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P51946

- CCNH_HUMAN

UniProt

P51946 - CCNH_HUMAN

Protein

Cyclin-H

Gene

CCNH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Regulates CDK7, the catalytic subunit of the CDK-activating kinase (CAK) enzymatic complex. CAK activates the cyclin-associated kinases CDK1, CDK2, CDK4 and CDK6 by threonine phosphorylation. 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. Involved in cell cycle control and in RNA transcription by RNA polymerase II. Its expression and activity are constant throughout the cell cycle.2 Publications

    GO - Molecular functioni

    1. cyclin-dependent protein serine/threonine kinase regulator activity Source: InterPro
    2. kinase activity Source: Ensembl
    3. protein binding Source: IntAct

    GO - Biological processi

    1. 7-methylguanosine mRNA capping Source: Reactome
    2. ATP catabolic process Source: GOC
    3. DNA repair Source: Reactome
    4. G1/S transition of mitotic cell cycle Source: Reactome
    5. G2/M transition of mitotic cell cycle Source: Reactome
    6. gene expression Source: Reactome
    7. mitotic cell cycle Source: Reactome
    8. nucleotide-excision repair Source: Reactome
    9. nucleotide-excision repair, DNA damage removal Source: Reactome
    10. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    11. positive regulation of viral transcription Source: Reactome
    12. protein phosphorylation Source: GOC
    13. regulation of cyclin-dependent protein serine/threonine kinase activity Source: InterPro
    14. termination of RNA polymerase I transcription Source: Reactome
    15. transcription-coupled nucleotide-excision repair Source: Reactome
    16. transcription elongation from RNA polymerase II promoter Source: Reactome
    17. transcription elongation from RNA polymerase I promoter Source: Reactome
    18. transcription from RNA polymerase II promoter Source: UniProtKB
    19. transcription from RNA polymerase I promoter Source: Reactome
    20. transcription initiation from RNA polymerase II promoter Source: Reactome
    21. transcription initiation from RNA polymerase I promoter Source: Reactome
    22. viral process Source: Reactome

    Keywords - Molecular functioni

    Cyclin

    Keywords - Biological processi

    Cell cycle, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_1074. RNA Polymerase I Transcription Termination.
    REACT_1470. mRNA Capping.
    REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_1913. RNA Polymerase I Promoter Escape.
    REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_200856. NoRC negatively regulates rRNA expression.
    REACT_2089. RNA Polymerase II Promoter Escape.
    REACT_2204. RNA Polymerase I Chain Elongation.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_2222. Dual incision reaction in TC-NER.
    REACT_257. Formation of incision complex in GG-NER.
    REACT_311. Dual incision reaction in GG-NER.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6233. Transcription of the HIV genome.
    REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6319. Formation of the HIV-1 Early Elongation Complex.
    REACT_6332. HIV Transcription Initiation.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_821. Cyclin D associated events in G1.
    REACT_833. RNA Polymerase II Transcription Elongation.
    REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
    REACT_846. Formation of the Early Elongation Complex.
    REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
    REACT_953. RNA Polymerase I Transcription Initiation.
    REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.
    SignaLinkiP51946.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cyclin-H
    Alternative name(s):
    MO15-associated protein
    p34
    p37
    Gene namesi
    Name:CCNH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:1594. CCNH.

    Subcellular locationi

    GO - Cellular componenti

    1. cyclin-dependent protein kinase activating kinase holoenzyme complex Source: UniProtKB
    2. holo TFIIH complex Source: UniProtKB
    3. nucleoplasm Source: Reactome
    4. nucleus Source: HPA
    5. TFIIK complex Source: InterPro

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi5 – 51S → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication
    Mutagenesisi304 – 3041S → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication

    Organism-specific databases

    PharmGKBiPA26159.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 323323Cyclin-HPRO_0000080471Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei5 – 51Phosphoserine; by CDK81 Publication
    Modified residuei132 – 1321Phosphoserine1 Publication
    Modified residuei304 – 3041Phosphoserine; by CDK81 Publication
    Modified residuei315 – 3151Phosphothreonine6 Publications
    Modified residuei322 – 3221Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP51946.
    PaxDbiP51946.
    PeptideAtlasiP51946.
    PRIDEiP51946.

