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P51946

- CCNH_HUMAN

UniProt

P51946 - CCNH_HUMAN

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Protein

Cyclin-H

Gene

CCNH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP51946.
CleanExiHS_CCNH.
ExpressionAtlasiP51946. baseline and differential.
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. 44 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 – 3621Combined sources
Beta strandi38 – 403Combined sources
Helixi50 – 7021Combined sources
Turni72 – 743Combined sources
Helixi77 – 9014Combined sources
Helixi91 – 933Combined sources
Turni96 – 983Combined sources
Helixi101 – 11515Combined sources
Helixi122 – 1254Combined sources
Helixi126 – 1283Combined sources
Beta strandi129 – 1313Combined sources
Helixi133 – 15321Combined sources
Turni154 – 1563Combined sources
Helixi164 – 17714Combined sources
Helixi179 – 1824Combined sources
Helixi184 – 19815Combined sources
Turni200 – 2023Combined sources
Helixi203 – 2064Combined sources
Helixi209 – 22416Combined sources
Helixi231 – 2355Combined sources
Beta strandi240 – 2423Combined sources
Helixi246 – 26015Combined sources
Helixi267 – 28216Combined sources

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.
GeneTreeiENSGT00390000008634.
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 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MYHNSSQKRH WTFSSEEQLA RLRADANRKF RCKAVANGKV LPNDPVFLEP
60 70 80 90 100
HEEMTLCKYY EKRLLEFCSV FKPAMPRSVV GTACMYFKRF YLNNSVMEYH
110 120 130 140 150
PRIIMLTCAF LACKVDEFNV SSPQFVGNLR ESPLGQEKAL EQILEYELLL
160 170 180 190 200
IQQLNFHLIV HNPYRPFEGF LIDLKTRYPI LENPEILRKT ADDFLNRIAL
210 220 230 240 250
TDAYLLYTPS QIALTAILSS ASRAGITMES YLSESLMLKE NRTCLSQLLD
260 270 280 290 300
IMKSMRNLVK KYEPPRSEEV AVLKQKLERC HSAELALNVI TKKRKGYEDD
310 320
DYVSKKSKHE EEEWTDDDLV ESL
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. 44 interactions.
DIPi DIP-5996N.
IntActi P51946. 16 interactions.
MINTi MINT-1434271.
STRINGi 9606.ENSP00000256897.

Chemistry

BindingDBi P51946.
ChEMBLi CHEMBL2111288.

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.
GeneTreei ENSGT00390000008634.
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

Bgeei P51946.
CleanExi HS_CCNH.
ExpressionAtlasi P51946. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 160 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