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Q14AX6

- CDK12_MOUSE

UniProt

Q14AX6 - CDK12_MOUSE

Protein

Cyclin-dependent kinase 12

Gene

Cdk12

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 2 (15 Jan 2008)
      Previous versions | rss
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    Functioni

    Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors.1 Publication

    Catalytic activityi

    ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
    ATP + a protein = ADP + a phosphoprotein.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei752 – 7521ATPPROSITE-ProRule annotation
    Active sitei855 – 8551Proton acceptorPROSITE-ProRule annotation
    Binding sitei1036 – 10361ATPPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi729 – 7379ATPPROSITE-ProRule annotation
    Nucleotide bindingi810 – 8156ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
    3. protein kinase activity Source: HGNC
    4. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB

    GO - Biological processi

    1. mRNA processing Source: UniProtKB-KW
    2. phosphorylation of RNA polymerase II C-terminal domain Source: UniProtKB
    3. protein autophosphorylation Source: HGNC
    4. regulation of MAP kinase activity Source: UniProtKB
    5. RNA splicing Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-dependent kinase 12 (EC:2.7.11.22, EC:2.7.11.23)
    Alternative name(s):
    Cdc2-related kinase, arginine/serine-rich
    Short name:
    CrkRS
    Cell division cycle 2-related protein kinase 7
    Short name:
    CDC2-related protein kinase 7
    Cell division protein kinase 12
    Gene namesi
    Name:Cdk12
    Synonyms:Crk7, Crkrs, Kiaa0904
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1098802. Cdk12.

    Subcellular locationi

    Nucleus By similarity. Nucleus speckle By similarity
    Note: Colocalized with nuclear speckles throughout interphase.By similarity

    GO - Cellular componenti

    1. cyclin K-CDK12 complex Source: Ensembl
    2. nuclear cyclin-dependent protein kinase holoenzyme complex Source: UniProtKB
    3. nuclear speck Source: UniProtKB
    4. nucleolus Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14841484Cyclin-dependent kinase 12PRO_0000314470Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei57 – 571PhosphothreonineBy similarity
    Modified residuei73 – 731PhosphotyrosineBy similarity
    Modified residuei235 – 2351PhosphoserineBy similarity
    Modified residuei248 – 2481PhosphoserineBy similarity
    Modified residuei273 – 2731PhosphoserineBy similarity
    Modified residuei275 – 2751PhosphoserineBy similarity
    Modified residuei300 – 3001PhosphoserineBy similarity
    Modified residuei302 – 3021PhosphoserineBy similarity
    Modified residuei309 – 3091PhosphoserineBy similarity
    Modified residuei311 – 3111PhosphoserineBy similarity
    Modified residuei317 – 3171PhosphoserineBy similarity
    Modified residuei322 – 3221PhosphoserineBy similarity
    Modified residuei324 – 3241PhosphoserineBy similarity
    Modified residuei331 – 3311PhosphoserineBy similarity
    Modified residuei332 – 3321PhosphoserineBy similarity
    Modified residuei333 – 3331PhosphoserineBy similarity
    Modified residuei337 – 3371PhosphoserineBy similarity
    Modified residuei344 – 3441PhosphoserineBy similarity
    Modified residuei382 – 3821Phosphoserine2 Publications
    Modified residuei384 – 3841Phosphoserine2 Publications
    Modified residuei399 – 3991PhosphoserineBy similarity
    Modified residuei419 – 4191PhosphoserineBy similarity
    Modified residuei422 – 4221PhosphoserineBy similarity
    Modified residuei511 – 5111PhosphothreonineBy similarity
    Modified residuei677 – 6771PhosphoserineBy similarity
    Modified residuei681 – 6811PhosphoserineBy similarity
    Modified residuei688 – 6881PhosphothreonineBy similarity
    Modified residuei889 – 8891PhosphothreonineBy similarity
    Modified residuei1049 – 10491PhosphoserineBy similarity
    Modified residuei1079 – 10791Phosphoserine1 Publication
    Modified residuei1240 – 12401PhosphothreonineBy similarity

    Post-translational modificationi

    Phosphorylation at Thr-889 increases kinase activity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ14AX6.
    PaxDbiQ14AX6.
    PRIDEiQ14AX6.

