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D2H526

- CDK12_AILME

UniProt

D2H526 - CDK12_AILME

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Protein
Cyclin-dependent kinase 12
Gene
CDK12, PANDA_004952
Organism
Ailuropoda melanoleuca (Giant panda)
Status
Reviewed - Annotation score: 5 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.

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 sitei757 – 7571ATP By similarity
Active sitei860 – 8601Proton acceptor By similarity
Binding sitei1041 – 10411ATP By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi734 – 7429ATP By similarity
Nucleotide bindingi815 – 8206ATP By similarity

GO - Molecular functioni

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

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: Ensembl
  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

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
ORF Names:PANDA_004952
OrganismiAiluropoda melanoleuca (Giant panda)
Taxonomic identifieri9646 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaUrsidaeAiluropoda
ProteomesiUP000008912: Unplaced

Subcellular locationi

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

GO - Cellular componenti

  1. cyclin K-CDK12 complex Source: Ensembl
  2. nuclear cyclin-dependent protein kinase holoenzyme complex Source: UniProtKB
  3. nuclear speck Source: UniProtKB
  4. nucleolus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14911491Cyclin-dependent kinase 12
PRO_0000406957Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei57 – 571Phosphothreonine By similarity
Modified residuei73 – 731Phosphotyrosine By similarity
Modified residuei237 – 2371Phosphoserine By similarity
Modified residuei250 – 2501Phosphoserine By similarity
Modified residuei275 – 2751Phosphoserine By similarity
Modified residuei277 – 2771Phosphoserine By similarity
Modified residuei302 – 3021Phosphoserine By similarity
Modified residuei304 – 3041Phosphoserine By similarity
Modified residuei311 – 3111Phosphoserine By similarity
Modified residuei313 – 3131Phosphoserine By similarity
Modified residuei319 – 3191Phosphoserine By similarity
Modified residuei324 – 3241Phosphoserine By similarity
Modified residuei326 – 3261Phosphoserine By similarity
Modified residuei333 – 3331Phosphoserine By similarity
Modified residuei334 – 3341Phosphoserine By similarity
Modified residuei335 – 3351Phosphoserine By similarity
Modified residuei339 – 3391Phosphoserine By similarity
Modified residuei346 – 3461Phosphoserine By similarity
Modified residuei384 – 3841Phosphoserine By similarity
Modified residuei386 – 3861Phosphoserine By similarity
Modified residuei401 – 4011Phosphoserine By similarity
Modified residuei421 – 4211Phosphoserine By similarity
Modified residuei424 – 4241Phosphoserine By similarity
Modified residuei515 – 5151Phosphothreonine By similarity
Modified residuei682 – 6821Phosphoserine By similarity
Modified residuei686 – 6861Phosphoserine By similarity
Modified residuei693 – 6931Phosphothreonine By similarity
Modified residuei894 – 8941Phosphothreonine By similarity
Modified residuei1054 – 10541Phosphoserine By similarity
Modified residuei1084 – 10841Phosphoserine By similarity
Modified residuei1245 – 12451Phosphothreonine By similarity

Post-translational modificationi

Phosphorylation at Thr-894 increases kinase activity By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiD2H526.

Interactioni

Subunit structurei

Interacts with CCNL1 and CCNL2 By similarity.

Structurei

3D structure databases

ProteinModelPortaliD2H526.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini728 – 1021294Protein kinase
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi137 – 395259Ser-rich
Add
BLAST
Compositional biasi408 – 4147Poly-Ala
Compositional biasi527 – 708182Pro-rich
Add
BLAST
Compositional biasi1239 – 128143Pro-rich
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00740000114964.
HOGENOMiHOG000049118.
KOiK08819.
OMAiEEIATPK.
OrthoDBiEOG76DTSM.
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]

Sequencei

Sequence statusi: Complete.

D2H526-1 [UniParc]FASTAAdd to Basket

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MPNPERHGGK KDGSGGASGT LQPSSGGGSS NSRERHRLVS KHKRHKSKHS     50
KDMGLVTPEA APLGTIIKPL VEYDDISSDS DTFSDDMAFK LDRRENDERR 100
GTDRSDRLHK HRHHQHRRSR DLLKTKQTEK EKNQEVSSKS GSMKDRISGS 150
SKRSNEENED YGKAQISKSS SNKESRSSKL HKEKTRKERE LKSGHKDRSK 200
SHRKRETPKS YKTVDSPKRR SRSPHRKWSD SPKQDDSPSG ASYGQDYDLS 250
PPRSHTSSNY DSYKKSPGST SRRQSISPPY KEPSAYQSST RSPSPYSRRQ 300
RSVSPYSRRR SSSYERSGSY SGRSPSPYGR RRSSSPFMSK RSLSRSPLPS 350
RKSMKSRSRS PAYSRHSSSH SKKKRSGSRS RHSSISPVRL PLNSSLGAEL 400
SRKKKERAAA AAAAKMDGKE SKGSPIFLPR KENSLVEAKD SGLESKKLTR 450
GVKLEKSAPD TELVNIPHLN TEVKNSLDTG KVKLDENSEK HPIKDLKAQG 500
SRDSKPIALK EEIVTPKETE TSEKETPPPV PAVTSPPPPL PTTSPPPQTP 550
PLPPLPPLPA IPQQPPLPPP QPAFSHVLAS STSTLPPSTH PRTSTLSSQA 600
NSQPLAQVSV KTQVSVTAAI PHLKTSTLPP LPLPPLLPGD DDMDSPKETP 650
PSKPVKKEKE QRPRHLLTDL PLPPELPGGD PSPPDSPEPK AVTPPQQPYK 700
KRPKICCPRY GERRQTESDW GKRCVDKFDI IGIIGEGTYG QVYKAKDKDT 750
GELVALKKVR LDNEKEGFPI TAIREIKILR QLIHRSVVNM KEIVTDKQDA 800
LDFKKDKGAF YLVFEYMDHD LMGLLESGLV HFSEDHIKSF MKQLMEGLDY 850
CHKKNFLHRD IKCSNILLNN SGQIKLADFG LARLYNSEES RPYTNKVITL 900
WYRPPELLLG EERYTPAIDV WSCGCILGEL FTKKPIFQAN LELAQLELIS 950
RLCGSPCPAV WPDVIKLPYF NTMKPKKQYR RRLREEFSFI PSAALDLLDH 1000
MLTLDPSKRC TAEQTLQSDF LKDVELSKMD PPDLPHWQDC HELWSKKRRR 1050
QRQSGVVIEE PPPSKASRKE TTSGTSAEPV KNSSPAPPQP ASGKVEPGTG 1100
DAIGLGDITQ QLNQSELAVL LNLLQSQTDL SIPQMAQLLN IHSNPEMQQQ 1150
LEALNQSISA LTEATSQQQD SEHMAPEESL KEAPPALVVQ PSAEQTTSEA 1200
SSTPADMQNM LAVLLSQLMK TQEPAGSLEE NNSDKNSGPQ GPRRTPTMPQ 1250
EEAAACPPHI LPPEKRPPEP PGPPPPPPPP PLIEGDLSSA PQELNPAVTA 1300
ALLQLLSQPE AEPPGHLPHE HQALRPMEYS TRPHPNRTYG NTDGPETGFS 1350
ATDTDERNSG PALTESLTQT LVKNRTFSGS VSHLGESSSY QGTGSVQFPG 1400
DQDLRFARVP LPLHSVVGQP FLKAEGSSNS VVHAETKLQN YGELGPGTTG 1450
ASSSGAGLNW GGSAQSSAYG KLYRGPTRVP PRGGRGRGVP Y 1491
Length:1,491
Mass (Da):164,479
Last modified:February 9, 2010 - v1
Checksum:iBA53304B554D1195
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GL192497 Genomic DNA. Translation: EFB19924.1.
RefSeqiXP_002916839.1. XM_002916793.1.

Genome annotation databases

EnsembliENSAMET00000004348; ENSAMEP00000004181; ENSAMEG00000003944.
GeneIDi100467815.
KEGGiaml:100467815.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
GL192497 Genomic DNA. Translation: EFB19924.1 .
RefSeqi XP_002916839.1. XM_002916793.1.

3D structure databases

ProteinModelPortali D2H526.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi D2H526.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSAMET00000004348 ; ENSAMEP00000004181 ; ENSAMEG00000003944 .
GeneIDi 100467815.
KEGGi aml:100467815.

Organism-specific databases

CTDi 51755.

Phylogenomic databases

GeneTreei ENSGT00740000114964.
HOGENOMi HOG000049118.
KOi K08819.
OMAi EEIATPK.
OrthoDBi EOG76DTSM.
TreeFami TF101060.

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. "The sequence and de novo assembly of the giant panda genome."
    Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B., Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.
    , Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A., Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B., Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W., Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M., Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G., Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C., Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D., Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W., Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q., Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X., Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y., Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L., Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J., Wang J.
    Nature 463:311-317(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiCDK12_AILME
AccessioniPrimary (citable) accession number: D2H526
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: February 9, 2010
Last modified: June 11, 2014
This is version 35 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

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