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Protein

CDK-activating kinase assembly factor MAT1

Gene

MNAT1

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

Functioni

Stabilizes the cyclin H-CDK7 complex to form a functional 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.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri6 – 50RING-typePROSITE-ProRule annotationAdd BLAST45

GO - Molecular functioni

  • protein N-terminus binding Source: UniProtKB
  • zinc ion binding Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000020426-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.
SignaLinkiP51948.

Names & Taxonomyi

Protein namesi
Recommended name:
CDK-activating kinase assembly factor MAT1
Alternative name(s):
CDK7/cyclin-H assembly factor
Cyclin-G1-interacting protein
Menage a trois
RING finger protein 66
RING finger protein MAT1
p35
p36
Gene namesi
Name:MNAT1
Synonyms:CAP35, MAT1, RNF66
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:7181. MNAT1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • holo TFIIH complex Source: UniProtKB
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi4331.
OpenTargetsiENSG00000020426.
PharmGKBiPA30894.

Chemistry databases

ChEMBLiCHEMBL3038473.

Polymorphism and mutation databases

BioMutaiMNAT1.
DMDMi1708932.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000559321 – 309CDK-activating kinase assembly factor MAT1Add BLAST309

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei51PhosphothreonineCombined sources1
Modified residuei279PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP51948.
MaxQBiP51948.
PaxDbiP51948.
PeptideAtlasiP51948.
PRIDEiP51948.

PTM databases

iPTMnetiP51948.
PhosphoSitePlusiP51948.

Expressioni

Tissue specificityi

Highest levels in colon and testis. Moderate levels are present thymus, prostate, ovary, and small intestine. The lowest levels are found in spleen and leukocytes.

Gene expression databases

BgeeiENSG00000020426.
CleanExiHS_MNAT1.
ExpressionAtlasiP51948. baseline and differential.
GenevisibleiP51948. HS.

Organism-specific databases

HPAiCAB004495.
HPA000701.
HPA001154.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • protein N-terminus binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110474. 59 interactors.
IntActiP51948. 33 interactors.
MINTiMINT-255129.
STRINGi9606.ENSP00000261245.

Chemistry databases

BindingDBiP51948.

Structurei

Secondary structure

1309
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni8 – 11Combined sources4
Helixi12 – 15Combined sources4
Beta strandi21 – 23Combined sources3
Helixi32 – 40Combined sources9
Beta strandi43 – 45Combined sources3
Turni47 – 49Combined sources3
Beta strandi59 – 61Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G25NMR-A1-65[»]
ProteinModelPortaliP51948.
SMRiP51948.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51948.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini142 – 161UIMPROSITE-ProRule annotationAdd BLAST20

Sequence similaritiesi

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
Contains 1 UIM (ubiquitin-interacting motif) domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri6 – 50RING-typePROSITE-ProRule annotationAdd BLAST45

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG3800. Eukaryota.
COG5220. LUCA.
GeneTreeiENSGT00390000002319.
HOGENOMiHOG000189680.
HOVERGENiHBG001144.
InParanoidiP51948.
KOiK10842.
OMAiPMVEKEV.
OrthoDBiEOG091G0D6M.
PhylomeDBiP51948.
TreeFamiTF106124.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR015877. Cdk-activating_kinase_MAT1_cen.
IPR004575. MAT1/Tfb3.
IPR003903. UIM_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR12683. PTHR12683. 1 hit.
PfamiPF06391. MAT1. 1 hit.
PF17121. zf-C3HC4_5. 1 hit.
[Graphical view]
PIRSFiPIRSF003338. MAT1_metazoa. 1 hit.
SMARTiSM00184. RING. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00570. cdk7. 1 hit.
PROSITEiPS50330. UIM. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P51948-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDDQGCPRCK TTKYRNPSLK LMVNVCGHTL CESCVDLLFV RGAGNCPECG
60 70 80 90 100
TPLRKSNFRV QLFEDPTVDK EVEIRKKVLK IYNKREEDFP SLREYNDFLE
110 120 130 140 150
EVEEIVFNLT NNVDLDNTKK KMEIYQKENK DVIQKNKLKL TREQEELEEA
160 170 180 190 200
LEVERQENEQ RRLFIQKEEQ LQQILKRKNK QAFLDELESS DLPVALLLAQ
210 220 230 240 250
HKDRSTQLEM QLEKPKPVKP VTFSTGIKMG QHISLAPIHK LEEALYEYQP
260 270 280 290 300
LQIETYGPHV PELEMLGRLG YLNHVRAASP QDLAGGYTSS LACHRALQDA

FSGLFWQPS
Length:309
Mass (Da):35,823
Last modified:October 1, 1996 - v1
Checksum:i6818DDE230E81A97
GO
Isoform 2 (identifier: P51948-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     188-229: Missing.

Show »
Length:267
Mass (Da):31,148
Checksum:i078565DB8EA02B92
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti247 – 248EY → DN in AAB05248 (Ref. 3) Curated2

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_052084282D → A.Corresponds to variant rs35188899dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_046772188 – 229Missing in isoform 2. 1 PublicationAdd BLAST42

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87843 mRNA. Translation: CAA61112.1.
X92669 mRNA. Translation: CAA63356.1.
U61835 mRNA. Translation: AAB05248.1.
AY165512 Genomic DNA. Translation: AAN47195.1.
AL132777 Genomic DNA. No translation available.
AL160236 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80788.1.
CR450336 mRNA. Translation: CAG29332.1.
CH471061 Genomic DNA. Translation: EAW80787.1.
BC000820 mRNA. Translation: AAH00820.1.
CCDSiCCDS53899.1. [P51948-2]
CCDS9750.1. [P51948-1]
PIRiG02764.
S60157.
RefSeqiNP_001171434.1. NM_001177963.1. [P51948-2]
NP_002422.1. NM_002431.3. [P51948-1]
XP_005267744.1. XM_005267687.2. [P51948-1]
UniGeneiHs.509523.

Genome annotation databases

EnsembliENST00000261245; ENSP00000261245; ENSG00000020426. [P51948-1]
ENST00000539616; ENSP00000446437; ENSG00000020426. [P51948-2]
GeneIDi4331.
KEGGihsa:4331.
UCSCiuc001xfd.4. human. [P51948-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X87843 mRNA. Translation: CAA61112.1.
X92669 mRNA. Translation: CAA63356.1.
U61835 mRNA. Translation: AAB05248.1.
AY165512 Genomic DNA. Translation: AAN47195.1.
AL132777 Genomic DNA. No translation available.
AL160236 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80788.1.
CR450336 mRNA. Translation: CAG29332.1.
CH471061 Genomic DNA. Translation: EAW80787.1.
BC000820 mRNA. Translation: AAH00820.1.
CCDSiCCDS53899.1. [P51948-2]
CCDS9750.1. [P51948-1]
PIRiG02764.
S60157.
RefSeqiNP_001171434.1. NM_001177963.1. [P51948-2]
NP_002422.1. NM_002431.3. [P51948-1]
XP_005267744.1. XM_005267687.2. [P51948-1]
UniGeneiHs.509523.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1G25NMR-A1-65[»]
ProteinModelPortaliP51948.
SMRiP51948.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110474. 59 interactors.
IntActiP51948. 33 interactors.
MINTiMINT-255129.
STRINGi9606.ENSP00000261245.

Chemistry databases

BindingDBiP51948.
ChEMBLiCHEMBL3038473.

PTM databases

iPTMnetiP51948.
PhosphoSitePlusiP51948.

Polymorphism and mutation databases

BioMutaiMNAT1.
DMDMi1708932.

Proteomic databases

EPDiP51948.
MaxQBiP51948.
PaxDbiP51948.
PeptideAtlasiP51948.
PRIDEiP51948.

Protocols and materials databases

DNASUi4331.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261245; ENSP00000261245; ENSG00000020426. [P51948-1]
ENST00000539616; ENSP00000446437; ENSG00000020426. [P51948-2]
GeneIDi4331.
KEGGihsa:4331.
UCSCiuc001xfd.4. human. [P51948-1]

Organism-specific databases

CTDi4331.
DisGeNETi4331.
GeneCardsiMNAT1.
HGNCiHGNC:7181. MNAT1.
HPAiCAB004495.
HPA000701.
HPA001154.
MIMi602659. gene.
neXtProtiNX_P51948.
OpenTargetsiENSG00000020426.
PharmGKBiPA30894.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3800. Eukaryota.
COG5220. LUCA.
GeneTreeiENSGT00390000002319.
HOGENOMiHOG000189680.
HOVERGENiHBG001144.
InParanoidiP51948.
KOiK10842.
OMAiPMVEKEV.
OrthoDBiEOG091G0D6M.
PhylomeDBiP51948.
TreeFamiTF106124.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000020426-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.
SignaLinkiP51948.

Miscellaneous databases

ChiTaRSiMNAT1. human.
EvolutionaryTraceiP51948.
GeneWikiiMNAT1.
GenomeRNAii4331.
PROiP51948.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000020426.
CleanExiHS_MNAT1.
ExpressionAtlasiP51948. baseline and differential.
GenevisibleiP51948. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR015877. Cdk-activating_kinase_MAT1_cen.
IPR004575. MAT1/Tfb3.
IPR003903. UIM_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR12683. PTHR12683. 1 hit.
PfamiPF06391. MAT1. 1 hit.
PF17121. zf-C3HC4_5. 1 hit.
[Graphical view]
PIRSFiPIRSF003338. MAT1_metazoa. 1 hit.
SMARTiSM00184. RING. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00570. cdk7. 1 hit.
PROSITEiPS50330. UIM. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMAT1_HUMAN
AccessioniPrimary (citable) accession number: P51948
Secondary accession number(s): G3V1U8, Q15817, Q6ICQ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 178 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 14
    Human chromosome 14: 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.