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Q9NYV4

- CDK12_HUMAN

UniProt

Q9NYV4 - CDK12_HUMAN

Protein

Cyclin-dependent kinase 12

Gene

CDK12

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (01 Oct 2014)
      Sequence version 2 (05 Oct 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.5 Publications

    Catalytic activityi

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

    Enzyme regulationi

    Inhibited by the ATP analog flavopiridol, purvalanol A, purvalanol B, staurosporine and CR8.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei756 – 7561ATP
    Active sitei859 – 8591Proton acceptorPROSITE-ProRule annotation
    Binding sitei1040 – 10401ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi733 – 7419ATP
    Nucleotide bindingi814 – 8196ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. cyclin binding Source: MGI
    3. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
    4. protein binding Source: UniProtKB
    5. protein kinase activity Source: HGNC
    6. 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

    Enzyme and pathway databases

    BRENDAi2.7.11.22. 2681.
    SignaLinkiQ9NYV4.

    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
    Short name:
    hCDK12
    Gene namesi
    Name:CDK12
    Synonyms:CRK7, CRKRS, KIAA0904
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:24224. CDK12.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Chromosomal aberrations involving CDK12 may be a cause gastric cancer. Deletions within 17q12 region producing fusion transcripts with ERBB2, leading to CDK12-ERBB2 fusion leading to trunctated CDK12 protein not in-frame with ERBB2.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi877 – 8771D → N: Abolishes kinase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA165431656.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14901490Cyclin-dependent kinase 12PRO_0000085715Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei57 – 571Phosphothreonine1 Publication
    Modified residuei73 – 731Phosphotyrosine1 Publication
    Modified residuei236 – 2361Phosphoserine3 Publications
    Modified residuei249 – 2491Phosphoserine3 Publications
    Modified residuei274 – 2741Phosphoserine1 Publication
    Modified residuei276 – 2761Phosphoserine1 Publication
    Modified residuei301 – 3011Phosphoserine2 Publications
    Modified residuei303 – 3031Phosphoserine2 Publications
    Modified residuei310 – 3101Phosphoserine1 Publication
    Modified residuei312 – 3121Phosphoserine1 Publication
    Modified residuei318 – 3181Phosphoserine1 Publication
    Modified residuei323 – 3231Phosphoserine1 Publication
    Modified residuei325 – 3251Phosphoserine1 Publication
    Modified residuei332 – 3321Phosphoserine2 Publications
    Modified residuei333 – 3331Phosphoserine2 Publications
    Modified residuei334 – 3341Phosphoserine2 Publications
    Modified residuei338 – 3381Phosphoserine1 Publication
    Modified residuei345 – 3451Phosphoserine1 Publication
    Modified residuei383 – 3831Phosphoserine2 Publications
    Modified residuei385 – 3851Phosphoserine3 Publications
    Modified residuei400 – 4001Phosphoserine3 Publications
    Modified residuei420 – 4201Phosphoserine1 Publication
    Modified residuei423 – 4231Phosphoserine4 Publications
    Modified residuei514 – 5141Phosphothreonine1 Publication
    Modified residuei681 – 6811Phosphoserine7 Publications
    Modified residuei685 – 6851Phosphoserine7 Publications
    Modified residuei692 – 6921Phosphothreonine3 Publications
    Modified residuei893 – 8931Phosphothreonine3 Publications
    Modified residuei1053 – 10531Phosphoserine1 Publication
    Modified residuei1083 – 10831Phosphoserine2 Publications
    Modified residuei1244 – 12441Phosphothreonine1 Publication

    Post-translational modificationi

    Phosphorylation at Thr-893 increases kinase activity.8 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NYV4.
    PaxDbiQ9NYV4.
    PRIDEiQ9NYV4.

    PTM databases

    PhosphoSiteiQ9NYV4.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ9NYV4.
    BgeeiQ9NYV4.
    CleanExiHS_CRKRS.
    GenevestigatoriQ9NYV4.

    Organism-specific databases

    HPAiHPA008038.

    Interactioni

    Subunit structurei

    Interacts with CCNL1 and CCNL2 By similarity. Interacts with CCNK.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi119715. 23 interactions.
    IntActiQ9NYV4. 6 interactions.
    MINTiMINT-1191969.
    STRINGi9606.ENSP00000398880.

    Structurei

    Secondary structure

    1
    1490
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi724 – 7263
    Beta strandi727 – 7359
    Beta strandi737 – 74610
    Turni747 – 7493
    Beta strandi752 – 7587
    Beta strandi762 – 7643
    Helixi769 – 77810
    Beta strandi789 – 7946
    Beta strandi802 – 8043
    Beta strandi809 – 8146
    Beta strandi817 – 8193
    Helixi820 – 8267
    Helixi833 – 85220
    Helixi862 – 8643
    Beta strandi865 – 8673
    Beta strandi873 – 8753
    Beta strandi886 – 8883
    Helixi899 – 9013
    Helixi904 – 9074
    Helixi916 – 93116
    Helixi941 – 95212
    Turni957 – 9593
    Helixi961 – 9655
    Turni967 – 9715
    Helixi982 – 9854
    Turni986 – 9883
    Helixi991 – 100010
    Turni1005 – 10073
    Helixi1011 – 10144
    Helixi1018 – 10214
    Helixi1025 – 10273
    Beta strandi1035 – 10373
    Helixi1041 – 10455

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4CXAX-ray3.15A/C715-1052[»]
    4NSTX-ray2.20A/C714-1063[»]
    4UN0X-ray3.15C/D715-1038[»]
    ProteinModelPortaliQ9NYV4.
    SMRiQ9NYV4. Positions 716-1046.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini727 – 1020294Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi407 – 4137Poly-Ala
    Compositional biasi535 – 5406Poly-Pro
    Compositional biasi1266 – 128015Poly-ProAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000049118.
    HOVERGENiHBG050852.
    InParanoidiQ9NYV4.
    KOiK08819.
    OMAiYSTRSHP.
    PhylomeDBiQ9NYV4.
    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: Q9NYV4-1) [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 LQPSSGGGSS NSRERHRLVS KHKRHKSKHS     50
    KDMGLVTPEA ASLGTVIKPL VEYDDISSDS DTFSDDMAFK LDRRENDERR 100
    GSDRSDRLHK HRHHQHRRSR DLLKAKQTEK EKSQEVSSKS GSMKDRISGS 150
    SKRSNEETDD YGKAQVAKSS SKESRSSKLH KEKTRKEREL KSGHKDRSKS 200
    HRKRETPKSY KTVDSPKRRS RSPHRKWSDS SKQDDSPSGA SYGQDYDLSP 250
    SRSHTSSNYD SYKKSPGSTS RRQSVSPPYK EPSAYQSSTR SPSPYSRRQR 300
    SVSPYSRRRS SSYERSGSYS GRSPSPYGRR RSSSPFLSKR SLSRSPLPSR 350
    KSMKSRSRSP AYSRHSSSHS KKKRSSSRSR HSSISPVRLP LNSSLGAELS 400
    RKKKERAAAA AAAKMDGKES KGSPVFLPRK ENSSVEAKDS GLESKKLPRS 450
    VKLEKSAPDT ELVNVTHLNT EVKNSSDTGK VKLDENSEKH LVKDLKAQGT 500
    RDSKPIALKE EIVTPKETET SEKETPPPLP TIASPPPPLP TTTPPPQTPP 550
    LPPLPPIPAL PQQPPLPPSQ PAFSQVPASS TSTLPPSTHS KTSAVSSQAN 600
    SQPPVQVSVK TQVSVTAAIP HLKTSTLPPL PLPPLLPGDD DMDSPKETLP 650
    SKPVKKEKEQ RTRHLLTDLP LPPELPGGDL SPPDSPEPKA ITPPQQPYKK 700
    RPKICCPRYG ERRQTESDWG KRCVDKFDII GIIGEGTYGQ VYKAKDKDTG 750
    ELVALKKVRL DNEKEGFPIT AIREIKILRQ LIHRSVVNMK EIVTDKQDAL 800
    DFKKDKGAFY LVFEYMDHDL MGLLESGLVH FSEDHIKSFM KQLMEGLEYC 850
    HKKNFLHRDI KCSNILLNNS GQIKLADFGL ARLYNSEESR PYTNKVITLW 900
    YRPPELLLGE ERYTPAIDVW SCGCILGELF TKKPIFQANL ELAQLELISR 950
    LCGSPCPAVW PDVIKLPYFN TMKPKKQYRR RLREEFSFIP SAALDLLDHM 1000
    LTLDPSKRCT AEQTLQSDFL KDVELSKMAP PDLPHWQDCH ELWSKKRRRQ 1050
    RQSGVVVEEP PPSKTSRKET TSGTSTEPVK NSSPAPPQPA PGKVESGAGD 1100
    AIGLADITQQ LNQSELAVLL NLLQSQTDLS IPQMAQLLNI HSNPEMQQQL 1150
    EALNQSISAL TEATSQQQDS ETMAPEESLK EAPSAPVILP SAEQTTLEAS 1200
    STPADMQNIL AVLLSQLMKT QEPAGSLEEN NSDKNSGPQG PRRTPTMPQE 1250
    EAAACPPHIL PPEKRPPEPP GPPPPPPPPP LVEGDLSSAP QELNPAVTAA 1300
    LLQLLSQPEA EPPGHLPHEH QALRPMEYST RPRPNRTYGN TDGPETGFSA 1350
    IDTDERNSGP ALTESLVQTL VKNRTFSGSL SHLGESSSYQ GTGSVQFPGD 1400
    QDLRFARVPL ALHPVVGQPF LKAEGSSNSV VHAETKLQNY GELGPGTTGA 1450
    SSSGAGLHWG GPTQSSAYGK LYRGPTRVPP RGGRGRGVPY 1490
    Length:1,490
    Mass (Da):164,155
    Last modified:October 5, 2010 - v2
    Checksum:iD6B04B998ECDE58E
    GO
    Isoform 2 (identifier: Q9NYV4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1254-1262: Missing.

