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Protein

DNA-directed RNA polymerases I, II, and III subunit RPABC2

Gene

POLR2F

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA-dependent RNA polymerases catalyze 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, POLR2F/RPB6 is part of the clamp element and together with parts of RPB1 and RPB2 forms a pocket to which the RPB4-RPB7 subcomplex binds (By similarity).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription

Enzyme and pathway databases

ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167160. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167242. Abortive elongation of HIV-1 transcript in the absence of Tat.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-1834949. Cytosolic sensors of pathogen-associated DNA.
R-HSA-203927. MicroRNA (miRNA) biogenesis.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-452723. Transcriptional regulation of pluripotent stem cells.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-5601884. PIWI-interacting RNA (piRNA) biogenesis.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-72086. mRNA Capping.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72165. mRNA Splicing - Minor Pathway.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
R-HSA-73772. RNA Polymerase I Promoter Escape.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-73780. RNA Polymerase III Chain Elongation.
R-HSA-73863. RNA Polymerase I Transcription Termination.
R-HSA-73980. RNA Polymerase III Transcription Termination.
R-HSA-749476. RNA Polymerase III Abortive And Retractive Initiation.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-HSA-76061. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
R-HSA-76066. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
R-HSA-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
R-HSA-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerases I, II, and III subunit RPABC2
Short name:
RNA polymerases I, II, and III subunit ABC2
Alternative name(s):
DNA-directed RNA polymerase II subunit F
DNA-directed RNA polymerases I, II, and III 14.4 kDa polypeptide
RPABC14.4
Short name:
RPB14.4
RPB6 homolog
RPC15
Gene namesi
Name:POLR2F
Synonyms:POLRF
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:9193. POLR2F.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • cytosol Source: Reactome
  • DNA-directed RNA polymerase I complex Source: GO_Central
  • DNA-directed RNA polymerase II, core complex Source: UniProtKB
  • DNA-directed RNA polymerase III complex Source: GO_Central
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33513.

Polymorphism and mutation databases

BioMutaiPOLR2F.
DMDMi47117761.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 127126DNA-directed RNA polymerases I, II, and III subunit RPABC2PRO_0000133799Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei2 – 21Phosphoserine; by CK2By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP61218.
MaxQBiP61218.
PaxDbiP61218.
PRIDEiP61218.

PTM databases

iPTMnetiP61218.
PhosphoSiteiP61218.

Expressioni

Gene expression databases

BgeeiP61218.
CleanExiHS_POLR2F.
ExpressionAtlasiP61218. baseline and differential.
GenevisibleiP61218. HS.

Organism-specific databases

HPAiCAB009882.
HPA000827.

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

Protein-protein interaction databases

BioGridi111431. 73 interactions.
IntActiP61218. 62 interactions.
STRINGi9606.ENSP00000403852.

Structurei

Secondary structure

1
127
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 165Combined sources
Beta strandi21 – 244Combined sources
Beta strandi35 – 417Combined sources
Helixi59 – 7517Combined sources
Beta strandi79 – 813Combined sources
Beta strandi83 – 864Combined sources
Beta strandi88 – 903Combined sources
Helixi91 – 999Combined sources
Beta strandi104 – 1107Combined sources
Turni111 – 1133Combined sources
Beta strandi114 – 12310Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QKLNMR-A1-127[»]
ProteinModelPortaliP61218.
SMRiP61218. Positions 1-127.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61218.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3405. Eukaryota.
COG1758. LUCA.
GeneTreeiENSGT00390000010415.
HOGENOMiHOG000225272.
HOVERGENiHBG002375.
InParanoidiP61218.
OMAiMKYERAR.
OrthoDBiEOG757D0G.
PhylomeDBiP61218.
TreeFamiTF103041.

Family and domain databases

Gene3Di3.90.940.10. 1 hit.
InterProiIPR020708. DNA-dir_RNA_polK_14-18kDa_CS.
IPR006110. Pol_omega/K/RPB6.
IPR012293. RNAP_RPB6_omega.
IPR028363. RPB6.
IPR006111. RpoK/Rpb6.
[Graphical view]
PANTHERiPTHR10773. PTHR10773. 1 hit.
PfamiPF01192. RNA_pol_Rpb6. 1 hit.
[Graphical view]
PIRSFiPIRSF500154. RPB6. 1 hit.
PIRSF000778. RpoK/RPB6. 1 hit.
SMARTiSM01409. RNA_pol_Rpb6. 1 hit.
[Graphical view]
SUPFAMiSSF63562. SSF63562. 1 hit.
PROSITEiPS01111. RNA_POL_K_14KD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P61218-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDNEDNFDG DDFDDVEEDE GLDDLENAEE EGQENVEILP SGERPQANQK
60 70 80 90 100
RITTPYMTKY ERARVLGTRA LQIAMCAPVM VELEGETDPL LIAMKELKAR
110 120
KIPIIIRRYL PDGSYEDWGV DELIITD
Length:127
Mass (Da):14,478
Last modified:May 10, 2004 - v1
Checksum:i6362B0D7EB3F0921
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti60 – 601Y → N in a breast cancer sample; somatic mutation. 1 Publication
VAR_036571

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z27113 Genomic DNA. Translation: CAA81629.1.
AF006501 Genomic DNA. No translation available.
CR456546 mRNA. Translation: CAG30432.1.
CR457021 mRNA. Translation: CAG33302.1.
AL031587 Genomic DNA. Translation: CAB62981.1.
CH471095 Genomic DNA. Translation: EAW60203.1.
BC003582 mRNA. Translation: AAH03582.1.
CCDSiCCDS13963.1.
PIRiI38175. S38627.
RefSeqiNP_068809.1. NM_021974.4.
UniGeneiHs.436578.
Hs.735742.

Genome annotation databases

EnsembliENST00000442738; ENSP00000403852; ENSG00000100142.
GeneIDi5435.
UCSCiuc003aul.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z27113 Genomic DNA. Translation: CAA81629.1.
AF006501 Genomic DNA. No translation available.
CR456546 mRNA. Translation: CAG30432.1.
CR457021 mRNA. Translation: CAG33302.1.
AL031587 Genomic DNA. Translation: CAB62981.1.
CH471095 Genomic DNA. Translation: EAW60203.1.
BC003582 mRNA. Translation: AAH03582.1.
CCDSiCCDS13963.1.
PIRiI38175. S38627.
RefSeqiNP_068809.1. NM_021974.4.
UniGeneiHs.436578.
Hs.735742.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QKLNMR-A1-127[»]
ProteinModelPortaliP61218.
SMRiP61218. Positions 1-127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111431. 73 interactions.
IntActiP61218. 62 interactions.
STRINGi9606.ENSP00000403852.

PTM databases

iPTMnetiP61218.
PhosphoSiteiP61218.

Polymorphism and mutation databases

BioMutaiPOLR2F.
DMDMi47117761.

Proteomic databases

EPDiP61218.
MaxQBiP61218.
PaxDbiP61218.
PRIDEiP61218.

Protocols and materials databases

DNASUi5435.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000442738; ENSP00000403852; ENSG00000100142.
GeneIDi5435.
UCSCiuc003aul.4. human.

Organism-specific databases

CTDi5435.
GeneCardsiPOLR2F.
HGNCiHGNC:9193. POLR2F.
HPAiCAB009882.
HPA000827.
MIMi604414. gene.
neXtProtiNX_P61218.
PharmGKBiPA33513.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3405. Eukaryota.
COG1758. LUCA.
GeneTreeiENSGT00390000010415.
HOGENOMiHOG000225272.
HOVERGENiHBG002375.
InParanoidiP61218.
OMAiMKYERAR.
OrthoDBiEOG757D0G.
PhylomeDBiP61218.
TreeFamiTF103041.

