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)

Q00655

- KSYK_PIG

UniProt

Q00655 - KSYK_PIG

Protein

Tyrosine-protein kinase SYK

Gene

SYK

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      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.3 Publications

    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 By similarity. May also be negatively regulated by PTPN6 through dephosphorylation By similarity. Downstream signaling adapters and intermediates like BLNK or RHOH may mediate positive and/or negative feedback regulation By similarity. Negatively regulated by CBL and CBLB through ubiquitination and probable degradation By similarity. Phosphorylates SH3BP2 which in turn may regulate SYK through LYN.By similarity2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei395 – 3951ATPPROSITE-ProRule annotation
    Active sitei487 – 4871Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi370 – 3789ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB

    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. protein phosphorylation Source: UniProtKB
    20. regulation of arachidonic acid secretion Source: UniProtKB
    21. regulation of ERK1 and ERK2 cascade Source: UniProtKB
    22. regulation of neutrophil degranulation Source: UniProtKB
    23. regulation of phagocytosis Source: UniProtKB
    24. regulation of platelet activation Source: UniProtKB
    25. regulation of platelet aggregation Source: UniProtKB
    26. regulation of superoxide anion generation Source: UniProtKB
    27. 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. 6170.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosine-protein kinase SYK (EC:2.7.10.2)
    Alternative name(s):
    Spleen tyrosine kinase
    Cleaved into the following 2 chains:
    Gene namesi
    Name:SYK
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    Chain 72 kDa tyrosine-protein kinase SYK : Cell membrane Curated. Cytoplasmcytosol
    Note: Mainly associated with membranes.
    Chain 40 kDa tyrosine-protein kinase SYK : Cell membrane Curated. Cytoplasmcytosol
    Note: Equally distributed between membranes and cytosol.

    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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi341 – 3411Y → F: Alters interaction with VAV1. 1 Publication
    Mutagenesisi345 – 3451Y → F: Moderately alters interaction with VAV1. 1 Publication
    Mutagenesisi395 – 3951K → R: Loss of kinase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 62862872 kDa tyrosine-protein kinase SYKPRO_0000024468Add
    BLAST
    Chaini313 – 62831640 kDa tyrosine-protein kinase SYKPRO_0000024469Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei23 – 231PhosphotyrosineBy similarity
    Modified residuei39 – 391PhosphoserineBy similarity
    Modified residuei42 – 421PhosphotyrosineBy similarity
    Modified residuei126 – 1261PhosphotyrosineBy similarity
    Modified residuei196 – 1961PhosphoserineBy similarity
    Modified residuei250 – 2501PhosphothreonineBy similarity
    Modified residuei288 – 2881PhosphoserineBy similarity
    Modified residuei289 – 2891PhosphotyrosineBy similarity
    Modified residuei290 – 2901PhosphoserineBy similarity
    Modified residuei309 – 3091PhosphoserineBy similarity
    Modified residuei312 – 3121PhosphoserineBy similarity
    Modified residuei316 – 3161Phosphotyrosine; by LYNBy similarity
    Modified residuei338 – 3381PhosphothreonineBy similarity
    Modified residuei341 – 3411Phosphotyrosine2 Publications
    Modified residuei343 – 3431PhosphoserineBy similarity
    Modified residuei345 – 3451PhosphotyrosineBy similarity
    Modified residuei357 – 3571PhosphotyrosineBy similarity
    Modified residuei372 – 3721PhosphoserineBy similarity
    Modified residuei377 – 3771PhosphothreonineBy similarity
    Modified residuei477 – 4771PhosphotyrosineBy similarity
    Modified residuei500 – 5001PhosphotyrosineBy similarity
    Modified residuei518 – 5181Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei519 – 5191PhosphotyrosineBy similarity
    Modified residuei523 – 5231PhosphothreonineBy similarity
    Modified residuei539 – 5391PhosphotyrosineBy similarity
    Modified residuei572 – 5721PhosphoserineBy similarity
    Modified residuei622 – 6221PhosphotyrosineBy similarity
    Modified residuei623 – 6231PhosphotyrosineBy similarity
    Modified residuei624 – 6241PhosphotyrosineBy similarity

    Post-translational modificationi

    Autophosphorylated. Phosphorylated on tyrosine residues by LYN following receptors engagement. Phosphorylation on Tyr-316 creates a binding site for CBL, an adapter protein that serves as a negative regulator of BCR-stimulated calcium ion signaling. Phosphorylation at Tyr-341 creates a binding site for VAV1 By similarity. Phosphorylation on Tyr-341 and Tyr-345 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-290 is very common, it peaks 5 minutes after BCR stimulation, and creates a binding site for YWHAG By similarity. Phosphorylation at Tyr-623 creates a binding site for BLNK By similarity. Dephosphorylated by PTPN6 By similarity.By similarity
    Shows high susceptibility to proteolysis.
    Ubiquitinated by CBLB after BCR activation; which promotes proteasomal degradation.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Expressioni

    Tissue specificityi

    Spleen and with lesser amounts in thymus.

    Interactioni

    Subunit structurei

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

    IntActiQ00655. 1 interaction.
    MINTiMINT-6622752.
    STRINGi9823.ENSSSCP00000010237.

