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Protein

Cyclin-dependent kinase 12

Gene

CDK12

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.
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)DescriptionActionsGraphical viewLength
Binding sitei756ATP1
Active sitei859Proton acceptorPROSITE-ProRule annotation1
Binding sitei1040ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi733 – 741ATP9
Nucleotide bindingi814 – 819ATP6

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cyclin binding Source: MGI
  • cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
  • protein kinase activity Source: HGNC
  • RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB

GO - Biological processi

  • mRNA processing Source: UniProtKB-KW
  • phosphorylation of RNA polymerase II C-terminal domain Source: UniProtKB
  • protein autophosphorylation Source: HGNC
  • regulation of MAP kinase activity Source: UniProtKB
  • regulation of RNA splicing Source: Ensembl
  • RNA splicing 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

BioCyciZFISH:HS09531-MONOMER.
BRENDAi2.7.11.22. 2681.
ReactomeiR-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
SignaLinkiQ9NYV4.
SIGNORiQ9NYV4.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:24224. CDK12.

Subcellular locationi

GO - Cellular componenti

  • cyclin K-CDK12 complex Source: MGI
  • nuclear cyclin-dependent protein kinase holoenzyme complex Source: UniProtKB
  • nuclear speck Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi877D → N: Abolishes kinase activity. 1 Publication1

Organism-specific databases

DisGeNETi51755.
OpenTargetsiENSG00000167258.
PharmGKBiPA165431656.

Chemistry databases

ChEMBLiCHEMBL3559691.

Polymorphism and mutation databases

BioMutaiCDK12.
DMDMi308153421.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000857151 – 1490Cyclin-dependent kinase 12Add BLAST1490

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei57PhosphothreonineCombined sources1
Modified residuei73PhosphotyrosineCombined sources1
Modified residuei236PhosphoserineCombined sources1
Modified residuei249PhosphoserineCombined sources1
Modified residuei265PhosphoserineCombined sources1
Modified residuei274PhosphoserineCombined sources1
Modified residuei276PhosphoserineCombined sources1
Modified residuei301PhosphoserineCombined sources1
Modified residuei303PhosphoserineCombined sources1
Modified residuei310PhosphoserineCombined sources1
Modified residuei312PhosphoserineCombined sources1
Modified residuei318PhosphoserineCombined sources1
Modified residuei323PhosphoserineCombined sources1
Modified residuei325PhosphoserineCombined sources1
Modified residuei332PhosphoserineCombined sources1
Modified residuei333PhosphoserineCombined sources1
Modified residuei334PhosphoserineCombined sources1
Modified residuei338PhosphoserineCombined sources1
Modified residuei341PhosphoserineCombined sources1
Modified residuei343PhosphoserineCombined sources1
Modified residuei345PhosphoserineCombined sources1
Modified residuei383PhosphoserineCombined sources1
Modified residuei385PhosphoserineCombined sources1
Modified residuei400PhosphoserineCombined sources1
Modified residuei420PhosphoserineCombined sources1
Modified residuei423PhosphoserineCombined sources1
Modified residuei514PhosphothreonineCombined sources1
Modified residuei614PhosphoserineCombined sources1
Modified residuei644PhosphoserineBy similarity1
Modified residuei681PhosphoserineCombined sources1
Modified residuei685PhosphoserineCombined sources1
Modified residuei692PhosphothreonineCombined sources1
Modified residuei889PhosphoserineCombined sources1
Modified residuei893PhosphothreonineCombined sources1 Publication1
Modified residuei1053PhosphoserineCombined sources1
Modified residuei1083PhosphoserineCombined sources1
Modified residuei1244PhosphothreonineCombined sources1
Modified residuei1246PhosphothreonineBy similarity1

Post-translational modificationi

Phosphorylation at Thr-893 increases kinase activity.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9NYV4.
MaxQBiQ9NYV4.
PaxDbiQ9NYV4.
PeptideAtlasiQ9NYV4.
PRIDEiQ9NYV4.

PTM databases

iPTMnetiQ9NYV4.
PhosphoSitePlusiQ9NYV4.

