007097]; nuclear pore localization [GO:0051664]; protein localization to nuclear envelope [GO:0090435] | intermediate filament [GO:0005882]; nuclear envelope [GO:0005635]; nuclear lamina [GO:0005652]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654] | structural constituent of cytoskeleton [GO:0005200] | PF00038;PF00932; | 1.20.5.170;2.60.40.1260;1.20.5.1160; | Intermediate filament family | PTM: Phosphorylation plays a key role in lamin organization, subcellular localization and nuclear envelope disintegration (PubMed:2188731). Phosphorylation by CDK1 at Ser-16 at the onset of mitosis drives lamin disassembly and nuclear envelope breakdown (PubMed:2188731). {ECO:0000269|PubMed:2188731}. | SUBCELLULAR LOCATION: Nucleus lamina {ECO:0000269|PubMed:2188731}. Nucleus envelope {ECO:0000250|UniProtKB:P02545}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P02545}. Nucleus matrix {ECO:0000250|UniProtKB:P02545}. | null | null | null | null | null | FUNCTION: 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:2188731). Lamins provide a framework for the nuclear envelope, bridging the nucl... | Gallus gallus (Chicken) |
P14733 | LMNB1_MOUSE | MATATPVQQQRAGSRASAPATPLSPTRLSRLQEKEELRELNDRLAVYIDKVRSLETENSALQLQVTEREEVRGRELTGLKALYETELADARRALDDTARERAKLQIELGKFKAEHDQLLLNYAKKESDLSGAQIKLREYEAALNSKDAALATALGDKKSLEGDLEDLKDQIAQLEASLSAAKKQLADETLLKVDLENRCQSLTEDLEFRKNMYEEEINETRRKHETRLVEVDSGRQIEYEYKLAQALHEMREQHDAQVRLYKEELEQTYHAKLENARLSSEMNTSTVNSAREELMESRMRIESLSSQLSNLQKESRACLE... | null | null | cellular response to L-glutamate [GO:1905232]; heterochromatin formation [GO:0031507]; nuclear envelope organization [GO:0006998]; nuclear migration [GO:0007097]; nuclear pore localization [GO:0051664]; positive regulation of G2/M transition of mitotic cell cycle [GO:0010971]; positive regulation of JNK cascade [GO:004... | lamin filament [GO:0005638]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]; nuclear lamina [GO:0005652]; nuclear matrix [GO:0016363]; nuclear membrane [GO:0031965]; nuclear periphery [GO:0034399]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | double-stranded DNA binding [GO:0003690]; JUN kinase binding [GO:0008432]; phospholipase binding [GO:0043274]; sequence-specific double-stranded DNA binding [GO:1990837]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of nuclear lamina [GO:0160123] | PF00038;PF00932; | 1.20.5.170;2.60.40.1260;1.20.5.1160; | Intermediate filament family | PTM: B-type lamins undergo a series of modifications, such as farnesylation and phosphorylation. Increased phosphorylation of the lamins occurs before envelope disintegration and probably plays a role in regulating lamin associations. {ECO:0000250|UniProtKB:P20700}.; PTM: Phosphorylation plays a key role in lamin organ... | SUBCELLULAR LOCATION: Nucleus lamina {ECO:0000269|PubMed:28241138}. | null | null | null | null | null | FUNCTION: 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:28241138). Lamins provide a framework for the nuclear envelope, bridging the nuc... | Mus musculus (Mouse) |
P14734 | FKH_DROME | MQKLYAEPPPSSAPVSMASSGGGGPPSGGGGGGGGGGGGGPPPPSNNNPNPTSNGGSMSPLARSAYTMNSMGLPVGGMSSVSPQAAATFSSSVLDSAAAVASMSASMSASMSASMNASMNGSMGAAAMNSMGGNCMTPSSMSYASMGSPLGNMGGCMAMSAASMSAAGLSGTYGAMPPGSREMETGSPNSLGRSRVDKPTTYRRSYTHAKPPYSYISLITMAIQNNPTRMLTLSEIYQFIMDLFPFYRQNQQRWQNSIRHSLSFNDCFVKIPRTPDKPGKGSFWTLHPDSGNMFENGCYLRRQKRFKDEKKEAIRQLHKS... | null | null | anatomical structure morphogenesis [GO:0009653]; autophagic cell death [GO:0048102]; cell differentiation [GO:0030154]; determination of adult lifespan [GO:0008340]; DNA endoreduplication [GO:0042023]; endoderm formation [GO:0001706]; insulin receptor signaling pathway [GO:0008286]; Malpighian tubule morphogenesis [GO:... | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein domain specific binding [GO:0019904]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977] | PF00250;PF08430; | 1.10.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Fkh promotes terminal as opposed to segmental development. In the absence of fkh, this developmental switch does not occur. The nuclear localization of the fkh protein suggest that fkh regulates the transcription of other, subordinate, genes. | Drosophila melanogaster (Fruit fly) |
P14735 | IDE_HUMAN | MRYRLAWLLHPALPSTFRSVLGARLPPPERLCGFQKKTYSKMNNPAIKRIGNHITKSPEDKREYRGLELANGIKVLLISDPTTDKSSAALDVHIGSLSDPPNIAGLSHFCEHMLFLGTKKYPKENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLEGALDRFAQFFLCPLFDESCKDREVNAVDSEHEKNVMNDAWRLFQLEKATGNPKHPFSKFGTGNKYTLETRPNQEGIDVRQELLKFHSAYYSSNLMAVCVLGRESLDDLTNLVVKLFSEVENKNVPLPEFPEHPFQEEHLKQLYKIVPIKDIRNLYVTFPIP... | 3.4.24.56 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0000269|PubMed:21098034, ECO:0000269|PubMed:23922390, ECO:0000269|PubMed:26394692}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:1898... | amyloid-beta clearance [GO:0097242]; amyloid-beta clearance by cellular catabolic process [GO:0150094]; amyloid-beta metabolic process [GO:0050435]; antigen processing and presentation of endogenous peptide antigen via MHC class I [GO:0019885]; bradykinin catabolic process [GO:0010815]; hormone catabolic process [GO:00... | basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; peroxisomal matrix [GO:0005782]; perox... | ATP binding [GO:0005524]; endopeptidase activity [GO:0004175]; identical protein binding [GO:0042802]; insulin binding [GO:0043559]; metalloendopeptidase activity [GO:0004222]; peptide binding [GO:0042277]; protein homodimerization activity [GO:0042803]; ubiquitin-dependent protein binding [GO:0140036]; virus receptor ... | PF00675;PF05193;PF16187; | 3.30.830.10; | Peptidase M16 family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:20364150, ECO:0000269|PubMed:9830016}. Cell membrane {ECO:0000250|UniProtKB:P35559}. Secreted {ECO:0000269|PubMed:9830016}. Note=Present at the cell surface of neuron cells. The membrane-associated isoform is approximately 5 kDa larger than the known cytosoli... | CATALYTIC ACTIVITY: Reaction=Degradation of insulin, glucagon and other polypeptides. No action on proteins.; EC=3.4.24.56; Evidence={ECO:0000269|PubMed:10684867, ECO:0000269|PubMed:17051221, ECO:0000269|PubMed:17613531, ECO:0000269|PubMed:18986166, ECO:0000269|PubMed:19321446, ECO:0000269|PubMed:21098034, ECO:0000269|... | null | null | null | null | FUNCTION: Plays a role in the cellular breakdown of insulin, APP peptides, IAPP peptides, natriuretic peptides, glucagon, bradykinin, kallidin, and other peptides, and thereby plays a role in intercellular peptide signaling (PubMed:10684867, PubMed:17051221, PubMed:17613531, PubMed:18986166, PubMed:19321446, PubMed:210... | Homo sapiens (Human) |
P14736 | RAD4_YEAST | MNEDLPKEYFELIRKALNEKEAEKAPLSRRRRVRRKNQPLPDAKKKFKTGLNELPRESVVTVNLDSSDDGVVTVPTDDSVEEIQSSEEDYDSEEFEDVTDGNEVAGVEDISVEIKPSSKRNSDARRTSRNVCSNEERKRRKYFHMLYLVCLMVHGFIRNEWINSKRLSRKLSNLVPEKVFELLHPQKDEELPLRSTRKLLDGLKKCMELWQKHWKITKKYDNVGLYMRTWKEIEMSANNKRKFKTLKRSDFLRAVSKGHGDPDISVQGFVAMLRACNVNARLIMSCQPPDFTNMKIDTSLNGNNAYKDMVKYPIFWCEVW... | null | null | DNA topological change [GO:0006265]; mismatch repair [GO:0006298]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nucleotide-excision repair [GO:0006289]; nucleotide-excision repair, DNA damage recognition [GO:0000715]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:00431... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleotide-excision repair factor 2 complex [GO:0000111]; nucleus [GO:0005634]; XPC complex [GO:0071942] | damaged DNA binding [GO:0003684]; single-strand break-containing DNA binding [GO:1990165]; single-stranded DNA binding [GO:0003697] | PF10403;PF10405;PF03835; | 2.20.20.110;3.30.60.290;3.30.70.2460;3.90.260.10; | XPC family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. | null | null | null | null | null | FUNCTION: Involved in nucleotide excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14737 | RAD9_YEAST | MSGQLVQWKSSPDRVTQSAIKEALHSPLADGDMNEMNVPVDPLENKVNSTNIIEGSPKANPNPVKFMNTSEIFQKSLGLLDESPRHDDELNIEVGDNDRPNANILHNERTPDLDRIANFFKSNRTPGKENLLTKYQSSDLEDTPLMLRKKMTFQTPTDPLEQKTFKKLKSDTGFCYYGEQNDGEENASLEVTEADATFVQMAERSADNYDCALEGIVTPKRYKDELSKSGGMQDERVQKTQIMISAESPNSISSYDKNKITGNGRTTRNVNKVFNNNEDNIGAIEEKNPVKKKSENYSSDDLRERNNQIIQSNESEEINE... | null | null | DNA damage checkpoint signaling [GO:0000077]; DNA repair [GO:0006281]; double-strand break repair [GO:0006302]; mitotic G1 DNA damage checkpoint signaling [GO:0031571]; mitotic intra-S DNA damage checkpoint signaling [GO:0031573]; negative regulation of DNA strand resection involved in replication fork processing [GO:0... | chromatin [GO:0000785]; nucleus [GO:0005634] | double-stranded DNA binding [GO:0003690]; enzyme activator activity [GO:0008047]; histone binding [GO:0042393] | PF00533;PF08605; | 3.40.50.10190; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Essential for cell cycle arrest at the G2 stage following DNA damage by X-irradiation or inactivation of DNA ligase. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14738 | FNBA_STAA8 | MKNNLRYGIRKHKLGAASVFLGTMIVVGMGQDKEAAASEQKTTTVEENGNSATDNKTSETQTTATNVNHIEETQSYNATVTEQPSNATQVTTEEAPKAVQAPQTAQPANIETVKEEVVKEEAKPQVKETTQSQDNSGDQRQVDLTPKKATQNQVAETQVEVAQPRTASESKPRVTRSADVAEAKEASNAKVETGTDVTSKVTVEIGSIEGHNNTNKVEPHAGQRAVLKYKLKFENGLHQGDYFDFTLSNNVNTHGVSTARKVPEIKNGSVVMATGEVLEGGKIRYTFTNDIEDKVDVTAELEINLFIDPKTVQTNGNQTI... | null | null | aggregation of unicellular organisms [GO:0098630]; cell adhesion [GO:0007155] | extracellular region [GO:0005576] | fibrinogen binding [GO:0070051]; fibronectin binding [GO:0001968] | PF17961;PF02986;PF00746;PF10425;PF04650; | 2.60.40.1280;2.60.40.1290; | null | null | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000305|PubMed:11830639}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477, ECO:0000305|PubMed:11830639, ECO:0000305|PubMed:14769030}. Note=Anchored to the cell wall by sortase A. {ECO:0000305|PubMed:11830639, ECO:0000305|Pub... | null | null | null | null | null | FUNCTION: Possesses multiple, substituting fibronectin (Fn) binding regions, each capable of conferring adherence to both soluble and immobilized forms of Fn. This confers to S.aureus the ability to invade endothelial cells both in vivo and in vitro, without requiring additional factors, although in a slow and ineffici... | Staphylococcus aureus (strain NCTC 8325 / PS 47) |
P14740 | DPP4_RAT | MKTPWKVLLGLLGVAALVTIITVPVVLLNKDEAAADSRRTYTLADYLKNTFRVKSYSLRWVSDSEYLYKQENNILLFNAEHGNSSIFLENSTFEIFGDSISDYSVSPDRLFVLLEYNYVKQWRHSYTASYSIYDLNKRQLITEEKIPNNTQWITWSQEGHKLAYVWKNDIYVKIEPHLPSHRITSTGKENVIFNGINDWVYEEEIFGAYSALWWSPNGTFLAYAQFNDTGVPLIEYSFYSDESLQYPKTVWIPYPKAGAVNPTVKFFIVNTDSLSSTTTTIPMQITAPASVTTGDHYLCDVAWVSEDRISLQWLRRIQNY... | 3.4.14.5 | null | B-1a B cell differentiation [GO:0002337]; behavioral fear response [GO:0001662]; cell adhesion [GO:0007155]; endothelial cell migration [GO:0043542]; locomotory exploration behavior [GO:0035641]; negative regulation of extracellular matrix disassembly [GO:0010716]; negative regulation of neutrophil chemotaxis [GO:00900... | apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; endocytic vesicle [GO:0030139]; extracellular region [GO:0005576]; intercellular canaliculus [GO:0046581]; lamellipodium [GO:0030027]; lamellipodium membrane [GO:0031258]; membrane raft [GO:0045121]; plasma membrane [GO:0005886] | aminopeptidase activity [GO:0004177]; chemorepellent activity [GO:0045499]; collagen binding [GO:0005518]; dipeptidyl-peptidase activity [GO:0008239]; identical protein binding [GO:0042802]; peptide binding [GO:0042277]; protease binding [GO:0002020]; protein homodimerization activity [GO:0042803]; serine-type endopept... | PF00930;PF18811;PF00326; | 3.40.50.1820;2.140.10.30; | Peptidase S9B family, DPPIV subfamily | PTM: The soluble form (Dipeptidyl peptidase 4 soluble form also named SDPP) derives from the membrane form (Dipeptidyl peptidase 4 membrane form also named MDPP) by proteolytic processing. {ECO:0000250}.; PTM: N- and O-Glycosylated. {ECO:0000250}.; PTM: Phosphorylated. Mannose 6-phosphate residues in the carbohydrate m... | SUBCELLULAR LOCATION: [Dipeptidyl peptidase 4 soluble form]: Secreted. Note=Detected in the serum and the seminal fluid. {ECO:0000250}.; SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane protein. Apical cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Cell projection, inv... | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.; EC=3.4.14.5; Evidence={ECO:0000250|UniProtKB:P27487, ECO:0000255|PROSITE-ProRule:PRU10084}; | null | null | null | null | FUNCTION: Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa... | Rattus norvegicus (Rat) |
