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F1M7Y5

- KPCI_RAT

UniProt

F1M7Y5 - KPCI_RAT

Protein

Protein kinase C iota type

Gene

Prkci

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 32 (01 Oct 2014)
      Sequence version 1 (03 May 2011)
      Previous versions | rss
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    Functioni

    Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI3K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis. Downstream of PI3K is required for insulin-stimulated glucose transport. Activates RAB4A and promotes its association with KIF3A which is required for the insulin-induced SLC2A4/GLUT4 translocation in adipocytes. Is essential in early embryogenesis and development of differentiating photoreceptors by playing a role in the establishment of epithelial and neuronal polarity By similarity.By similarity

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Atypical PKCs (PRKCI and PRKCZ) exhibit an elevated basal enzymatic activity (that may be due to the interaction with SMG1 or SQSTM1) and are not regulated by diacylglycerol, phosphatidylserine, phorbol esters or calcium ions. Two specific sites, Thr-412 (activation loop of the kinase domain) and Thr-564 (turn motif), need to be phosphorylated for its full activation. Might also be a target for novel lipid activators that are elevated during nutrient-stimulated insulin secretion By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei283 – 2831ATPPROSITE-ProRule annotation
    Active sitei378 – 3781Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri140 – 19051Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST
    Nucleotide bindingi260 – 2689ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: RGD
    2. phospholipid binding Source: Ensembl
    3. protein domain specific binding Source: RGD
    4. protein kinase activity Source: UniProtKB
    5. protein kinase C activity Source: RGD
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. actin filament organization Source: Ensembl
    2. cell-cell junction organization Source: Ensembl
    3. cell migration Source: RGD
    4. cellular protein localization Source: RGD
    5. cellular response to insulin stimulus Source: RGD
    6. establishment of apical/basal cell polarity Source: Ensembl
    7. eye photoreceptor cell development Source: Ensembl
    8. Golgi vesicle budding Source: RGD
    9. intracellular signal transduction Source: InterPro
    10. negative regulation of glial cell apoptotic process Source: UniProtKB
    11. negative regulation of neuron apoptotic process Source: UniProtKB
    12. positive regulation of endothelial cell apoptotic process Source: UniProtKB
    13. positive regulation of establishment of protein localization to plasma membrane Source: Ensembl
    14. positive regulation of glial cell proliferation Source: UniProtKB
    15. positive regulation of glucose import Source: Ensembl
    16. positive regulation of neuron projection development Source: UniProtKB
    17. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    18. protein phosphorylation Source: RGD
    19. response to interleukin-1 Source: RGD
    20. response to peptide hormone Source: RGD

    Keywords - Molecular functioni

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

    Keywords - Ligandi

    ATP-binding, Metal-binding, Nucleotide-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein kinase C iota type (EC:2.7.11.13)
    Alternative name(s):
    Atypical protein kinase C-lambda/iota
    Short name:
    aPKC-lambda/iota
    nPKC-iota
    Gene namesi
    Name:Prkci
    Synonyms:Pkcl
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 2

    Organism-specific databases

    RGDi620961. Prkci.

    Subcellular locationi

    Cytoplasm 1 Publication. Membrane By similarity. Endosome By similarity. Nucleus 1 Publication
    Note: Transported into the endosome through interaction with SQSTM1/p62. After phosphorylation by SRC, transported into the nucleus through interaction with KPNB1. Colocalizes with CDK7 in the cytoplasm and nucleus. Transported to vesicular tubular clusters (VTCs) through interaction with RAB2A.

    GO - Cellular componenti

    1. apical plasma membrane Source: Ensembl
    2. cell leading edge Source: RGD
    3. cytosol Source: UniProtKB
    4. endosome Source: UniProtKB-SubCell
    5. Golgi membrane Source: GOC
    6. nucleus Source: UniProtKB
    7. plasma membrane Source: RGD
    8. protein complex Source: RGD
    9. Schmidt-Lanterman incisure Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi265 – 2651Y → F: Loss of phosphorylation and nuclear import. 1 Publication

