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E1BB50

- CDK12_BOVIN

UniProt

E1BB50 - CDK12_BOVIN

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Protein

Cyclin-dependent kinase 12

Gene

CDK12

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

Cyclin-dependent kinase that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation. Regulates the expression of genes involved in DNA repair and is required for the maintenance of genomic stability. Preferentially phosphorylates 'Ser-5' in CTD repeats that are already phosphorylated at 'Ser-7', but can also phosphorylate 'Ser-2'. Required for RNA splicing, possibly by phosphorylating SRSF1/SF2. Involved in regulation of MAP kinase activity, possibly leading to affect the response to estrogen inhibitors By similarity.By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei756 – 7561ATPPROSITE-ProRule annotation
Active sitei859 – 8591Proton acceptorPROSITE-ProRule annotation
Binding sitei1042 – 10421ATPPROSITE-ProRule annotation

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cyclin-dependent protein serine/threonine kinase activity Source: UniProtKB-EC
  3. RNA polymerase II carboxy-terminal domain kinase activity Source: UniProtKB

GO - Biological processi

  1. mRNA processing Source: UniProtKB-KW
  2. phosphorylation of RNA polymerase II C-terminal domain Source: UniProtKB
  3. regulation of MAP kinase activity Source: UniProtKB
  4. RNA splicing Source: UniProtKB
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

Names & Taxonomyi

Protein namesi
Recommended name:
Cyclin-dependent kinase 12 (EC:2.7.11.22, EC:2.7.11.23)
Alternative name(s):
Cell division protein kinase 12
Gene namesi
Name:CDK12
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
ProteomesiUP000009136: Unplaced

Subcellular locationi

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Post-translational modificationi

Phosphorylation at Thr-893 increases kinase activity.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiE1BB50.

Interactioni

Subunit structurei

Interacts with CCNL1 and CCNL2.By similarity

Structurei

3D structure databases

ProteinModelPortaliE1BB50.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Compositional bias

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

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiE1BB50.

Family and domain databases

InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

E1BB50-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPNPERHGGK KDGSGGASGT LQPSSGGGSS NSRERHRLGS KHKRHKSKHS
60 70 80 90 100
KDMGLVTPEA APLGTVIKPL VEYDDISSDS DTFSDDLAFK VDRRENDERR
110 120 130 140 150
GTDRSDRLHK HRHHQHRRTR DLLKTKQTEK EKNLEASSKS GSTKDRISGS
160 170 180 190 200
SKRSNEENDD HGKAQISKSS NKESRSSKLH KEKTRKEREL KSGHKDRSKS
210 220 230 240 250
HRKRETPKSY KTVDSPKRRS RSPHRKWSDS PKQDDSPSGA SYGQDYDLSP
260 270 280 290 300
PRSHTSSNYD SYKKSPGSTS RRQSISPPYK EPSAYQSSTR SPSPYSRRQR
310 320 330 340 350
SVSPYSRRRS SSYERSGSYS GRSPSPYGRR RSSSPFLSKR SLSRSPLPSR
360 370 380 390 400
KSMKSRSRSP AYSRHSSSHS KKKRSGSRSR HSSISPVRLP LNSSLGAELS
410 420 430 440 450
RKKKERAAAA AAAKMDGKES KGSPIFLPKK ENSSVEAKDS GLEPKKLPRG
460 470 480 490 500
VKLEKSAPDT ELVNVTHLNT EVKNSLDTGK VKLDENSEKH PVLKDTKVQG
510 520 530 540 550
TKDSKPVALK EEIVTPKETE TSEKETLPPL PTVTSPPPLP TTTPPPQTPP
560 570 580 590 600
LPPLPPLPAI PQQPPLPPPQ PTFSQVLSSS TSTLPPSVHP RTSTLSSQAN
610 620 630 640 650
SQPSVQVSVK TQVSVTAAIP HLKTSTLPPL PLPPLLLGDD DMDSPKETLP
660 670 680 690 700
SKPVKKEKEQ RPRHLLTDLP LPPELPGGDP 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 KQLMEGLDYC
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 RLREEFSFFF LPWGALDLLD
1010 1020 1030 1040 1050
HMLTLDPSKR CTAEQTLQSD FLKDVELSKM DPPDLPHWQD CHELWSKKRR
1060 1070 1080 1090 1100
RQRQSGVLVE EPPPPKASRK ETISGTSAEP VKNSSPAPPQ PAPGKVEPGA
1110 1120 1130 1140 1150
GDAIGLGDIT QQLNQSELAV LLNLLQSQTD LSIPQMAQLL NIHSNPEMQQ
1160 1170 1180 1190 1200
QLEALNQSIS ALTAATSQQQ DSEPTAPEES LKEIAPAPAV QPSAEQTTPE
1210 1220 1230 1240 1250
ASSTPADMQN MLAVLLSQLM KTQEPAGNLE ENNSDKNSGP QGPRRTPTMP
1260
QEEAAGKQTG HESH
Length:1,264
Mass (Da):140,642
Last modified:November 2, 2010 - v1
Checksum:iA074D89C354DBAC7
GO

Sequence databases

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

Cross-referencesi

Sequence databases

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

3D structure databases

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

Proteomic databases

PRIDEi E1BB50.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

InParanoidi E1BB50.

Family and domain databases

InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
[Graphical view ]
SMARTi SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

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

Entry informationi

Entry nameiCDK12_BOVIN
AccessioniPrimary (citable) accession number: E1BB50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: November 2, 2010
Last modified: October 29, 2014
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3