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Q64729

- TGFR1_MOUSE

UniProt

Q64729 - TGFR1_MOUSE

Protein

TGF-beta receptor type-1

Gene

Tgfbr1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 144 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Transmembrane serine/threonine kinase forming with the TGF-beta type II serine/threonine kinase receptor, TGFBR2, the non-promiscuous receptor for the TGF-beta cytokines TGFB1, TGFB2 and TGFB3. Transduces the TGFB1, TGFB2 and TGFB3 signal from the cell surface to the cytoplasm and is thus regulating a plethora of physiological and pathological processes including cell cycle arrest in epithelial and hematopoietic cells, control of mesenchymal cell proliferation and differentiation, wound healing, extracellular matrix production, immunosuppression and carcinogenesis. The formation of the receptor complex composed of 2 TGFBR1 and 2 TGFBR2 molecules symmetrically bound to the cytokine dimer results in the phosphorylation and the activation of TGFBR1 by the constitutively active TGFBR2. Activated TGFBR1 phosphorylates SMAD2 which dissociates from the receptor and interacts with SMAD4. The SMAD2-SMAD4 complex is subsequently translocated to the nucleus where it modulates the transcription of the TGF-beta-regulated genes. This constitutes the canonical SMAD-dependent TGF-beta signaling cascade. Also involved in non-canonical, SMAD-independent TGF-beta signaling pathways. For instance, TGFBR1 induces TRAF6 autoubiquitination which in turn results in MAP3K7 ubiquitination and activation to trigger apoptosis. Also regulates epithelial to mesenchymal transition through a SMAD-independent signaling pathway through PARD6A phosphorylation and activation By similarity.By similarity

    Catalytic activityi

    ATP + [receptor-protein] = ADP + [receptor-protein] phosphate.

    Cofactori

    Magnesium or manganese.By similarity

    Enzyme regulationi

    Kept in an inactive conformation by FKBP1A preventing receptor activation in absence of ligand. CD109 is another inhibitor of the receptor By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei232 – 2321ATPPROSITE-ProRule annotation
    Active sitei333 – 3331Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi211 – 2199ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. receptor signaling protein serine/threonine kinase activity Source: InterPro
    5. SMAD binding Source: BHF-UCL
    6. transforming growth factor beta-activated receptor activity Source: MGI
    7. transforming growth factor beta binding Source: MGI
    8. transforming growth factor beta receptor activity, type I Source: Ensembl

    GO - Biological processi

    1. activation of MAPKK activity Source: Ensembl
    2. angiogenesis Source: MGI
    3. anterior/posterior pattern specification Source: MGI
    4. apoptotic process Source: UniProtKB-KW
    5. artery morphogenesis Source: MGI
    6. blastocyst development Source: MGI
    7. cellular response to transforming growth factor beta stimulus Source: BHF-UCL
    8. collagen fibril organization Source: MGI
    9. embryonic cranial skeleton morphogenesis Source: MGI
    10. endothelial cell migration Source: MGI
    11. epithelial to mesenchymal transition Source: Ensembl
    12. germ cell migration Source: MGI
    13. heart development Source: MGI
    14. in utero embryonic development Source: MGI
    15. kidney development Source: MGI
    16. lens development in camera-type eye Source: MGI
    17. negative regulation of apoptotic process Source: MGI
    18. negative regulation of chondrocyte differentiation Source: BHF-UCL
    19. negative regulation of endothelial cell proliferation Source: MGI
    20. negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
    21. neuron fate commitment Source: MGI
    22. palate development Source: MGI
    23. parathyroid gland development Source: MGI
    24. pathway-restricted SMAD protein phosphorylation Source: Ensembl
    25. peptidyl-serine phosphorylation Source: Ensembl
    26. peptidyl-threonine phosphorylation Source: Ensembl
    27. pharyngeal system development Source: MGI
    28. positive regulation of apoptotic signaling pathway Source: Ensembl
    29. positive regulation of cell growth Source: Ensembl
    30. positive regulation of cell proliferation Source: Ensembl
    31. positive regulation of cellular component movement Source: Ensembl
    32. positive regulation of filopodium assembly Source: MGI
    33. positive regulation of pathway-restricted SMAD protein phosphorylation Source: Ensembl
    34. positive regulation of protein kinase B signaling Source: Ensembl
    35. positive regulation of SMAD protein import into nucleus Source: Ensembl
    36. positive regulation of transcription, DNA-templated Source: Ensembl
    37. post-embryonic development Source: MGI
    38. regulation of gene expression Source: MGI
    39. regulation of protein binding Source: MGI
    40. regulation of protein ubiquitination Source: Ensembl
    41. response to cholesterol Source: BHF-UCL
    42. skeletal system development Source: MGI
    43. skeletal system morphogenesis Source: MGI
    44. thymus development Source: MGI
    45. transforming growth factor beta receptor signaling pathway Source: MGI

