P51948 (MAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	MNAT1
Synonyms:	CAP35, MAT1, RNF66

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	309 AA.
Sequence status	Complete.
Protein existence	Evidence 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-terminus 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.9
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.8
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 process	Cell cycle Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	7-methylguanosine mRNA capping Traceable author statement. Source: Reactome G1 phase of mitotic cell cycle 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 S phase of mitotic cell cycle Traceable author statement. Source: Reactome adult heart development Inferred from electronic annotation. Source: Compara apoptotic process Inferred from electronic annotation. Source: Compara cell proliferation Traceable author statement Ref.1. Source: ProtInc multicellular organismal metabolic process Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara nucleotide-excision repair, DNA damage removal Traceable author statement. Source: Reactome positive regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara 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.8. Source: GOC regulation of cyclin-dependent protein serine/threonine kinase activity Traceable author statement Ref.1. Source: ProtInc response to calcium ion Inferred from electronic annotation. Source: Compara 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 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: Compara viral reproduction Traceable author statement. Source: Reactome
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA holo TFIIH complex Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	zinc ion binding Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 309

309

CDK-activating kinase assembly factor MAT1

PRO_0000055932

Regions

Repeat

142 – 161

20

UIM

Zinc finger

6 – 50

45

RING-type

Amino acid modifications

Modified residue

51

1

Phosphothreonine Ref.10

Modified residue

279

1

Phosphoserine Ref.10 Ref.11

Natural variations

Natural variant

282

1

D → A.
Corresponds to variant rs35188899 [ dbSNP | Ensembl ].

VAR_052084

Experimental info

Sequence conflict

188 – 229

42

Missing in AAB05248. Ref.3

Sequence conflict

247 – 248

2

EY → DN in AAB05248. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

309

Helix Strand Turn

Details...

Turn

8 – 11

4

Helix

12 – 15

4

Beta strand

21 – 23

3

Helix

32 – 40

9

Beta strand

43 – 45

3

Turn

47 – 49

3

Beta strand

59 – 61

3

Sequences

	Sequence		Length	Mass (Da)
	P51948 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 6818DDE230E81A97	FASTA	309	35,823
	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

References

	« Hide 'large scale' referencesShow '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], 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]. 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].
[4]	NIEHS SNPs program Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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].
[6]	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. , 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].
[7]	"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]. Tissue: Placenta.
[8]	"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.
[9]	"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.
[10]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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, MASS SPECTROMETRY.
[12]	"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].
[13]	"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

NIEHS-SNPs

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.
CR450336 mRNA. Translation: CAG29332.1.
CH471061 Genomic DNA. Translation: EAW80787.1.
BC000820 mRNA. Translation: AAH00820.1.

IPI

IPI00294701.

PIR

G02764.
S60157.

RefSeq

NP_001171434.1. NM_001177963.1.
NP_002422.1. NM_002431.3.

UniGene

Hs.509523.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1G25	NMR	-	A	1-65	[»]

ProteinModelPortal

P51948.

ModBase

Search...

Protein-protein interaction databases

IntAct

P51948. 26 interactions.

MINT

MINT-255129.

STRING

9606.ENSP00000261245.

PTM databases

PhosphoSite

P51948.

Polymorphism databases

DMDM

1708932.

Proteomic databases

PaxDb

P51948.

PRIDE

P51948.

Protocols and materials databases

DNASU

4331.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261245; ENSP00000261245; ENSG00000020426.

GeneID

4331.

KEGG

hsa:4331.

UCSC

uc001xfd.3. human.

Organism-specific databases

CTD

4331.

GeneCards

GC14P061201.

HGNC

HGNC:7181. MNAT1.

HPA

CAB004495.
HPA000701.

MIM

602659. gene.

neXtProt

NX_P51948.

PharmGKB

PA30894.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5220.

HOGENOM

HOG000189680.

HOVERGEN

HBG001144.

InParanoid

P51948.

KO

K10842.

OMA

PLRRNNF.

OrthoDB

EOG40S0G4.

PhylomeDB

P51948.

Enzyme and pathway databases

Pathway_Interaction_DB

retinoic_acid_pathway. Retinoic acid receptors-mediated signaling.

Reactome

REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_1675. mRNA Processing.
REACT_1788. Transcription.
REACT_216. DNA Repair.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P51948.

Bgee

P51948.

CleanEx

HS_MNAT1.

Genevestigator

P51948.

GermOnline

ENSG00000020426. Homo sapiens.

Family and domain databases

Gene3D

3.30.40.10. 1 hit.

InterPro

IPR015877. 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]

PANTHER

PTHR12683. PTHR12683. 1 hit.

Pfam

PF06391. MAT1. 1 hit.
[Graphical view]

PIRSF

PIRSF003338. MAT1_metazoa. 1 hit.

SMART

SM00184. RING. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00570. cdk7. 1 hit.

PROSITE

PS50330. UIM. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P51948.

ChEMBL

CHEMBL5053.

EvolutionaryTrace

P51948.

GenomeRNAi

4331.

NextBio

17043.

SOURCE

Search...

Entry information

Entry name

MAT1_HUMAN

Accession

Primary (citable) accession number: P51948
Secondary accession number(s): Q15817, Q6ICQ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 140 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.