Q5I0E6 (RPAP2_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
RNA polymerase II subunit B1 CTD phosphatase Rpap2
EC=3.1.3.16

Alternative name(s):
Putative RNA polymerase II-associated protein 2

Gene names

Name:

Rpap2

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	609 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Protein phosphatase that displays CTD phosphatase activity and regulates transcription of snRNA genes. Recognizes and binds phosphorylated 'Ser-7' of the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and mediates dephosphorylation of 'Ser-5' of the CTD, thereby promoting transcription of snRNA genes By similarity.
Catalytic activity	A phosphoprotein + H2O = a protein + phosphate.
Subunit structure	Associates with the RNA polymerase II complex. Interacts with transcribing RNA polymerase II phosphorylated on 'Ser-7' on CTD By similarity.
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Note: Shuttles between the cytoplasm and the nucleus in a CRM1-dependent manner By similarity.
Sequence similarities	Belongs to the RPAP2 family. Contains 1 RTR1-type zinc finger.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dephosphorylation of RNA polymerase II C-terminal domain Inferred from sequence or structural similarity. Source: UniProtKB snRNA transcription Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	DNA-directed RNA polymerase II, holoenzyme Inferred from sequence or structural similarity. Source: UniProtKB cytoplasm Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	CTD phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q5I0E6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q5I0E6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     214-218: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 609	609	RNA polymerase II subunit B1 CTD phosphatase Rpap2		PRO_0000250651
Regions
	Zinc finger	77 – 160	84	RTR1-type
	Coiled coil	33 – 69	37	Potential
Amino acid modifications
	Modified residue	476	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	214 – 218	5	Missing in isoform 2.		VSP_042584

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: AB4E505B6037636D	FASTA	609	67,892
	10 20 30 40 50 60 MADSAVPYSL GPSARASSTH RVATGTKQTS ALKRRDASKR QAELEAALQR KVESERRAVR 70 80 90 100 110 120 LVEQLLEENI TEEFLKECGM FITPAHYSDV VDERAIIKLC GYPLCQKKLG VIPKQKYRIS 130 140 150 160 170 180 TKTNKVYDIT ERKSFCSNFC YKASKFFEAQ IPKTPVWVRE EERPPEFQLL KKGQSGCSGE 190 200 210 220 230 240 VVQFFRDAVT AADVDAYGAF DAQCEPASSS TWSERASDER ASDEEGPGFV SSLLPGNRPK 250 260 270 280 290 300 AVGTKPQPHR QSSTVKKKAA QKMTSKHGEQ TVSEVTEQLS NCRLDSQEKV ATCKLPAKKE 310 320 330 340 350 360 NTQISSPGPL CDRLNTSTVS ENKHSVSQVT LVGISKKSAE HFRSKFAKSN PGSGSASGLV 370 380 390 400 410 420 QVRPEVAKAN LLRVLKDTLT EWKTDETLKF LYGQDHGSVC LQPSAASGPD EELDEDDISC 430 440 450 460 470 480 QAQNTLDETL PFRGSDTAIK PLPSYESLKK ETEMLNLRVR EFYRGRCVLN EDSTKSQDSK 490 500 510 520 530 540 ENELQRDPSF PLIDSSSQNQ IRRRIVLEKL SKVLPGLLGP LQITMGDIYT ELKNLVQTFR 550 560 570 580 590 600 LSNRNIIHKP VEWTLIAVVL LSLLTPILGI QKHSPKNVVF TQFIATLLTE LHLKCEDLEN LAMIFRTSC
	Isoform 2 [UniParc]. Checksum: 6DC2B969BA54B3CD	FASTA	604	67,334
	10 20 30 40 50 60 MADSAVPYSL GPSARASSTH RVATGTKQTS ALKRRDASKR QAELEAALQR KVESERRAVR 70 80 90 100 110 120 LVEQLLEENI TEEFLKECGM FITPAHYSDV VDERAIIKLC GYPLCQKKLG VIPKQKYRIS 130 140 150 160 170 180 TKTNKVYDIT ERKSFCSNFC YKASKFFEAQ IPKTPVWVRE EERPPEFQLL KKGQSGCSGE 190 200 210 220 230 240 VVQFFRDAVT AADVDAYGAF DAQCEPASSS TWSERASDEE GPGFVSSLLP GNRPKAVGTK 250 260 270 280 290 300 PQPHRQSSTV KKKAAQKMTS KHGEQTVSEV TEQLSNCRLD SQEKVATCKL PAKKENTQIS 310 320 330 340 350 360 SPGPLCDRLN TSTVSENKHS VSQVTLVGIS KKSAEHFRSK FAKSNPGSGS ASGLVQVRPE 370 380 390 400 410 420 VAKANLLRVL KDTLTEWKTD ETLKFLYGQD HGSVCLQPSA ASGPDEELDE DDISCQAQNT 430 440 450 460 470 480 LDETLPFRGS DTAIKPLPSY ESLKKETEML NLRVREFYRG RCVLNEDSTK SQDSKENELQ 490 500 510 520 530 540 RDPSFPLIDS SSQNQIRRRI VLEKLSKVLP GLLGPLQITM GDIYTELKNL VQTFRLSNRN 550 560 570 580 590 600 IIHKPVEWTL IAVVLLSLLT PILGIQKHSP KNVVFTQFIA TLLTELHLKC EDLENLAMIF RTSC

References

[1]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S. Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[2]	"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] (ISOFORM 1). Tissue: Lung.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC088426 mRNA. Translation: AAH88426.1.
IPI	IPI00363683.
RefSeq	NP_001014009.1. NM_001013987.1.
UniGene	Rn.49042.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000002815.
Proteomic databases
PaxDb	Q5I0E6.
PRIDE	Q5I0E6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000002815; ENSRNOP00000002815; ENSRNOG00000023484.
GeneID	305120.
KEGG	rno:305120.
UCSC	RGD:1309034. rat.
Organism-specific databases
CTD	79871.
RGD	1309034. Rpap2.
Phylogenomic databases
eggNOG	NOG241465.
GeneTree	ENSGT00390000017965.
HOGENOM	HOG000253960.
HOVERGEN	HBG080953.
InParanoid	Q5I0E6.
OMA	ECGKFIT.
OrthoDB	EOG44F69F.
Gene expression databases
ArrayExpress	Q5I0E6.
Genevestigator	Q5I0E6.
GermOnline	ENSRNOG00000023484. Rattus norvegicus.
Family and domain databases
InterPro	IPR007308. DUF408. [Graphical view]
Pfam	PF04181. RPAP2_Rtr1. 1 hit. [Graphical view]
PROSITE	PS51479. ZF_RTR1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	654102.

Entry information

Entry name

RPAP2_RAT

Accession

Primary (citable) accession number: Q5I0E6
Secondary accession number(s): D4A5J9, D4A672

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2006
Last sequence update:	February 15, 2005
Last modified:	April 3, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program