    Keywords - Molecular functioni

    Kinase, Receptor, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Differentiation, Growth regulation

    Keywords - Ligandi

    ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 3474.
    ReactomeiREACT_196549. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_203510. TGF-beta receptor signaling activates SMADs.
    REACT_215733. Downregulation of TGF-beta receptor signaling.
    REACT_216792. SMAD2/3 MH2 Domain Mutants in Cancer.
    REACT_217958. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
    REACT_224217. TGFBR1 LBD Mutants in Cancer.
    REACT_224787. TGFBR2 Kinase Domain Mutants in Cancer.
    REACT_224802. TGFBR1 KD Mutants in Cancer.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    TGF-beta receptor type-1 (EC:2.7.11.30)
    Short name:
    TGFR-1
    Alternative name(s):
    ESK2
    Transforming growth factor-beta receptor type I
    Short name:
    TGF-beta receptor type I
    Short name:
    TbetaR-I
    Gene namesi
    Name:Tgfbr1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:98728. Tgfbr1.

    Subcellular locationi

    Cell membrane By similarity; Single-pass type I membrane protein By similarity. Cell junctiontight junction By similarity

    GO - Cellular componenti

    1. caveola Source: MGI
    2. endosome Source: UniProt
    3. integral component of membrane Source: UniProtKB-KW
    4. membrane raft Source: MGI
    5. receptor complex Source: Ensembl
    6. tight junction Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Tight junction

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929By similarityAdd
    BLAST
    Chaini30 – 503474TGF-beta receptor type-1PRO_0000024424Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi32 ↔ 50By similarity
    Disulfide bondi34 ↔ 37By similarity
    Glycosylationi41 – 411N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi44 ↔ 67By similarity
    Disulfide bondi82 ↔ 96By similarity
    Disulfide bondi97 ↔ 102By similarity
    Modified residuei165 – 1651PhosphoserineBy similarity
    Modified residuei185 – 1851Phosphothreonine; by TGFBR2By similarity
    Modified residuei186 – 1861Phosphothreonine; by TGFBR2By similarity
    Modified residuei187 – 1871Phosphoserine; by TGFBR2By similarity
    Modified residuei189 – 1891Phosphoserine; by TGFBR2By similarity
    Modified residuei191 – 1911Phosphoserine; by TGFBR2By similarity
    Cross-linki391 – 391Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

    Post-translational modificationi

    Phosphorylated at basal levels in the absence of ligand. Activated upon phosphorylation by TGFBR2, mainly in the GS domain. Phosphorylation in the GS domain abrogates FKBP1A-binding By similarity.By similarity
    N-Glycosylated.By similarity
    Ubiquitinated; undergoes ubiquitination catalyzed by several E3 ubiquitin ligases including SMURF1, SMURF2 and NEDD4L2. Results in the proteasomal and/or lysosomal degradation of the receptor thereby negatively regulating its activity. Deubiquitinated by USP15, leading to stabilization of the protein and enhanced TGF-beta signal By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ64729.

    PTM databases

    PhosphoSiteiQ64729.

    Expressioni

    Gene expression databases

    ArrayExpressiQ64729.
    BgeeiQ64729.
    CleanExiMM_TGFBR1.
    GenevestigatoriQ64729.

