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O70126

- AURKB_MOUSE

UniProt

O70126 - AURKB_MOUSE

Protein

Aurora kinase B

Gene

Aurkb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. Involved in the bipolar attachment of spindle microtubules to kinetochores and is a key regulator for the onset of cytokinesis during mitosis. Required for central/midzone spindle assembly and cleavage furrow formation. Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: phosphorylates CHMP4C, leading to retain abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. AURKB phosphorylates the CPC complex subunits BIRC5/survivin, CDCA8/borealin and INCENP. Phosphorylation of INCENP leads to increased AURKB activity. Other known AURKB substrates involved in centromeric functions and mitosis are CENPA, DES/desmin, GPAF, KIF2C, NSUN2, RACGAP1, SEPT1, VIM/vimentin, GSG2/Haspin and histone H3. A positive feedback loop involving GSG2 and AURKB contributes to localization of CPC to centromeres. Phosphorylation of VIM controls vimentin filament segregation in cytokinetic process, whereas histone H3 is phosphorylated at 'Ser-10' and 'Ser-28' during mitosis (H3S10ph and H3S28ph, respectively). AURKB is also required for kinetochore localization of BUB1 and SGOL1. Phosphorylation of p53/TP53 negatively regulates its transcriptional activity. Key regulator of active promoters in resting B- and T-lymphocytes: acts by mediating phosphorylation of H3S28ph at active promoters in resting B-cells, inhibiting RNF2/RING1B-mediated ubiquitination of histone H2A and enhancing binding and activity of the USP16 deubiquitinase at transcribed genes.2 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Cofactori

    Magnesium.

    Enzyme regulationi

    Activity is greatly increased when AURKB is within the CPC complex. In particular, AURKA-phosphorylated INCENP acts as an activator of AURKB By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei111 – 1111ATPPROSITE-ProRule annotation
    Active sitei205 – 2051Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi88 – 969ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. histone serine kinase activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. abscission Source: UniProtKB
    2. aging Source: Ensembl
    3. cell proliferation Source: Ensembl
    4. cellular response to UV Source: UniProtKB
    5. cleavage furrow formation Source: UniProtKB
    6. cytokinesis checkpoint Source: UniProtKB
    7. histone H3-S28 phosphorylation Source: UniProtKB
    8. negative regulation of B cell apoptotic process Source: UniProtKB
    9. negative regulation of cytokinesis Source: UniProtKB
    10. negative regulation of protein binding Source: Ensembl
    11. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    12. positive regulation of cytokinesis Source: UniProtKB
    13. protein localization to kinetochore Source: UniProtKB
    14. protein phosphorylation Source: UniProtKB
    15. spindle checkpoint Source: InterPro
    16. spindle midzone assembly involved in mitosis Source: UniProtKB
    17. spindle stabilization Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    ReactomeiREACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_207679. Separation of Sister Chromatids.
    REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aurora kinase B (EC:2.7.11.1)
    Alternative name(s):
    Aurora 1
    Aurora- and IPL1-like midbody-associated protein 1
    Aurora/IPL1-related kinase 2
    Short name:
    ARK-2
    Short name:
    Aurora-related kinase 2
    STK-1
    Serine/threonine-protein kinase 12
    Serine/threonine-protein kinase 5
    Serine/threonine-protein kinase aurora-B
    Gene namesi
    Name:Aurkb
    Synonyms:Aik2, Aim1, Airk2, Ark2, Stk1, Stk12, Stk5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:107168. Aurkb.

    Subcellular locationi

    Nucleus By similarity. Chromosome By similarity. Chromosomecentromere By similarity. Cytoplasmcytoskeletonspindle By similarity. Midbody By similarity
    Note: Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis. Colocalized with gamma tubulin in the mid-body By similarity. Proper localization of the active, Thr-237-phosphorylated form during metaphase may be dependent upon interaction with SPDYC. Colocalized with SIRT2 during cytokinesis with the midbody By similarity.By similarity

    GO - Cellular componenti

    1. chromocenter Source: MGI
    2. chromosome passenger complex Source: MGI
    3. condensed nuclear chromosome, centromeric region Source: Ensembl
    4. cytoplasm Source: UniProtKB-KW
    5. kinetochore Source: MGI
    6. midbody Source: MGI
    7. mitotic spindle pole Source: MGI
    8. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 345345Aurora kinase BPRO_0000085657Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei35 – 351PhosphothreonineBy similarity
    Modified residuei62 – 621PhosphoserineBy similarity
    Modified residuei237 – 2371Phosphothreonine; by autocatalysisBy similarity

