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P51948 (MAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:MNAT1
Synonyms:CAP35, MAT1, RNF66
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10

Subunit structure

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. Ref.9

Subcellular location

Nucleus.

Tissue specificity

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.

Sequence similarities

Contains 1 RING-type zinc finger.

Contains 1 UIM (ubiquitin-interacting motif) repeat.

Ontologies

Keywords
   Biological processCell cycle
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandMetal-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine mRNA capping

Traceable author statement. Source: Reactome

ATP catabolic process

Inferred from direct assay Ref.9. Source: GOC

DNA repair

Traceable author statement. Source: Reactome

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

G2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

adult heart development

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Traceable author statement Ref.1. Source: ProtInc

gene expression

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

nucleotide-excision repair

Traceable author statement. Source: Reactome

nucleotide-excision repair, DNA damage removal

Traceable author statement. Source: Reactome

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 8692841. Source: UniProtKB

positive regulation of viral transcription

Traceable author statement. Source: Reactome

protein complex assembly

Traceable author statement Ref.1. Source: ProtInc

protein phosphorylation

Inferred from direct assay Ref.9. Source: GOC

regulation of cyclin-dependent protein serine/threonine kinase activity

Traceable author statement Ref.1. Source: ProtInc

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 10801852. Source: UniProtKB

response to calcium ion

Inferred from electronic annotation. Source: Ensembl

termination of RNA polymerase I transcription

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.9. Source: UniProtKB

transcription initiation from RNA polymerase I promoter

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription-coupled nucleotide-excision repair

Traceable author statement. Source: Reactome

ventricular system development

Inferred from electronic annotation. Source: Ensembl

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

holo TFIIH complex

Inferred from direct assay Ref.9. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionprotein N-terminus binding

Inferred from physical interaction PubMed 11445587. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 10801852PubMed 8692842. Source: UniProtKB

zinc ion binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P51948-1)

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.
Isoform 2 (identifier: P51948-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309CDK-activating kinase assembly factor MAT1
PRO_0000055932

Regions

Repeat142 – 16120UIM
Zinc finger6 – 5045RING-type

Amino acid modifications

Modified residue11N-acetylmethionine Ref.12
Modified residue511Phosphothreonine Ref.11
Modified residue2791Phosphoserine Ref.11 Ref.13

Natural variations

Alternative sequence188 – 22942Missing in isoform 2.
VSP_046772
Natural variant2821D → A.
Corresponds to variant rs35188899 [ dbSNP | Ensembl ].
VAR_052084

Experimental info

Sequence conflict247 – 2482EY → DN in AAB05248. Ref.3

Secondary structure

.............. 309
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 6818DDE230E81A97

FASTA30935,823
        10         20         30         40         50         60 
MDDQGCPRCK TTKYRNPSLK LMVNVCGHTL CESCVDLLFV RGAGNCPECG TPLRKSNFRV 

        70         80         90        100        110        120 
QLFEDPTVDK EVEIRKKVLK IYNKREEDFP SLREYNDFLE EVEEIVFNLT NNVDLDNTKK 

       130        140        150        160        170        180 
KMEIYQKENK DVIQKNKLKL TREQEELEEA LEVERQENEQ RRLFIQKEEQ LQQILKRKNK 

       190        200        210        220        230        240 
QAFLDELESS DLPVALLLAQ HKDRSTQLEM QLEKPKPVKP VTFSTGIKMG QHISLAPIHK 

       250        260        270        280        290        300 
LEEALYEYQP LQIETYGPHV PELEMLGRLG YLNHVRAASP QDLAGGYTSS LACHRALQDA 


FSGLFWQPS 

« Hide

Isoform 2 [UniParc].

Checksum: 078565DB8EA02B92
Show »

FASTA26731,148

References

« Hide 'large scale' references
[1]"In vitro assembly of a functional human CDK7-cyclin H complex requires MAT1, a novel 36 kDa RING finger protein."
Tassan J.-P., Jaquenoud M., Fry A.M., Frutiger S., Hughes G.J., Nigg E.A.
EMBO J. 14:5608-5617(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 23-48 AND 123-147.
Tissue: Placenta.
[2]"Molecular cloning of CDK7-associated human MAT1, a cyclin-dependent kinase-activating kinase (CAK) assembly factor."
Yee A., Nichols M., Wu L., Hall F.L., Kobayashi R., Xiong Y.
Cancer Res. 55:6058-6062(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Cervix carcinoma.
[3]Xu F., Hall F.L., Starnes V., Wu L.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[4]NIEHS SNPs program
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[5]"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] (ISOFORM 1).
[6]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] (ISOFORM 1).
Tissue: Placenta.
[9]"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.
[10]"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.
[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 THR-51 AND SER-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Solution structure of the N-terminal domain of the human TFIIH MAT1 subunit: new insights into the RING finger family."
Gervais V., Busso D., Wasielewski E., Poterszman A., Egly J.-M., Thierry J.-C., Kieffer B.
J. Biol. Chem. 276:7457-7464(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-65.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS53899.1. [P51948-2]
CCDS9750.1. [P51948-1]
PIRG02764.
S60157.
RefSeqNP_001171434.1. NM_001177963.1. [P51948-2]
NP_002422.1. NM_002431.3. [P51948-1]
XP_005267744.1. XM_005267687.1. [P51948-1]
UniGeneHs.509523.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G25NMR-A1-65[»]
ProteinModelPortalP51948.
SMRP51948. Positions 1-65.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110474. 54 interactions.
IntActP51948. 26 interactions.
MINTMINT-255129.
STRING9606.ENSP00000261245.

Chemistry

BindingDBP51948.
ChEMBLCHEMBL3038473.

PTM databases

PhosphoSiteP51948.

Polymorphism databases

DMDM1708932.

Proteomic databases

MaxQBP51948.
PaxDbP51948.
PRIDEP51948.

Protocols and materials databases

DNASU4331.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261245; ENSP00000261245; ENSG00000020426. [P51948-1]
ENST00000539616; ENSP00000446437; ENSG00000020426. [P51948-2]
GeneID4331.
KEGGhsa:4331.
UCSCuc001xfd.3. human. [P51948-1]
uc001xfe.3. human.

Organism-specific databases

CTD4331.
GeneCardsGC14P061201.
HGNCHGNC:7181. MNAT1.
HPACAB004495.
HPA000701.
HPA001154.
MIM602659. gene.
neXtProtNX_P51948.
PharmGKBPA30894.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5220.
HOGENOMHOG000189680.
HOVERGENHBG001144.
InParanoidP51948.
KOK10842.
OMAETCGPQV.
OrthoDBEOG71VST2.
PhylomeDBP51948.
TreeFamTF106124.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_1788. Transcription.
REACT_216. DNA Repair.
REACT_71. Gene Expression.
SignaLinkP51948.

Gene expression databases

ArrayExpressP51948.
BgeeP51948.
CleanExHS_MNAT1.
GenevestigatorP51948.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR015877. Cdk-activating_kinase_MAT1_cen.
IPR004575. MAT1/Tfb3.
IPR003903. Ubiquitin-int_motif.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERPTHR12683. PTHR12683. 1 hit.
PfamPF06391. MAT1. 1 hit.
[Graphical view]
PIRSFPIRSF003338. MAT1_metazoa. 1 hit.
SMARTSM00184. RING. 1 hit.
[Graphical view]
TIGRFAMsTIGR00570. cdk7. 1 hit.
PROSITEPS50330. UIM. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP51948.
GeneWikiMNAT1.
GenomeRNAi4331.
NextBio17043.
PROP51948.
SOURCESearch...

Entry information

Entry nameMAT1_HUMAN
AccessionPrimary (citable) accession number: P51948
Secondary accession number(s): G3V1U8, Q15817, Q6ICQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM