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Q9NYV4 (CDK12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:CDK12
Synonyms:CRK7, CRKRS, KIAA0904
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1490 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cyclin-dependent kinase which displays CTD kinase activity and is required for RNA splicing. Has CTD kinase activity by hyperphosphorylating the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit RPB1, thereby acting as a key regulator of transcription elongation. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogn inhibitors. Ref.1 Ref.13 Ref.16

Catalytic activity

ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate. Ref.16

ATP + a protein = ADP + a phosphoprotein. Ref.16

Subunit structure

Interacts with CCNL1 and CCNL2 By similarity.

Subcellular location

Nucleus. Nucleus speckle. Note: Colocalized with nuclear speckles throughout interphase. Ref.1

Tissue specificity

Ubiquitously expressed. Ref.1

Involvement in disease

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.

Sequence similarities

Belongs to the protein kinase superfamily. CMGC Ser/Thr protein kinase family. CDC2/CDKX subfamily.

Contains 1 protein kinase domain.

Sequence caution

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

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

phosphorylation of RNA polymerase II C-terminal domain

Inferred from mutant phenotype Ref.16. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.1. Source: HGNC

regulation of MAP kinase activity

Inferred from mutant phenotype Ref.13. Source: UniProtKB

   Cellular_componentcyclin K-CDK12 complex

Inferred from physical interaction PubMed 22012619. Source: MGI

nuclear cyclin-dependent protein kinase holoenzyme complex

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear speck

Inferred from direct assay Ref.1. Source: UniProtKB

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II carboxy-terminal domain kinase activity

Inferred from mutant phenotype Ref.16. Source: UniProtKB

cyclin binding

Inferred from physical interaction PubMed 22012619. Source: MGI

cyclin-dependent protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein kinase activity

Inferred from direct assay Ref.1. Source: HGNC

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NYV4-1)

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.
Isoform 2 (identifier: Q9NYV4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1254-1262: Missing.
Isoform 3 (identifier: Q9NYV4-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14901490Cyclin-dependent kinase 12
PRO_0000085715

Regions

Domain727 – 1020294Protein kinase
Nucleotide binding733 – 7419ATP By similarity
Compositional bias407 – 4137Poly-Ala
Compositional bias535 – 5406Poly-Pro
Compositional bias1266 – 128015Poly-Pro

Sites

Active site8591Proton acceptor By similarity
Binding site7561ATP By similarity

Amino acid modifications

Modified residue571Phosphothreonine Ref.10
Modified residue731Phosphotyrosine Ref.10
Modified residue2361Phosphoserine Ref.15 Ref.17 Ref.20
Modified residue2491Phosphoserine Ref.11 Ref.17 Ref.20
Modified residue2741Phosphoserine Ref.20
Modified residue2761Phosphoserine Ref.20
Modified residue3011Phosphoserine Ref.11 Ref.20
Modified residue3031Phosphoserine Ref.11 Ref.20
Modified residue3101Phosphoserine Ref.20
Modified residue3121Phosphoserine Ref.20
Modified residue3181Phosphoserine Ref.11
Modified residue3231Phosphoserine Ref.11
Modified residue3251Phosphoserine Ref.11
Modified residue3321Phosphoserine Ref.11 Ref.20
Modified residue3331Phosphoserine Ref.11 Ref.20
Modified residue3341Phosphoserine Ref.11 Ref.20
Modified residue3381Phosphoserine Ref.20
Modified residue3451Phosphoserine Ref.11
Modified residue3831Phosphoserine Ref.11 Ref.15
Modified residue3851Phosphoserine Ref.11 Ref.15 Ref.17
Modified residue4001Phosphoserine Ref.10 Ref.11 Ref.17
Modified residue4201Phosphoserine Ref.14
Modified residue4231Phosphoserine Ref.10 Ref.14 Ref.17 Ref.20
Modified residue5141Phosphothreonine Ref.10
Modified residue6811Phosphoserine Ref.8 Ref.10 Ref.11 Ref.14 Ref.15 Ref.17 Ref.20
Modified residue6851Phosphoserine Ref.8 Ref.10 Ref.11 Ref.14 Ref.15 Ref.17 Ref.20
Modified residue6921Phosphothreonine Ref.10 Ref.11 Ref.14
Modified residue8931Phosphothreonine Ref.17 Ref.20
Modified residue10531Phosphoserine Ref.14
Modified residue10831Phosphoserine Ref.17 Ref.20
Modified residue12441Phosphothreonine Ref.15

Natural variations

Alternative sequence3491Missing in isoform 3.
VSP_040908
Alternative sequence1205 – 127470DMQNI…PGPPP → ILWYMQRPNCKTMGSWGQEP LGPAAQEQAFTGGAQLSLLL MENSIGGLQESHQEGEEGEE FLTNPETSVS in isoform 3.
VSP_040909
Alternative sequence1254 – 12629Missing in isoform 2.
VSP_030284
Alternative sequence1275 – 1490216Missing in isoform 3.
VSP_040910
Natural variant5301P → A. Ref.21
Corresponds to variant rs56121596 [ dbSNP | Ensembl ].
VAR_041968
Natural variant9121R → H in a colorectal adenocarcinoma sample; somatic mutation. Ref.21
VAR_041969
Natural variant11891L → Q. Ref.21
Corresponds to variant rs56362165 [ dbSNP | Ensembl ].
VAR_041970
Natural variant12751P → L. Ref.21
Corresponds to variant rs34070318 [ dbSNP | Ensembl ].
VAR_041971

Experimental info

Sequence conflict1331S → G in BAG63886. Ref.4
Sequence conflict2681S → G in BAG63886. Ref.4
Sequence conflict6391D → G in AAF36401. Ref.1
Sequence conflict7371T → I in BAG63886. Ref.4
Sequence conflict7451K → R in AAF36401. Ref.1
Sequence conflict8221G → V in BAG63886. Ref.4
Sequence conflict11951T → M in AAF36401. Ref.1
Sequence conflict11951T → M in BAA74927. Ref.2
Sequence conflict11951T → M in AAI50266. Ref.6

Secondary structure

......................................... 1490
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: D6B04B998ECDE58E

FASTA1,490164,155
        10         20         30         40         50         60 
MPNSERHGGK KDGSGGASGT LQPSSGGGSS NSRERHRLVS KHKRHKSKHS KDMGLVTPEA 

        70         80         90        100        110        120 
ASLGTVIKPL VEYDDISSDS DTFSDDMAFK LDRRENDERR GSDRSDRLHK HRHHQHRRSR 

       130        140        150        160        170        180 
DLLKAKQTEK EKSQEVSSKS GSMKDRISGS SKRSNEETDD YGKAQVAKSS SKESRSSKLH 

       190        200        210        220        230        240 
KEKTRKEREL KSGHKDRSKS HRKRETPKSY KTVDSPKRRS RSPHRKWSDS SKQDDSPSGA 

       250        260        270        280        290        300 
SYGQDYDLSP SRSHTSSNYD SYKKSPGSTS RRQSVSPPYK EPSAYQSSTR SPSPYSRRQR 

       310        320        330        340        350        360 
SVSPYSRRRS SSYERSGSYS GRSPSPYGRR RSSSPFLSKR SLSRSPLPSR KSMKSRSRSP 

       370        380        390        400        410        420 
AYSRHSSSHS KKKRSSSRSR HSSISPVRLP LNSSLGAELS RKKKERAAAA AAAKMDGKES 

       430        440        450        460        470        480 
KGSPVFLPRK ENSSVEAKDS GLESKKLPRS VKLEKSAPDT ELVNVTHLNT EVKNSSDTGK 

       490        500        510        520        530        540 
VKLDENSEKH LVKDLKAQGT RDSKPIALKE EIVTPKETET SEKETPPPLP TIASPPPPLP 

       550        560        570        580        590        600 
TTTPPPQTPP LPPLPPIPAL PQQPPLPPSQ PAFSQVPASS TSTLPPSTHS KTSAVSSQAN 

       610        620        630        640        650        660 
SQPPVQVSVK TQVSVTAAIP HLKTSTLPPL PLPPLLPGDD DMDSPKETLP SKPVKKEKEQ 

       670        680        690        700        710        720 
RTRHLLTDLP LPPELPGGDL SPPDSPEPKA ITPPQQPYKK RPKICCPRYG ERRQTESDWG 

       730        740        750        760        770        780 
KRCVDKFDII GIIGEGTYGQ VYKAKDKDTG ELVALKKVRL DNEKEGFPIT AIREIKILRQ 

       790        800        810        820        830        840 
LIHRSVVNMK EIVTDKQDAL DFKKDKGAFY LVFEYMDHDL MGLLESGLVH FSEDHIKSFM 

       850        860        870        880        890        900 
KQLMEGLEYC HKKNFLHRDI KCSNILLNNS GQIKLADFGL ARLYNSEESR PYTNKVITLW 

