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P09760

- FER_RAT

UniProt

P09760 - FER_RAT

Protein

Tyrosine-protein kinase Fer

Gene

Fer

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (21 Sep 2011)
      Previous versions | rss
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    Functioni

    Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream of EGFR to promote activation of NF-kappa-B and cell proliferation. May play a role in the regulation of the mitotic cell cycle. Plays a role in the insulin receptor signaling pathway and in activation of phosphatidylinositol 3-kinase. Acts downstream of the activated FCER1 receptor and plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Plays a role in the regulation of mast cell degranulation. Plays a role in leukocyte recruitment and diapedesis in response to bacterial lipopolysaccharide (LPS). Plays a role in neuronal cell death after brain damage. Phosphorylates CTTN, CTNND1, PTK2/FAK1, GAB1, PECAM1 and PTPN11. May phosphorylate JUP and PTPN1. Can phosphorylate STAT3, but the biological relevance of this clearly depends on cell type and stimulus By similarity. Plays a role in synapse organization, trafficking of synaptic vesicles, the generation of excitatory postsynaptic currents and neuron-neuron synaptic transmission.By similarity1 Publication

    Catalytic activityi

    ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei592 – 5921ATPPROSITE-ProRule annotation
    Active sitei685 – 6851Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi570 – 5789ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. actin binding Source: RGD
    2. ATP binding Source: UniProtKB-KW
    3. cadherin binding Source: RGD
    4. cell adhesion molecule binding Source: RGD
    5. cytoskeletal protein binding Source: RGD
    6. epidermal growth factor receptor binding Source: UniProtKB
    7. gamma-catenin binding Source: RGD
    8. lipid binding Source: UniProtKB
    9. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
    10. protein kinase binding Source: RGD
    11. Rab GTPase binding Source: RGD

    GO - Biological processi

    1. actin cytoskeleton reorganization Source: UniProtKB
    2. cell-cell adhesion mediated by cadherin Source: UniProtKB
    3. cell proliferation Source: Ensembl
    4. cellular response to insulin stimulus Source: UniProtKB
    5. cellular response to macrophage colony-stimulating factor stimulus Source: Ensembl
    6. cellular response to reactive oxygen species Source: UniProtKB
    7. chemotaxis Source: Ensembl
    8. cytokine-mediated signaling pathway Source: UniProtKB
    9. diapedesis Source: UniProtKB
    10. extracellular matrix-cell signaling Source: UniProtKB
    11. Fc-epsilon receptor signaling pathway Source: UniProtKB
    12. insulin receptor signaling pathway via phosphatidylinositol 3-kinase Source: UniProtKB
    13. interleukin-6-mediated signaling pathway Source: Ensembl
    14. Kit signaling pathway Source: UniProtKB
    15. microtubule cytoskeleton organization Source: UniProtKB
    16. mitotic cell cycle Source: Ensembl
    17. negative regulation of mast cell activation involved in immune response Source: UniProtKB
    18. peptidyl-tyrosine phosphorylation Source: UniProtKB
    19. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
    20. positive regulation of actin filament polymerization Source: UniProtKB
    21. positive regulation of cell migration Source: UniProtKB
    22. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    23. protein autophosphorylation Source: Ensembl
    24. regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
    25. regulation of fibroblast migration Source: Ensembl
    26. regulation of lamellipodium assembly Source: UniProtKB
    27. regulation of protein phosphorylation Source: UniProtKB
    28. response to lipopolysaccharide Source: UniProtKB
    29. response to platelet-derived growth factor Source: UniProtKB
    30. substrate adhesion-dependent cell spreading Source: UniProtKB
    31. tyrosine phosphorylation of Stat3 protein Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Lipid-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_195025. Signaling by SCF-KIT.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase Fer (EC:2.7.10.2)
    Alternative name(s):
    Proto-oncogene c-Fer
    Tyrosine-protein kinase FLK
    p94-Fer
    Gene namesi
    Name:Fer
    Synonyms:Fert2, Flk
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 9

    Organism-specific databases

    RGDi1306273. Fert2.