    Show »
    Length:1,481
    Mass (Da):163,228
    Checksum:iD0CF4B898D3032D4
    GO
    Isoform 3 (identifier: Q9NYV4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         349-349: Missing.
         1205-1274: DMQNILAVLL...RPPEPPGPPP → ILWYMQRPNC...FLTNPETSVS
         1275-1490: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,273
    Mass (Da):141,449
    Checksum:i85B012B87EDC02F1
    GO

    Sequence cautioni

    The sequence BAA74927.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti133 – 1331S → G in BAG63886. (PubMed:14702039)Curated
    Sequence conflicti268 – 2681S → G in BAG63886. (PubMed:14702039)Curated
    Sequence conflicti639 – 6391D → G in AAF36401. (PubMed:11683387)Curated
    Sequence conflicti737 – 7371T → I in BAG63886. (PubMed:14702039)Curated
    Sequence conflicti745 – 7451K → R in AAF36401. (PubMed:11683387)Curated
    Sequence conflicti822 – 8221G → V in BAG63886. (PubMed:14702039)Curated
    Sequence conflicti1195 – 11951T → M in AAF36401. (PubMed:11683387)Curated
    Sequence conflicti1195 – 11951T → M in BAA74927. (PubMed:10048485)Curated
    Sequence conflicti1195 – 11951T → M in AAI50266. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti530 – 5301P → A.1 Publication
    Corresponds to variant rs56121596 [ dbSNP | Ensembl ].
    VAR_041968
    Natural varianti912 – 9121R → H in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041969
    Natural varianti1189 – 11891L → Q.1 Publication
    Corresponds to variant rs56362165 [ dbSNP | Ensembl ].
    VAR_041970
    Natural varianti1275 – 12751P → L.1 Publication
    Corresponds to variant rs34070318 [ dbSNP | Ensembl ].
    VAR_041971

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei349 – 3491Missing in isoform 3. 1 PublicationVSP_040908
    Alternative sequencei1205 – 127470DMQNI…PGPPP → ILWYMQRPNCKTMGSWGQEP LGPAAQEQAFTGGAQLSLLL MENSIGGLQESHQEGEEGEE FLTNPETSVS in isoform 3. 1 PublicationVSP_040909Add
    BLAST
    Alternative sequencei1254 – 12629Missing in isoform 2. 2 PublicationsVSP_030284
    Alternative sequencei1275 – 1490216Missing in isoform 3. 1 PublicationVSP_040910Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF227198 mRNA. Translation: AAF36401.1.
    AB020711 mRNA. Translation: BAA74927.2. Different initiation.
    AK302645 mRNA. Translation: BAG63886.1.
    AC009283 Genomic DNA. No translation available.
    CH471152 Genomic DNA. Translation: EAW60577.1.
    BC140854 mRNA. Translation: AAI40855.1.
    BC150265 mRNA. Translation: AAI50266.1.
    CCDSiCCDS11337.1. [Q9NYV4-1]
    CCDS45666.1. [Q9NYV4-2]
    RefSeqiNP_055898.1. NM_015083.2. [Q9NYV4-2]
    NP_057591.2. NM_016507.3. [Q9NYV4-1]
    UniGeneiHs.416108.

    Genome annotation databases

    EnsembliENST00000430627; ENSP00000407720; ENSG00000167258. [Q9NYV4-2]
    ENST00000447079; ENSP00000398880; ENSG00000167258. [Q9NYV4-1]
    GeneIDi51755.
    KEGGihsa:51755.
    UCSCiuc002hrw.4. human. [Q9NYV4-2]
    uc010cvv.3. human. [Q9NYV4-1]

    Polymorphism databases

    DMDMi308153421.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF227198 mRNA. Translation: AAF36401.1 .
    AB020711 mRNA. Translation: BAA74927.2 . Different initiation.
    AK302645 mRNA. Translation: BAG63886.1 .
    AC009283 Genomic DNA. No translation available.
    CH471152 Genomic DNA. Translation: EAW60577.1 .
    BC140854 mRNA. Translation: AAI40855.1 .
    BC150265 mRNA. Translation: AAI50266.1 .
    CCDSi CCDS11337.1. [Q9NYV4-1 ]
    CCDS45666.1. [Q9NYV4-2 ]
    RefSeqi NP_055898.1. NM_015083.2. [Q9NYV4-2 ]
    NP_057591.2. NM_016507.3. [Q9NYV4-1 ]
    UniGenei Hs.416108.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4CXA X-ray 3.15 A/C 715-1052 [» ]
    4NST X-ray 2.20 A/C 714-1063 [» ]
    4UN0 X-ray 3.15 C/D 715-1038 [» ]
    ProteinModelPortali Q9NYV4.
    SMRi Q9NYV4. Positions 716-1046.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119715. 23 interactions.
    IntActi Q9NYV4. 6 interactions.
    MINTi MINT-1191969.
    STRINGi 9606.ENSP00000398880.

    PTM databases

    PhosphoSitei Q9NYV4.

    Polymorphism databases

    DMDMi 308153421.

    Proteomic databases

    MaxQBi Q9NYV4.
    PaxDbi Q9NYV4.
    PRIDEi Q9NYV4.

    Protocols and materials databases

    DNASUi 51755.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000430627 ; ENSP00000407720 ; ENSG00000167258 . [Q9NYV4-2 ]
    ENST00000447079 ; ENSP00000398880 ; ENSG00000167258 . [Q9NYV4-1 ]
    GeneIDi 51755.
    KEGGi hsa:51755.
    UCSCi uc002hrw.4. human. [Q9NYV4-2 ]
    uc010cvv.3. human. [Q9NYV4-1 ]

    Organism-specific databases

    CTDi 51755.
    GeneCardsi GC17P037618.
    H-InvDB HIX0013777.
    HGNCi HGNC:24224. CDK12.
    HPAi HPA008038.
    neXtProti NX_Q9NYV4.
    PharmGKBi PA165431656.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000049118.
    HOVERGENi HBG050852.
    InParanoidi Q9NYV4.
    KOi K08819.
    OMAi YSTRSHP.
    PhylomeDBi Q9NYV4.
    TreeFami TF101060.

    Enzyme and pathway databases

    BRENDAi 2.7.11.22. 2681.
    SignaLinki Q9NYV4.

    Miscellaneous databases

    ChiTaRSi CDK12. human.
    GeneWikii CRKRS.
    GenomeRNAii 51755.
    NextBioi 55858.
    PROi Q9NYV4.

    Gene expression databases

    ArrayExpressi Q9NYV4.
    Bgeei Q9NYV4.
    CleanExi HS_CRKRS.
    Genevestigatori Q9NYV4.

    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. "CrkRS: a novel conserved Cdc2-related protein kinase that colocalises with SC35 speckles."
      Ko T.K., Kelly E., Pines J.
      J. Cell Sci. 114:2591-2603(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
    2. "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:355-364(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Testis.
    5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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).
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-681 AND SER-685, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; TYR-73; SER-400; SER-423; THR-514; SER-681; SER-685 AND THR-692, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249; SER-301; SER-303; SER-318; SER-323; SER-325; SER-332; SER-333; SER-334; SER-345; SER-383; SER-385; SER-400; SER-681; SER-685 AND THR-692, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "CRK7 modifies the MAPK pathway and influences the response to endocrine therapy."
      Iorns E., Martens-de Kemp S.R., Lord C.J., Ashworth A.
      Carcinogenesis 30:1696-1701(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-420; SER-423; SER-681; SER-685; THR-692 AND SER-1053, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-383; SER-385; SER-681; SER-685 AND THR-1244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "CDK12 is a transcription elongation-associated CTD kinase, the metazoan ortholog of yeast Ctk1."
      Bartkowiak B., Liu P., Phatnani H.P., Fuda N.J., Cooper J.J., Price D.H., Adelman K., Lis J.T., Greenleaf A.L.
      Genes Dev. 24:2303-2316(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-249; SER-385; SER-400; SER-423; SER-681; SER-685; THR-893 AND SER-1083, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Genetic and structural variation in the gastric cancer kinome revealed through targeted deep sequencing."
      Zang Z.J., Ong C.K., Cutcutache I., Yu W., Zhang S.L., Huang D., Ler L.D., Dykema K., Gan A., Tao J., Lim S., Liu Y., Futreal P.A., Grabsch H., Furge K.A., Goh L.K., Rozen S., Teh B.T., Tan P.
      Cancer Res. 71:29-39(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL REARRANGEMENT WITH ERBB2, POSSIBLE INVOLVEMENT IN GASTRIC CANCER.
    20. "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.
    21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236; SER-249; SER-274; SER-276; SER-301; SER-303; SER-310; SER-312; SER-332; SER-333; SER-334; SER-338; SER-423; SER-681; SER-685; THR-893 AND SER-1083, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 714-1063 IN COMPLEX WITH ADP; TRANSITION STATE ANALOG AND CCNK, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH CCNK, PHOSPHORYLATION AT THR-893, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF ASP-877, ENZYME REGULATION.
    23. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] ALA-530; HIS-912; GLN-1189 AND LEU-1275.

    Entry informationi

    Entry nameiCDK12_HUMAN
    AccessioniPrimary (citable) accession number: Q9NYV4
    Secondary accession number(s): A7E2B2
    , B4DYX4, B9EIQ6, O94978
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 133 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3