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P51948

- MAT1_HUMAN

UniProt

P51948 - MAT1_HUMAN

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Protein
CDK-activating kinase assembly factor MAT1
Gene
MNAT1, CAP35, MAT1, RNF66
Organism
Homo sapiens (Human)
Status
Reviewed - 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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri6 – 5045RING-type
Add
BLAST

GO - Molecular functioni

  1. protein N-terminus binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. zinc ion binding Source: ProtInc
Complete GO annotation...

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. adult heart development Source: Ensembl
  7. cell proliferation Source: ProtInc
  8. gene expression Source: Reactome
  9. mitotic cell cycle Source: Reactome
  10. negative regulation of apoptotic process Source: Ensembl
  11. nucleotide-excision repair Source: Reactome
  12. nucleotide-excision repair, DNA damage removal Source: Reactome
  13. positive regulation of smooth muscle cell proliferation Source: Ensembl
  14. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  15. positive regulation of viral transcription Source: Reactome
  16. protein complex assembly Source: ProtInc
  17. protein phosphorylation Source: GOC
  18. regulation of cyclin-dependent protein serine/threonine kinase activity Source: ProtInc
  19. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  20. response to calcium ion Source: Ensembl
  21. termination of RNA polymerase I transcription Source: Reactome
  22. transcription elongation from RNA polymerase I promoter Source: Reactome
  23. transcription elongation from RNA polymerase II promoter Source: Reactome
  24. transcription from RNA polymerase I promoter Source: Reactome
  25. transcription from RNA polymerase II promoter Source: UniProtKB
  26. transcription initiation from RNA polymerase I promoter Source: Reactome
  27. transcription initiation from RNA polymerase II promoter Source: Reactome
  28. transcription-coupled nucleotide-excision repair Source: Reactome
  29. ventricular system development Source: Ensembl
  30. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

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.
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
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:7181. MNAT1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. holo TFIIH complex Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30894.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 309309CDK-activating kinase assembly factor MAT1
PRO_0000055932Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei51 – 511Phosphothreonine1 Publication
Modified residuei279 – 2791Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP51948.
PaxDbiP51948.
PRIDEiP51948.

PTM databases

PhosphoSiteiP51948.

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

ArrayExpressiP51948.
BgeeiP51948.
CleanExiHS_MNAT1.
GenevestigatoriP51948.

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

Protein-protein interaction databases

BioGridi110474. 54 interactions.
IntActiP51948. 26 interactions.
MINTiMINT-255129.
STRINGi9606.ENSP00000261245.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni8 – 114
Helixi12 – 154
Beta strandi21 – 233
Helixi32 – 409
Beta strandi43 – 453
Turni47 – 493
Beta strandi59 – 613

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1G25NMR-A1-65[»]
ProteinModelPortaliP51948.
SMRiP51948. Positions 1-65.

Miscellaneous databases

EvolutionaryTraceiP51948.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati142 – 16120UIM
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5220.
HOGENOMiHOG000189680.
HOVERGENiHBG001144.
InParanoidiP51948.
KOiK10842.
OMAiETCGPQV.
OrthoDBiEOG71VST2.
PhylomeDBiP51948.
TreeFamiTF106124.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR015877. 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]
PANTHERiPTHR12683. PTHR12683. 1 hit.
PfamiPF06391. MAT1. 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. Align

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

MDDQGCPRCK TTKYRNPSLK LMVNVCGHTL CESCVDLLFV RGAGNCPECG    50
TPLRKSNFRV QLFEDPTVDK EVEIRKKVLK IYNKREEDFP SLREYNDFLE 100
EVEEIVFNLT NNVDLDNTKK KMEIYQKENK DVIQKNKLKL TREQEELEEA 150
LEVERQENEQ RRLFIQKEEQ LQQILKRKNK QAFLDELESS DLPVALLLAQ 200
HKDRSTQLEM QLEKPKPVKP VTFSTGIKMG QHISLAPIHK LEEALYEYQP 250
LQIETYGPHV PELEMLGRLG YLNHVRAASP QDLAGGYTSS LACHRALQDA 300
FSGLFWQPS 309
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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti282 – 2821D → A.
Corresponds to variant rs35188899 [ dbSNP | Ensembl ].
VAR_052084

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei188 – 22942Missing in isoform 2.
VSP_046772Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti247 – 2482EY → DN in AAB05248. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_005267687.1. [P51948-1]
UniGeneiHs.509523.

Genome annotation databases

EnsembliENST00000261245; ENSP00000261245; ENSG00000020426. [P51948-1]
ENST00000539616; ENSP00000446437; ENSG00000020426. [P51948-2]
GeneIDi4331.
KEGGihsa:4331.
UCSCiuc001xfd.3. human. [P51948-1]
uc001xfe.3. human.

Polymorphism databases

DMDMi1708932.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS53899.1. [P51948-2 ]
CCDS9750.1. [P51948-1 ]
PIRi G02764.
S60157.
RefSeqi NP_001171434.1. NM_001177963.1. [P51948-2 ]
NP_002422.1. NM_002431.3. [P51948-1 ]
XP_005267744.1. XM_005267687.1. [P51948-1 ]
UniGenei Hs.509523.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1G25 NMR - A 1-65 [» ]
ProteinModelPortali P51948.
SMRi P51948. Positions 1-65.
ModBasei Search...

Protein-protein interaction databases

BioGridi 110474. 54 interactions.
IntActi P51948. 26 interactions.
MINTi MINT-255129.
STRINGi 9606.ENSP00000261245.

Chemistry

BindingDBi P51948.
ChEMBLi CHEMBL3038473.

PTM databases

PhosphoSitei P51948.

Polymorphism databases

DMDMi 1708932.

Proteomic databases

MaxQBi P51948.
PaxDbi P51948.
PRIDEi P51948.

Protocols and materials databases

DNASUi 4331.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261245 ; ENSP00000261245 ; ENSG00000020426 . [P51948-1 ]
ENST00000539616 ; ENSP00000446437 ; ENSG00000020426 . [P51948-2 ]
GeneIDi 4331.
KEGGi hsa:4331.
UCSCi uc001xfd.3. human. [P51948-1 ]
uc001xfe.3. human.

Organism-specific databases

CTDi 4331.
GeneCardsi GC14P061201.
HGNCi HGNC:7181. MNAT1.
HPAi CAB004495.
HPA000701.
HPA001154.
MIMi 602659. gene.
neXtProti NX_P51948.
PharmGKBi PA30894.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5220.
HOGENOMi HOG000189680.
HOVERGENi HBG001144.
InParanoidi P51948.
KOi K10842.
OMAi ETCGPQV.
OrthoDBi EOG71VST2.
PhylomeDBi P51948.
TreeFami TF106124.

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 P51948.

Miscellaneous databases

EvolutionaryTracei P51948.
GeneWikii MNAT1.
GenomeRNAii 4331.
NextBioi 17043.
PROi P51948.
SOURCEi Search...

Gene expression databases

ArrayExpressi P51948.
Bgeei P51948.
CleanExi HS_MNAT1.
Genevestigatori P51948.

Family and domain databases

Gene3Di 3.30.40.10. 1 hit.
InterProi 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 ]
PANTHERi PTHR12683. PTHR12683. 1 hit.
Pfami PF06391. MAT1. 1 hit.
[Graphical view ]
PIRSFi PIRSF003338. MAT1_metazoa. 1 hit.
SMARTi SM00184. RING. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00570. cdk7. 1 hit.
PROSITEi PS50330. UIM. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. 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.

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: September 3, 2014
This is version 155 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

External Data

Dasty 3

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