    PTM databases

    PhosphoSiteiP51946.

    Expressioni

    Gene expression databases

    ArrayExpressiP51946.
    BgeeiP51946.
    CleanExiHS_CCNH.
    GenevestigatoriP51946.

    Organism-specific databases

    HPAiCAB019416.
    HPA044138.

    Interactioni

    Subunit structurei

    Associates primarily with CDK7 and MAT1 to form the CAK complex. CAK can further associate with the core-TFIIH to form the TFIIH basal transcription factor.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CDK2P249412EBI-741406,EBI-375096
    CTBP2P565455EBI-741406,EBI-741533

    Protein-protein interaction databases

    BioGridi107342. 41 interactions.
    DIPiDIP-5996N.
    IntActiP51946. 16 interactions.
    MINTiMINT-1434271.
    STRINGi9606.ENSP00000256897.

    Structurei

    Secondary structure

    1
    323
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi16 – 3621
    Beta strandi38 – 403
    Helixi50 – 7021
    Turni72 – 743
    Helixi77 – 9014
    Helixi91 – 933
    Turni96 – 983
    Helixi101 – 11515
    Helixi122 – 1254
    Helixi126 – 1283
    Beta strandi129 – 1313
    Helixi133 – 15321
    Turni154 – 1563
    Helixi164 – 17714
    Helixi179 – 1824
    Helixi184 – 19815
    Turni200 – 2023
    Helixi203 – 2064
    Helixi209 – 22416
    Helixi231 – 2355
    Beta strandi240 – 2423
    Helixi246 – 26015
    Helixi267 – 28216

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JKWX-ray2.60A1-323[»]
    1KXUX-ray2.60A1-323[»]
    DisProtiDP00307.
    ProteinModelPortaliP51946.
    SMRiP51946. Positions 11-286.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51946.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi310 – 3134Poly-Glu

    Sequence similaritiesi

    Belongs to the cyclin family. Cyclin C subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG5333.
    HOGENOMiHOG000232149.
    HOVERGENiHBG050840.
    InParanoidiP51946.
    KOiK06634.
    OMAiAFHYFKR.
    PhylomeDBiP51946.
    TreeFamiTF101008.

    Family and domain databases

    Gene3Di1.10.472.10. 2 hits.
    InterProiIPR013763. Cyclin-like.
    IPR015429. Cyclin_C/H/T/L.
    IPR006671. Cyclin_N.
    IPR023598. CyclinC.
    IPR027081. CyclinH/Ccl1.
    [Graphical view]
    PANTHERiPTHR10026. PTHR10026. 1 hit.
    PfamiPF00134. Cyclin_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF028758. PIRSF028758. 1 hit.
    SMARTiSM00385. CYCLIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF47954. SSF47954. 2 hits.
    TIGRFAMsiTIGR00569. ccl1. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P51946-1 [UniParc]FASTAAdd to Basket

    « Hide

    MYHNSSQKRH WTFSSEEQLA RLRADANRKF RCKAVANGKV LPNDPVFLEP    50
    HEEMTLCKYY EKRLLEFCSV FKPAMPRSVV GTACMYFKRF YLNNSVMEYH 100
    PRIIMLTCAF LACKVDEFNV SSPQFVGNLR ESPLGQEKAL EQILEYELLL 150
    IQQLNFHLIV HNPYRPFEGF LIDLKTRYPI LENPEILRKT ADDFLNRIAL 200
    TDAYLLYTPS QIALTAILSS ASRAGITMES YLSESLMLKE NRTCLSQLLD 250
    IMKSMRNLVK KYEPPRSEEV AVLKQKLERC HSAELALNVI TKKRKGYEDD 300
    DYVSKKSKHE EEEWTDDDLV ESL 323
    Length:323
    Mass (Da):37,643
    Last modified:October 1, 1996 - v1
    Checksum:iBB48D55DA397A0E4
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti28 – 281R → L.1 Publication
    Corresponds to variant rs2234942 [ dbSNP | Ensembl ].
    VAR_013067
    Natural varianti54 – 541M → V.1 Publication
    Corresponds to variant rs3093785 [ dbSNP | Ensembl ].
    VAR_013068
    Natural varianti138 – 1381K → R.1 Publication
    Corresponds to variant rs2266691 [ dbSNP | Ensembl ].
    VAR_013069
    Natural varianti270 – 2701V → A.3 Publications
    Corresponds to variant rs2230641 [ dbSNP | Ensembl ].
    VAR_013070

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U11791 mRNA. Translation: AAA21361.1.
    U12685 mRNA. Translation: AAA57006.1.
    CR407658 mRNA. Translation: CAG28586.1.
    AF477979 Genomic DNA. Translation: AAL74271.1.
    BC005280 mRNA. Translation: AAH05280.1.
    BC016705 mRNA. Translation: AAH16705.1.
    BC016823 mRNA. Translation: AAH16823.1.
    BC022351 mRNA. Translation: AAH22351.1.
    CCDSiCCDS4064.1.
    PIRiI38731.
    RefSeqiNP_001230.1. NM_001239.3.
    UniGeneiHs.292524.

    Genome annotation databases

    EnsembliENST00000256897; ENSP00000256897; ENSG00000134480.
    GeneIDi902.
    KEGGihsa:902.
    UCSCiuc003kja.3. human.

    Polymorphism databases

    DMDMi1706232.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U11791 mRNA. Translation: AAA21361.1 .
    U12685 mRNA. Translation: AAA57006.1 .
    CR407658 mRNA. Translation: CAG28586.1 .
    AF477979 Genomic DNA. Translation: AAL74271.1 .
    BC005280 mRNA. Translation: AAH05280.1 .
    BC016705 mRNA. Translation: AAH16705.1 .
    BC016823 mRNA. Translation: AAH16823.1 .
    BC022351 mRNA. Translation: AAH22351.1 .
    CCDSi CCDS4064.1.
    PIRi I38731.
    RefSeqi NP_001230.1. NM_001239.3.
    UniGenei Hs.292524.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JKW X-ray 2.60 A 1-323 [» ]
    1KXU X-ray 2.60 A 1-323 [» ]
    DisProti DP00307.
    ProteinModelPortali P51946.
    SMRi P51946. Positions 11-286.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107342. 41 interactions.
    DIPi DIP-5996N.
    IntActi P51946. 16 interactions.
    MINTi MINT-1434271.
    STRINGi 9606.ENSP00000256897.

    Chemistry

    BindingDBi P51946.
    ChEMBLi CHEMBL3038473.

    PTM databases

    PhosphoSitei P51946.

    Polymorphism databases

    DMDMi 1706232.

    Proteomic databases

    MaxQBi P51946.
    PaxDbi P51946.
    PeptideAtlasi P51946.
    PRIDEi P51946.

    Protocols and materials databases

    DNASUi 902.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000256897 ; ENSP00000256897 ; ENSG00000134480 .
    GeneIDi 902.
    KEGGi hsa:902.
    UCSCi uc003kja.3. human.

    Organism-specific databases

    CTDi 902.
    GeneCardsi GC05M086690.
    HGNCi HGNC:1594. CCNH.
    HPAi CAB019416.
    HPA044138.
    MIMi 601953. gene.
    neXtProti NX_P51946.
    PharmGKBi PA26159.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5333.
    HOGENOMi HOG000232149.
    HOVERGENi HBG050840.
    InParanoidi P51946.
    KOi K06634.
    OMAi AFHYFKR.
    PhylomeDBi P51946.
    TreeFami TF101008.

