P52435 (RPB11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	117 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription
Cellular component	DNA-directed RNA polymerase Nucleus
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	7-methylguanosine mRNA capping Traceable author statement. Source: Reactome mRNA splicing, via spliceosome Traceable author statement. Source: Reactome positive regulation of viral transcription Traceable author statement. Source: Reactome protein phosphorylation Inferred from direct assay Ref.7. Source: GOC transcription elongation from RNA polymerase II promoter Traceable author statement. Source: Reactome transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome transcription-coupled nucleotide-excision repair Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome
Cellular_component	DNA-directed RNA polymerase II, core complex Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	DNA binding Inferred from electronic annotation. Source: InterPro DNA-directed RNA polymerase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 117	117	DNA-directed RNA polymerase II subunit RPB11-a		PRO_0000149309
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P52435 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 6F78AB256EF8F647	FASTA	117	13,293
	10 20 30 40 50 60 MNAPPAFESF LLFEGEKKIT INKDTKVPNA CLFTINKEDH TLGNIIKSQL LKDPQVLFAG 70 80 90 100 110 YKVPHPLEHK IIIRVQTTPD YSPQEAFTNA ITDLISELSL LEERFRVAIK DKQEGIE

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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.
IPI	IPI00939577.
PIR	S71325.
RefSeq	NP_006225.1. NM_006234.4.
UniGene	Hs.654952.
3D structure databases
ProteinModelPortal	P52435.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-32913N.
IntAct	P52435. 12 interactions.
MINT	MINT-131416.
STRING	9606.ENSP00000292614.
PTM databases
PhosphoSite	P52435.
Polymorphism databases
DMDM	1710661.
Proteomic databases
PaxDb	P52435.
PRIDE	P52435.
Protocols and materials databases
DNASU	5439.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000292614; ENSP00000292614; ENSG00000005075.
GeneID	5439.
KEGG	hsa:5439.
UCSC	uc003uzp.1. human.
Organism-specific databases
CTD	5439.
GeneCards	GC07M102113.
H-InvDB	HIX0025314.
HGNC	HGNC:9197. POLR2J.
HPA	HPA044010. HPA046970.
MIM	604150. gene.
neXtProt	NX_P52435.
PharmGKB	PA33517.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1761.
HOGENOM	HOG000179862.
HOVERGEN	HBG073419.
KO	K03008.
OrthoDB	EOG4FJ8B1.
Enzyme and pathway databases
Reactome	REACT_116125. Disease. REACT_1675. mRNA Processing. REACT_1788. Transcription. REACT_1892. Elongation arrest and recovery. REACT_216. DNA Repair. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	P52435.
Bgee	P52435.
CleanEx	HS_POLR2J.
Genevestigator	P52435.
GermOnline	ENSG00000005075. Homo sapiens.
Family and domain databases
InterPro	IPR009025. DNA-dir_RNA_pol_RBP11-like. IPR008193. RNA_pol_Rpb11_13-16kDa_CS. [Graphical view]
SUPFAM	SSF55257. RNAP_RBP11-like. 1 hit.
PROSITE	PS01154. RNA_POL_L_13KD. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	POLR2J. human.
GenomeRNAi	5439.
NextBio	21045.
SOURCE	Search...

Entry information

Entry name

RPB11_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 122 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.