    Interactioni

    Subunit structurei

    Homodimer; in the endoplasmic reticulum but also at the cell membrane. Heterohexamer; TGFB1, TGFB2 and TGFB3 homodimeric ligands assemble a functional receptor composed of two TGFBR1 and TGFBR2 heterodimers to form a ligand-receptor heterohexamer. The respective affinity of TGBRB1 and TGFBR2 for the ligands may modulate the kinetics of assembly of the receptor and may explain the different biological activities of TGFB1, TGFB2 and TGFB3. Interacts with CD109; inhibits TGF-beta receptor activation in keratinocytes. Interacts with RBPMS. Interacts (unphosphorylated) with FKBP1A; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation. Interacts with SMAD2, SMAD3 and ZFYVE9; ZFYVE9 recruits SMAD2 and SMAD3 to the TGF-beta receptor. Interacts with TRAF6 and MAP3K7; induces MAP3K7 activation by TRAF6. Interacts with PARD6A; involved in TGF-beta induced epithelial to mesenchymal transition. Interacts with SMAD7, NEDD4L, SMURF1 and SMURF2; SMAD7 recruits NEDD4L, SMURF1 and SMURF2 to the TGF-beta receptor By similarity. Interacts with USP15 and VPS39 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Cdh5P552842EBI-2899393,EBI-7087433
    DLG5Q8TDM63EBI-2899393,EBI-715138From a different organism.
    Shc1P98083-23EBI-2899393,EBI-1019301

    Protein-protein interaction databases

    BioGridi204163. 9 interactions.
    DIPiDIP-42262N.
    IntActiQ64729. 9 interactions.
    MINTiMINT-1341331.

    Structurei

    3D structure databases

    ProteinModelPortaliQ64729.
    SMRiQ64729. Positions 27-110, 175-500.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini30 – 12697ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini148 – 503356CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei127 – 14721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini175 – 20430GSPROSITE-ProRule annotationAdd
    BLAST
    Domaini205 – 495291Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi193 – 1942FKBP1A-binding

    Sequence similaritiesi

    Contains 1 GS domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00730000110337.
    HOGENOMiHOG000230587.
    HOVERGENiHBG054502.
    InParanoidiQ64729.
    KOiK04674.
    OMAiLYICHNR.
    OrthoDBiEOG7Q8CN3.
    PhylomeDBiQ64729.
    TreeFamiTF314724.

    Family and domain databases

    InterProiIPR000472. Activin_rcpt.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    IPR003605. TGF_beta_rcpt_GS.
    IPR000333. TGFB_receptor.
    [Graphical view]
    PANTHERiPTHR23255. PTHR23255. 1 hit.
    PfamiPF01064. Activin_recp. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF08515. TGF_beta_GS. 1 hit.
    [Graphical view]
    SMARTiSM00467. GS. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51256. GS. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q64729-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEAAAAAPRR PQLLIVLVAA ATLLPGAKAL QCFCHLCTKD NFTCETDGLC    50
    FVSVTETTDK VIHNSMCIAE IDLIPRDRPF VCAPSSKTGA VTTTYCCNQD 100
    HCNKIELPTT GPFSEKQSAG LGPVELAAVI AGPVCFVCIA LMLMVYICHN 150
    RTVIHHRVPN EEDPSLDRPF ISEGTTLKDL IYDMTTSGSG SGLPLLVQRT 200
    IARTIVLQES IGKGRFGEVW RGKWRGEEVA VKIFSSREER SWFREAEIYQ 250
    TVMLRHENIL GFIAADNKDN GTWTQLWLVS DYHEHGSLFD YLNRYTVTVE 300
    GMIKLALSTA SGLAHLHMEI VGTQGKPAIA HRDLKSKNIL VKKNGTCCIA 350
    DLGLAVRHDS ATDTIDIAPN HRVGTKRYMA PEVLDDSINM KHFESFKRAD 400
    IYAMGLVFWE IARRCSIGGI HEDYQLPYYD LVPSDPSVEE MRKVVCEQKL 450
    RPNIPNRWQS CEALRVMAKI MRECWYANGA ARLTALRIKK TLSQLSQQEG 500
    IKM 503
    Length:503
    Mass (Da):56,179
    Last modified:November 1, 1996 - v1
    Checksum:iBB8BB6D2261793AF
    GO
    Isoform 2 (identifier: Q64729-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         111-114: Missing.

    Note: May be due to a competing donnor splice site.

    Show »
    Length:499
    Mass (Da):55,790
    Checksum:i914DE6236B689C1C
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei111 – 1144Missing in isoform 2. 1 PublicationVSP_021593

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D28526 mRNA. Translation: BAA05878.1.
    D25540 mRNA. Translation: BAA05023.1.
    AL772232, AL772150 Genomic DNA. Translation: CAM13897.1.
    AL772150, AL772232 Genomic DNA. Translation: CAM24923.1.
    BC063260 mRNA. Translation: AAH63260.1.
    CCDSiCCDS18160.1. [Q64729-1]
    PIRiJC2061.
    JC2062.
    RefSeqiNP_033396.1. NM_009370.2. [Q64729-1]
    UniGeneiMm.197552.

