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P51948

- MAT1_HUMAN

UniProt

P51948 - MAT1_HUMAN

Protein

CDK-activating kinase assembly factor MAT1

Gene

MNAT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    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-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. 7-methylguanosine mRNA capping Source: Reactome
    2. adult heart development Source: Ensembl
    3. ATP catabolic process Source: GOC
    4. cell proliferation Source: ProtInc
    5. DNA repair Source: Reactome
    6. G1/S transition of mitotic cell cycle Source: Reactome
    7. G2/M transition of mitotic cell cycle Source: Reactome
    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-coupled nucleotide-excision repair Source: Reactome
    23. transcription elongation from RNA polymerase II promoter Source: Reactome
    24. transcription elongation from RNA polymerase I promoter Source: Reactome
    25. transcription from RNA polymerase II promoter Source: UniProtKB
    26. transcription from RNA polymerase I promoter Source: Reactome
    27. transcription initiation from RNA polymerase II promoter Source: Reactome
    28. transcription initiation from RNA polymerase I promoter Source: Reactome
    29. ventricular system development Source: Ensembl
    30. viral process Source: Reactome

    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

    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 MAT1PRO_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

    1
    309
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51948.

    Family & Domainsi

    Domains and Repeats

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

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri6 – 5045RING-typePROSITE-ProRule annotationAdd
    BLAST

    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

    Experimental Info

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

    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. 1 PublicationVSP_046772Add
    BLAST

    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 156 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