Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q64725

- KSYK_RAT

UniProt

Q64725 - KSYK_RAT

Protein

Tyrosine-protein kinase SYK

Gene

Syk

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Non-receptor tyrosine kinase which mediates signal transduction downstream of a variety of transmembrane receptors including classical immunoreceptors like the B-cell receptor (BCR). Regulates several biological processes including innate and adaptive immunity, cell adhesion, osteoclast maturation, platelet activation and vascular development. Assembles into signaling complexes with activated receptors at the plasma membrane via interaction between its SH2 domains and the receptor tyrosine-phosphorylated ITAM domains. The association with the receptor can also be indirect and mediated by adapter proteins containing ITAM or partial hemITAM domains. The phosphorylation of the ITAM domains is generally mediated by SRC subfamily kinases upon engagement of the receptor. More rarely signal transduction via SYK could be ITAM-independent. Direct downstream effectors phosphorylated by SYK include VAV1, PLCG1, PI-3-kinase, LCP2 and BLNK. Initially identified as essential in B-cell receptor (BCR) signaling, it is necessary for the maturation of B-cells most probably at the pro-B to pre-B transition. Activated upon BCR engagement, it phosphorylates and activates BLNK an adapter linking the activated BCR to downstream signaling adapters and effectors. It also phosphorylates and activates PLCG1 and the PKC signaling pathway. It also phosphorylates BTK and regulates its activity in B-cell antigen receptor (BCR)-coupled signaling. In addition to its function downstream of BCR plays also a role in T-cell receptor signaling. Plays also a crucial role in the innate immune response to fungal, bacterial and viral pathogens. It is for instance activated by the membrane lectin CLEC7A. Upon stimulation by fungal proteins, CLEC7A together with SYK activates immune cells inducing the production of ROS. Also activates the inflammasome and NF-kappa-B-mediated transcription of chemokines and cytokines in presence of pathogens. Regulates neutrophil degranulation and phagocytosis through activation of the MAPK signaling cascade. Also mediates the activation of dendritic cells by cell necrosis stimuli. Also involved in mast cells activation. Also functions downstream of receptors mediating cell adhesion. Relays for instance, integrin-mediated neutrophils and macrophages activation and P-selectin receptor/SELPG-mediated recruitment of leukocytes to inflammatory loci. Plays also a role in non-immune processes. It is for instance involved in vascular development where it may regulate blood and lymphatic vascular separation. It is also required for osteoclast development and function. Functions in the activation of platelets by collagen, mediating PLCG2 phosphorylation and activation. May be coupled to the collagen receptor by the ITAM domain-containing FCER1G. Also activated by the membrane lectin CLEC1B that is required for activation of platelets by PDPN/podoplanin. Involved in platelet adhesion being activated by ITGB3 engaged by fibrinogen.1 Publication

    Catalytic activityi

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

    Enzyme regulationi

    Autoinhibited. Intramolecular binding of the interdomains A and B (also called linker region) to parts of the catalytic domain keep the catalytic center in an inactive conformation. The phosphorylation of the interdomains or the binding of the SH2 domains with dually phosphorylated ITAM domains on transmembrane proteins disrupt those intramolecular interactions allowing the kinase domain to adopt an active conformation. The phosphorylation of SYK and of the ITAM domains which is responsible for SYK activation is essentially mediated by SRC subfamily kinases, like LYN, upon transmembrane receptors engagement. May also be negatively regulated by PTPN6 through dephosphorylation. Downstream signaling adapters and intermediates like BLNK or RHOH may mediate positive and/or negative feedback regulation. Negatively regulated by CBL and CBLB through ubiquitination and probable degradation By similarity. Phosphorylates SH3BP2 which in turn may regulate SYK through LYN By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei396 – 3961ATPPROSITE-ProRule annotation
    Active sitei488 – 4881Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi371 – 3799ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein domain specific binding Source: RGD
    5. protein kinase activity Source: RGD

