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P19388

- RPAB1_HUMAN

UniProt

P19388 - RPAB1_HUMAN

Protein

DNA-directed RNA polymerases I, II, and III subunit RPABC1

Gene

POLR2E

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 4 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively. Pol II is the central component of the basal RNA polymerase II transcription machinery. Pols are composed of mobile elements that move relative to each other. In Pol II, POLR2E/RPB5 is part of the lower jaw surrounding the central large cleft and thought to grab the incoming DNA template. Seems to be the major component in this process By similarity.By similarity

    GO - Molecular functioni

    1. DNA binding Source: InterPro
    2. DNA-directed RNA polymerase activity Source: ProtInc
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. 7-methylguanosine mRNA capping Source: Reactome
    2. DNA repair Source: Reactome
    3. gene expression Source: Reactome
    4. innate immune response Source: Reactome
    5. mRNA splicing, via spliceosome Source: Reactome
    6. nucleotide-excision repair Source: Reactome
    7. positive regulation of type I interferon production Source: Reactome
    8. positive regulation of viral transcription Source: Reactome
    9. RNA splicing Source: Reactome
    10. termination of RNA polymerase III transcription Source: Reactome
    11. transcription-coupled nucleotide-excision repair Source: Reactome
    12. transcription elongation from RNA polymerase III promoter Source: Reactome
    13. transcription elongation from RNA polymerase II promoter Source: Reactome
    14. transcription from RNA polymerase III promoter Source: Reactome
    15. transcription from RNA polymerase II promoter Source: UniProtKB
    16. transcription from RNA polymerase I promoter Source: GOC
    17. transcription initiation from RNA polymerase II promoter Source: Reactome
    18. viral process Source: Reactome

    Keywords - Biological processi

    Host-virus interaction, Transcription

    Enzyme and pathway databases

    ReactomeiREACT_1036. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
    REACT_12417. MicroRNA (miRNA) biogenesis.
    REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_1470. mRNA Capping.
    REACT_1628. Transcription-coupled NER (TC-NER).
    REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_1753. mRNA Splicing - Minor Pathway.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_2089. RNA Polymerase II Promoter Escape.
    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_22339. RNA Polymerase III Abortive And Retractive Initiation.
    REACT_347. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
    REACT_467. mRNA Splicing - Major Pathway.
    REACT_571. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
    REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
    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_6244. Pausing and recovery of HIV elongation.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6259. HIV elongation arrest and recovery.
    REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
    REACT_63. RNA Polymerase III Transcription Termination.
    REACT_6319. Formation of the HIV-1 Early Elongation Complex.
    REACT_6332. HIV Transcription Initiation.
    REACT_6344. Tat-mediated HIV elongation arrest and recovery.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_6354. Viral Messenger RNA Synthesis.
    REACT_756. RNA Polymerase III Chain Elongation.
    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_975. RNA Pol II CTD phosphorylation and interaction with CE.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA-directed RNA polymerases I, II, and III subunit RPABC1
    Short name:
    RNA polymerases I, II, and III subunit ABC1
    Alternative name(s):
    DNA-directed RNA polymerase II 23 kDa polypeptide
    DNA-directed RNA polymerase II subunit E
    RPB5 homolog
    XAP4
    Gene namesi
    Name:POLR2E
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9192. POLR2E.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. DNA-directed RNA polymerase I complex Source: RefGenome
    3. DNA-directed RNA polymerase II, core complex Source: UniProtKB
    4. DNA-directed RNA polymerase III complex Source: RefGenome
    5. nucleoplasm Source: Reactome
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    DNA-directed RNA polymerase, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33512.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 210210DNA-directed RNA polymerases I, II, and III subunit RPABC1PRO_0000146075Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP19388.
    PaxDbiP19388.
    PeptideAtlasiP19388.
    PRIDEiP19388.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00291093.
    SWISS-2DPAGEP19388.

    PTM databases

    PhosphoSiteiP19388.

    Expressioni

    Gene expression databases

    ArrayExpressiP19388.
    BgeeiP19388.
    CleanExiHS_POLR2E.
    GenevestigatoriP19388.

    Interactioni

    Subunit structurei

    Component of the RNA polymerase I (Pol I), RNA polymerase II (Pol II) and RNA polymerase III (Pol III) complexes consisting of at least 13, 12 and 17 subunits, respectively By similarity. In RNA Pol II, this subunit is present in 2-fold molar excess over the other subunits. Interacts with URI1. Interacts with HBV protein X.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    URI1O947632EBI-395189,EBI-357067

    Protein-protein interaction databases

    BioGridi111430. 83 interactions.
    DIPiDIP-56N.
    IntActiP19388. 26 interactions.
    MINTiMINT-193645.
    STRINGi9606.ENSP00000215587.

    Structurei

    3D structure databases

    ProteinModelPortaliP19388.
    SMRiP19388. Positions 3-210.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2012.
    HOGENOMiHOG000205213.
    HOVERGENiHBG057019.
    InParanoidiP19388.
    KOiK03013.
    OMAiDEAETYK.
    OrthoDBiEOG7M6D8D.
    PhylomeDBiP19388.

    Family and domain databases

    Gene3Di3.40.1340.10. 1 hit.
    3.90.940.20. 1 hit.
    HAMAPiMF_00025. RNApol_RpoH_RPB5.
    InterProiIPR014381. DNA_RNA_pol_RPB5_euk/virus.
    IPR005571. RNA_pol_Rpb5_N.
    IPR000783. RNA_pol_subH/Rpb5_C.
    IPR020608. RNA_pol_subH/Rpb5_CS.
    IPR020609. RpoH/RPB5.
    [Graphical view]
    PfamiPF01191. RNA_pol_Rpb5_C. 1 hit.
    PF03871. RNA_pol_Rpb5_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000747. RPB5. 1 hit.
    ProDomiPD005155. RNA_pol_subH/Rpb5_C. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SUPFAMiSSF53036. SSF53036. 1 hit.
    SSF55287. SSF55287. 1 hit.
    PROSITEiPS01110. RNA_POL_H_23KD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P19388-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDDEEETYRL WKIRKTIMQL CHDRGYLVTQ DELDQTLEEF KAQSGDKPSE    50
    GRPRRTDLTV LVAHNDDPTD QMFVFFPEEP KVGIKTIKVY CQRMQEENIT 100
    RALIVVQQGM TPSAKQSLVD MAPKYILEQF LQQELLINIT EHELVPEHVV 150
    MTKEEVTELL ARYKLRENQL PRIQAGDPVA RYFGIKRGQV VKIIRPSETA 200
    GRYITYRLVQ 210
    Length:210
    Mass (Da):24,551
    Last modified:October 17, 2006 - v4
    Checksum:i1E88AFDBCF9C8535
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti132 – 1321Q → E(PubMed:2753903)Curated
    Sequence conflicti132 – 1321Q → E(PubMed:7828586)Curated
    Sequence conflicti157 – 1571T → S in BAA07406. (PubMed:7828586)Curated
    Sequence conflicti185 – 1851I → V in AAH34144. (PubMed:15489334)Curated
    Sequence conflicti186 – 1861K → R in BAA07406. (PubMed:7828586)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti44 – 441S → F.5 Publications
    Corresponds to variant rs12459404 [ dbSNP | Ensembl ].
    VAR_028259

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04965 mRNA. Translation: AAA62401.1. Sequence problems.
    S42643 mRNA. Translation: AAB19339.1.
    D38251 mRNA. Translation: BAA07406.1.
    AK312625 mRNA. Translation: BAG35511.1.
    AC004151 Genomic DNA. Translation: AAC03238.1.
    CH471139 Genomic DNA. Translation: EAW69548.1.
    CH471139 Genomic DNA. Translation: EAW69549.1.
    BC004441 mRNA. Translation: AAH04441.1.
    BC034144 mRNA. Translation: AAH34144.1.
    CCDSiCCDS12056.1.
    PIRiS52002. A32618.
    RefSeqiNP_002686.2. NM_002695.3.
    UniGeneiHs.24301.

    Genome annotation databases

    EnsembliENST00000215587; ENSP00000215587; ENSG00000099817.
    ENST00000586746; ENSP00000464739; ENSG00000099817.
    GeneIDi5434.
    KEGGihsa:5434.
    UCSCiuc002lre.4. human.

    Polymorphism databases

    DMDMi116242767.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04965 mRNA. Translation: AAA62401.1 . Sequence problems.
    S42643 mRNA. Translation: AAB19339.1 .
    D38251 mRNA. Translation: BAA07406.1 .
    AK312625 mRNA. Translation: BAG35511.1 .
    AC004151 Genomic DNA. Translation: AAC03238.1 .
    CH471139 Genomic DNA. Translation: EAW69548.1 .
    CH471139 Genomic DNA. Translation: EAW69549.1 .
    BC004441 mRNA. Translation: AAH04441.1 .
    BC034144 mRNA. Translation: AAH34144.1 .
    CCDSi CCDS12056.1.
    PIRi S52002. A32618.
    RefSeqi NP_002686.2. NM_002695.3.
    UniGenei Hs.24301.

    3D structure databases

    ProteinModelPortali P19388.
    SMRi P19388. Positions 3-210.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111430. 83 interactions.
    DIPi DIP-56N.
    IntActi P19388. 26 interactions.
    MINTi MINT-193645.
    STRINGi 9606.ENSP00000215587.

    PTM databases

    PhosphoSitei P19388.

    Polymorphism databases

    DMDMi 116242767.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00291093.
    SWISS-2DPAGE P19388.

    Proteomic databases

    MaxQBi P19388.
    PaxDbi P19388.
    PeptideAtlasi P19388.
    PRIDEi P19388.

    Protocols and materials databases

    DNASUi 5434.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000215587 ; ENSP00000215587 ; ENSG00000099817 .
    ENST00000586746 ; ENSP00000464739 ; ENSG00000099817 .
    GeneIDi 5434.
    KEGGi hsa:5434.
    UCSCi uc002lre.4. human.