P14741 | EI2BA_YEAST | MSEFNITETYLRFLEEDTEMTMPIAAIEALVTLLRIKTPETAAEMINTIKSSTEELIKSIPNSVSLRAGCDIFMRFVLRNLHLYGDWENCKQHLIENGQLFVSRAKKSRNKIAEIGVDFIADDDIILVHGYSRAVFSLLNHAANKFIRFRCVVTESRPSKQGNQLYTLLEQKGIPVTLIVDSAVGAVIDKVDKVFVGAEGVAESGGIINLVGTYSVGVLAHNARKPFYVVTESHKFVRMFPLSSDDLPMAGPPLDFTRRTDDLEDALRGPTIDYTAQEYITALITDLGVLTPSAVSEELIKMWYD | null | null | cytoplasmic translational initiation [GO:0002183]; positive regulation of cellular response to amino acid starvation [GO:1903833]; regulation of translational initiation [GO:0006446]; translational initiation [GO:0006413] | cytosol [GO:0005829]; eukaryotic translation initiation factor 2B complex [GO:0005851]; guanyl-nucleotide exchange factor complex [GO:0032045] | enzyme regulator activity [GO:0030234]; guanyl-nucleotide exchange factor activity [GO:0005085]; translation initiation factor activity [GO:0003743] | PF01008; | 1.20.120.1070; | EIF-2B alpha/beta/delta subunits family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9USP0}. | null | null | null | null | null | FUNCTION: Acts as a component of the translation initiation factor 2B (eIF2B) complex, which catalyzes the exchange of GDP for GTP on the eukaryotic initiation factor 2 (eIF2) complex gamma subunit (PubMed:8506384, PubMed:9472020). Its guanine nucleotide exchange factor activity is repressed when bound to eIF2 complex ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14742 | GFA1_YEAST | MCGIFGYCNYLVERSRGEIIDTLVDGLQRLEYRGYDSTGIAIDGDEADSTFIYKQIGKVSALKEEITKQNPNRDVTFVSHCGIAHTRWATHGRPEQVNCHPQRSDPEDQFVVVHNGIITNFRELKTLLINKGYKFESDTDTECIAKLYLHLYNTNLQNGHDLDFHELTKLVLLELEGSYGLLCKSCHYPNEVIATRKGSPLLIGVKSEKKLKVDFVDVEFPEENAGQPEIPLKSNNKSFGLGPKKAREFEAGSQNANLLPIAANEFNLRHSQSRAFLSEDGSPTPVEFFVSSDAASVVKHTKKVLFLEDDDLAHIYDGEL... | 2.6.1.16 | null | fructose 6-phosphate metabolic process [GO:0006002]; fungal-type cell wall chitin biosynthetic process [GO:0034221]; glutamine metabolic process [GO:0006541]; protein N-linked glycosylation [GO:0006487]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048]; UDP-N-acetylglucosamine metabolic process [GO:0006047] | cytosol [GO:0005829] | carbohydrate derivative binding [GO:0097367]; glutamine-fructose-6-phosphate transaminase (isomerizing) activity [GO:0004360] | PF13522;PF01380; | 3.60.20.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000269|PubMed:15699032}; | null | PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1. | null | null | FUNCTION: Involved in amino sugar synthesis (formation of chitin, supplies the amino sugars of asparagine-linked oligosaccharides of glycoproteins). {ECO:0000269|PubMed:15699032}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14743 | NMT_YEAST | MSEEDKAKKLENLLKLLQLNNDDTSKFTQEQKKAMKDHKFWRTQPVKDFDEKVVEEGPIDKPKTPEDISDKPLPLLSSFEWCSIDVDNKKQLEDVFVLLNENYVEDRDAGFRFNYTKEFFNWALKSPGWKKDWHIGVRVKETQKLVAFISAIPVTLGVRGKQVPSVEINFLCVHKQLRSKRLTPVLIKEITRRVNKCDIWHALYTAGIVLPAPVSTCRYTHRPLNWKKLYEVDFTGLPDGHTEEDMIAENALPAKTKTAGLRKLKKEDIDQVFELFKRYQSRFELIQIFTKEEFEHNFIGEESLPLDKQVIFSYVVEQPD... | 2.3.1.97 | null | N-terminal peptidyl-glycine N-myristoylation [GO:0018008] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | glycylpeptide N-tetradecanoyltransferase activity [GO:0004379] | PF01233;PF02799; | 3.40.630.30; | NMT family | PTM: The N-terminus is blocked. {ECO:0000305|PubMed:2644694}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=N-terminal glycyl-[protein] + tetradecanoyl-CoA = CoA + H(+) + N-tetradecanoylglycyl-[protein]; Xref=Rhea:RHEA:15521, Rhea:RHEA-COMP:12666, Rhea:RHEA-COMP:12667, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:64723, ChEBI:CHEBI:133050; EC=2.3.1.97; Evidence={ECO:000026... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 uM for myristoyl-CoA {ECO:0000269|PubMed:11478885, ECO:0000269|PubMed:3106975}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:11478885, ECO:0000269|PubMed:3106975}; | null | FUNCTION: Adds a myristoyl group to the N-terminal glycine residue of certain cellular proteins. Substrate specificity requires an N-terminal glycine in the nascent polypeptide substrates. Uncharged amino acids are preferred at position 2 while neutral residues are favored at positions 3 and 4. Ser is present at positi... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14745 | CD44_PAPHA | MDKFWWRAAWGLCLVQLSLAQIDLNITCRFEGIYHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPRIHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPGEDCTSVTDLPNAFDGPITITIVNRDGTRYVKKGEYRTNPEDINPSSPTDDDVSSGSSSERSSTLGGYIFYNHFSTSPPIPDEDGPWITDSTDRTPATRDQGAFDPSGGSHTTHGSESAGHSHGSREGGANTTSGPLRTPQIPEWLIILASLLALALILAVCIAVNSRRRCGQKKKLVINNGNGAVEDRKSSGLN... | null | null | cell adhesion [GO:0007155]; inflammatory response [GO:0006954]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; regulation of lamellipodium morphogenesis [GO:2000392]; wound healing, spreading of cells [GO:0044319] | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cell projection [GO:0042995]; extracellular region [GO:0005576]; lamellipodium membrane [GO:0031258]; macrophage migration inhibitory factor receptor complex [GO:0035692]; microvillus [GO:0005902]; plasma membrane [GO:0005886] | cytokine receptor activity [GO:0004896]; hyaluronic acid binding [GO:0005540] | PF00193; | 3.10.100.10; | null | PTM: Phosphorylated; activation of PKC results in the dephosphorylation of Ser-326 (constitutive phosphorylation site), and the phosphorylation of Ser-292. {ECO:0000250|UniProtKB:P16070}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:P16070}.; PTM: O-glycosylated; contains chondroitin sulfate glycans which can be more o... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15379}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P15379}. Cell projection, microvillus {ECO:0000250|UniProtKB:P15379}. Secreted {ECO:0000250|UniProtKB:P16070}. Note=Colocalizes with actin in membrane protrusions at wounding edges. Co-localize... | null | null | null | null | null | FUNCTION: Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematop... | Papio hamadryas (Hamadryas baboon) |
P14747 | PP2B2_YEAST | MSSDAIRNTEQINAAIKIIENKTERPQSSTTPIDSKASTVAAANSTATETSRDLTQYTLDDGRVVSTNRRIMNKVPAITSHVPTDEELFQPNGIPRHEFLRDHFKREGKLSAAQAARIVTLATELFSKEPNLISVPAPITVCGDIHGQYFDLLKLFEVGGDPATTSYLFLGDYVDRGSFSFECLIYLYSLKLNFNDHFWLLRGNHECKHLTSYFTFKNEMLHKYNLDIYEKCCESFNNLPLAALMNGQYLCVHGGISPELNSLQDINNLNRFREIPSHGLMCDLLWADPIEEYDEVLDKDLTEEDIVNSKTMVPHHGKMA... | 3.1.3.16 | COFACTOR: Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250}; Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | calcineurin-mediated signaling [GO:0097720]; cellular response to pheromone [GO:0071444]; fungal-type cell wall organization [GO:0031505]; intracellular monoatomic ion homeostasis [GO:0006873]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of cell morphogenesis [GO:0022604] | calcineurin complex [GO:0005955]; cytoplasm [GO:0005737] | calmodulin binding [GO:0005516]; calmodulin-dependent protein phosphatase activity [GO:0033192]; metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018] | PF00149; | 3.60.21.10; | PPP phosphatase family, PP-2B subfamily | null | null | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-... | null | null | null | null | FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14753 | EPOR_MOUSE | MDKLRVPLWPRVGPLCLLLAGAAWAPSPSLPDPKFESKAALLASRGSEELLCFTQRLEDLVCFWEEAASSGMDFNYSFSYQLEGESRKSCSLHQAPTVRGSVRFWCSLPTADTSSFVPLELQVTEASGSPRYHRIIHINEVVLLDAPAGLLARRAEEGSHVVLRWLPPPGAPMTTHIRYEVDVSAGNRAGGTQRVEVLEGRTECVLSNLRGGTRYTFAVRARMAEPSFSGFWSAWSEPASLLTASDLDPLILTLSLILVLISLLLTVLALLSHRRTLQQKIWPGIPSPESEFEGLFTTHKGNFQLWLLQRDGCLWWSPGS... | null | null | brain development [GO:0007420]; cardiac muscle tissue morphogenesis [GO:0055008]; cytokine-mediated signaling pathway [GO:0019221]; decidualization [GO:0046697]; heart development [GO:0007507]; heart morphogenesis [GO:0003007]; hemopoiesis [GO:0030097]; negative regulation of neuron apoptotic process [GO:0043524]; nega... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; nuclear speck [GO:0016607]; plasma membrane [GO:0005886] | erythropoietin receptor activity [GO:0004900]; identical protein binding [GO:0042802] | PF09067;PF00041; | 2.60.40.10; | Type I cytokine receptor family, Type 1 subfamily | PTM: The identity of the C-linked hexose on the WXXW motif has not been determined. It is probably mannose.; PTM: On EPO stimulation, phosphorylated on C-terminal tyrosine residues by JAK2. The phosphotyrosine motifs are also recruitment sites for several SH2-containing proteins and adapter proteins which mediate cell ... | SUBCELLULAR LOCATION: [Isoform EPOR-F]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform EPOR-S]: Secreted. | null | null | null | null | null | FUNCTION: Receptor for erythropoietin. Mediates erythropoietin-induced erythroblast proliferation and differentiation. Upon EPO stimulation, EPOR dimerizes triggering the JAK2/STAT5 signaling cascade. In some cell types, can also activate STAT1 and STAT3. May also activate the LYN tyrosine kinase. {ECO:0000269|PubMed:8... | Mus musculus (Mouse) |
P14755 | CRYL1_RABIT | MASPAAGDVLIVGSGLVGRSWAMLFASGGFRVKLYDIEPRQITGALENIRKEMKSLQQSGSLKGSLSAEEQLSLISSCTNLAEAVEGVVHIQECVPENLDLKRKIFAQLDSIVDDRVVLSSSSSCLLPSKLFTGLAHVKQCIVAHPVNPPYYIPLVELVPHPETSPATVDRTHALMRKIGQSPVRVLKEIDGFVLNRLQYAIISEAWRLVEEGIVSPSDLDLVMSDGLGMRYAFIGPLETMHLNAEGMLSYCDRYSEGMKRVLKSFGSIPEFSGATVEKVNQAMCKKVPADPEHLAARREWRDECLKRLAKLKRQMQPQ | 1.1.1.45 | null | fatty acid metabolic process [GO:0006631] | cytosol [GO:0005829] | L-gulonate 3-dehydrogenase activity [GO:0050104]; NAD+ binding [GO:0070403]; protein homodimerization activity [GO:0042803]; structural constituent of eye lens [GO:0005212] | PF00725;PF02737; | 3.40.50.720; | 3-hydroxyacyl-CoA dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15809331}. | CATALYTIC ACTIVITY: Reaction=L-gulonate + NAD(+) = 3-dehydro-L-gulonate + H(+) + NADH; Xref=Rhea:RHEA:12889, ChEBI:CHEBI:13115, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57655, ChEBI:CHEBI:57945; EC=1.1.1.45; Evidence={ECO:0000269|PubMed:15809331}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.011 mM for NAD {ECO:0000269|PubMed:15809331}; KM=5.0E-4 mM for NADH {ECO:0000269|PubMed:15809331}; | null | null | null | FUNCTION: Functions as a crystallin in the rabbit eye lens. Has high L-gulonate 3-dehydrogenase activity. It also exhibits low dehydrogenase activity toward L-3-hydroxybutyrate (HBA) and L-threonate. {ECO:0000269|PubMed:15809331}. | Oryctolagus cuniculus (Rabbit) |
P14756 | ELAS_PSEAE | MKKVSTLDLLFVAIMGVSPAAFAADLIDVSKLPSKAAQGAPGPVTLQAAVGAGGADELKAIRSTTLPNGKQVTRYEQFHNGVRVVGEAITEVKGPGKSVAAQRSGHFVANIAADLPGSTTAAVSAEQVLAQAKSLKAQGRKTENDKVELVIRLGENNIAQLVYNVSYLIPGEGLSRPHFVIDAKTGEVLDQWEGLAHAEAGGPGGNQKIGKYTYGSDYGPLIVNDRCEMDDGNVITVDMNSSTDDSKTTPFRFACPTNTYKQVNGAYSPLNDAHFFGGVVFKLYRDWFGTSPLTHKLYMKVHYGRSVENAYWDGTAMLFG... | 3.4.24.26 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16, ECO:0000269|Ref.17}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:1899664, ECO:0000269|Ref.16, ECO:0000269|Ref.17}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:1899664, EC... | bacterial-type flagellum-dependent swarming motility [GO:0071978]; protein secretion by the type II secretion system [GO:0015628]; protein transport by the Sec complex [GO:0043952]; proteolysis [GO:0006508]; single-species biofilm formation [GO:0044010] | extracellular region [GO:0005576] | endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF07504;PF03413;PF01447;PF02868; | 3.10.170.10;3.10.450.40;3.10.450.490;1.10.390.10; | Peptidase M4 family | PTM: Made as a membrane-associated pre-pro-protein, which is exported to the periplasm (yielding pro-elastase) with removal of the signal peptide. Under certain conditions pro-elastase can accumulate. The pro-peptide is removed in the periplasm yielding a (mature length) 33 kDa protein, probably by autocatalysis (PubMe... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1597429, ECO:0000269|PubMed:3141383, ECO:0000269|PubMed:9642203}. Note=Secreted in an Xcp-dependent fashion (a type II secretion pathway). {ECO:0000269|PubMed:9642203}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins including elastin, collagen types III and IV, fibronectin and immunoglobulin A, generally with bulky hydrophobic group at P1'. Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects.; EC=3.4.24.26; | null | null | null | null | FUNCTION: Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase (PubMed:11533066). Autocatalyses processing of its pro-peptide (PubMed:1744034, PubMed:9642203). Processes the pro-peptide of pro-chitin-binding protein (cbpD) (PubMed:9642203). Involved in the path... | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