    GO - Biological processi

    1. adaptive immune response Source: UniProtKB
    2. angiogenesis Source: UniProtKB-KW
    3. B cell receptor signaling pathway Source: UniProtKB
    4. blood vessel morphogenesis Source: UniProtKB
    5. cellular response to molecule of fungal origin Source: UniProtKB
    6. defense response to bacterium Source: UniProtKB
    7. innate immune response Source: UniProtKB
    8. integrin-mediated signaling pathway Source: UniProtKB
    9. intracellular signal transduction Source: InterPro
    10. leukocyte activation involved in immune response Source: UniProtKB
    11. leukocyte cell-cell adhesion Source: UniProtKB
    12. lymph vessel development Source: UniProtKB
    13. macrophage activation involved in immune response Source: UniProtKB
    14. neutrophil activation involved in immune response Source: UniProtKB
    15. neutrophil chemotaxis Source: UniProtKB
    16. peptidyl-tyrosine phosphorylation Source: GOC
    17. positive regulation of bone resorption Source: UniProtKB
    18. positive regulation of cell adhesion mediated by integrin Source: UniProtKB
    19. positive regulation of mast cell degranulation Source: RGD
    20. protein autophosphorylation Source: RGD
    21. protein phosphorylation Source: UniProtKB
    22. regulation of arachidonic acid secretion Source: UniProtKB
    23. regulation of ERK1 and ERK2 cascade Source: UniProtKB
    24. regulation of immune response Source: RGD
    25. regulation of neutrophil degranulation Source: UniProtKB
    26. regulation of phagocytosis Source: UniProtKB
    27. regulation of platelet activation Source: UniProtKB
    28. regulation of platelet aggregation Source: UniProtKB
    29. regulation of superoxide anion generation Source: UniProtKB
    30. serotonin secretion by platelet Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Adaptive immunity, Angiogenesis, Immunity, Innate immunity

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.2. 5301.
    ReactomeiREACT_198646. FCGR activation.
    REACT_213009. Fc epsilon receptor (FCERI) signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase SYK (EC:2.7.10.2)
    Alternative name(s):
    Spleen tyrosine kinase
    p72Syk
    Gene namesi
    Name:Syk
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi3796. Syk.

    Subcellular locationi

    Cell membrane Curated. Cytoplasmcytosol Curated

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. early phagosome Source: UniProtKB
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 629629Tyrosine-protein kinase SYKPRO_0000088167Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei27 – 271PhosphotyrosineBy similarity
    Modified residuei43 – 431PhosphoserineBy similarity
    Modified residuei46 – 461PhosphotyrosineBy similarity
    Modified residuei130 – 1301PhosphotyrosineBy similarity
    Modified residuei201 – 2011PhosphoserineBy similarity
    Modified residuei255 – 2551PhosphothreonineBy similarity
    Modified residuei289 – 2891PhosphoserineBy similarity
    Modified residuei290 – 2901PhosphotyrosineBy similarity
    Modified residuei291 – 2911PhosphoserineBy similarity
    Modified residuei310 – 3101PhosphoserineBy similarity
    Modified residuei311 – 3111PhosphothreonineBy similarity
    Modified residuei313 – 3131PhosphoserineBy similarity
    Modified residuei317 – 3171Phosphotyrosine; by LYN1 Publication
    Modified residuei339 – 3391PhosphothreonineBy similarity
    Modified residuei342 – 3421Phosphotyrosine1 Publication
    Modified residuei344 – 3441PhosphoserineBy similarity
    Modified residuei346 – 3461Phosphotyrosine1 Publication
    Modified residuei358 – 3581PhosphotyrosineBy similarity
    Modified residuei373 – 3731PhosphoserineBy similarity
    Modified residuei378 – 3781PhosphothreonineBy similarity
    Modified residuei478 – 4781PhosphotyrosineBy similarity
    Modified residuei501 – 5011PhosphotyrosineBy similarity
    Modified residuei519 – 5191Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei520 – 5201PhosphotyrosineBy similarity
    Modified residuei524 – 5241PhosphothreonineBy similarity
    Modified residuei540 – 5401PhosphotyrosineBy similarity
    Modified residuei573 – 5731PhosphoserineBy similarity
    Modified residuei576 – 5761PhosphothreonineBy similarity
    Modified residuei623 – 6231PhosphotyrosineBy similarity
    Modified residuei624 – 6241PhosphotyrosineBy similarity
    Modified residuei625 – 6251PhosphotyrosineBy similarity

    Post-translational modificationi

    Autophosphorylated. Phosphorylated on tyrosine residues by LYN following receptors engagement. Phosphorylation on Tyr-317 creates a binding site for CBL, an adapter protein that serves as a negative regulator of BCR-stimulated calcium ion signaling By similarity. Phosphorylation at Tyr-342 creates a binding site for VAV1 By similarity. Phosphorylation on Tyr-342 and Tyr-346 enhances the phosphorylation and activation of phospholipase C-gamma and the early phase of calcium ion mobilization via a phosphoinositide 3-kinase-independent pathway By similarity. Phosphorylation on Ser-291 is very common, it peaks 5 minutes after BCR stimulation, and creates a binding site for YWHAG By similarity. Phosphorylation at Tyr-624 creates a binding site for BLNK By similarity. Dephosphorylated by PTPN6 By similarity.By similarity
    Ubiquitinated by CBLB after BCR activation; which promotes proteasomal degradation.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ64725.
    PRIDEiQ64725.

