UniProtKB - P17246 (TGFB1_RAT)
Transforming growth factor beta-1 proprotein
Tgfb1
Functioni
GO - Molecular functioni
- antigen binding Source: AgBase
- cytokine activity Source: GO_Central
- enzyme binding Source: RGD
- growth factor activity Source: UniProtKB-KW
- identical protein binding Source: RGD
- protein-containing complex binding Source: RGD
- protein N-terminus binding Source: RGD
- protein serine/threonine kinase activator activity Source: RGD
- transforming growth factor beta receptor binding Source: RGD
- type III transforming growth factor beta receptor binding Source: AgBase
- type II transforming growth factor beta receptor binding Source: UniProtKB
- type I transforming growth factor beta receptor binding Source: AgBase
GO - Biological processi
- adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains Source: RGD
- aging Source: RGD
- animal organ regeneration Source: RGD
- aortic valve morphogenesis Source: RGD
- ATP biosynthetic process Source: UniProtKB
- BMP signaling pathway Source: GO_Central
- branch elongation involved in mammary gland duct branching Source: RGD
- cell activation Source: RGD
- cell-cell junction organization Source: UniProtKB
- cell cycle arrest Source: UniProtKB
- cell migration Source: UniProtKB
- cell population proliferation Source: RGD
- cellular calcium ion homeostasis Source: RGD
- cellular response to dexamethasone stimulus Source: UniProtKB
- cellular response to growth factor stimulus Source: RGD
- cellular response to insulin-like growth factor stimulus Source: RGD
- cellular response to ionizing radiation Source: RGD
- cellular response to mechanical stimulus Source: RGD
- cellular response to organic cyclic compound Source: UniProtKB
- cellular response to transforming growth factor beta stimulus Source: AgBase
- chondrocyte differentiation Source: UniProtKB
- common-partner SMAD protein phosphorylation Source: UniProtKB
- connective tissue development Source: RGD
- defense response to fungus, incompatible interaction Source: RGD
- digestive tract development Source: RGD
- embryonic liver development Source: RGD
- endoderm development Source: RGD
- epidermal growth factor receptor signaling pathway Source: UniProtKB
- epithelial to mesenchymal transition Source: RGD
- extracellular matrix assembly Source: UniProtKB
- extrinsic apoptotic signaling pathway Source: BHF-UCL
- face morphogenesis Source: RGD
- female pregnancy Source: RGD
- frontal suture morphogenesis Source: RGD
- germ cell migration Source: RGD
- heart development Source: RGD
- heart valve morphogenesis Source: RGD
- hematopoietic progenitor cell differentiation Source: UniProtKB
- hyaluronan catabolic process Source: UniProtKB
- inflammatory response Source: AgBase
- inner ear development Source: RGD
- lens fiber cell differentiation Source: RGD
- lipopolysaccharide-mediated signaling pathway Source: UniProtKB
- liver regeneration Source: RGD
- lung development Source: RGD
- lymph node development Source: RGD
- mammary gland branching involved in thelarche Source: RGD
- mammary gland development Source: RGD
- MAPK cascade Source: UniProtKB
- membrane protein intracellular domain proteolysis Source: UniProtKB
- mitotic cell cycle checkpoint Source: UniProtKB
- mononuclear cell proliferation Source: RGD
- morphogenesis of a branching structure Source: RGD
- muscle cell cellular homeostasis Source: RGD
- myelination Source: RGD
- myeloid dendritic cell differentiation Source: RGD
- negative regulation of biomineral tissue development Source: RGD
- negative regulation of blood vessel endothelial cell migration Source: UniProtKB
- negative regulation of cell-cell adhesion Source: UniProtKB
- negative regulation of cell cycle Source: UniProtKB
- negative regulation of cell differentiation Source: RGD
- negative regulation of cell growth Source: UniProtKB
- negative regulation of cell population proliferation Source: UniProtKB
- negative regulation of cytolysis Source: RGD
- negative regulation of epithelial cell proliferation Source: RGD
- negative regulation of fat cell differentiation Source: UniProtKB
- negative regulation of gene expression Source: BHF-UCL
- negative regulation of gene silencing by miRNA Source: RGD
- negative regulation of hyaluronan biosynthetic process Source: UniProtKB
- negative regulation of immune response Source: RGD
- negative regulation of interleukin-17 production Source: RGD
- negative regulation of macrophage cytokine production Source: AgBase
- negative regulation of mitotic cell cycle Source: UniProtKB
- negative regulation of myoblast differentiation Source: UniProtKB
- negative regulation of neuroblast proliferation Source: RGD
- negative regulation of ossification Source: RGD
- negative regulation of phagocytosis Source: RGD
- negative regulation of production of miRNAs involved in gene silencing by miRNA Source: RGD
- negative regulation of protein localization to plasma membrane Source: RGD