    Keywords - Diseasei

    Proto-oncogene, Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 596595Protein kinase C iota typePRO_0000414090Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylprolineBy similarity
    Modified residuei3 – 31PhosphothreonineBy similarity
    Modified residuei7 – 71PhosphoserineBy similarity
    Modified residuei8 – 81PhosphoserineBy similarity
    Modified residuei9 – 91PhosphothreonineBy similarity
    Modified residuei265 – 2651Phosphotyrosine; by SRC1 Publication
    Modified residuei280 – 2801Phosphotyrosine; by SRCBy similarity
    Modified residuei334 – 3341Phosphotyrosine; by SRCBy similarity
    Modified residuei412 – 4121Phosphothreonine; by PDPK1By similarity
    Modified residuei564 – 5641PhosphothreonineBy similarity

    Post-translational modificationi

    Phosphorylation at Thr-412 in the activation loop is not mandatory for activation By similarity. Upon neuronal growth factor (NGF) stimulation, phosphorylated by SRC at Tyr-265, Tyr-280 and Tyr-334. Phosphorylation at Tyr-265 facilitates binding to KPNB1/importin-beta regulating entry of PRKCI into the nucleus. Phosphorylation on Tyr-334 is important for NF-kappa-B stimulation.By similarity1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiF1M7Y5.

    Interactioni

    Subunit structurei

    Forms a complex with SQSTM1 and MP2K5 By similarity. Interacts directly with SQSTM1 Probable. Interacts with IKBKB. Interacts with PARD6A, PARD6B and PARD6G. Part of a quaternary complex containing aPKC, PARD3, a PARD6 protein (PARD6A, PARD6B or PARD6G) and a GTPase protein (CDC42 or RAC1). Part of a complex with LLGL1 and PARD6B. Interacts with ADAP1/CENTA1. Interaction with SMG1, through the ZN-finger domain, activates the kinase activity. Interacts with CDK7. Forms a complex with RAB2A and GAPDH involved in recruitment onto the membrane of vesicular tubular clusters (VTCs). Interacts with ECT2 ('Thr-359' phosphorylated form) By similarity.By similarityCurated

    Protein-protein interaction databases

    IntActiF1M7Y5. 2 interactions.
    STRINGi10116.ENSRNOP00000012924.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 10782OPRAdd
    BLAST
    Domaini254 – 522269Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini523 – 59472AGC-kinase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 253252Regulatory domainBy similarityAdd
    BLAST
    Regioni2 – 2827Required for interaction with RAB2By similarityAdd
    BLAST
    Regioni72 – 9120Interaction with PARD6ABy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi125 – 13410PseudosubstrateBy similarity

    Domaini

    The OPR domain mediates interaction with SQSTM1.By similarity
    The C1 zinc finger does not bind diacylglycerol (DAG).By similarity
    The pseudosubstrate motif resembles the sequence around sites phosphorylated on target proteins, except the presence of a non-phosphorylatable residue in place of Ser, it modulates activity by competing with substrates.By similarity

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 OPR domain.Curated
    Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri140 – 19051Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00750000117322.
    HOGENOMiHOG000233033.
    HOVERGENiHBG108317.
    KOiK06069.
    OMAiFEPSISY.
    OrthoDBiEOG7HF1J3.
    TreeFamiTF102004.

    Family and domain databases

    InterProiIPR000961. AGC-kinase_C.
    IPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR000270. OPR_PB1.
    IPR012233. PKC_zeta.
    IPR017892. Pkinase_C.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PANTHERiPTHR24357:SF60. PTHR24357:SF60. 1 hit.
    PfamiPF00130. C1_1. 1 hit.
    PF00564. PB1. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000554. PKC_zeta. 1 hit.
    PRINTSiPR00008. DAGPEDOMAIN.
    SMARTiSM00109. C1. 1 hit.
    SM00666. PB1. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS00479. ZF_DAG_PE_1. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    F1M7Y5-1 [UniParc]FASTAAdd to Basket

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    MPTQRDSSTM SHTVACGGGG DHSHQVRVKA YYRGDIMITH FEPSISFEGL    50
    CSEVRDMCSF DNEQPFTMKW IDEEGDPCTV SSQLELEEAF RLYELNKDSE 100
    LLIHVFPCVP ERPGMPCPGE DKSIYRRGAR RWRKLYCANG HTFQAKRFNR 150
    RAHCAICTDR IWGLGRQGYK CINCKLLVHK KCHKLVTIEC GRHSLPPEPM 200
    MPMDQSSMHP DHTQTVIPYN PSSHESLDQV GEEKEAMNTR ESGKASSSLG 250
    LQDFDLLRVI GRGSYAKVLL VRLKKTDRIY AMKVVKKELV NDDEDIDWVQ 300
    TEKHVFEQAS NHPFLVGLHS CFQTESRLFF VIEYVNGGDL MFHMQRQRKL 350
    PEEHARFYSA EISLALNYLH ERGIIYRDLK LDNVLLDSEG HIKLTDYGMC 400
    KEGLRPGDTT STFCGTPNYI APEILRGEDY GFSVDWWALG VLMFEMMAGR 450
    SPFDIVGSSD NPDQNTEDYL FQVILEKQIR IPRSLSVKAA SVLKSFLNKD 500
    PKERLGCHPQ TGFADIQGHP FFRNVDWDMM EQKQVVPPFK PNISGEFGLD 550
    NFDSQFTNEP VQLTPDDDDI VRKIDQSEFE GFEYINPLLM SAEECV 596
    Length:596
    Mass (Da):68,276
    Last modified:May 3, 2011 - v1
    Checksum:i60035F56E7547C57
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti171 – 1711C → R in ACA66272. (PubMed:19090727)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EU517502 mRNA. Translation: ACA66272.1.
    RefSeqiNP_114448.1. NM_032059.1.
    UniGeneiRn.1388.

    Genome annotation databases

    EnsembliENSRNOT00000012924; ENSRNOP00000012924; ENSRNOG00000009652.
    GeneIDi84006.
    KEGGirno:84006.
    UCSCiRGD:620961. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EU517502 mRNA. Translation: ACA66272.1 .
    RefSeqi NP_114448.1. NM_032059.1.
    UniGenei Rn.1388.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi F1M7Y5. 2 interactions.
    STRINGi 10116.ENSRNOP00000012924.

    Proteomic databases

    PRIDEi F1M7Y5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000012924 ; ENSRNOP00000012924 ; ENSRNOG00000009652 .
    GeneIDi 84006.
    KEGGi rno:84006.
    UCSCi RGD:620961. rat.

    Organism-specific databases

    CTDi 5584.
    RGDi 620961. Prkci.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00750000117322.
    HOGENOMi HOG000233033.
    HOVERGENi HBG108317.
    KOi K06069.
    OMAi FEPSISY.
    OrthoDBi EOG7HF1J3.
    TreeFami TF102004.

    Miscellaneous databases

    NextBioi 616517.

    Family and domain databases

    InterProi IPR000961. AGC-kinase_C.
    IPR020454. DAG/PE-bd.
    IPR011009. Kinase-like_dom.
    IPR000270. OPR_PB1.
    IPR012233. PKC_zeta.
    IPR017892. Pkinase_C.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    PANTHERi PTHR24357:SF60. PTHR24357:SF60. 1 hit.
    Pfami PF00130. C1_1. 1 hit.
    PF00564. PB1. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000554. PKC_zeta. 1 hit.
    PRINTSi PR00008. DAGPEDOMAIN.
    SMARTi SM00109. C1. 1 hit.
    SM00666. PB1. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS00479. ZF_DAG_PE_1. 1 hit.
    PS50081. ZF_DAG_PE_2. 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], IDENTIFICATION.
      Strain: Brown Norway.
    2. "Expression and localization of atypical PKC isoforms in liver parenchymal cells."
      Stross C., Keitel V., Winands E., Haussinger D., Kubitz R.
      Biol. Chem. 390:235-244(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-596.
      Strain: Wistar.
    3. "Phosphorylation of tyrosine 256 facilitates nuclear import of atypical protein kinase C."
      White W.O., Seibenhener M.L., Wooten M.W.
      J. Cell. Biochem. 85:42-53(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-265, MUTAGENESIS OF TYR-265.

    Entry informationi

    Entry nameiKPCI_RAT
    AccessioniPrimary (citable) accession number: F1M7Y5
    Secondary accession number(s): B1PZT8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 14, 2011
    Last sequence update: May 3, 2011
    Last modified: October 1, 2014
    This is version 32 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