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P52435 (RPB11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA-directed RNA polymerase II subunit RPB11-a

Short name=RNA polymerase II subunit B11-a
Short name=RPB11a
Alternative name(s):
DNA-directed RNA polymerase II subunit J-1
RNA polymerase II 13.3 kDa subunit
Gene names
Name:POLR2J
Synonyms:POLR2J1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length117 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB11 is part of the core element with the central large cleft By similarity. Ref.7

Subunit structure

Component of the RNA polymerase II (Pol II) complex consisting of 12 subunits. Interacts with AATF. Ref.7 Ref.8

Subcellular location

Nucleus Ref.7.

Tissue specificity

Ubiquitously expressed. High expression was found in heart and skeletal muscle. Ref.9

Sequence similarities

Belongs to the archaeal RpoL/eukaryotic RPB11/RPC19 RNA polymerase subunit family.

Ontologies

Keywords
   Biological processTranscription
   Cellular componentDNA-directed RNA polymerase
Nucleus
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process7-methylguanosine mRNA capping

Traceable author statement. Source: Reactome

DNA repair

Traceable author statement. Source: Reactome

RNA splicing

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Traceable author statement. Source: Reactome

nucleotide-excision repair

Traceable author statement. Source: Reactome

positive regulation of viral transcription

Traceable author statement. Source: Reactome

transcription elongation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.7. Source: UniProtKB

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription-coupled nucleotide-excision repair

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentDNA-directed RNA polymerase II, core complex

Inferred from direct assay Ref.7. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

DNA-directed RNA polymerase activity

Traceable author statement Ref.1. Source: ProtInc

LRR domain binding

Inferred from physical interaction Ref.8. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 117117DNA-directed RNA polymerase II subunit RPB11-a
PRO_0000149309

Amino acid modifications

Modified residue11N-acetylmethionine Ref.6

Sequences

Sequence LengthMass (Da)Tools
P52435 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 6F78AB256EF8F647

FASTA11713,293
        10         20         30         40         50         60 
MNAPPAFESF LLFEGEKKIT INKDTKVPNA CLFTINKEDH TLGNIIKSQL LKDPQVLFAG 

        70         80         90        100        110 
YKVPHPLEHK IIIRVQTTPD YSPQEAFTNA ITDLISELSL LEERFRVAIK DKQEGIE 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of a novel human RNA polymerase II subunit downregulated by doxorubicin: new potential mechanisms of drug related toxicity."
Fanciulli M., Bruno T., Cerboni C., Bonetto F., Iacobini C., Frati L., Piccoli M., Floridi A., Santoni A., Punturieri A.
FEBS Lett. 384:48-52(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Colon.
[2]"Interactions between the human RNA polymerase II subunits."
Acker J., de Graaff M., Cheynel I., Khazak V., Kedinger C., Vigneron M.
J. Biol. Chem. 272:16815-16821(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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. expand/collapse author list , 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].
Tissue: Brain.
[4]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: Bone marrow and Kidney.
[6]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-18; 27-37; 48-62 AND 75-104, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Embryonic kidney.
[7]"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.
[8]"Identification of a novel partner of RNA polymerase II subunit 11, Che-1, which interacts with and affects the growth suppression function of Rb."
Fanciulli M., Bruno T., Di Padova M., De Angelis R., Iezzi S., Iacobini C., Floridi A., Passananti C.
FASEB J. 14:904-912(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH AATF.
[9]"A human RNA polymerase II subunit is encoded by a recently generated multigene family."
Grandemange S., Schaller S., Yamano S., Du Manoir S., Shpakovski G.V., Mattei M.-G., Kedinger C., Vigneron M.
BMC Mol. Biol. 2:14-14(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X82385 mRNA. Translation: CAA57785.1.
L37127 mRNA. Translation: AAD05361.1.
X98433 mRNA. Translation: CAA67075.1.
AK290515 mRNA. Translation: BAF83204.1.
AC093668 Genomic DNA. No translation available.
BC024165 mRNA. Translation: AAH24165.1.
BC065711 mRNA. Translation: AAH65711.1.
BC139902 mRNA. Translation: AAI39903.1.
BC141830 mRNA. Translation: AAI41831.1.
PIRS71325.
RefSeqNP_006225.1. NM_006234.4.
UniGeneHs.654952.

3D structure databases

ProteinModelPortalP52435.
SMRP52435. Positions 1-105.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111435. 40 interactions.
DIPDIP-32913N.
IntActP52435. 12 interactions.
MINTMINT-131416.
STRING9606.ENSP00000292614.

PTM databases

PhosphoSiteP52435.

Proteomic databases

PaxDbP52435.
PRIDEP52435.

Protocols and materials databases

DNASU5439.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000292614; ENSP00000292614; ENSG00000005075.
GeneID5439.
KEGGhsa:5439.
UCSCuc003uzp.1. human.

Organism-specific databases

CTD5439.
GeneCardsGC07M102113.
H-InvDBHIX0025314.
HGNCHGNC:9197. POLR2J.
HPAHPA044010.
HPA046970.
MIM604150. gene.
neXtProtNX_P52435.
PharmGKBPA33517.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1761.
HOGENOMHOG000179862.
HOVERGENHBG073419.
KOK03008.
OrthoDBEOG7GN2P7.
PhylomeDBP52435.
TreeFamTF103044.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_1788. Transcription.
REACT_1892. Elongation arrest and recovery.
REACT_216. DNA Repair.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP52435.
BgeeP52435.
CleanExHS_POLR2J.
GenevestigatorP52435.

Family and domain databases

InterProIPR009025. RBP11-like_dimer.
IPR008193. RNA_pol_Rpb11_13-16kDa_CS.
[Graphical view]
SUPFAMSSF55257. SSF55257. 1 hit.
PROSITEPS01154. RNA_POL_L_13KD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPOLR2J. human.
GeneWikiPOLR2J.
GenomeRNAi5439.
NextBio21045.
PROP52435.
SOURCESearch...

Entry information

Entry nameRPB11_HUMAN
AccessionPrimary (citable) accession number: P52435
Secondary accession number(s): A5D6V8, O43375
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 16, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM