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Protein

Cyclin-H

Gene

CCNH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Cyclin

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciZFISH:ENSG00000134480-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167160. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-69202. Cyclin E associated events during G1/S transition.
R-HSA-69231. Cyclin D associated events in G1.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
R-HSA-69656. Cyclin A:Cdk2-associated events at S phase entry.
R-HSA-72086. mRNA Capping.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
R-HSA-73772. RNA Polymerase I Promoter Escape.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-73863. RNA Polymerase I Transcription Termination.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-HSA-77075. RNA Pol II CTD phosphorylation and interaction with CE.
SignaLinkiP51946.
SIGNORiP51946.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:1594. CCNH.

Subcellular locationi

GO - Cellular componenti

  • cyclin-dependent protein kinase activating kinase holoenzyme complex Source: UniProtKB
  • holo TFIIH complex Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: ProtInc
  • TFIIK complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi5S → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication1
Mutagenesisi304S → A: No effect on the transcriptional activity of the reconstituted TFIIH complex. 1 Publication1

Organism-specific databases

DisGeNETi902.
OpenTargetsiENSG00000134480.
PharmGKBiPA26159.

Chemistry databases

ChEMBLiCHEMBL2111288.

Polymorphism and mutation databases

BioMutaiCCNH.
DMDMi1706232.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000804711 – 323Cyclin-HAdd BLAST323

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei5Phosphoserine; by CDK81 Publication1
Modified residuei132PhosphoserineCombined sources1
Modified residuei304Phosphoserine; by CDK81 Publication1
Modified residuei315PhosphothreonineCombined sources1
Modified residuei322PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP51946.
MaxQBiP51946.
PaxDbiP51946.
PeptideAtlasiP51946.
PRIDEiP51946.

PTM databases

iPTMnetiP51946.
PhosphoSitePlusiP51946.

Expressioni

Gene expression databases

BgeeiENSG00000134480.
CleanExiHS_CCNH.
ExpressionAtlasiP51946. baseline and differential.
GenevisibleiP51946. HS.

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
CALCOCO2Q131373EBI-741406,EBI-739580
CCDC170Q8IYT33EBI-741406,EBI-2808089
CDK2P249413EBI-741406,EBI-375096
CTBP2P565455EBI-741406,EBI-741533
DUSP12Q9UNI63EBI-741406,EBI-715161
GOLGA2Q083795EBI-741406,EBI-618309
KLC3Q6P5973EBI-741406,EBI-1643885
NDC80O147773EBI-741406,EBI-715849
PPFIA1Q131363EBI-741406,EBI-745426
PSMA1P257864EBI-741406,EBI-359352
SFNP319473EBI-741406,EBI-476295
SSSCA1O602324EBI-741406,EBI-741415
SSX2IPQ9Y2D84EBI-741406,EBI-2212028

Protein-protein interaction databases

BioGridi107342. 53 interactors.
DIPiDIP-5996N.
IntActiP51946. 29 interactors.
MINTiMINT-1434271.
STRINGi9606.ENSP00000256897.

Chemistry databases

BindingDBiP51946.

Structurei

Secondary structure

1323
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi16 – 36Combined sources21
Beta strandi38 – 40Combined sources3
Helixi50 – 70Combined sources21
Turni72 – 74Combined sources3
Helixi77 – 90Combined sources14
Helixi91 – 93Combined sources3
Turni96 – 98Combined sources3
Helixi101 – 115Combined sources15
Helixi122 – 125Combined sources4
Helixi126 – 128Combined sources3
Beta strandi129 – 131Combined sources3
Helixi133 – 153Combined sources21
Turni154 – 156Combined sources3
Helixi164 – 177Combined sources14
Helixi179 – 182Combined sources4
Helixi184 – 198Combined sources15
Turni200 – 202Combined sources3
Helixi203 – 206Combined sources4
Helixi209 – 224Combined sources16
Helixi231 – 235Combined sources5
Beta strandi240 – 242Combined sources3
Helixi246 – 260Combined sources15
Helixi267 – 282Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JKWX-ray2.60A1-323[»]
1KXUX-ray2.60A1-323[»]
DisProtiDP00307.
ProteinModelPortaliP51946.
SMRiP51946.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51946.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi310 – 313Poly-Glu4

Sequence similaritiesi

Belongs to the cyclin family. Cyclin C subfamily.Curated

Phylogenomic databases

eggNOGiKOG2496. Eukaryota.
COG5333. LUCA.
GeneTreeiENSGT00390000008634.
HOGENOMiHOG000232149.
HOVERGENiHBG050840.
InParanoidiP51946.
KOiK06634.
OMAiRKFKCKV.
OrthoDBiEOG091G0CEG.
PhylomeDBiP51946.
TreeFamiTF101008.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR031658. Cyclin_C_2.
IPR006671. Cyclin_N.
IPR027081. CyclinH/Ccl1.
[Graphical view]
PfamiPF16899. Cyclin_C_2. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
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

        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)DescriptionActionsGraphical viewLength
Natural variantiVAR_01306728R → L.1 PublicationCorresponds to variant rs2234942dbSNPEnsembl.1
Natural variantiVAR_01306854M → V.1 PublicationCorresponds to variant rs3093785dbSNPEnsembl.1
Natural variantiVAR_013069138K → R.1 PublicationCorresponds to variant rs2266691dbSNPEnsembl.1
Natural variantiVAR_013070270V → A.3 PublicationsCorresponds to variant rs2230641dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
UCSCiuc003kjb.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JKWX-ray2.60A1-323[»]
1KXUX-ray2.60A1-323[»]
DisProtiDP00307.
ProteinModelPortaliP51946.
SMRiP51946.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107342. 53 interactors.
DIPiDIP-5996N.
IntActiP51946. 29 interactors.
MINTiMINT-1434271.
STRINGi9606.ENSP00000256897.

Chemistry databases

BindingDBiP51946.
ChEMBLiCHEMBL2111288.

PTM databases

iPTMnetiP51946.
PhosphoSitePlusiP51946.

Polymorphism and mutation databases

BioMutaiCCNH.
DMDMi1706232.

Proteomic databases

EPDiP51946.
MaxQBiP51946.
PaxDbiP51946.
PeptideAtlasiP51946.
PRIDEiP51946.

Protocols and materials databases

DNASUi902.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000256897; ENSP00000256897; ENSG00000134480.
GeneIDi902.
KEGGihsa:902.
UCSCiuc003kjb.4. human.

Organism-specific databases

CTDi902.
DisGeNETi902.
GeneCardsiCCNH.
HGNCiHGNC:1594. CCNH.
HPAiCAB019416.
HPA044138.
MIMi601953. gene.
neXtProtiNX_P51946.
OpenTargetsiENSG00000134480.
PharmGKBiPA26159.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2496. Eukaryota.
COG5333. LUCA.
GeneTreeiENSGT00390000008634.
HOGENOMiHOG000232149.
HOVERGENiHBG050840.
InParanoidiP51946.
KOiK06634.
OMAiRKFKCKV.
OrthoDBiEOG091G0CEG.
PhylomeDBiP51946.
TreeFamiTF101008.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000134480-MONOMER.
ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167160. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-6796648. TP53 Regulates Transcription of DNA Repair Genes.
R-HSA-69202. Cyclin E associated events during G1/S transition.
R-HSA-69231. Cyclin D associated events in G1.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
R-HSA-69656. Cyclin A:Cdk2-associated events at S phase entry.
R-HSA-72086. mRNA Capping.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
R-HSA-73772. RNA Polymerase I Promoter Escape.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-73863. RNA Polymerase I Transcription Termination.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-HSA-77075. RNA Pol II CTD phosphorylation and interaction with CE.
SignaLinkiP51946.
SIGNORiP51946.

Miscellaneous databases

ChiTaRSiCCNH. human.
EvolutionaryTraceiP51946.
GeneWikiiCyclin_H.
GenomeRNAii902.
PROiP51946.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000134480.
CleanExiHS_CCNH.
ExpressionAtlasiP51946. baseline and differential.
GenevisibleiP51946. HS.

Family and domain databases

Gene3Di1.10.472.10. 2 hits.
InterProiIPR013763. Cyclin-like.
IPR031658. Cyclin_C_2.
IPR006671. Cyclin_N.
IPR027081. CyclinH/Ccl1.
[Graphical view]
PfamiPF16899. Cyclin_C_2. 1 hit.
PF00134. Cyclin_N. 1 hit.
[Graphical view]
SMARTiSM00385. CYCLIN. 1 hit.
[Graphical view]
SUPFAMiSSF47954. SSF47954. 2 hits.
TIGRFAMsiTIGR00569. ccl1. 1 hit.
ProtoNetiSearch...

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: November 30, 2016
This is version 181 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.