- negative regulation of protein phosphorylation Source: UniProtKB
- negative regulation of release of sequestered calcium ion into cytosol Source: RGD
- negative regulation of skeletal muscle tissue development Source: UniProtKB
- negative regulation of T cell activation Source: RGD
- negative regulation of T cell proliferation Source: RGD
- negative regulation of transcription, DNA-templated Source: UniProtKB
- negative regulation of transcription by RNA polymerase II Source: RGD
- neural tube closure Source: RGD
- neural tube development Source: RGD
- Notch signaling pathway Source: RGD
- odontogenesis of dentin-containing tooth Source: RGD
- oligodendrocyte development Source: RGD
- ossification involved in bone remodeling Source: AgBase
- osteoclast differentiation Source: RGD
- pathway-restricted SMAD protein phosphorylation Source: UniProtKB
- phosphate-containing compound metabolic process Source: UniProtKB
- positive regulation of apoptotic process Source: RGD
- positive regulation of blood vessel endothelial cell migration Source: UniProtKB
- positive regulation of bone mineralization Source: AgBase
- positive regulation of branching involved in ureteric bud morphogenesis Source: UniProtKB
- positive regulation of canonical Wnt signaling pathway Source: RGD
- positive regulation of cardiac muscle cell differentiation Source: RGD
- positive regulation of cell cycle arrest Source: RGD
- positive regulation of cell division Source: UniProtKB-KW
- positive regulation of cell migration Source: BHF-UCL
- positive regulation of cell population proliferation Source: UniProtKB
- positive regulation of cellular protein metabolic process Source: UniProtKB
- positive regulation of chemotaxis Source: UniProtKB
- positive regulation of collagen biosynthetic process Source: RGD
- positive regulation of epithelial cell proliferation Source: RGD
- positive regulation of epithelial to mesenchymal transition Source: UniProtKB
- positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
- positive regulation of exit from mitosis Source: RGD
- positive regulation of fibroblast migration Source: UniProtKB
- positive regulation of fibroblast proliferation Source: RGD
- positive regulation of gene expression Source: UniProtKB
- positive regulation of histone acetylation Source: RGD
- positive regulation of histone deacetylation Source: RGD
- positive regulation of interleukin-17 production Source: UniProtKB
- positive regulation of isotype switching to IgA isotypes Source: AgBase
- positive regulation of MAP kinase activity Source: UniProtKB
- positive regulation of microglia differentiation Source: UniProtKB
- positive regulation of mononuclear cell migration Source: RGD
- positive regulation of NAD+ ADP-ribosyltransferase activity Source: UniProtKB
- positive regulation of NF-kappaB transcription factor activity Source: RGD
- positive regulation of odontogenesis Source: RGD
- positive regulation of pathway-restricted SMAD protein phosphorylation Source: UniProtKB
- positive regulation of peptidyl-serine phosphorylation Source: UniProtKB
- positive regulation of peptidyl-threonine phosphorylation Source: UniProtKB
- positive regulation of peptidyl-tyrosine phosphorylation Source: RGD
- positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
- positive regulation of pri-miRNA transcription by RNA polymerase II Source: RGD
- positive regulation of production of miRNAs involved in gene silencing by miRNA Source: RGD
- positive regulation of protein-containing complex assembly Source: UniProtKB
- positive regulation of protein dephosphorylation Source: UniProtKB
- positive regulation of protein import into nucleus Source: AgBase
- positive regulation of protein kinase B signaling Source: UniProtKB
- positive regulation of protein localization to nucleus Source: RGD
- positive regulation of protein phosphorylation Source: UniProtKB
- positive regulation of protein secretion Source: UniProtKB
- positive regulation of receptor clustering Source: RGD
- positive regulation of regulatory T cell differentiation Source: RGD
- positive regulation of SMAD protein signal transduction Source: AgBase
- positive regulation of smooth muscle cell differentiation Source: MGI
- positive regulation of superoxide anion generation Source: UniProtKB
- positive regulation of transcription, DNA-templated Source: UniProtKB
- positive regulation of transcription by RNA polymerase II Source: AgBase
- positive regulation of transcription regulatory region DNA binding Source: UniProtKB
- positive regulation of vascular permeability Source: RGD
- protein export from nucleus Source: UniProtKB
- protein kinase B signaling Source: UniProtKB
- protein phosphorylation Source: CACAO
- receptor catabolic process Source: UniProtKB
- regulation of actin cytoskeleton reorganization Source: RGD
- regulation of binding Source: RGD
- regulation of branching involved in mammary gland duct morphogenesis Source: RGD
- regulation of cartilage development Source: RGD
- regulation of cell growth Source: RGD
- regulation of cell population proliferation Source: RGD
- regulation of DNA binding Source: RGD
- regulation of gene expression Source: RGD
- regulation of interleukin-23 production Source: RGD
- regulation of protein import into nucleus Source: RGD
- regulation of regulatory T cell differentiation Source: RGD
- regulation of SMAD protein signal transduction Source: UniProtKB
- regulation of sodium ion transport Source: RGD
- regulation of striated muscle tissue development Source: RGD
- regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
- regulatory T cell differentiation Source: RGD
- response to cholesterol Source: UniProtKB
- response to drug Source: RGD
- response to estradiol Source: RGD
- response to glucose Source: RGD
- response to hypoxia Source: RGD
- response to immobilization stress Source: RGD
- response to laminar fluid shear stress Source: RGD
- response to organic cyclic compound Source: RGD
- response to organic substance Source: RGD
- response to progesterone Source: UniProtKB
- response to radiation Source: RGD
- response to salt Source: RGD
- response to vitamin D Source: RGD
- response to wounding Source: AgBase
- salivary gland morphogenesis Source: AgBase
- SMAD protein complex assembly Source: UniProtKB
- SMAD protein signal transduction Source: GO_Central
- T cell activation Source: RGD
- T cell differentiation Source: RGD
- T cell homeostasis Source: RGD
- tolerance induction to self antigen Source: RGD
- transforming growth factor beta receptor signaling pathway Source: UniProtKB
- transforming growth factor beta receptor signaling pathway involved in heart development Source: RGD
- ureteric bud development Source: RGD
- vasculogenesis Source: RGD
- ventricular cardiac muscle tissue morphogenesis Source: RGD
- wound healing Source: RGD
Keywordsi
Molecular function | Growth factor, Mitogen |
Enzyme and pathway databases
Reactomei | R-RNO-114608, Platelet degranulation R-RNO-202733, Cell surface interactions at the vascular wall R-RNO-2129379, Molecules associated with elastic fibres R-RNO-2173788, Downregulation of TGF-beta receptor signaling R-RNO-2173789, TGF-beta receptor signaling activates SMADs R-RNO-2173791, TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) R-RNO-3000170, Syndecan interactions R-RNO-8941855, RUNX3 regulates CDKN1A transcription R-RNO-8941858, Regulation of RUNX3 expression and activity |
Names & Taxonomyi
Protein namesi | Recommended name: Transforming growth factor beta-1 proproteinCleaved into the following 2 chains: |
Gene namesi | Name:Tgfb1 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 69051, Tgfb1 |
Subcellular locationi
Extracellular region or secreted
- extracellular matrix By similarity
Extracellular region or secreted
- Secreted By similarity
Extracellular region or secreted
- blood microparticle Source: AgBase
- collagen-containing extracellular matrix Source: RGD
- extracellular matrix Source: RGD
- extracellular space Source: RGD
Nucleus
- nucleus Source: UniProtKB
Other locations
- axon Source: RGD
- cell surface Source: BHF-UCL
- cytoplasm Source: RGD
- neuronal cell body Source: RGD
- secretory granule Source: RGD
Keywords - Cellular componenti
Extracellular matrix, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 29 | By similarityAdd BLAST | 29 | |
ChainiPRO_0000033770 | 30 – 278 | Latency-associated peptideBy similarityAdd BLAST | 249 | |
ChainiPRO_0000033771 | 279 – 390 | Transforming growth factor beta-1By similarityAdd BLAST | 112 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Disulfide bondi | 33 | Interchain (with C-1359 or C-1384 in LTBP1); in inactive formBy similarity | ||
Glycosylationi | 82 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 136 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 176 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 223 | Interchain (with C-225)By similarity | ||
Disulfide bondi | 225 | Interchain (with C-223)By similarity | ||
Disulfide bondi | 285 ↔ 294 | By similarity | ||
Disulfide bondi | 293 ↔ 356 | By similarity | ||
Disulfide bondi | 322 ↔ 387 | By similarity | ||
Disulfide bondi | 326 ↔ 389 | By similarity | ||
Disulfide bondi | 355 | InterchainBy similarity |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 278 – 279 | Cleavage; by FURINBy similarity | 2 |
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, GlycoproteinProteomic databases
jPOSTi | P17246 |
PaxDbi | P17246 |
PRIDEi | P17246 |
PTM databases
GlyGeni | P17246, 3 sites |
PhosphoSitePlusi | P17246 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSRNOG00000020652, Expressed in spleen and 21 other tissues |
Genevisiblei | P17246, RN |
Interactioni
Subunit structurei
Homodimer; disulfide-linked (By similarity).
Interacts with the serine proteases, HTRA1 and HTRA3: the interaction with either inhibits TGFB1-mediated signaling. The HTRA protease activity is required for this inhibition. May interact with THSD4; this interaction may lead to sequestration by FBN1 microfibril assembly and attenuation of TGFB signaling (By similarity).
Interacts with CD109, DPT and ASPN. Latency-associated peptide: Homodimer; disulfide-linked. Latency-associated peptide:
Interacts with Transforming growth factor beta-1 (TGF-beta-1) chain; interaction is non-covalent and maintains (TGF-beta-1) in a latent state; each Latency-associated peptide (LAP) monomer interacts with TGF-beta-1 in the other monomer. Latency-associated peptide:
Interacts with LTBP1; leading to regulate activation of TGF-beta-1. Latency-associated peptide:
Interacts with LRRC32/GARP; leading to regulate activation of TGF-beta-1 on the surface of activated regulatory T-cells (Tregs).
Interacts with LRRC33/NRROS; leading to regulate activation of TGF-beta-1 in macrophages and microglia. Latency-associated peptide:
Interacts (via cell attachment site) with integrins ITGAV and ITGB6 (ITGAV:ITGB6), leading to release of the active TGF-beta-1 (By similarity). Latency-associated peptide:
Interacts with NREP; the interaction results in a decrease in TGFB1 autoinduction (By similarity). Latency-associated peptide:
Interacts with HSP90AB1; inhibits latent TGFB1 activation. Transforming growth factor beta-1: Homodimer; disulfide-linked. Transforming growth factor beta-1:
Interacts with TGF-beta receptors (TGFBR1 and TGFBR2), leading to signal transduction (By similarity).
By similarityGO - Molecular functioni
- cytokine activity Source: GO_Central
- enzyme binding Source: RGD
- growth factor activity Source: UniProtKB-KW
- identical protein binding Source: RGD
- protein N-terminus binding Source: RGD
- transforming growth factor beta receptor binding Source: RGD
- type III transforming growth factor beta receptor binding Source: AgBase
- type II transforming growth factor beta receptor binding Source: UniProtKB
- type I transforming growth factor beta receptor binding Source: AgBase
Protein-protein interaction databases
BioGRIDi | 248721, 1 interactor |
DIPi | DIP-6247N |
STRINGi | 10116.ENSRNOP00000028051 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 30 – 74 | Straightjacket domainBy similarityAdd BLAST | 45 | |
Regioni | 75 – 271 | Arm domainBy similarityAdd BLAST | 197 | |
Regioni | 226 – 252 | Bowtie tailBy similarityAdd BLAST | 27 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 244 – 246 | Cell attachment siteSequence analysis | 3 |
Domaini
Sequence similaritiesi
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | KOG3900, Eukaryota |
GeneTreei | ENSGT00940000160457 |
HOGENOMi | CLU_039840_0_0_1 |
InParanoidi | P17246 |
OMAi | FSAHCSC |
OrthoDBi | 643840at2759 |
PhylomeDBi | P17246 |
TreeFami | TF318514 |
Family and domain databases
Gene3Di | 2.10.90.10, 1 hit |
InterProi | View protein in InterPro IPR029034, Cystine-knot_cytokine IPR001839, TGF-b_C IPR001111, TGF-b_propeptide IPR016319, TGF-beta IPR015615, TGF-beta-rel IPR003939, TGFb1 IPR017948, TGFb_CS |
PANTHERi | PTHR11848, PTHR11848, 1 hit |
Pfami | View protein in Pfam PF00019, TGF_beta, 1 hit PF00688, TGFb_propeptide, 1 hit |
PIRSFi | PIRSF001787, TGF-beta, 1 hit |
PRINTSi | PR01423, TGFBETA PR01424, TGFBETA1 |
SMARTi | View protein in SMART SM00204, TGFB, 1 hit |
SUPFAMi | SSF57501, SSF57501, 1 hit |
PROSITEi | View protein in PROSITE PS00250, TGF_BETA_1, 1 hit PS51362, TGF_BETA_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
10 20 30 40 50