    Structurei

    3D structure databases

    ProteinModelPortaliQ00655.
    SMRiQ00655. Positions 4-256, 356-628.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini10 – 10293SH2 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini163 – 25391SH2 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini364 – 624261Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni103 – 16260Interdomain ABy similarityAdd
    BLAST
    Regioni254 – 363110Interdomain 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.
    KOiK05855.

    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. 3 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]

    Sequencei

    Sequence statusi: Complete.

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

    Q00655-1 [UniParc]FASTAAdd to Basket

    « Hide

    MADSANHLPF FFGQITREEA EDYLVQGGMS DGLYLLRQSR NYLGGFALSV    50
    AYDRKAHHYT IERELNGTYA ISGGRTHGSP AELCHYHSQE LDGLVCLLKN 100
    PFNRPPGVQP KTGPFEDLKE NLIREYVKQT WNLQGQALEQ AIISQKPQLE 150
    KLIATTAHEK MPWFHGKISR DESEQIVLIG SKTNGKFLIR ARDNGSYALG 200
    LLHEGKVLHY RIDKDKTGKL SIPGGKNFDT LWQLVEHYSY KSDGLLRVLT 250
    VPCQKIGGQT GNDSFRPQLP SAHPATWSAG GIISRIKSYS FPKPGHRKAS 300
    SPQGNRPESL VSYNPYESDR GPWANEREAQ REALPMDTEV YESPYADPEE 350
    IRPKEVYLDR KLLTLEDKEL GSGNFGTVKK GYYQMKKVVK TVAVKILKNE 400
    ANDPALKDEL LAEANVMQQL DNPYIVRMIG ICEAESWMLV MEMAELGPLN 450
    KYLQQNRHVK DKNIIELVHQ VSMGMKYLEE CNFVHRDLAA RNVLLVTQHY 500
    AKISDFGLSK ALRADENYYK AQTHGKWPVK WYAPECINYY KFSSKSDVWS 550
    FGVLMWEAFS YGQKPYRGMK GSEVSAMLEK GERMGCPPGC PREMYELMTL 600
    CWTYDVENRP GFVAVELRLR NYYYDVVN 628
    Length:628
    Mass (Da):71,620
    Last modified:April 1, 1993 - v1
    Checksum:iD7C0CEF7EBBEBC1E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73237 mRNA. Translation: AAA31112.1.
    PIRiA40802.
    RefSeqiNP_001098422.1. NM_001104952.1.
    UniGeneiSsc.55112.

    Genome annotation databases

    GeneIDi100125540.
    KEGGissc:100125540.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73237 mRNA. Translation: AAA31112.1 .
    PIRi A40802.
    RefSeqi NP_001098422.1. NM_001104952.1.
    UniGenei Ssc.55112.

    3D structure databases

    ProteinModelPortali Q00655.
    SMRi Q00655. Positions 4-256, 356-628.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q00655. 1 interaction.
    MINTi MINT-6622752.
    STRINGi 9823.ENSSSCP00000010237.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100125540.
    KEGGi ssc:100125540.

    Organism-specific databases

    CTDi 6850.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000113264.
    HOVERGENi HBG001540.
    KOi K05855.

    Enzyme and pathway databases

    BRENDAi 2.7.10.2. 6170.

    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. 3 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 a porcine gene syk that encodes a 72-kDa protein-tyrosine kinase showing high susceptibility to proteolysis."
      Taniguchi T., Kobayashi T., Kondo J., Takahashi K., Nakamura H., Suzuki J., Nagai K., Yamada T., Nakamura S., Yamamura H.
      J. Biol. Chem. 266:15790-15796(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 313-333; 346-354 AND 369-379.
      Tissue: Spleen.
    2. "Syk activation by the Src-family tyrosine kinase in the B cell receptor signaling."
      Kurosaki T., Takata M., Yamanashi Y., Inazu T., Taniguchi T., Yamamoto T., Yamamura H.
      J. Exp. Med. 179:1725-1729(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY LYN, INTERACTION WITH LYN, AUTOPHOSPHORYLATION.
    3. "Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product."
      Deckert M., Tartare-Deckert S., Couture C., Mustelin T., Altman A.
      Immunity 5:591-604(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSCRIPTION REGULATION, INTERACTION WITH VAV1, MUTAGENESIS OF TYR-341 AND TYR-345, PHOSPHORYLATION AT TYR-341.
    4. Cited for: FUNCTION IN PHOSPHORYLATION OF BTK.
    5. "Adaptor protein 3BP2 is a potential ligand of Src homology 2 and 3 domains of Lyn protein-tyrosine kinase."
      Maeno K., Sada K., Kyo S., Miah S.M., Kawauchi-Kamata K., Qu X., Shi Y., Yamamura H.
      J. Biol. Chem. 278:24912-24920(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF SH3BP2, MUTAGENESIS OF LYS-395, ENZYME REGULATION.
    6. "Interdomain A is crucial for ITAM-dependent and -independent regulation of Syk."
      Adachi T., Wienands J., Tsubata T., Kurosaki T.
      Biochem. Biophys. Res. Commun. 364:111-117(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.

    Entry informationi

    Entry nameiKSYK_PIG
    AccessioniPrimary (citable) accession number: Q00655
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 125 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, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3