Expressioni

Tissue specificityi

Ubiquitously expressed.1 Publication

Gene expression databases

BgeeiENSG00000167258.
CleanExiHS_CRKRS.
ExpressionAtlasiQ9NYV4. baseline and differential.
GenevisibleiQ9NYV4. HS.

Organism-specific databases

HPAiHPA008038.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • cyclin binding Source: MGI

Protein-protein interaction databases

BioGridi119715. 38 interactors.
DIPiDIP-39768N.
IntActiQ9NYV4. 12 interactors.
MINTiMINT-1191969.
STRINGi9606.ENSP00000398880.

Structurei

Secondary structure

11490
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi724 – 726Combined sources3
Beta strandi727 – 735Combined sources9
Beta strandi737 – 746Combined sources10
Turni747 – 749Combined sources3
Beta strandi752 – 758Combined sources7
Beta strandi761 – 763Combined sources3
Beta strandi764 – 767Combined sources4
Helixi769 – 778Combined sources10
Beta strandi789 – 794Combined sources6
Turni802 – 804Combined sources3
Beta strandi809 – 814Combined sources6
Beta strandi817 – 819Combined sources3
Helixi820 – 826Combined sources7
Helixi833 – 852Combined sources20
Helixi862 – 864Combined sources3
Beta strandi865 – 867Combined sources3
Beta strandi873 – 875Combined sources3
Beta strandi886 – 888Combined sources3
Helixi899 – 901Combined sources3
Helixi904 – 907Combined sources4
Helixi916 – 931Combined sources16
Helixi941 – 952Combined sources12
Turni957 – 959Combined sources3
Helixi961 – 965Combined sources5
Turni967 – 971Combined sources5
Helixi982 – 985Combined sources4
Turni986 – 988Combined sources3
Helixi991 – 1000Combined sources10
Turni1005 – 1007Combined sources3
Helixi1011 – 1014Combined sources4
Helixi1018 – 1021Combined sources4
Helixi1025 – 1027Combined sources3
Beta strandi1035 – 1037Combined sources3
Helixi1041 – 1045Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4CXAX-ray3.15A/C715-1052[»]
4NSTX-ray2.20A/C714-1063[»]
4UN0X-ray3.15C/D715-1038[»]
5ACBX-ray2.70C/D715-1052[»]
ProteinModelPortaliQ9NYV4.
SMRiQ9NYV4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini727 – 1020Protein kinasePROSITE-ProRule annotationAdd BLAST294

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi407 – 413Poly-Ala7
Compositional biasi535 – 540Poly-Pro6
Compositional biasi1266 – 1280Poly-ProAdd BLAST15

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0600. Eukaryota.
ENOG410XPIR. LUCA.
GeneTreeiENSGT00860000133755.
HOGENOMiHOG000049118.
HOVERGENiHBG050852.
InParanoidiQ9NYV4.
KOiK08819.
OMAiXCILGEL.
OrthoDBiEOG091G08Z8.
PhylomeDBiQ9NYV4.
TreeFamiTF101060.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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. AlignAdd to basket