P14769 | GGTA1_BOVIN | MNVKGKVILSMLVVSTVIVVFWEYIHSPEGSLFWINPSRNPEVGGSSIQKGWWLPRWFNNGYHEEDGDINEEKEQRNEDESKLKLSDWFNPFKRPEVVTMTKWKAPVVWEGTYNRAVLDNYYAKQKITVGLTVFAVGRYIEHYLEEFLTSANKHFMVGHPVIFYIMVDDVSRMPLIELGPLRSFKVFKIKPEKRWQDISMMRMKTIGEHIVAHIQHEVDFLFCMDVDQVFQDKFGVETLGESVAQLQAWWYKADPNDFTYERRKESAAYIPFGEGDFYYHAAIFGGTPTQVLNITQECFKGILKDKKNDIEAQWHDESHL... | 2.4.1.87 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:11179209, ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:11179209, ECO:0000269|PubMed:11592969, ECO:0000269|PubMed:12011052}; | carbohydrate metabolic process [GO:0005975]; lipid glycosylation [GO:0030259]; protein glycosylation [GO:0006486] | Golgi apparatus [GO:0005794]; Golgi cisterna [GO:0031985]; Golgi cisterna membrane [GO:0032580]; vesicle [GO:0031982] | glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872]; N-acetyllactosaminide 3-alpha-galactosyltransferase activity [GO:0047276] | PF03414; | null | Glycosyltransferase 6 family | null | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein. Note=Membrane-bound form in trans cisternae of Golgi. | CATALYTIC ACTIVITY: Reaction=a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = an alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:13013, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914, ChEBI:CHEBI... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}. | null | null | FUNCTION: Synthesizes the galactose-alpha(1,3)-galactose group by catalyzing the transfer of a galactose residue, with an alpha-1,3 linkage, on terminal lactosaminide (Gal-beta-1,4-GlcNAc-R) disaccharide borne by a glycoprotein or a glycolipid. Preferentially glycosylates proteins, can synthesize galactose-alpha(1,3)-g... | Bos taurus (Bovine) |
P14770 | GPIX_HUMAN | MPAWGALFLLWATAEATKDCPSPCTCRALETMGLWVDCRGHGLTALPALPARTRHLLLANNSLQSVPPGAFDHLPQLQTLDVTQNPWHCDCSLTYLRLWLEDRTPEALLQVRCASPSLAAHGPLGRLTGYQLGSCGWQLQASWVRPGVLWDVALVAVAALGLALLAGLLCATTEALD | null | null | blood coagulation [GO:0007596]; blood coagulation, intrinsic pathway [GO:0007597]; cell adhesion [GO:0007155]; megakaryocyte development [GO:0035855]; positive regulation of platelet activation [GO:0010572]; release of sequestered calcium ion into cytosol [GO:0051209] | glycoprotein Ib-IX-V complex [GO:1990779]; plasma membrane [GO:0005886] | null | PF13855;PF01462; | 3.80.10.10; | null | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: The GPIb-V-IX complex functions as the vWF receptor and mediates vWF-dependent platelet adhesion to blood vessels. The adhesion of platelets to injured vascular surfaces in the arterial circulation is a critical initiating event in hemostasis. GP-IX may provide for membrane insertion and orientation of GP-Ib. | Homo sapiens (Human) |
P14772 | BPT1_YEAST | MSSLEVVDGCPYGYRPYPDSGTNALNPCFISVISAWQAVFFLLIGSYQLWKLYKNNKVPPRFKNFPTLPSKINSRHLTHLTNVCFQSTLIICELALVSQSSDRVYPFILKKALYLNLLFNLGISLPTQYLAYFKSTFSMGNQLFYYMFQILLQLFLILQRYYHGSSNERLTVISGQTAMILEVLLLFNSVAIFIYDLCIFEPINELSEYYKKNGWYPPVHVLSYITFIWMNKLIVETYRNKKIKDPNQLPLPPVDLNIKSISKEFKANWELEKWLNRNSLWRAIWKSFGRTISVAMLYETTSDLLSVVQPQFLRIFIDGL... | null | null | bilirubin transport [GO:0015723]; cadmium ion transport [GO:0015691]; transmembrane transport [GO:0055085]; vacuole fusion, non-autophagic [GO:0042144] | endoplasmic reticulum [GO:0005783]; fungal-type vacuole membrane [GO:0000329]; membrane [GO:0016020] | ABC-type transporter activity [GO:0140359]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; bilirubin transmembrane transporter activity [GO:0015127]; cadmium ion transmembrane transporter activity [GO:0015086] | PF00664;PF00005; | 1.20.1560.10;3.40.50.300; | ABC transporter superfamily | null | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:12044871}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441, ECO:0000269|PubMed:12044871}. | null | null | null | null | null | FUNCTION: Cooperates for the ATP-dependent vacuolar transport of bilirubin and glutathione conjugates. {ECO:0000269|PubMed:10790694, ECO:0000269|PubMed:12044871}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P14773 | HMDH_DROME | MIGRLFRAHGEFCASHPWEVIVALLTITACMLTVDKNNTLDASSGLGTATASAAAAGGSGSGAGSGASGTIPPSSMGGSATSSRHRPCHGWSQSCDGLEAEYNAADVILMTIVRCTAVLYCYYQFCSLHRLGSKYVLGIAGLFTVFSSFIFTTAIIKFLGSDISELKDALFFLLLVIDLSNSGRLAQLALSGSNQAEVTQNIARGLELLGPAISLDTIVEVLLVGVGTLSGVQRLEVLCMFAVLSVLVNYVVFMTFYPACLSLIFDLSRSGVDMSVVREKAKGSLLLKSLTEEEQKANPVLQRVKLIMTTGLMAVHIYSR... | 1.1.1.34 | null | coenzyme A metabolic process [GO:0015936]; ecdysis, chitin-based cuticle [GO:0018990]; embryonic heart tube development [GO:0035050]; ergosterol biosynthetic process [GO:0006696]; germ cell attraction [GO:0035232]; germ cell migration [GO:0008354]; gonad development [GO:0008406]; isoprenoid biosynthetic process [GO:000... | endoplasmic reticulum membrane [GO:0005789]; peroxisomal membrane [GO:0005778] | hydroxymethylglutaryl-CoA reductase (NADPH) activity [GO:0004420]; NADP binding [GO:0050661] | PF00368;PF12349; | 1.10.3270.10;3.30.70.420; | HMG-CoA reductase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + CoA + 2 NADP(+) = (3S)-hydroxy-3-methylglutaryl-CoA + 2 H(+) + 2 NADPH; Xref=Rhea:RHEA:15989, ChEBI:CHEBI:15378, ChEBI:CHEBI:36464, ChEBI:CHEBI:43074, ChEBI:CHEBI:57287, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.34; Evidence={ECO:0000255|PROSITE-ProRule:PRU10003}; | null | PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. | null | null | FUNCTION: Synthesis of mevalonate for the production of non-sterol isoprenoids, which are essential for growth differentiation. Provides spatial information during embryogenesis to guide migrating primordial germ cells (the pole cells) from the ectoderm to the mesoderm. Also required for association of the pole cells w... | Drosophila melanogaster (Fruit fly) |
P14778 | IL1R1_HUMAN | MKVLLRLICFIALLISSLEADKCKEREEKIILVSSANEIDVRPCPLNPNEHKGTITWYKDDSKTPVSTEQASRIHQHKEKLWFVPAKVEDSGHYYCVVRNSSYCLRIKISAKFVENEPNLCYNAQAIFKQKLPVAGDGGLVCPYMEFFKNENNELPKLQWYKDCKPLLLDNIHFSGVKDRLIVMNVAEKHRGNYTCHASYTYLGKQYPITRVIEFITLEENKPTRPVIVSPANETMEVDLGSQIQLICNVTGQLSDIAYWKWNGSVIDEDDPVLGEDYYSVENPANKRRSTLITVLNISEIESRFYKHPFTCFAKNTHGI... | 3.2.2.6 | null | cell surface receptor signaling pathway [GO:0007166]; immune response [GO:0006955]; inflammatory response [GO:0006954]; interleukin-1-mediated signaling pathway [GO:0070498]; positive regulation of interleukin-1-mediated signaling pathway [GO:2000661]; positive regulation of neutrophil extravasation [GO:2000391]; posit... | external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; membrane [GO:0016020]; plasma membrane [GO:0005886] | interleukin-1 binding [GO:0019966]; interleukin-1 receptor activity [GO:0004908]; interleukin-1, type I, activating receptor activity [GO:0004909]; NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]; platelet-derived growth factor receptor binding [GO:0005161]; proteas... | PF13895;PF18452;PF01582; | 2.60.40.10;3.40.50.10140; | Interleukin-1 receptor family | PTM: A soluble form (sIL1R1) is probably produced by proteolytic cleavage at the cell surface (shedding). {ECO:0000269|PubMed:8142597}.; PTM: Rapidly phosphorylated on Tyr-496 in response to IL-1, which creates a SH2 binding site for the PI 3-kinase regulatory subunit PIK3R1. {ECO:0000269|PubMed:9821957}. | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8142597}; Single-pass type I membrane protein {ECO:0000269|PubMed:8142597}. Cell membrane {ECO:0000305|PubMed:8142597}. Secreted {ECO:0000269|PubMed:8142597}. | CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU00204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Ev... | null | null | null | null | FUNCTION: Receptor for IL1A, IL1B and IL1RN (PubMed:2950091, PubMed:37315560). After binding to interleukin-1 associates with the coreceptor IL1RAP to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. Signaling involves the re... | Homo sapiens (Human) |
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