    PTM databases

    PhosphoSiteiQ14AX6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ14AX6.
    BgeeiQ14AX6.
    CleanExiMM_CRKRS.
    GenevestigatoriQ14AX6.

    Interactioni

    Subunit structurei

    Interacts with CCNL1 and CCNL2.By similarity

    Protein-protein interaction databases

    BioGridi213247. 1 interaction.
    IntActiQ14AX6. 1 interaction.
    MINTiMINT-4119098.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14AX6.
    SMRiQ14AX6. Positions 712-1042.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini723 – 1016294Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi137 – 393257Ser-richAdd
    BLAST
    Compositional biasi406 – 4127Poly-Ala
    Compositional biasi524 – 703180Pro-richAdd
    BLAST
    Compositional biasi1234 – 127643Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00740000114964.
    HOGENOMiHOG000049118.
    HOVERGENiHBG050852.
    InParanoidiQ14AX6.
    KOiK08819.
    OMAiYSTRSHP.
    OrthoDBiEOG76DTSM.
    PhylomeDBiQ14AX6.
    TreeFamiTF101060.

    Family and domain databases

    InterProiIPR011009. 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]
    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]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14AX6-1) [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

    MPNSERHGGK KDGSGGASGT SQPSSGGGSS NSRERHRLVS KHKRHKSKHS     50
    KDVGLVTPEA ASLGTIIKPL VEYDDISSDS DTFSDDTAFK SDRRENEERR 100
    GTDRSDRLHR HRHHQHRRSR DLLKTKQTEK EKNQEVSKSG SMKDRVSGSS 150
    KRSVEGSDDY GKAQLSKSGS KESRSSKMHK EKTRKERELK SGYKDRSKSH 200
    RKRETPKSYK TVASPKRRSR SPHRKWSDSS KQDDSPSGAS YGQDYDLSPP 250
    RSHTSSNYDS YKKSPGSTSR RQSISPPYKE PSAYQSSTRS PSPYSRRQRS 300
    VSPYSRRRSS SYERSGSYSG RSPSPYGRRR SSSPFLSKRS LSRSPLPSRK 350
    SMKSRSRSPA YSRHSSSHSK KKRSGSRSRH SSISPVRLPL NSSLGAELSR 400
    KKKERAAAAA AAKMDGKESK SSPIILPKKE KLEVKESGLE SKKLPRSIKS 450
    EKSTPDTELV TVAHSNPEVK HCLDTGKVRL DENLQKHPAK DLKAQGTKDV 500
    KPVAPKEVIV TSKETETSEK ETLPPLPTIT SPPPLPATTP PPQTPPLPPL 550
    PPLPAIPLQP PLPPPQPPFS QVPVSSTSIL PSSPHPRTST LSSQTNSQPP 600
    VQVSMKTQVS ITAAIPHLKT STLPPLPLPP LLPGDDDMDS PKETLPSKPA 650
    KKEKEQRTRH LLTDLPLPPE LPGGDPSPPD SPEPKAITPP QQPYKKRPKI 700
    CCPRYGERRQ TESDWGKRCV DKFDIIGIIG EGTYGQVYKA KDKDTGELVA 750
    LKKVRLDNEK EGFPITAIRE IKILRQLVHQ SVVNMKEIVT DKQDALDFKK 800
    DKGAFYLVFE YMDHDLMGLL ESGLVHFSED HIKSFMKQLM EGLDYCHKKN 850
    FLHRDIKCSN ILLNNSGQIK LADFGLARLY NSEESRPYTN KVITLWYRPP 900
    ELLLGEERYT PAIDVWSCGC ILGELFTKKP IFQANLELAQ LELISRLCGS 950
    PCPAVWPDVI KLPYFNTMKP KKQYRRRLRE EFSFIPSAAL DLLDHMLTLD 1000
    PSKRCTAEQT LQSDFLKDVE LSKMAPPDLP HWQDCHELWS KKRRRQRQSG 1050
    IVIEDPPPSK ASRKETTSGT TAEPVKNNSP APPQPAPVKA EPGPGDAVGL 1100
    GDITQQLNQS ELAVLLNLLQ SQTDLSIPQM AQLLNIHSNP EMQQQLEALN 1150
    QSISALTEAS SQQQDSESIA PEESLKEVPS VPVVLPPAEQ TTPEASNTPA 1200
    DMQNVLAVLL SQLMKTQEPA GNLEENTNDK NSGPQGPRRT PTMPQEEAAA 1250
    CPPHILPPEK RPPEPPGPPP PPPPPPLVEG DLSSAPQELN PAVTAALLQL 1300
    LSQPEAEPPG HLPHEHQALR PMEYSTRSHP NRTYGNTDGP ETGFSSADTD 1350
    ERSSGPALTE SLVQTPVKNR TFSGSVSHLG ESNSYQGTGS VQFPGDQDLR 1400
    FTRVPLALHS VVGQPFLKSE GNSNSVVHAE TKLQNYGELG PGTTGANSSG 1450
    TTLQWGGPAQ SYGKPYRGAA RVLPRGGRGR GVPY 1484
    Length:1,484
    Mass (Da):163,681
    Last modified:January 15, 2008 - v2
    Checksum:i5FCEE8D1903DF803
    GO
    Isoform 2 (identifier: Q14AX6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1250-1258: ACPPHILPP → GKQTGHESH
         1259-1484: Missing.