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

        10         20         30         40         50
MPNSERHGGK KDGSGGASGT LQPSSGGGSS NSRERHRLVS KHKRHKSKHS
60 70 80 90 100
KDMGLVTPEA ASLGTVIKPL VEYDDISSDS DTFSDDMAFK LDRRENDERR
110 120 130 140 150
GSDRSDRLHK HRHHQHRRSR DLLKAKQTEK EKSQEVSSKS GSMKDRISGS
160 170 180 190 200
SKRSNEETDD YGKAQVAKSS SKESRSSKLH KEKTRKEREL KSGHKDRSKS
210 220 230 240 250
HRKRETPKSY KTVDSPKRRS RSPHRKWSDS SKQDDSPSGA SYGQDYDLSP
260 270 280 290 300
SRSHTSSNYD SYKKSPGSTS RRQSVSPPYK EPSAYQSSTR SPSPYSRRQR
310 320 330 340 350
SVSPYSRRRS SSYERSGSYS GRSPSPYGRR RSSSPFLSKR SLSRSPLPSR
360 370 380 390 400
KSMKSRSRSP AYSRHSSSHS KKKRSSSRSR HSSISPVRLP LNSSLGAELS
410 420 430 440 450
RKKKERAAAA AAAKMDGKES KGSPVFLPRK ENSSVEAKDS GLESKKLPRS
460 470 480 490 500
VKLEKSAPDT ELVNVTHLNT EVKNSSDTGK VKLDENSEKH LVKDLKAQGT
510 520 530 540 550
RDSKPIALKE EIVTPKETET SEKETPPPLP TIASPPPPLP TTTPPPQTPP
560 570 580 590 600
LPPLPPIPAL PQQPPLPPSQ PAFSQVPASS TSTLPPSTHS KTSAVSSQAN
610 620 630 640 650
SQPPVQVSVK TQVSVTAAIP HLKTSTLPPL PLPPLLPGDD DMDSPKETLP
660 670 680 690 700
SKPVKKEKEQ RTRHLLTDLP LPPELPGGDL SPPDSPEPKA ITPPQQPYKK
710 720 730 740 750
RPKICCPRYG ERRQTESDWG KRCVDKFDII GIIGEGTYGQ VYKAKDKDTG
760 770 780 790 800
ELVALKKVRL DNEKEGFPIT AIREIKILRQ LIHRSVVNMK EIVTDKQDAL
810 820 830 840 850
DFKKDKGAFY LVFEYMDHDL MGLLESGLVH FSEDHIKSFM KQLMEGLEYC
860 870 880 890 900
HKKNFLHRDI KCSNILLNNS GQIKLADFGL ARLYNSEESR PYTNKVITLW
910 920 930 940 950
YRPPELLLGE ERYTPAIDVW SCGCILGELF TKKPIFQANL ELAQLELISR
960 970 980 990 1000
LCGSPCPAVW PDVIKLPYFN TMKPKKQYRR RLREEFSFIP SAALDLLDHM
1010 1020 1030 1040 1050
LTLDPSKRCT AEQTLQSDFL KDVELSKMAP PDLPHWQDCH ELWSKKRRRQ
1060 1070 1080 1090 1100
RQSGVVVEEP PPSKTSRKET TSGTSTEPVK NSSPAPPQPA PGKVESGAGD
1110 1120 1130 1140 1150
AIGLADITQQ LNQSELAVLL NLLQSQTDLS IPQMAQLLNI HSNPEMQQQL
1160 1170 1180 1190 1200
EALNQSISAL TEATSQQQDS ETMAPEESLK EAPSAPVILP SAEQTTLEAS
1210 1220 1230 1240 1250
STPADMQNIL AVLLSQLMKT QEPAGSLEEN NSDKNSGPQG PRRTPTMPQE
1260 1270 1280 1290 1300
EAAACPPHIL PPEKRPPEPP GPPPPPPPPP LVEGDLSSAP QELNPAVTAA
1310 1320 1330 1340 1350
LLQLLSQPEA EPPGHLPHEH QALRPMEYST RPRPNRTYGN TDGPETGFSA
1360 1370 1380 1390 1400
IDTDERNSGP ALTESLVQTL VKNRTFSGSL SHLGESSSYQ GTGSVQFPGD
1410 1420 1430 1440 1450
QDLRFARVPL ALHPVVGQPF LKAEGSSNSV VHAETKLQNY GELGPGTTGA
1460 1470 1480 1490
SSSGAGLHWG GPTQSSAYGK LYRGPTRVPP RGGRGRGVPY
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti133S → G in BAG63886 (PubMed:14702039).Curated1
Sequence conflicti268S → G in BAG63886 (PubMed:14702039).Curated1
Sequence conflicti639D → G in AAF36401 (PubMed:11683387).Curated1
Sequence conflicti737T → I in BAG63886 (PubMed:14702039).Curated1
Sequence conflicti745K → R in AAF36401 (PubMed:11683387).Curated1
Sequence conflicti822G → V in BAG63886 (PubMed:14702039).Curated1
Sequence conflicti1195T → M in AAF36401 (PubMed:11683387).Curated1
Sequence conflicti1195T → M in BAA74927 (PubMed:10048485).Curated1
Sequence conflicti1195T → M in AAI50266 (Ref. 6) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_041968530P → A.1 PublicationCorresponds to variant rs56121596dbSNPEnsembl.1
Natural variantiVAR_041969912R → H in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_0419701189L → Q.1 PublicationCorresponds to variant rs56362165dbSNPEnsembl.1
Natural variantiVAR_0419711275P → L.1 PublicationCorresponds to variant rs34070318dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_040908349Missing in isoform 3. 1 Publication1
Alternative sequenceiVSP_0409091205 – 1274DMQNI…PGPPP → ILWYMQRPNCKTMGSWGQEP LGPAAQEQAFTGGAQLSLLL MENSIGGLQESHQEGEEGEE FLTNPETSVS in isoform 3. 1 PublicationAdd BLAST70
Alternative sequenceiVSP_0302841254 – 1262Missing in isoform 2. 2 Publications9
Alternative sequenceiVSP_0409101275 – 1490Missing in isoform 3. 1 PublicationAdd BLAST216

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.345028.
Hs.416108.

Genome annotation databases

EnsembliENST00000430627; ENSP00000407720; ENSG00000167258. [Q9NYV4-2]
ENST00000447079; ENSP00000398880; ENSG00000167258. [Q9NYV4-1]
GeneIDi51755.
KEGGihsa:51755.
UCSCiuc002hrw.6. human. [Q9NYV4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.345028.
Hs.416108.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4CXAX-ray3.15A/C715-1052[»]
4NSTX-ray2.20A/C714-1063[»]
4UN0X-ray3.15C/D715-1038[»]
5ACBX-ray2.70C/D715-1052[»]
ProteinModelPortaliQ9NYV4.
SMRiQ9NYV4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119715. 38 interactors.
DIPiDIP-39768N.
IntActiQ9NYV4. 12 interactors.
MINTiMINT-1191969.
STRINGi9606.ENSP00000398880.

Chemistry databases

ChEMBLiCHEMBL3559691.

PTM databases

iPTMnetiQ9NYV4.
PhosphoSitePlusiQ9NYV4.

Polymorphism and mutation databases

BioMutaiCDK12.
DMDMi308153421.

Proteomic databases

EPDiQ9NYV4.
MaxQBiQ9NYV4.
PaxDbiQ9NYV4.
PeptideAtlasiQ9NYV4.
PRIDEiQ9NYV4.

Protocols and materials databases

DNASUi51755.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000430627; ENSP00000407720; ENSG00000167258. [Q9NYV4-2]
ENST00000447079; ENSP00000398880; ENSG00000167258. [Q9NYV4-1]
GeneIDi51755.
KEGGihsa:51755.
UCSCiuc002hrw.6. human. [Q9NYV4-1]

Organism-specific databases

CTDi51755.
DisGeNETi51755.
GeneCardsiCDK12.
H-InvDBHIX0013777.
HGNCiHGNC:24224. CDK12.
HPAiHPA008038.
MIMi615514. gene.
neXtProtiNX_Q9NYV4.
OpenTargetsiENSG00000167258.
PharmGKBiPA165431656.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0600. Eukaryota.
ENOG410XPIR. LUCA.
GeneTreeiENSGT00860000133755.
HOGENOMiHOG000049118.
HOVERGENiHBG050852.
InParanoidiQ9NYV4.
KOiK08819.
OMAiXCILGEL.
OrthoDBiEOG091G08Z8.
PhylomeDBiQ9NYV4.
TreeFamiTF101060.

Enzyme and pathway databases

BioCyciZFISH:HS09531-MONOMER.
BRENDAi2.7.11.22. 2681.
ReactomeiR-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
SignaLinkiQ9NYV4.
SIGNORiQ9NYV4.

Miscellaneous databases

ChiTaRSiCDK12. human.
GeneWikiiCRKRS.
GenomeRNAii51755.
PROiQ9NYV4.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000167258.
CleanExiHS_CRKRS.
ExpressionAtlasiQ9NYV4. baseline and differential.
GenevisibleiQ9NYV4. HS.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 158 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.