Enzyme and pathway databases

ReactomeiR-HSA-112382. Formation of RNA Pol II elongation complex.
R-HSA-113418. Formation of the Early Elongation Complex.
R-HSA-167152. Formation of HIV elongation complex in the absence of HIV Tat.
R-HSA-167158. Formation of the HIV-1 Early Elongation Complex.
R-HSA-167160. RNA Pol II CTD phosphorylation and interaction with CE.
R-HSA-167161. HIV Transcription Initiation.
R-HSA-167162. RNA Polymerase II HIV Promoter Escape.
R-HSA-167172. Transcription of the HIV genome.
R-HSA-167200. Formation of HIV-1 elongation complex containing HIV-1 Tat.
R-HSA-167238. Pausing and recovery of Tat-mediated HIV elongation.
R-HSA-167242. Abortive elongation of HIV-1 transcript in the absence of Tat.
R-HSA-167243. Tat-mediated HIV elongation arrest and recovery.
R-HSA-167246. Tat-mediated elongation of the HIV-1 transcript.
R-HSA-167287. HIV elongation arrest and recovery.
R-HSA-167290. Pausing and recovery of HIV elongation.
R-HSA-168325. Viral Messenger RNA Synthesis.
R-HSA-1834949. Cytosolic sensors of pathogen-associated DNA.
R-HSA-203927. MicroRNA (miRNA) biogenesis.
R-HSA-427413. NoRC negatively regulates rRNA expression.
R-HSA-452723. Transcriptional regulation of pluripotent stem cells.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-5601884. PIWI-interacting RNA (piRNA) biogenesis.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
R-HSA-674695. RNA Polymerase II Pre-transcription Events.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-72086. mRNA Capping.
R-HSA-72163. mRNA Splicing - Major Pathway.
R-HSA-72165. mRNA Splicing - Minor Pathway.
R-HSA-72203. Processing of Capped Intron-Containing Pre-mRNA.
R-HSA-73762. RNA Polymerase I Transcription Initiation.
R-HSA-73772. RNA Polymerase I Promoter Escape.
R-HSA-73776. RNA Polymerase II Promoter Escape.
R-HSA-73777. RNA Polymerase I Chain Elongation.
R-HSA-73779. RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
R-HSA-73780. RNA Polymerase III Chain Elongation.
R-HSA-73863. RNA Polymerase I Transcription Termination.
R-HSA-73980. RNA Polymerase III Transcription Termination.
R-HSA-749476. RNA Polymerase III Abortive And Retractive Initiation.
R-HSA-75953. RNA Polymerase II Transcription Initiation.
R-HSA-75955. RNA Polymerase II Transcription Elongation.
R-HSA-76042. RNA Polymerase II Transcription Initiation And Promoter Clearance.
R-HSA-76061. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
R-HSA-76066. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
R-HSA-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.
R-HSA-77075. RNA Pol II CTD phosphorylation and interaction with CE.

Miscellaneous databases

ChiTaRSiPOLR2F. human.
EvolutionaryTraceiP61218.
GeneWikiiPOLR2F.
GenomeRNAii5435.
NextBioi21029.
PROiP61218.
SOURCEiSearch...

Gene expression databases

BgeeiP61218.
CleanExiHS_POLR2F.
ExpressionAtlasiP61218. baseline and differential.
GenevisibleiP61218. HS.

Family and domain databases

Gene3Di3.90.940.10. 1 hit.
InterProiIPR020708. DNA-dir_RNA_polK_14-18kDa_CS.
IPR006110. Pol_omega/K/RPB6.
IPR012293. RNAP_RPB6_omega.
IPR028363. RPB6.
IPR006111. RpoK/Rpb6.
[Graphical view]
PANTHERiPTHR10773. PTHR10773. 1 hit.
PfamiPF01192. RNA_pol_Rpb6. 1 hit.
[Graphical view]
PIRSFiPIRSF500154. RPB6. 1 hit.
PIRSF000778. RpoK/RPB6. 1 hit.
SMARTiSM01409. RNA_pol_Rpb6. 1 hit.
[Graphical view]
SUPFAMiSSF63562. SSF63562. 1 hit.
PROSITEiPS01111. RNA_POL_K_14KD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A 14.4 KDa acidic subunit of human RNA polymerase II with a putative leucine-zipper."
    Acker J., Wintzerith M., Vigneron M., Kedinger C.
    DNA Seq. 4:329-331(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Genomic structure of the RNA polymerase II small subunit (hRPB14.4) locus (POLRF) and mapping to 22q13.1 by sequence identity."
    Pusch C., Wang Z., Roe B., Blin N.
    Genomics 34:440-442(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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 (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Placenta.
  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. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "Solution structure of the hRPABC14.4 subunit of human RNA polymerases."
    del Rio-Portilla F., Gaskell A., Gilbert D., Ladias J.A., Wagner G.
    Nat. Struct. Biol. 6:1039-1042(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  12. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-60.

Entry informationi

Entry nameiRPAB2_HUMAN
AccessioniPrimary (citable) accession number: P61218
Secondary accession number(s): P41584, Q6IAY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: May 11, 2016
This is version 131 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, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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

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 one 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.