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D2H526

- CDK12_AILME

UniProt

D2H526 - CDK12_AILME

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Protein

Cyclin-dependent kinase 12

Gene

CDK12

Organism
Ailuropoda melanoleuca (Giant panda)
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 sitei757 – 7571ATPPROSITE-ProRule annotation
Active sitei860 – 8601Proton acceptorPROSITE-ProRule annotation
Binding sitei1041 – 10411ATPPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi734 – 7429ATPPROSITE-ProRule annotation
Nucleotide bindingi815 – 8206ATPPROSITE-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. protein autophosphorylation Source: Ensembl
  4. regulation of MAP kinase activity Source: UniProtKB
  5. 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
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 12PRO_0000406957Add
BLAST

Amino acid modifications

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini728 – 1021294Protein kinasePROSITE-ProRule annotationAdd
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00770000120511.
HOGENOMiHOG000049118.
InParanoidiD2H526.
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.
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

« Hide

        10         20         30         40         50
MPNPERHGGK KDGSGGASGT LQPSSGGGSS NSRERHRLVS KHKRHKSKHS
60 70 80 90 100
KDMGLVTPEA APLGTIIKPL VEYDDISSDS DTFSDDMAFK LDRRENDERR
110 120 130 140 150
GTDRSDRLHK HRHHQHRRSR DLLKTKQTEK EKNQEVSSKS GSMKDRISGS
160 170 180 190 200
SKRSNEENED YGKAQISKSS SNKESRSSKL HKEKTRKERE LKSGHKDRSK
210 220 230 240 250
SHRKRETPKS YKTVDSPKRR SRSPHRKWSD SPKQDDSPSG ASYGQDYDLS
260 270 280 290 300
PPRSHTSSNY DSYKKSPGST SRRQSISPPY KEPSAYQSST RSPSPYSRRQ
310 320 330 340 350
RSVSPYSRRR SSSYERSGSY SGRSPSPYGR RRSSSPFMSK RSLSRSPLPS
360 370 380 390 400
RKSMKSRSRS PAYSRHSSSH SKKKRSGSRS RHSSISPVRL PLNSSLGAEL
410 420 430 440 450
SRKKKERAAA AAAAKMDGKE SKGSPIFLPR KENSLVEAKD SGLESKKLTR
460 470 480 490 500
GVKLEKSAPD TELVNIPHLN TEVKNSLDTG KVKLDENSEK HPIKDLKAQG
510 520 530 540 550
SRDSKPIALK EEIVTPKETE TSEKETPPPV PAVTSPPPPL PTTSPPPQTP
560 570 580 590 600
PLPPLPPLPA IPQQPPLPPP QPAFSHVLAS STSTLPPSTH PRTSTLSSQA
610 620 630 640 650
NSQPLAQVSV KTQVSVTAAI PHLKTSTLPP LPLPPLLPGD DDMDSPKETP
660 670 680 690 700
PSKPVKKEKE QRPRHLLTDL PLPPELPGGD PSPPDSPEPK AVTPPQQPYK
710 720 730 740 750
KRPKICCPRY GERRQTESDW GKRCVDKFDI IGIIGEGTYG QVYKAKDKDT
760 770 780 790 800
GELVALKKVR LDNEKEGFPI TAIREIKILR QLIHRSVVNM KEIVTDKQDA
810 820 830 840 850
LDFKKDKGAF YLVFEYMDHD LMGLLESGLV HFSEDHIKSF MKQLMEGLDY
860 870 880 890 900
CHKKNFLHRD IKCSNILLNN SGQIKLADFG LARLYNSEES RPYTNKVITL
910 920 930 940 950
WYRPPELLLG EERYTPAIDV WSCGCILGEL FTKKPIFQAN LELAQLELIS
960 970 980 990 1000
RLCGSPCPAV WPDVIKLPYF NTMKPKKQYR RRLREEFSFI PSAALDLLDH
1010 1020 1030 1040 1050
MLTLDPSKRC TAEQTLQSDF LKDVELSKMD PPDLPHWQDC HELWSKKRRR
1060 1070 1080 1090 1100
QRQSGVVIEE PPPSKASRKE TTSGTSAEPV KNSSPAPPQP ASGKVEPGTG
1110 1120 1130 1140 1150
DAIGLGDITQ QLNQSELAVL LNLLQSQTDL SIPQMAQLLN IHSNPEMQQQ
1160 1170 1180 1190 1200
LEALNQSISA LTEATSQQQD SEHMAPEESL KEAPPALVVQ PSAEQTTSEA
1210 1220 1230 1240 1250
SSTPADMQNM LAVLLSQLMK TQEPAGSLEE NNSDKNSGPQ GPRRTPTMPQ
1260 1270 1280 1290 1300
EEAAACPPHI LPPEKRPPEP PGPPPPPPPP PLIEGDLSSA PQELNPAVTA
1310 1320 1330 1340 1350
ALLQLLSQPE AEPPGHLPHE HQALRPMEYS TRPHPNRTYG NTDGPETGFS
1360 1370 1380 1390 1400
ATDTDERNSG PALTESLTQT LVKNRTFSGS VSHLGESSSY QGTGSVQFPG
1410 1420 1430 1440 1450
DQDLRFARVP LPLHSVVGQP FLKAEGSSNS VVHAETKLQN YGELGPGTTG
1460 1470 1480 1490
ASSSGAGLNW GGSAQSSAYG KLYRGPTRVP PRGGRGRGVP Y
Length:1,491
Mass (Da):164,479
Last modified:February 9, 2010 - v1
Checksum:iBA53304B554D1195
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 ENSGT00770000120511.
HOGENOMi HOG000049118.
InParanoidi D2H526.
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.
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: November 26, 2014
This is version 38 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