    Post-translational modificationi

    The phosphorylation of Thr-237 requires the binding to INCENP and occurs by means of an autophosphorylation mechanism. Thr-237 phosphorylation is indispensable for the AURKB kinase activity By similarity.By similarity
    Ubiquitinated by different BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complexes. Ubiquitinated by the BCR(KLHL9-KLHL13) E3 ubiquitin ligase complex, ubiquitination leads to removal from mitotic chromosomes and is required for cytokinesis. During anaphase, the BCR(KLHL21) E3 ubiquitin ligase complex recruits the CPC complex from chromosomes to the spindle midzone and mediates the ubiquitination of AURKB. Ubiquitination of AURKB by BCR(KLHL21) E3 ubiquitin ligase complex may not lead to its degradation by the proteasome By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiO70126.
    PRIDEiO70126.

    PTM databases

    PhosphoSiteiO70126.

    Expressioni

    Tissue specificityi

    Expressed in testis, intestine and spleen. All of them are tissues that contain a large number of proliferating cells. Expressed during S phase, in a cell-cycle-dependent fashion.

    Developmental stagei

    Strongly expressed in 8.5 and 12.5 dpc.

    Gene expression databases

    BgeeiO70126.
    CleanExiMM_AURKB.
    GenevestigatoriO70126.

    Interactioni

    Subunit structurei

    Component of the chromosomal passenger complex (CPC) composed of at least BIRC5/survivin, CDCA8/borealin, INCENP, AURKB and AURKC By similarity. Associates with RACGAP1 during M phase. Interacts with CDCA1, EVI5, JTB, NDC80, PSMA3, SEPT1, SIRT2 and TACC1 By similarity. Interacts with SPDYC; this interaction may be required for proper localization of active, Thr-237-phosphorylated AURKB form during prometaphase and metaphase. Interacts with p53/TP53. Interacts (via the middle kinase domain) with NOC2L (via the N- and C-terminus domains) By similarity. Interacts with TTC28 By similarity. Interacts with RNF2/RING1B.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi203547. 16 interactions.
    IntActiO70126. 8 interactions.
    MINTiMINT-1341009.

    Structurei

    3D structure databases

    ProteinModelPortaliO70126.
    SMRiO70126. Positions 41-343.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini82 – 332251Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Aurora subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00550000074590.
    HOGENOMiHOG000233016.
    HOVERGENiHBG108519.
    InParanoidiQ8C6C1.
    KOiK11479.
    OMAiHPWVRAN.
    OrthoDBiEOG74FF1F.
    TreeFamiTF351439.

    Family and domain databases

    InterProiIPR028772. AURKB.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PANTHERiPTHR24350:SF4. PTHR24350:SF4. 1 hit.
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O70126-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAQKENAYPW PYGSKTSQSG LNTLSQRVLR KEPATTSALA LVNRFNSQST    50
    AAPGQKLAEN KSQGSTASQG SQNKQPFTID NFEIGRPLGK GKFGNVYLAR 100
    EKKSRFIVAL KILFKSQIEK EGVEHQLRRE IEIQAHLKHP NILQLYNYFY 150
    DQQRIYLILE YAPRGELYKE LQKSRTFDEQ RTATIMEELS DALTYCHKKK 200
    VIHRDIKPEN LLLGLQGELK IADFGWSVHA PSLRRKTMCG TLDYLPPEMI 250
    EGRMHNEMVD LWCIGVLCYE LMVGNPPFES PSHSETYRRI VKVDLKFPSS 300
    VPSGAQDLIS KLLKHNPWQR LPLAEVAAHP WVRANSRRVL PPSAL 345
    Length:345
    Mass (Da):39,384
    Last modified:July 27, 2011 - v2
    Checksum:iD204D8B91CFF00A4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti44 – 441R → W in BAA04658. (PubMed:8647446)Curated
    Sequence conflicti45 – 451F → S in BAA04658. (PubMed:8647446)Curated
    Sequence conflicti45 – 451F → S in AAC12683. (PubMed:9514916)Curated
    Sequence conflicti45 – 451F → S in AAH03261. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D21099 mRNA. Translation: BAA04658.1.
    U69107 mRNA. Translation: AAC12683.1.
    AK075951 mRNA. Translation: BAC36078.1.
    AK132006 mRNA. Translation: BAE20935.1.
    AL645902 Genomic DNA. Translation: CAI24442.1.
    CH466601 Genomic DNA. Translation: EDL10472.1.
    BC003261 mRNA. Translation: AAH03261.1.
    CCDSiCCDS24877.1.
    PIRiJC4665.
    RefSeqiNP_035626.1. NM_011496.1.
    UniGeneiMm.3488.

