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Q9NYV4

- CDK12_HUMAN

UniProt

Q9NYV4 - CDK12_HUMAN

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Protein
Cyclin-dependent kinase 12
Gene
CDK12, CRK7, CRKRS, KIAA0904
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.2 Publications
ATP + a protein = ADP + a phosphoprotein.2 Publications

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 acceptor By similarity
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. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB
  3. cyclin binding Source: MGI
  4. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
  5. protein binding Source: UniProtKB
  6. protein kinase activity Source: HGNC

GO - Biological processi

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

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.2 Publications

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
Complete GO annotation...

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 12
PRO_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.

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.2 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini727 – 1020294Protein kinase
Add
BLAST

Compositional bias

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

Sequence similaritiesi

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.

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.
VSP_040908
Alternative sequencei1205 – 127470DMQNI…PGPPP → ILWYMQRPNCKTMGSWGQEP LGPAAQEQAFTGGAQLSLLL MENSIGGLQESHQEGEEGEE FLTNPETSVS in isoform 3.
VSP_040909Add
BLAST
Alternative sequencei1254 – 12629Missing in isoform 2.
VSP_030284
Alternative sequencei1275 – 1490216Missing in isoform 3.
VSP_040910Add
BLAST

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 132 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

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