       910        920        930        940        950        960 
YRPPELLLGE ERYTPAIDVW SCGCILGELF TKKPIFQANL ELAQLELISR LCGSPCPAVW 

       970        980        990       1000       1010       1020 
PDVIKLPYFN TMKPKKQYRR RLREEFSFIP SAALDLLDHM LTLDPSKRCT AEQTLQSDFL 

      1030       1040       1050       1060       1070       1080 
KDVELSKMAP PDLPHWQDCH ELWSKKRRRQ RQSGVVVEEP PPSKTSRKET TSGTSTEPVK 

      1090       1100       1110       1120       1130       1140 
NSSPAPPQPA PGKVESGAGD AIGLADITQQ LNQSELAVLL NLLQSQTDLS IPQMAQLLNI 

      1150       1160       1170       1180       1190       1200 
HSNPEMQQQL EALNQSISAL TEATSQQQDS ETMAPEESLK EAPSAPVILP SAEQTTLEAS 

      1210       1220       1230       1240       1250       1260 
STPADMQNIL AVLLSQLMKT QEPAGSLEEN NSDKNSGPQG PRRTPTMPQE EAAACPPHIL 

      1270       1280       1290       1300       1310       1320 
PPEKRPPEPP GPPPPPPPPP LVEGDLSSAP QELNPAVTAA LLQLLSQPEA EPPGHLPHEH 

      1330       1340       1350       1360       1370       1380 
QALRPMEYST RPRPNRTYGN TDGPETGFSA IDTDERNSGP ALTESLVQTL VKNRTFSGSL 

      1390       1400       1410       1420       1430       1440 
SHLGESSSYQ GTGSVQFPGD QDLRFARVPL ALHPVVGQPF LKAEGSSNSV VHAETKLQNY 

      1450       1460       1470       1480       1490 
GELGPGTTGA SSSGAGLHWG GPTQSSAYGK LYRGPTRVPP RGGRGRGVPY 

« Hide

Isoform 2 [UniParc].

Checksum: D0CF4B898D3032D4
Show »

FASTA1,481163,228
Isoform 3 [UniParc].

Checksum: 85B012B87EDC02F1
Show »

FASTA1,273141,449

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"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].
[21]"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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_055898.1. NM_015083.2.
NP_057591.2. NM_016507.3.
UniGeneHs.416108.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4CJYX-ray3.15C/D715-1038[»]
ProteinModelPortalQ9NYV4.
SMRQ9NYV4. Positions 706-1054.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119715. 23 interactions.
IntActQ9NYV4. 6 interactions.
MINTMINT-1191969.
STRING9606.ENSP00000398880.

PTM databases

PhosphoSiteQ9NYV4.

Polymorphism databases

DMDM308153421.

Proteomic databases

PaxDbQ9NYV4.
PRIDEQ9NYV4.

Protocols and materials databases

DNASU51755.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000430627; ENSP00000407720; ENSG00000167258. [Q9NYV4-2]
ENST00000447079; ENSP00000398880; ENSG00000167258. [Q9NYV4-1]
GeneID51755.
KEGGhsa:51755.
UCSCuc002hrw.4. human. [Q9NYV4-2]
uc010cvv.3. human. [Q9NYV4-1]

Organism-specific databases

CTD51755.
GeneCardsGC17P037618.
H-InvDBHIX0013777.
HGNCHGNC:24224. CDK12.
HPAHPA008038.
neXtProtNX_Q9NYV4.
PharmGKBPA165431656.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000049118.
HOVERGENHBG050852.
InParanoidQ9NYV4.
KOK08819.
OMAYSTRSHP.
PhylomeDBQ9NYV4.
TreeFamTF101060.

Enzyme and pathway databases

BRENDA2.7.11.22. 2681.
SignaLinkQ9NYV4.

Gene expression databases

ArrayExpressQ9NYV4.
BgeeQ9NYV4.
CleanExHS_CRKRS.
GenevestigatorQ9NYV4.

Family and domain databases

InterProIPR011009. 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]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCDK12. human.
GeneWikiCRKRS.
GenomeRNAi51755.
NextBio55858.
PROQ9NYV4.

Entry information

Entry nameCDK12_HUMAN
AccessionPrimary (citable) accession number: Q9NYV4
Secondary accession number(s): A7E2B2 expand/collapse secondary AC list , B4DYX4, B9EIQ6, O94978
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: October 5, 2010
Last modified: April 16, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM