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P19388

- RPAB1_HUMAN

UniProt

P19388 - RPAB1_HUMAN

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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

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.1 Publication

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

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

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 RPABC1UniRule annotation
PRO_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.4 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi111430. 83 interactions.
DIPiDIP-56N.
IntActiP19388. 25 interactions.
MINTiMINT-193645.
STRINGi9606.ENSP00000215587.

Structurei

3D structure databases

ProteinModelPortaliP19388.
SMRiP19388. Positions 3-210.

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

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321Q → E1 Publication
Sequence conflicti132 – 1321Q → E1 Publication
Sequence conflicti157 – 1571T → S in BAA07406. 1 Publication
Sequence conflicti185 – 1851I → V in AAH34144. 1 Publication
Sequence conflicti186 – 1861K → R in BAA07406. 1 Publication

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. 25 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 155 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

Similar proteinsi