    Show »
    Length:1,258
    Mass (Da):139,883
    Checksum:iF21408B379D9EFB5
    GO
    Isoform 3 (identifier: Q14AX6-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1250-1258: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,475
    Mass (Da):162,755
    Checksum:i53626C566777F0CA
    GO

    Sequence cautioni

    The sequence CAM21270.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti346 – 3461L → I in AAL69526. 1 PublicationCurated
    Sequence conflicti363 – 3631R → S in AAL69526. 1 PublicationCurated
    Sequence conflicti377 – 3771R → H in AAL69526. 1 PublicationCurated
    Sequence conflicti425 – 4273ILP → FCL in BAC98047. (PubMed:14621295)Curated
    Sequence conflicti496 – 4961G → V in AAL69526. 1 PublicationCurated
    Sequence conflicti562 – 5621L → V in AAL69526. 1 PublicationCurated
    Sequence conflicti854 – 8541R → Q in AAL69526. 1 PublicationCurated
    Sequence conflicti863 – 8631L → V in AAL69526. 1 PublicationCurated
    Sequence conflicti870 – 8701K → R in AAL69526. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1250 – 12589ACPPHILPP → GKQTGHESH in isoform 2. 2 PublicationsVSP_030285
    Alternative sequencei1250 – 12589Missing in isoform 3. 1 PublicationVSP_030286
    Alternative sequencei1259 – 1484226Missing in isoform 2. 2 PublicationsVSP_030287Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY072295 mRNA. Translation: AAL69526.1.
    AL591205 Genomic DNA. Translation: CAM21267.1.
    AL591205 Genomic DNA. Translation: CAM21268.1.
    AL591205 Genomic DNA. Translation: CAM21269.1.
    AL591205 Genomic DNA. Translation: CAM21270.1. Sequence problems.
    BC116645 mRNA. Translation: AAI16646.1.
    AK129237 mRNA. Translation: BAC98047.1.
    CCDSiCCDS25342.1. [Q14AX6-2]
    CCDS48901.1. [Q14AX6-1]
    CCDS48902.1. [Q14AX6-3]
    RefSeqiNP_001103096.1. NM_001109626.1. [Q14AX6-1]
    NP_001103098.1. NM_001109628.1. [Q14AX6-3]
    NP_081228.2. NM_026952.2. [Q14AX6-2]
    UniGeneiMm.260516.
    Mm.486492.
    Mm.488484.