    Subcellular locationi

    Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cell projection By similarity. Cell junction By similarity. Membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Nucleus By similarity. Cytoplasmcell cortex By similarity
    Note: Associated with the chromatin. Detected on microtubules in polarized and motile vascular endothelial cells. Colocalizes with F-actin at the cell cortex. Colocalizes with PECAM1 and CTNND1 at nascent cell-cell contacts By similarity.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: Ensembl
    2. cell cortex Source: UniProtKB-SubCell
    3. cell junction Source: UniProtKB-SubCell
    4. cytoplasm Source: UniProtKB
    5. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
    6. lamellipodium Source: Ensembl
    7. microtubule cytoskeleton Source: Ensembl
    8. nuclear chromatin Source: Ensembl

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 823823Tyrosine-protein kinase FerPRO_0000088093Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei402 – 4021PhosphotyrosineBy similarity
    Modified residuei434 – 4341PhosphoserineBy similarity
    Modified residuei616 – 6161Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei715 – 7151Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    Autophosphorylated.By similarity
    Polyubiquitinated; this leads to proteasomal degradation.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP09760.
    PRIDEiP09760.

    PTM databases

    PhosphoSiteiP09760.

    Expressioni

    Gene expression databases

    GenevestigatoriP09760.

    Interactioni

    Subunit structurei

    Homotrimer. Interacts with IRS1, JAK1, NRP1, PIK3R1, PLEC and TMF1. Interacts with PPP1CA and regulates its phosphorylation at 'Thr-320'. Interacts with CTNND1, EGFR, FLT3, PECAM1, PDGFR and STAT3. Interacts (via SH2 domain) with CTTN. Interacts with HSP90; this stabilizes phosphorylated FER and protects FER against proteasomal degradation. Component of a complex that contains at least FER, CTTN and PTK2/FAK1 By similarity. Interacts with ARHGDIA.By similarity1 Publication

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000021758.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 5858FCHPROSITE-ProRule annotationAdd
    BLAST
    Domaini461 – 55191SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini564 – 815252Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 300300Important for interaction with membranes containing phosphoinositidesBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili123 – 18563Sequence AnalysisAdd
    BLAST
    Coiled coili301 – 38282Sequence AnalysisAdd
    BLAST

    Domaini

    The coiled coil domains mediate homooligomerization and are required for location at microtubules.By similarity
    The N-terminal region including the first coiled coil domain mediates interaction with phosphoinositide-containing membranes.By similarity

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. Fes/fps subfamily.PROSITE-ProRule annotation
    Contains 1 FCH domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, SH2 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117264.
    HOGENOMiHOG000233858.
    HOVERGENiHBG001540.
    InParanoidiP09760.
    KOiK08889.
    OMAiFVDNLYR.
    OrthoDBiEOG708VXW.
    TreeFamiTF315363.

    Family and domain databases

    Gene3Di3.30.505.10. 1 hit.
    InterProiIPR001060. FCH_dom.
    IPR028539. Fer.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR016250. Tyr-prot_kinase_Fes/Fps.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view]
    PANTHERiPTHR24418:SF227. PTHR24418:SF227. 1 hit.
    PfamiPF00611. FCH. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000632. TyrPK_fps. 1 hit.
    PRINTSiPR00401. SH2DOMAIN.
    PR00109. TYRKINASE.
    SMARTiSM00055. FCH. 1 hit.
    SM00252. SH2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50133. FCH. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P09760-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGFGSDLKNS QEAVLKLQDW ELRLLETVKK FMALRIKSDK EYAYTLQNLC    50
    NQVDKDSTVQ VNYVSNVSKS WLLMIQQTEQ LSRIMKTHAE DLNSGPLHRL 100
    TMMIKDKQQV KKSYVGIHQQ IEAEMIKVTK TELEKLKSSY RQLIKEMNSA 150
    KEKYKEALAK GKETEKAKER CDKATMKLHM LHNQYVLALK GAQLHQSQYY 200
    DTTLPLLLDS VQKMQEEMIK ALKGIFDEYS EITSLVTEEI VNVHKEIQMS 250
    VDQIDPSTEY NDFIDVHRTT AAKEQEIEFD TSLLEENENL QANEIMWNNL 300
    TADSLQVMLK TLAEELTQTQ QMLLHKEAAV LELEKRIEES SETCAKKSDI 350
    VLLLGQKQAL EELKQSVQQL RCTEAKCAAQ KELLEQKVQE NDGKEPPPVV 400
    NYEEDARSVT SMERKERLSK FESIRHSIAG IIKSPKSVLG SSTQLSDVIS 450
    VGEKPLAEHD WYHGAIPRIE AQELLKQQGD FLVRESHGKP GEYVLSVYSD 500
    GQRRHFIIQF VDNLYRFEGT GFSNIPQLID HHFNTKQVIT KKSGVVLLNP 550
    IPKDKKWVLN HEDVSLGELL GKGNFGEVYK GTLKDKTPVA VKTCKEDLPQ 600
    ELKIKFLQEA KILKQYDHPN IVKLIGVCTQ RQPVYIIMEL VPGGDFLSFL 650
    RKRKDELKLK QLVRFSLDVA AGMLYLEGKN CIHRDLAARN CLVGENNTLK 700
    ISDFGMSRQE DGGVYSSSGL KQIPIKWTAP EALNYGRYSS ESDVWSFGIL 750
    LWETFSLGVC PYPGMTNQQA REQVERGYRM SAPQNCPEEI FTIMMKCWDY 800
    KPENRPKFSD LHKELTAIKK KIT 823
    Length:823
    Mass (Da):94,314
    Last modified:September 21, 2011 - v2
    Checksum:iCA4F31E375F747DA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti501 – 5011G → R in CAA31778. (PubMed:2485255)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13412 mRNA. Translation: CAA31778.1.
    PIRiS04328.
    RefSeqiXP_006245662.1. XM_006245600.1.
    UniGeneiRn.102629.