    Organism-specific databases

    CTDi 5434.
    GeneCardsi GC19M001086.
    HGNCi HGNC:9192. POLR2E.
    MIMi 180664. gene.
    neXtProti NX_P19388.
    PharmGKBi PA33512.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2012.
    HOGENOMi HOG000205213.
    HOVERGENi HBG057019.
    InParanoidi P19388.
    KOi K03013.
    OMAi DEAETYK.
    OrthoDBi EOG7M6D8D.
    PhylomeDBi P19388.

    Enzyme and pathway databases

    Reactomei REACT_1036. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
    REACT_12417. MicroRNA (miRNA) biogenesis.
    REACT_125. Processing of Capped Intron-Containing Pre-mRNA.
    REACT_1470. mRNA Capping.
    REACT_1628. Transcription-coupled NER (TC-NER).
    REACT_1655. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
    REACT_1753. mRNA Splicing - Minor Pathway.
    REACT_1851. RNA Polymerase II Transcription Initiation.
    REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
    REACT_2089. RNA Polymerase II Promoter Escape.
    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_22339. RNA Polymerase III Abortive And Retractive Initiation.
    REACT_347. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
    REACT_467. mRNA Splicing - Major Pathway.
    REACT_571. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
    REACT_6143. Pausing and recovery of Tat-mediated HIV elongation.
    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_6244. Pausing and recovery of HIV elongation.
    REACT_6253. RNA Polymerase II HIV Promoter Escape.
    REACT_6259. HIV elongation arrest and recovery.
    REACT_6261. Abortive elongation of HIV-1 transcript in the absence of Tat.
    REACT_63. RNA Polymerase III Transcription Termination.
    REACT_6319. Formation of the HIV-1 Early Elongation Complex.
    REACT_6332. HIV Transcription Initiation.
    REACT_6344. Tat-mediated HIV elongation arrest and recovery.
    REACT_6346. Formation of HIV-1 elongation complex containing HIV-1 Tat.
    REACT_6354. Viral Messenger RNA Synthesis.
    REACT_756. RNA Polymerase III Chain Elongation.
    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_975. RNA Pol II CTD phosphorylation and interaction with CE.

    Miscellaneous databases

    GeneWikii POLR2E.
    GenomeRNAii 5434.
    NextBioi 21025.
    PROi P19388.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19388.
    Bgeei P19388.
    CleanExi HS_POLR2E.
    Genevestigatori P19388.

    Family and domain databases

    Gene3Di 3.40.1340.10. 1 hit.
    3.90.940.20. 1 hit.
    HAMAPi MF_00025. RNApol_RpoH_RPB5.
    InterProi IPR014381. DNA_RNA_pol_RPB5_euk/virus.
    IPR005571. RNA_pol_Rpb5_N.
    IPR000783. RNA_pol_subH/Rpb5_C.
    IPR020608. RNA_pol_subH/Rpb5_CS.
    IPR020609. RpoH/RPB5.
    [Graphical view ]
    Pfami PF01191. RNA_pol_Rpb5_C. 1 hit.
    PF03871. RNA_pol_Rpb5_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000747. RPB5. 1 hit.
    ProDomi PD005155. RNA_pol_subH/Rpb5_C. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SUPFAMi SSF53036. SSF53036. 1 hit.
    SSF55287. SSF55287. 1 hit.
    PROSITEi PS01110. RNA_POL_H_23KD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and molecular characterization of a cDNA encoding the 23-kDa subunit of human RNA polymerase II."
      Pati U.K., Weissman S.M.
      J. Biol. Chem. 264:13114-13121(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT PHE-44.
    2. Erratum
      Pati U.K., Weissman S.M.
      J. Biol. Chem. 266:13468-13468(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    3. "Human RPB5, a subunit shared by eukaryotic nuclear RNA polymerases, binds human hepatitis B virus X protein and may play a role in X transactivation."
      Cheong J.H., Yi M., Lin Y., Murakami S.
      EMBO J. 14:143-150(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PHE-44, INTERACTION WITH HBV PROTEIN X.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PHE-44.
      Tissue: Heart.
    5. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PHE-44.
    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], VARIANT PHE-44.
      Tissue: Lung.
    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: FUNCTION, IDENTIFICATION IN THE RNA POLYMERASE II CORE-COMPLEX, SUBCELLULAR LOCATION.
    9. "RMP, a novel RNA polymerase II subunit 5-interacting protein, counteracts transactivation by hepatitis B virus X protein."
      Dorjsuren D., Lin Y., Wei W., Yamashita T., Nomura T., Hayashi N., Murakami S.
      Mol. Cell. Biol. 18:7546-7555(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH URI1.
    10. "RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation of transcription by upstream binding factor."
      Panov K.I., Panova T.B., Gadal O., Nishiyama K., Saito T., Russell J., Zomerdijk J.C.B.M.
      Mol. Cell. Biol. 26:5436-5448(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE RNA POL I COMPLEX.
    11. "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].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRPAB1_HUMAN
    AccessioniPrimary (citable) accession number: P19388
    Secondary accession number(s): B2R6L4
    , D6W5Y1, O43380, Q6PIH5, Q9BT06
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 156 of the entry and version 4 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3