    Enzyme and pathway databases

    Reactomei REACT_1074. RNA Polymerase I Transcription Termination.
    REACT_1470. mRNA Capping.
    REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_1913. RNA Polymerase I Promoter Escape.
    REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_200856. NoRC negatively regulates rRNA expression.
    REACT_2089. RNA Polymerase II Promoter Escape.
    REACT_2204. RNA Polymerase I Chain Elongation.
    REACT_22107. RNA Polymerase II Pre-transcription Events.
    REACT_22201. Formation of HIV elongation complex in the absence of HIV Tat.
    REACT_2222. Dual incision reaction in TC-NER.
    REACT_257. Formation of incision complex in GG-NER.
    REACT_311. Dual incision reaction in GG-NER.
    REACT_6162. Tat-mediated elongation of the HIV-1 transcript.
    REACT_6233. Transcription of the HIV genome.
    REACT_6237. RNA Pol II CTD phosphorylation and interaction with CE.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6319. Formation of the HIV-1 Early Elongation Complex.
    REACT_6332. HIV Transcription Initiation.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_821. Cyclin D associated events in G1.
    REACT_833. RNA Polymerase II Transcription Elongation.
    REACT_834. RNA Polymerase II Transcription Initiation And Promoter Clearance.
    REACT_846. Formation of the Early Elongation Complex.
    REACT_9029. Cyclin A:Cdk2-associated events at S phase entry.
    REACT_953. RNA Polymerase I Transcription Initiation.
    REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.
    SignaLinki P51946.

    Miscellaneous databases

    ChiTaRSi CCNH. human.
    EvolutionaryTracei P51946.
    GeneWikii Cyclin_H.
    GenomeRNAii 902.
    NextBioi 3728.
    PROi P51946.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51946.
    Bgeei P51946.
    CleanExi HS_CCNH.
    Genevestigatori P51946.

    Family and domain databases

    Gene3Di 1.10.472.10. 2 hits.
    InterProi IPR013763. Cyclin-like.
    IPR015429. Cyclin_C/H/T/L.
    IPR006671. Cyclin_N.
    IPR023598. CyclinC.
    IPR027081. CyclinH/Ccl1.
    [Graphical view ]
    PANTHERi PTHR10026. PTHR10026. 1 hit.
    Pfami PF00134. Cyclin_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF028758. PIRSF028758. 1 hit.
    SMARTi SM00385. CYCLIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47954. SSF47954. 2 hits.
    TIGRFAMsi TIGR00569. ccl1. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-20; 106-133 AND 256-279.
      Tissue: Liver.
    2. "A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase."
      Fisher R.P., Morgan D.O.
      Cell 78:713-724(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 10-21; 90-102 AND 190-197.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-270.
    4. NIEHS SNPs program
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-28; VAL-54; ARG-138 AND ALA-270.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-270.
      Tissue: Bone marrow, Brain, Embryonic brain and Urinary bladder.
    6. "Cdk-activating kinase complex is a component of human transcription factor TFIIH."
      Shiekhattar R., Mermelstein F., Fisher R.P., Drapkin R., Dynlacht B., Wessling H.C., Morgan D.O., Reinberg D.
      Nature 374:283-287(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes."
      Kershnar E., Wu S.-Y., Chiang C.-M.
      J. Biol. Chem. 273:34444-34453(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE TFIIH BASAL TRANSCRIPTION FACTOR.
    8. "Reconstitution of the transcription factor TFIIH: assignment of functions for the three enzymatic subunits, XPB, XPD, and cdk7."
      Tirode F., Busso D., Coin F., Egly J.-M.
      Mol. Cell 3:87-95(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "TFIIH is negatively regulated by cdk8-containing mediator complexes."
      Akoulitchev S., Chuikov S., Reinberg D.
      Nature 407:102-106(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-5 AND SER-304, MUTAGENESIS OF SER-5 AND SER-304.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132; THR-315 AND SER-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315 AND SER-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Three-dimensional structure of human cyclin H, a positive regulator of the CDK-activating kinase."
      Kim K.K., Chamberlin H.M., Morgan D.O., Kim S.-H.
      Nat. Struct. Biol. 3:849-855(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
    19. "The structure of cyclin H: common mode of kinase activation and specific features."
      Andersen G., Busso D., Poterszman A., Hwang J.R., Wurtz J.-M., Ripp R., Thierry J.-C., Egly J.-M., Moras D.
      EMBO J. 16:958-967(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 11-287.

    Entry informationi

    Entry nameiCCNH_HUMAN
    AccessioniPrimary (citable) accession number: P51946
    Secondary accession number(s): Q53X72, Q8TBL9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 159 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3