    Genome annotation databases

    EnsembliENSMUST00000003203; ENSMUSP00000003203; ENSMUSG00000003119. [Q14AX6-2]
    ENSMUST00000107538; ENSMUSP00000103162; ENSMUSG00000003119. [Q14AX6-1]
    ENSMUST00000107539; ENSMUSP00000103163; ENSMUSG00000003119. [Q14AX6-3]
    GeneIDi69131.
    KEGGimmu:69131.
    UCSCiuc007lfr.2. mouse. [Q14AX6-1]
    uc007lfs.2. mouse. [Q14AX6-2]
    uc007lfu.2. mouse. [Q14AX6-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY072295 mRNA. Translation: AAL69526.1 .
    AL591205 Genomic DNA. Translation: CAM21267.1 .
    AL591205 Genomic DNA. Translation: CAM21268.1 .
    AL591205 Genomic DNA. Translation: CAM21269.1 .
    AL591205 Genomic DNA. Translation: CAM21270.1 . Sequence problems.
    BC116645 mRNA. Translation: AAI16646.1 .
    AK129237 mRNA. Translation: BAC98047.1 .
    CCDSi CCDS25342.1. [Q14AX6-2 ]
    CCDS48901.1. [Q14AX6-1 ]
    CCDS48902.1. [Q14AX6-3 ]
    RefSeqi NP_001103096.1. NM_001109626.1. [Q14AX6-1 ]
    NP_001103098.1. NM_001109628.1. [Q14AX6-3 ]
    NP_081228.2. NM_026952.2. [Q14AX6-2 ]
    UniGenei Mm.260516.
    Mm.486492.
    Mm.488484.

    3D structure databases

    ProteinModelPortali Q14AX6.
    SMRi Q14AX6. Positions 712-1042.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 213247. 1 interaction.
    IntActi Q14AX6. 1 interaction.
    MINTi MINT-4119098.

    PTM databases

    PhosphoSitei Q14AX6.

    Proteomic databases

    MaxQBi Q14AX6.
    PaxDbi Q14AX6.
    PRIDEi Q14AX6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000003203 ; ENSMUSP00000003203 ; ENSMUSG00000003119 . [Q14AX6-2 ]
    ENSMUST00000107538 ; ENSMUSP00000103162 ; ENSMUSG00000003119 . [Q14AX6-1 ]
    ENSMUST00000107539 ; ENSMUSP00000103163 ; ENSMUSG00000003119 . [Q14AX6-3 ]
    GeneIDi 69131.
    KEGGi mmu:69131.
    UCSCi uc007lfr.2. mouse. [Q14AX6-1 ]
    uc007lfs.2. mouse. [Q14AX6-2 ]
    uc007lfu.2. mouse. [Q14AX6-3 ]

    Organism-specific databases

    CTDi 51755.
    MGIi MGI:1098802. Cdk12.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000114964.
    HOGENOMi HOG000049118.
    HOVERGENi HBG050852.
    InParanoidi Q14AX6.
    KOi K08819.
    OMAi YSTRSHP.
    OrthoDBi EOG76DTSM.
    PhylomeDBi Q14AX6.
    TreeFami TF101060.

    Miscellaneous databases

    NextBioi 328674.
    PROi Q14AX6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14AX6.
    Bgeei Q14AX6.
    CleanExi MM_CRKRS.
    Genevestigatori Q14AX6.

    Family and domain databases

    InterProi 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 ]
    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. "Characterization of a putative SR-related protein kinase that is differentially expressed in the embryonic nervous system."
      Lin S.-F., Chen H.-H., Fann M.-J.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: BALB/c.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "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] (ISOFORM 2).
    4. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
      DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 425-1484 (ISOFORM 3).
      Tissue: Embryonic tail.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382; SER-384 AND SER-1079, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382 AND SER-384, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    7. "The Cyclin K/Cdk12 complex maintains genomic stability via regulation of expression of DNA damage response genes."
      Blazek D., Kohoutek J., Bartholomeeusen K., Johansen E., Hulinkova P., Luo Z., Cimermancic P., Ule J., Peterlin B.M.
      Genes Dev. 25:2158-2172(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiCDK12_MOUSE
    AccessioniPrimary (citable) accession number: Q14AX6
    Secondary accession number(s): A2A530
    , A2A531, B1AQH7, Q6ZQ27, Q8R457
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 80 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