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E1BB50

- CDK12_BOVIN

UniProt

E1BB50 - CDK12_BOVIN

Protein

Cyclin-dependent kinase 12

Gene

CDK12

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 27 (01 Oct 2014)
      Sequence version 1 (02 Nov 2010)
      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 By similarity.By similarity

    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 sitei756 – 7561ATPPROSITE-ProRule annotation
    Active sitei859 – 8591Proton acceptorPROSITE-ProRule annotation
    Binding sitei1042 – 10421ATPPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi733 – 7419ATPPROSITE-ProRule annotation
    Nucleotide bindingi814 – 8196ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
    3. 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. regulation of MAP kinase activity Source: UniProtKB
    4. 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):
    Cell division protein kinase 12
    Gene namesi
    Name:CDK12
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Unplaced

    Subcellular locationi

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

    GO - Cellular componenti

    1. nuclear cyclin-dependent protein kinase holoenzyme complex Source: UniProtKB
    2. nuclear speck Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12641264Cyclin-dependent kinase 12PRO_0000406958Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei57 – 571PhosphothreonineBy similarity
    Modified residuei73 – 731PhosphotyrosineBy similarity
    Modified residuei236 – 2361PhosphoserineBy similarity
    Modified residuei249 – 2491PhosphoserineBy similarity
    Modified residuei274 – 2741PhosphoserineBy similarity
    Modified residuei276 – 2761PhosphoserineBy similarity
    Modified residuei301 – 3011PhosphoserineBy similarity
    Modified residuei303 – 3031PhosphoserineBy similarity
    Modified residuei310 – 3101PhosphoserineBy similarity
    Modified residuei312 – 3121PhosphoserineBy similarity
    Modified residuei318 – 3181PhosphoserineBy similarity
    Modified residuei323 – 3231PhosphoserineBy similarity
    Modified residuei325 – 3251PhosphoserineBy similarity
    Modified residuei332 – 3321PhosphoserineBy similarity
    Modified residuei333 – 3331PhosphoserineBy similarity
    Modified residuei334 – 3341PhosphoserineBy similarity
    Modified residuei338 – 3381PhosphoserineBy similarity
    Modified residuei345 – 3451PhosphoserineBy similarity
    Modified residuei383 – 3831PhosphoserineBy similarity
    Modified residuei385 – 3851PhosphoserineBy similarity
    Modified residuei400 – 4001PhosphoserineBy similarity
    Modified residuei420 – 4201PhosphoserineBy similarity
    Modified residuei423 – 4231PhosphoserineBy similarity
    Modified residuei515 – 5151PhosphothreonineBy similarity
    Modified residuei681 – 6811PhosphoserineBy similarity
    Modified residuei685 – 6851PhosphoserineBy similarity
    Modified residuei692 – 6921PhosphothreonineBy similarity
    Modified residuei893 – 8931PhosphothreonineBy similarity
    Modified residuei1055 – 10551PhosphoserineBy similarity
    Modified residuei1085 – 10851PhosphoserineBy similarity
    Modified residuei1246 – 12461PhosphothreonineBy similarity

    Post-translational modificationi

    Phosphorylation at Thr-893 increases kinase activity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiE1BB50.

    Interactioni

    Subunit structurei

    Interacts with CCNL1 and CCNL2.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliE1BB50.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini727 – 1022296Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi137 – 394258Ser-richAdd
    BLAST
    Compositional biasi407 – 4137Poly-Ala
    Compositional biasi528 – 707180Pro-richAdd
    BLAST
    Compositional biasi1062 – 10654Poly-Pro

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    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]

    Sequencei

    Sequence statusi: Complete.

    E1BB50-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPNPERHGGK KDGSGGASGT LQPSSGGGSS NSRERHRLGS KHKRHKSKHS     50
    KDMGLVTPEA APLGTVIKPL VEYDDISSDS DTFSDDLAFK VDRRENDERR 100
    GTDRSDRLHK HRHHQHRRTR DLLKTKQTEK EKNLEASSKS GSTKDRISGS 150
    SKRSNEENDD HGKAQISKSS NKESRSSKLH KEKTRKEREL KSGHKDRSKS 200
    HRKRETPKSY KTVDSPKRRS RSPHRKWSDS PKQDDSPSGA SYGQDYDLSP 250
    PRSHTSSNYD SYKKSPGSTS RRQSISPPYK EPSAYQSSTR SPSPYSRRQR 300
    SVSPYSRRRS SSYERSGSYS GRSPSPYGRR RSSSPFLSKR SLSRSPLPSR 350
    KSMKSRSRSP AYSRHSSSHS KKKRSGSRSR HSSISPVRLP LNSSLGAELS 400
    RKKKERAAAA AAAKMDGKES KGSPIFLPKK ENSSVEAKDS GLEPKKLPRG 450
    VKLEKSAPDT ELVNVTHLNT EVKNSLDTGK VKLDENSEKH PVLKDTKVQG 500
    TKDSKPVALK EEIVTPKETE TSEKETLPPL PTVTSPPPLP TTTPPPQTPP 550
    LPPLPPLPAI PQQPPLPPPQ PTFSQVLSSS TSTLPPSVHP RTSTLSSQAN 600
    SQPSVQVSVK TQVSVTAAIP HLKTSTLPPL PLPPLLLGDD DMDSPKETLP 650
    SKPVKKEKEQ RPRHLLTDLP LPPELPGGDP SPPDSPEPKA ITPPQQPYKK 700
    RPKICCPRYG ERRQTESDWG KRCVDKFDII GIIGEGTYGQ VYKAKDKDTG 750
    ELVALKKVRL DNEKEGFPIT AIREIKILRQ LIHRSVVNMK EIVTDKQDAL 800
    DFKKDKGAFY LVFEYMDHDL MGLLESGLVH FSEDHIKSFM KQLMEGLDYC 850
    HKKNFLHRDI KCSNILLNNS GQIKLADFGL ARLYNSEESR PYTNKVITLW 900
    YRPPELLLGE ERYTPAIDVW SCGCILGELF TKKPIFQANL ELAQLELISR 950
    LCGSPCPAVW PDVIKLPYFN TMKPKKQYRR RLREEFSFFF LPWGALDLLD 1000
    HMLTLDPSKR CTAEQTLQSD FLKDVELSKM DPPDLPHWQD CHELWSKKRR 1050
    RQRQSGVLVE EPPPPKASRK ETISGTSAEP VKNSSPAPPQ PAPGKVEPGA 1100
    GDAIGLGDIT QQLNQSELAV LLNLLQSQTD LSIPQMAQLL NIHSNPEMQQ 1150
    QLEALNQSIS ALTAATSQQQ DSEPTAPEES LKEIAPAPAV QPSAEQTTPE 1200
    ASSTPADMQN MLAVLLSQLM KTQEPAGNLE ENNSDKNSGP QGPRRTPTMP 1250
    QEEAAGKQTG HESH 1264
    Length:1,264
    Mass (Da):140,642
    Last modified:November 2, 2010 - v1
    Checksum:iA074D89C354DBAC7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFC03033685 Genomic DNA. No translation available.
    AAFC03036812 Genomic DNA. No translation available.
    AAFC03053477 Genomic DNA. No translation available.
    AAFC03053478 Genomic DNA. No translation available.
    UniGeneiBt.67418.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAFC03033685 Genomic DNA. No translation available.
    AAFC03036812 Genomic DNA. No translation available.
    AAFC03053477 Genomic DNA. No translation available.
    AAFC03053478 Genomic DNA. No translation available.
    UniGenei Bt.67418.

    3D structure databases

    ProteinModelPortali E1BB50.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi E1BB50.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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. "The genome sequence of taurine cattle: a window to ruminant biology and evolution."
      The bovine genome sequencing and analysis consortium
      Science 324:522-528(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiCDK12_BOVIN
    AccessioniPrimary (citable) accession number: E1BB50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 5, 2011
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 27 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