    Genome annotation databases

    EnsembliENSMUST00000021277; ENSMUSP00000021277; ENSMUSG00000020897.
    ENSMUST00000108666; ENSMUSP00000104306; ENSMUSG00000020897.
    GeneIDi20877.
    KEGGimmu:20877.
    UCSCiuc007jpa.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D21099 mRNA. Translation: BAA04658.1 .
    U69107 mRNA. Translation: AAC12683.1 .
    AK075951 mRNA. Translation: BAC36078.1 .
    AK132006 mRNA. Translation: BAE20935.1 .
    AL645902 Genomic DNA. Translation: CAI24442.1 .
    CH466601 Genomic DNA. Translation: EDL10472.1 .
    BC003261 mRNA. Translation: AAH03261.1 .
    CCDSi CCDS24877.1.
    PIRi JC4665.
    RefSeqi NP_035626.1. NM_011496.1.
    UniGenei Mm.3488.

    3D structure databases

    ProteinModelPortali O70126.
    SMRi O70126. Positions 41-343.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203547. 16 interactions.
    IntActi O70126. 8 interactions.
    MINTi MINT-1341009.

    Chemistry

    ChEMBLi CHEMBL1075275.

    PTM databases

    PhosphoSitei O70126.

    Proteomic databases

    PaxDbi O70126.
    PRIDEi O70126.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000021277 ; ENSMUSP00000021277 ; ENSMUSG00000020897 .
    ENSMUST00000108666 ; ENSMUSP00000104306 ; ENSMUSG00000020897 .
    GeneIDi 20877.
    KEGGi mmu:20877.
    UCSCi uc007jpa.1. mouse.

    Organism-specific databases

    CTDi 9212.
    MGIi MGI:107168. Aurkb.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00550000074590.
    HOGENOMi HOG000233016.
    HOVERGENi HBG108519.
    InParanoidi Q8C6C1.
    KOi K11479.
    OMAi HPWVRAN.
    OrthoDBi EOG74FF1F.
    TreeFami TF351439.

    Enzyme and pathway databases

    Reactomei REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_207679. Separation of Sister Chromatids.
    REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.

    Miscellaneous databases

    ChiTaRSi AURKB. mouse.
    NextBioi 299727.
    PROi O70126.
    SOURCEi Search...

    Gene expression databases

    Bgeei O70126.
    CleanExi MM_AURKB.
    Genevestigatori O70126.

    Family and domain databases

    InterProi IPR028772. AURKB.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    PANTHERi PTHR24350:SF4. PTHR24350:SF4. 1 hit.
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cell-cycle-dependent expression of the STK-1 gene encoding a novel murine putative protein kinase."
      Niwa H., Abe K., Kunisada T., Yamamura K.
      Gene 169:197-201(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
      Tissue: Testis.
    2. "cDNA cloning, expression, subcellular localization, and chromosomal assignment of mammalian aurora homologues, aurora-related kinase (ARK) 1 and 2."
      Shindo M., Nakano H., Kuroyanagi H., Shirasawa T., Mihara M., Gilbert D.J., Jenkins N.A., Copeland N.G., Yagita H., Okumura K.
      Biochem. Biophys. Res. Commun. 244:285-292(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Embryo and Embryonic stem cell.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
      Tissue: Mammary gland.
    7. "Mitotic phosphorylation of histone H3: spatio-temporal regulation by mammalian Aurora kinases."
      Crosio C., Fimia G.M., Loury R., Kimura M., Okano Y., Zhou H., Sen S., Allis C.D., Sassone-Corsi P.
      Mol. Cell. Biol. 22:874-885(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
    8. "The Aurora B kinase and the Polycomb protein Ring1B combine to regulate active promoters in quiescent lymphocytes."
      Frangini A., Sjoberg M., Roman-Trufero M., Dharmalingam G., Haberle V., Bartke T., Lenhard B., Malumbres M., Vidal M., Dillon N.
      Mol. Cell 51:647-661(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH RNF2.

    Entry informationi

    Entry nameiAURKB_MOUSE
    AccessioniPrimary (citable) accession number: O70126
    Secondary accession number(s): Q61882, Q8C6C1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 17, 2003
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 147 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. 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