    PTM databases

    PhosphoSiteiQ64725.

    Expressioni

    Gene expression databases

    GenevestigatoriQ64725.

    Interactioni

    Subunit structurei

    Interacts with LYN; phosphorylates SYK. Interacts with RHOH (phosphorylated); regulates mast cells activation. Interacts with NFAM1 (phosphorylated); probably involved in BCR signaling. Interacts with VAV1 (via SH2 domain); phosphorylates VAV1 upon BCR activation. Interacts with GAB2 (phosphorylated); probably involved in IgE Fc receptor signaling. Interacts (via its SH2 domains) with CD79A (via its phosphorylated ITAM domain); the interaction stimulates SYK autophosphorylation and activation. Interacts with FCRL3. Interacts (via SH2 domains) with FCER1G (via ITAM domain); activates SYK and mediates neutrophils and macrophages integrin-mediated activation. Interacts with ITGB2 and FGR; involved in ITGB2 downstream signaling. Interacts with ITGB3; upon activation by ITGB3 promotes platelet adhesion. Interacts (via SH2 domains) with TYROBP (via ITAM domain); involved in neutrophils and macrophages integrin-mediated activation. Interacts with MSN and SELPLG; mediates the selectin-dependent activation of SYK by SELPLG. Interacts with BLNK (via SH2 domain). Interacts (via the second SH2 domain) with USP25 (via C-terminus); phosphorylates USP25 and regulates USP25 intracellular levels. Interacts (via SH2 domains) with CLEC1B (dimer). Interacts with CLEC7A; participates in leukocyte activation in presence of fungal pathogens. Interacts (phosphorylated) with SLA; may regulate SYK through CBL recruitment. Interacts with YWHAG; attenuates BCR-induced membrane translocation and activation of SYK By similarity. Interacts (via SH2 domains) with GCSAM; the interaction increases after B-cell receptor stimulation, resulting in enhanced SYK autophosphorylation and activity By similarity.By similarity

    Protein-protein interaction databases

    BioGridi247220. 2 interactions.
    IntActiQ64725. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ64725.
    SMRiQ64725. Positions 8-261, 357-629.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 10693SH2 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini167 – 25892SH2 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini365 – 625261Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni107 – 16660Interdomain ABy similarityAdd
    BLAST
    Regioni259 – 364106Interdomain BBy similarityAdd
    BLAST

    Domaini

    The SH2 domains mediate the interaction of SYK with the phosphorylated ITAM domains of transmembrane proteins. Some proteins like CLEC1B have a partial ITAM domain (also called hemITAM) containing a single YxxL motif. The interaction with SYK requires CLEC1B homodimerization By similarity.By similarity

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. SYK/ZAP-70 subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 2 SH2 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, SH2 domain

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000113264.
    HOVERGENiHBG001540.
    InParanoidiQ64725.
    KOiK05855.
    PhylomeDBiQ64725.

    Family and domain databases

    Gene3Di1.10.930.10. 1 hit.
    3.30.505.10. 2 hits.
    InterProiIPR011009. Kinase-like_dom.
    IPR023420. Kinase_SYK/ZAP-70_inter-SH2.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR012234. Tyr_kinase_non-rcpt_SYK/ZAP70.
    [Graphical view]
    PfamiPF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000604. TyrPK_SYK. 1 hit.
    PRINTSiPR00401. SH2DOMAIN.
    PR00109. TYRKINASE.
    SMARTiSM00252. SH2. 2 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF55550. SSF55550. 2 hits.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform SykB (identifier: Q64725-1) [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

