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P51953

- CDK7_CARAU

UniProt

P51953 - CDK7_CARAU

Protein

Cyclin-dependent kinase 7

Gene

cdk7

Organism
Carassius auratus (Goldfish)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Serine/threonine kinase involved in cell cycle control and in RNA polymerase II-mediated RNA transcription. Cyclin-dependent kinases (CDKs) are activated by the binding to a cyclin and mediate the progression through the cell cycle. Each different complex controls a specific transition between 2 subsequent phases in the cell cycle. Required for both activation and complex formation of cdk1/cyclin-B during G2-M transition, and for activation of cdk2/cyclins during G1-S transition (but not complex formation). cdk7 is the catalytic subunit of the CDK-activating kinase (CAK) complex. CAK activates the cyclin-associated kinases cdk1, cdk2, cdk4 and cdk6 by threonine phosphorylation, thus regulating cell cycle progression. CAK complexed to the core-TFIIH basal transcription factor activates RNA polymerase II by serine phosphorylation of the repetitive C-terminal domain (CTD) of its large subunit (polr2a), allowing its escape from the promoter and elongation of the transcripts By similarity.By similarity

    Catalytic activityi

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

    Enzyme regulationi

    Phosphorylation at Thr-169 is required for enzymatic activity.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei41 – 411ATPPROSITE-ProRule annotation
    Active sitei136 – 1361Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi18 – 269ATPPROSITE-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-EC

    GO - Biological processi

    1. meiotic nuclear division Source: UniProtKB-KW

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Meiosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-dependent kinase 7 (EC:2.7.11.22, EC:2.7.11.23)
    Alternative name(s):
    40 kDa protein kinase
    CDC2/CDK2,4-activating kinase
    Cell division protein kinase 7
    P40 MO15
    Gene namesi
    Name:cdk7
    Synonyms:mo15
    OrganismiCarassius auratus (Goldfish)
    Taxonomic identifieri7957 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiOstariophysiCypriniformesCyprinidaeCarassius

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 344344Cyclin-dependent kinase 7PRO_0000085794Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei163 – 1631Phosphoserine; by CDK1 and CDK2By similarity
    Modified residuei169 – 1691Phosphothreonine; by CDK2By similarity

    Post-translational modificationi

    Phosphorylation of Ser-163 during mitosis inactivates the enzyme. Phosphorylation of Thr-169 is required for activity. Phosphorylated at Ser-163 and Thr-169 by CDK2 By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Interactioni

    Subunit structurei

    Probably associates with cyclin-H (ccnh) and mat1 to form a multimeric active enzyme.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP51953.
    SMRiP51953. Positions 13-310.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 294283Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    HOVERGENiHBG014652.

    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.

    P51953-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALDVKSRAK LYEKLDFLGE GQFATVYKAR DKTTNTIVAI KKIKVGHRTE    50
    AKDGINRTAL REIKLLQELS HPNIIGLLDA FGHKSNISLL CFMETDLEVI 100
    IKDTSLVLTP ANIKAYILMS LQGLEYMHNH WILHRDLKPN NLLLDENGVL 150
    KLADFGLAKA FGSPNRVYTH QVVTRWYRAP ELLFGARMYG VGVDMWAVGS 200
    ILAELLLRVP FLAGDSDLDQ LTGIFEALGT PTEETWPGMS NLPDYVSFKL 250
    FPGTPLEHIF SAAGDDLLEL LKGLFTFNPC TRTTASQALK MRYFSIRPGP 300
    TPGPQLPRPN SSTEALKEKE NLLIGIKRKR DSIEQGTLKK KLVF 344
    Length:344
    Mass (Da):38,510
    Last modified:October 1, 1996 - v1
    Checksum:i2AE835FFBEFAA1BA
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38631 mRNA. Translation: BAA07611.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D38631 mRNA. Translation: BAA07611.1 .

    3D structure databases

    ProteinModelPortali P51953.
    SMRi P51953. Positions 13-310.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG014652.

    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. "A fish homolog of the cdc2-related protein p40 MO15: its cDNA cloning and expression in oocytes."
      Onoe S., Yamashita M., Kajiura H., Katsu Y., Jianquao J., Nagahama Y.
      Biomed. Res. 14:441-444(1993)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Oocyte.

    Entry informationi

    Entry nameiCDK7_CARAU
    AccessioniPrimary (citable) accession number: P51953
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 75 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3