MPPSGLRLLP LLLPLPWLLV LTPGRPAAGL STCKTIDMEL VKRKRIEAIR
60 70 80 90 100
GQILSKLRLA SPPSQGEVPP GPLPEAVLAL YNSTRDRVAG ESADPEPEPE
110 120 130 140 150
ADYYAKEVTR VLMVDRNNAI YDKTKDITHS IYMFFNTSDI REAVPEPPLL
160 170 180 190 200
SRAELRLQRF KSTVEQHVEL YQKYSNNSWR YLGNRLLTPT DTPEWLSFDV
210 220 230 240 250
TGVVRQWLNQ GDGIQGFRFS AHCSCDSKDN VLHVEINGIS PKRRGDLGTI
260 270 280 290 300
HDMNRPFLLL MATPLERAQH LHSSRHRRAL DTNYCFSSTE KNCCVRQLYI
310 320 330 340 350
DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA
360 370 380 390
SASPCCVPQA LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X52498 mRNA Translation: CAA36741.1 AY550025 mRNA Translation: AAS55640.1 BC076380 mRNA Translation: AAH76380.1 |
PIRi | S10219 |
RefSeqi | NP_067589.1, NM_021578.2 |
Genome annotation databases
Ensembli | ENSRNOT00000028051; ENSRNOP00000028051; ENSRNOG00000020652 |
GeneIDi | 59086 |
KEGGi | rno:59086 |
UCSCi | RGD:69051, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X52498 mRNA Translation: CAA36741.1 AY550025 mRNA Translation: AAS55640.1 BC076380 mRNA Translation: AAH76380.1 |
PIRi | S10219 |
RefSeqi | NP_067589.1, NM_021578.2 |
3D structure databases
SMRi | P17246 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 248721, 1 interactor |
DIPi | DIP-6247N |
STRINGi | 10116.ENSRNOP00000028051 |
PTM databases
GlyGeni | P17246, 3 sites |
PhosphoSitePlusi | P17246 |
Proteomic databases
jPOSTi | P17246 |
PaxDbi | P17246 |
PRIDEi | P17246 |
Genome annotation databases
Ensembli | ENSRNOT00000028051; ENSRNOP00000028051; ENSRNOG00000020652 |
GeneIDi | 59086 |
KEGGi | rno:59086 |
UCSCi | RGD:69051, rat |
Organism-specific databases
CTDi | 7040 |
RGDi | 69051, Tgfb1 |
Phylogenomic databases
eggNOGi | KOG3900, Eukaryota |
GeneTreei | ENSGT00940000160457 |
HOGENOMi | CLU_039840_0_0_1 |
InParanoidi | P17246 |
OMAi | FSAHCSC |
OrthoDBi | 643840at2759 |
PhylomeDBi | P17246 |
TreeFami | TF318514 |
Enzyme and pathway databases
Reactomei | R-RNO-114608, Platelet degranulation R-RNO-202733, Cell surface interactions at the vascular wall R-RNO-2129379, Molecules associated with elastic fibres R-RNO-2173788, Downregulation of TGF-beta receptor signaling R-RNO-2173789, TGF-beta receptor signaling activates SMADs R-RNO-2173791, TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) R-RNO-3000170, Syndecan interactions R-RNO-8941855, RUNX3 regulates CDKN1A transcription R-RNO-8941858, Regulation of RUNX3 expression and activity |
Miscellaneous databases
PROi | PR:P17246 |
Gene expression databases
Bgeei | ENSRNOG00000020652, Expressed in spleen and 21 other tissues |
Genevisiblei | P17246, RN |
Family and domain databases
Gene3Di | 2.10.90.10, 1 hit |
InterProi | View protein in InterPro IPR029034, Cystine-knot_cytokine IPR001839, TGF-b_C IPR001111, TGF-b_propeptide IPR016319, TGF-beta IPR015615, TGF-beta-rel IPR003939, TGFb1 IPR017948, TGFb_CS |
PANTHERi | PTHR11848, PTHR11848, 1 hit |
Pfami | View protein in Pfam PF00019, TGF_beta, 1 hit PF00688, TGFb_propeptide, 1 hit |
PIRSFi | PIRSF001787, TGF-beta, 1 hit |
PRINTSi | PR01423, TGFBETA PR01424, TGFBETA1 |
SMARTi | View protein in SMART SM00204, TGFB, 1 hit |
SUPFAMi | SSF57501, SSF57501, 1 hit |
PROSITEi | View protein in PROSITE PS00250, TGF_BETA_1, 1 hit PS51362, TGF_BETA_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TGFB1_RAT | |
Accessioni | P17246Primary (citable) accession number: P17246 Secondary accession number(s): Q53YM8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1990 |
Last sequence update: | August 1, 1990 | |
Last modified: | December 2, 2020 | |
This is version 184 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families