    MAGNAVDNAN HLTYFFGNIT REEAEDYLVQ GGMTDGLYLL RQSRNYLGGF    50
    ALSVAHNRKA HHYTIERELN GTYAISGGRA HASPADLCHY HSQEPEGLVC 100
    LLKKPFNRPP GVQPKTGPFE DLKENLIREY VKQTWNLQGQ ALEQAIISQK 150
    PQLEKLIATT AHEKMPWFHG NISRDESEQT VLIGSKTNGK FLIRARDNNG 200
    SFALCLLHEG KVLHYRIDRD KTGKLSIPEG KKFDTLWQLV EHYSYKPDGL 250
    LRVLTVPCQK IGVQMGHPGS SNAHPVTWSP GGIISRIKSY SFPKPGHKKP 300
    PPPQGSRPES TVSFNPYEPT GGAWGPDRGL QREALPMDTE VYESPYADPE 350
    EIRPKEVYLD RKLLTLEDNE LGSGNFGTVK KGYYQMKKVV KTVAVKILKN 400
    EANDPALKDE LLAEANVMQQ LDNPYIVRMI GICEAESWML VMEMAAWGPL 450
    NKYLQQNRHI KDKNIIELVH QVSMGMKYLE ESNFVHRDLA ARNVLLVTQH 500
    YAKISDFGLS KALRADENYY KAQTHGKWPV KWYAPECINY FKFSSKSDVW 550
    SFGVLMWEAF SYGQKPYRGM KGSEVTAMLE KGERMGCPPG CPREMYDLMF 600
    LCWTYDVENR PGFAAVELRL RNYYYDVVN 629
    Length:629
    Mass (Da):71,529
    Last modified:November 1, 1996 - v1
    Checksum:i81169A643EC6A6FE
    GO
    Isoform SykA (identifier: Q64725-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         277-299: Missing.

    Show »
    Length:606
    Mass (Da):68,975
    Checksum:i084007CC11CDFE0F
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei277 – 29923Missing in isoform SykA. CuratedVSP_005011Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U21684 mRNA. Translation: AAA75167.1.
    U21683 mRNA. Translation: AAA75166.1.
    RefSeqiNP_036890.1. NM_012758.1. [Q64725-1]
    UniGeneiRn.87407.

    Genome annotation databases

    GeneIDi25155.
    KEGGirno:25155.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U21684 mRNA. Translation: AAA75167.1 .
    U21683 mRNA. Translation: AAA75166.1 .
    RefSeqi NP_036890.1. NM_012758.1. [Q64725-1 ]
    UniGenei Rn.87407.

    3D structure databases

    ProteinModelPortali Q64725.
    SMRi Q64725. Positions 8-261, 357-629.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247220. 2 interactions.
    IntActi Q64725. 1 interaction.

    Chemistry

    BindingDBi Q64725.
    ChEMBLi CHEMBL4364.

    PTM databases

    PhosphoSitei Q64725.

    Proteomic databases

    PaxDbi Q64725.
    PRIDEi Q64725.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 25155.
    KEGGi rno:25155.

    Organism-specific databases

    CTDi 6850.
    RGDi 3796. Syk.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000113264.
    HOVERGENi HBG001540.
    InParanoidi Q64725.
    KOi K05855.
    PhylomeDBi Q64725.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 5301.
    Reactomei REACT_198646. FCGR activation.
    REACT_213009. Fc epsilon receptor (FCERI) signaling.

    Miscellaneous databases

    NextBioi 605611.
    PROi Q64725.

    Gene expression databases

    Genevestigatori Q64725.

    Family and domain databases

    Gene3Di 1.10.930.10. 1 hit.
    3.30.505.10. 2 hits.
    InterProi IPR011009. Kinase-like_dom.
    IPR023420. Kinase_SYK/ZAP-70_inter-SH2.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
    IPR000980. SH2.
    IPR008266. Tyr_kinase_AS.
    IPR020635. Tyr_kinase_cat_dom.
    IPR012234. Tyr_kinase_non-rcpt_SYK/ZAP70.
    [Graphical view ]
    Pfami PF07714. Pkinase_Tyr. 1 hit.
    PF00017. SH2. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF000604. TyrPK_SYK. 1 hit.
    PRINTSi PR00401. SH2DOMAIN.
    PR00109. TYRKINASE.
    SMARTi SM00252. SH2. 2 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55550. SSF55550. 2 hits.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    PS50001. SH2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of rodent p72Syk. Evidence of alternative mRNA splicing."
      Rowley R.B., Bolen J.B., Fargnoli J.
      J. Biol. Chem. 270:12659-12664(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING (ISOFORMS SYKA AND SYKB).
    2. "SH2 domains mediate the sequential phosphorylation of HS1 protein by p72syk and Src-related protein tyrosine kinases."
      Ruzzene M., Brunati A.M., Marin O., Donella-Deana A., Pinna L.A.
      Biochemistry 35:5327-5332(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HCLS1.
    3. "Regulation of signaling in B cells through the phosphorylation of Syk on linker region tyrosines. A mechanism for negative signaling by the Lyn tyrosine kinase."
      Hong J.J., Yankee T.M., Harrison M.L., Geahlen R.L.
      J. Biol. Chem. 277:31703-31714(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-317 BY LYN, PHOSPHORYLATION AT TYR-342 AND TYR-346.

    Entry informationi

    Entry nameiKSYK_RAT
    AccessioniPrimary (citable) accession number: Q64725
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 132 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3