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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: 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).By similarity

GO - Molecular functioni

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

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. negative regulation of gene expression, epigenetic Source: Reactome
  7. nucleotide-excision repair Source: Reactome
  8. piRNA metabolic process Source: Reactome
  9. positive regulation of type I interferon production Source: Reactome
  10. positive regulation of viral transcription Source: Reactome
  11. regulation of gene expression, epigenetic Source: Reactome
  12. RNA splicing Source: Reactome
  13. somatic stem cell maintenance Source: Reactome
  14. termination of RNA polymerase III transcription Source: Reactome
  15. termination of RNA polymerase I transcription Source: Reactome
  16. transcription-coupled nucleotide-excision repair Source: Reactome
  17. transcription elongation from RNA polymerase III promoter Source: Reactome
  18. transcription elongation from RNA polymerase II promoter Source: Reactome
  19. transcription elongation from RNA polymerase I promoter Source: Reactome
  20. transcription from RNA polymerase III promoter Source: Reactome
  21. transcription from RNA polymerase II promoter Source: UniProtKB
  22. transcription from RNA polymerase I promoter Source: Reactome
  23. transcription initiation from RNA polymerase II promoter Source: Reactome
  24. transcription initiation from RNA polymerase I promoter Source: Reactome
  25. 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_1074. RNA Polymerase I Transcription Termination.
REACT_118823. Cytosolic sensors of pathogen-associated DNA.
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_1845. Formation of RNA Pol II elongation complex.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_1913. RNA Polymerase I Promoter Escape.
REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
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_22339. RNA Polymerase III Abortive And Retractive Initiation.
REACT_263856. Transcriptional regulation of pluripotent stem cells.
REACT_263965. NoRC negatively regulates rRNA expression.
REACT_264617. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
REACT_267790. PIWI-interacting RNA (piRNA) biogenesis.
REACT_268530. Transcriptional regulation by small RNAs.
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_953. RNA Polymerase I Transcription Initiation.
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 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:9192. POLR2E.

Subcellular locationi

  1. Nucleus 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. DNA-directed RNA polymerase I complex Source: GO_Central
  3. DNA-directed RNA polymerase II, core complex Source: UniProtKB
  4. DNA-directed RNA polymerase III complex Source: GO_Central
  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.

Polymorphism and mutation databases

BioMutaiPOLR2E.
DMDMi116242767.

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

BgeeiP19388.
CleanExiHS_POLR2E.
ExpressionAtlasiP19388. baseline and differential.
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. 94 interactions.
DIPiDIP-56N.
IntActiP19388. 27 interactions.
MINTiMINT-193645.
STRINGi9606.ENSP00000215587.

Structurei

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2012.
GeneTreeiENSGT00390000013841.
HOGENOMiHOG000205213.
HOVERGENiHBG057019.
InParanoidiP19388.
KOiK03013.
OMAiNQLMRIQ.
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

        10         20         30         40         50
MDDEEETYRL WKIRKTIMQL CHDRGYLVTQ DELDQTLEEF KAQSGDKPSE
60 70 80 90 100
GRPRRTDLTV LVAHNDDPTD QMFVFFPEEP KVGIKTIKVY CQRMQEENIT
110 120 130 140 150
RALIVVQQGM TPSAKQSLVD MAPKYILEQF LQQELLINIT EHELVPEHVV
160 170 180 190 200
MTKEEVTELL ARYKLRENQL PRIQAGDPVA RYFGIKRGQV VKIIRPSETA
210
GRYITYRLVQ
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:
EMBLi
GenBanki
DDBJi
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

EnsembliENST00000586746; ENSP00000464739; ENSG00000099817.
ENST00000612655; ENSP00000485021; ENSG00000099817.
ENST00000615234; ENSP00000478303; ENSG00000099817.
GeneIDi5434.
KEGGihsa:5434.
UCSCiuc002lre.4. human.

Polymorphism and mutation databases

BioMutaiPOLR2E.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi111430. 94 interactions.
DIPiDIP-56N.
IntActiP19388. 27 interactions.
MINTiMINT-193645.
STRINGi9606.ENSP00000215587.

PTM databases

PhosphoSiteiP19388.

Polymorphism and mutation databases

BioMutaiPOLR2E.
DMDMi116242767.

2D gel databases

REPRODUCTION-2DPAGEIPI00291093.
SWISS-2DPAGEP19388.

Proteomic databases

MaxQBiP19388.
PaxDbiP19388.
PeptideAtlasiP19388.
PRIDEiP19388.

Protocols and materials databases

DNASUi5434.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000586746; ENSP00000464739; ENSG00000099817.
ENST00000612655; ENSP00000485021; ENSG00000099817.
ENST00000615234; ENSP00000478303; ENSG00000099817.
GeneIDi5434.
KEGGihsa:5434.
UCSCiuc002lre.4. human.

Organism-specific databases

CTDi5434.
GeneCardsiGC19M001086.
HGNCiHGNC:9192. POLR2E.
MIMi180664. gene.
neXtProtiNX_P19388.
PharmGKBiPA33512.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2012.
GeneTreeiENSGT00390000013841.
HOGENOMiHOG000205213.
HOVERGENiHBG057019.
InParanoidiP19388.
KOiK03013.
OMAiNQLMRIQ.
OrthoDBiEOG7M6D8D.
PhylomeDBiP19388.

Enzyme and pathway databases

ReactomeiREACT_1036. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
REACT_1074. RNA Polymerase I Transcription Termination.
REACT_118823. Cytosolic sensors of pathogen-associated DNA.
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_1845. Formation of RNA Pol II elongation complex.
REACT_1851. RNA Polymerase II Transcription Initiation.
REACT_1913. RNA Polymerase I Promoter Escape.
REACT_1941. Formation of transcription-coupled NER (TC-NER) repair complex.
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_22339. RNA Polymerase III Abortive And Retractive Initiation.
REACT_263856. Transcriptional regulation of pluripotent stem cells.
REACT_263965. NoRC negatively regulates rRNA expression.
REACT_264617. POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation.
REACT_267790. PIWI-interacting RNA (piRNA) biogenesis.
REACT_268530. Transcriptional regulation by small RNAs.
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_953. RNA Polymerase I Transcription Initiation.
REACT_975. RNA Pol II CTD phosphorylation and interaction with CE.

Miscellaneous databases

ChiTaRSiPOLR2E. human.
GeneWikiiPOLR2E.
GenomeRNAii5434.
NextBioi21025.
PROiP19388.
SOURCEiSearch...

Gene expression databases

BgeeiP19388.
CleanExiHS_POLR2E.
ExpressionAtlasiP19388. baseline and differential.
GenevestigatoriP19388.

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]
ProtoNetiSearch...

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: April 29, 2015
This is version 163 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

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.