Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

D2H526

- CDK12_AILME

UniProt

D2H526 - CDK12_AILME

Protein

Cyclin-dependent kinase 12

Gene

CDK12

Organism
Ailuropoda melanoleuca (Giant panda)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 36 (01 Oct 2014)
      Sequence version 1 (09 Feb 2010)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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

    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

    « Hide

    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: October 1, 2014
    This is version 36 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