    Genome annotation databases

    EnsembliENSRNOT00000021758; ENSRNOP00000021758; ENSRNOG00000015898.
    GeneIDi301737.
    KEGGirno:301737.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X13412 mRNA. Translation: CAA31778.1 .
    PIRi S04328.
    RefSeqi XP_006245662.1. XM_006245600.1.
    UniGenei Rn.102629.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000021758.

    PTM databases

    PhosphoSitei P09760.

    Proteomic databases

    PaxDbi P09760.
    PRIDEi P09760.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000021758 ; ENSRNOP00000021758 ; ENSRNOG00000015898 .
    GeneIDi 301737.
    KEGGi rno:301737.

    Organism-specific databases

    CTDi 14158.
    RGDi 1306273. Fert2.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117264.
    HOGENOMi HOG000233858.
    HOVERGENi HBG001540.
    InParanoidi P09760.
    KOi K08889.
    OMAi FVDNLYR.
    OrthoDBi EOG708VXW.
    TreeFami TF315363.

    Enzyme and pathway databases

    Reactomei REACT_195025. Signaling by SCF-KIT.

    Miscellaneous databases

    PROi P09760.

    Gene expression databases

    Genevestigatori P09760.

    Family and domain databases

    Gene3Di 3.30.505.10. 1 hit.
    InterProi IPR001060. FCH_dom.
    IPR028539. Fer.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR016250. Tyr-prot_kinase_Fes/Fps.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    [Graphical view ]
    PANTHERi PTHR24418:SF227. PTHR24418:SF227. 1 hit.
    Pfami PF00611. FCH. 1 hit.
    PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000632. TyrPK_fps. 1 hit.
    PRINTSi PR00401. SH2DOMAIN.
    PR00109. TYRKINASE.
    SMARTi SM00055. FCH. 1 hit.
    SM00252. SH2. 1 hit.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55550. SSF55550. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50133. FCH. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
      Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
      , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
      Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Brown Norway.
    2. "Novel protein-tyrosine kinase cDNAs related to fps/fes and eph cloned using anti-phosphotyrosine antibody."
      Letwin K., Yee S.P., Pawson T.
      Oncogene 3:621-627(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 501-823.
      Strain: Wistar.
      Tissue: Brain.
    3. "Synapses are regulated by the cytoplasmic tyrosine kinase Fer in a pathway mediated by p120catenin, Fer, SHP-2, and beta-catenin."
      Lee S.H., Peng I.F., Ng Y.G., Yanagisawa M., Bamji S.X., Elia L.P., Balsamo J., Lilien J., Anastasiadis P.Z., Ullian E.M., Reichardt L.F.
      J. Cell Biol. 183:893-908(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SYNAPSE ORGANIZATION AND SYNAPTIC TRANSMISSION.
    4. "The Fer tyrosine kinase regulates interactions of Rho GDP-Dissociation Inhibitor alpha with the small GTPase Rac."
      Fei F., Kweon S.M., Haataja L., De Sepulveda P., Groffen J., Heisterkamp N.
      BMC Biochem. 11:48-48(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ARHGDIA.

    Entry informationi

    Entry nameiFER_RAT
    AccessioniPrimary (citable) accession number: P09760
    Secondary accession number(s): F1MA12
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: September 21, 2011
    Last modified: October 1, 2014
    This is version 133 of the entry and version 2 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3