    Genome annotation databases

    EnsembliENSMUST00000007757; ENSMUSP00000007757; ENSMUSG00000007613. [Q64729-1]
    ENSMUST00000044234; ENSMUSP00000048501; ENSMUSG00000007613. [Q64729-2]
    GeneIDi21812.
    KEGGimmu:21812.
    UCSCiuc008sun.1. mouse. [Q64729-1]
    uc008suo.1. mouse. [Q64729-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D28526 mRNA. Translation: BAA05878.1 .
    D25540 mRNA. Translation: BAA05023.1 .
    AL772232 , AL772150 Genomic DNA. Translation: CAM13897.1 .
    AL772150 , AL772232 Genomic DNA. Translation: CAM24923.1 .
    BC063260 mRNA. Translation: AAH63260.1 .
    CCDSi CCDS18160.1. [Q64729-1 ]
    PIRi JC2061.
    JC2062.
    RefSeqi NP_033396.1. NM_009370.2. [Q64729-1 ]
    UniGenei Mm.197552.

    3D structure databases

    ProteinModelPortali Q64729.
    SMRi Q64729. Positions 27-110, 175-500.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204163. 9 interactions.
    DIPi DIP-42262N.
    IntActi Q64729. 9 interactions.
    MINTi MINT-1341331.

    Chemistry

    ChEMBLi CHEMBL2021750.

    PTM databases

    PhosphoSitei Q64729.

    Proteomic databases

    PRIDEi Q64729.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000007757 ; ENSMUSP00000007757 ; ENSMUSG00000007613 . [Q64729-1 ]
    ENSMUST00000044234 ; ENSMUSP00000048501 ; ENSMUSG00000007613 . [Q64729-2 ]
    GeneIDi 21812.
    KEGGi mmu:21812.
    UCSCi uc008sun.1. mouse. [Q64729-1 ]
    uc008suo.1. mouse. [Q64729-2 ]

    Organism-specific databases

    CTDi 7046.
    MGIi MGI:98728. Tgfbr1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00730000110337.
    HOGENOMi HOG000230587.
    HOVERGENi HBG054502.
    InParanoidi Q64729.
    KOi K04674.
    OMAi LYICHNR.
    OrthoDBi EOG7Q8CN3.
    PhylomeDBi Q64729.
    TreeFami TF314724.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 3474.
    Reactomei REACT_196549. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_203510. TGF-beta receptor signaling activates SMADs.
    REACT_215733. Downregulation of TGF-beta receptor signaling.
    REACT_216792. SMAD2/3 MH2 Domain Mutants in Cancer.
    REACT_217958. SMAD2/3 Phosphorylation Motif Mutants in Cancer.
    REACT_224217. TGFBR1 LBD Mutants in Cancer.
    REACT_224787. TGFBR2 Kinase Domain Mutants in Cancer.
    REACT_224802. TGFBR1 KD Mutants in Cancer.

    Miscellaneous databases

    ChiTaRSi TGFBR1. mouse.
    NextBioi 301202.
    PROi Q64729.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q64729.
    Bgeei Q64729.
    CleanExi MM_TGFBR1.
    Genevestigatori Q64729.

    Family and domain databases

    InterProi IPR000472. Activin_rcpt.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR008271. Ser/Thr_kinase_AS.
    IPR003605. TGF_beta_rcpt_GS.
    IPR000333. TGFB_receptor.
    [Graphical view ]
    PANTHERi PTHR23255. PTHR23255. 1 hit.
    Pfami PF01064. Activin_recp. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF08515. TGF_beta_GS. 1 hit.
    [Graphical view ]
    SMARTi SM00467. GS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51256. GS. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a mouse counterpart for human TGF-beta type I receptor."
      Tomoda T., Kudoh T., Noma T., Nakazawa A., Muramatsu M.-A., Arai K.
      Biochem. Biophys. Res. Commun. 198:1054-1062(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain and Testis.
    2. "A mouse TGF-beta type I receptor that requires type II receptor for ligand binding."
      Suzuki A., Shioda N., Maeda T., Tada M., Ueno N.
      Biochem. Biophys. Res. Commun. 198:1063-1069(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6.
      Tissue: Brain.

    Entry informationi

    Entry nameiTGFR1_MOUSE
    AccessioniPrimary (citable) accession number: Q64729
    Secondary accession number(s): A2AJN0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 144 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3