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Q5I0E6

- RPAP2_RAT

UniProt

Q5I0E6 - RPAP2_RAT

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Protein

RNA polymerase II subunit B1 CTD phosphatase Rpap2

Gene

Rpap2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri77 – 16084RTR1-typeAdd
BLAST

GO - Molecular functioni

  1. CTD phosphatase activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. dephosphorylation of RNA polymerase II C-terminal domain Source: UniProtKB
  2. snRNA transcription Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
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 namesi
Name:Rpap2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 14

Organism-specific databases

RGDi1309034. Rpap2.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity
Note: Shuttles between the cytoplasm and the nucleus in a CRM1-dependent manner.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. DNA-directed RNA polymerase II, holoenzyme Source: UniProtKB
  3. nucleolus Source: Ensembl
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 609608RNA polymerase II subunit B1 CTD phosphatase Rpap2PRO_0000250651Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei476 – 4761PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ5I0E6.
PRIDEiQ5I0E6.

Expressioni

Gene expression databases

GenevestigatoriQ5I0E6.

Interactioni

Subunit structurei

Associates with the RNA polymerase II complex. Interacts with transcribing RNA polymerase II phosphorylated on 'Ser-7' on CTD (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000002815.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili33 – 6937Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the RPAP2 family.Curated
Contains 1 RTR1-type zinc finger.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri77 – 16084RTR1-typeAdd
BLAST

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiNOG241465.
GeneTreeiENSGT00390000017965.
HOGENOMiHOG000253960.
HOVERGENiHBG080953.
InParanoidiQ5I0E6.
OMAiIIFRTSC.
OrthoDBiEOG7XWPQD.
PhylomeDBiQ5I0E6.
TreeFamiTF331431.

Family and domain databases

InterProiIPR007308. DUF408.
[Graphical view]
PfamiPF04181. RPAP2_Rtr1. 1 hit.
[Graphical view]
PROSITEiPS51479. ZF_RTR1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q5I0E6-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MADSAVPYSL GPSARASSTH RVATGTKQTS ALKRRDASKR QAELEAALQR
60 70 80 90 100
KVESERRAVR LVEQLLEENI TEEFLKECGM FITPAHYSDV VDERAIIKLC
110 120 130 140 150
GYPLCQKKLG VIPKQKYRIS TKTNKVYDIT ERKSFCSNFC YKASKFFEAQ
160 170 180 190 200
IPKTPVWVRE EERPPEFQLL KKGQSGCSGE VVQFFRDAVT AADVDAYGAF
210 220 230 240 250
DAQCEPASSS TWSERASDER ASDEEGPGFV SSLLPGNRPK AVGTKPQPHR
260 270 280 290 300
QSSTVKKKAA QKMTSKHGEQ TVSEVTEQLS NCRLDSQEKV ATCKLPAKKE
310 320 330 340 350
NTQISSPGPL CDRLNTSTVS ENKHSVSQVT LVGISKKSAE HFRSKFAKSN
360 370 380 390 400
PGSGSASGLV QVRPEVAKAN LLRVLKDTLT EWKTDETLKF LYGQDHGSVC
410 420 430 440 450
LQPSAASGPD EELDEDDISC QAQNTLDETL PFRGSDTAIK PLPSYESLKK
460 470 480 490 500
ETEMLNLRVR EFYRGRCVLN EDSTKSQDSK ENELQRDPSF PLIDSSSQNQ
510 520 530 540 550
IRRRIVLEKL SKVLPGLLGP LQITMGDIYT ELKNLVQTFR LSNRNIIHKP
560 570 580 590 600
VEWTLIAVVL LSLLTPILGI QKHSPKNVVF TQFIATLLTE LHLKCEDLEN

LAMIFRTSC
Length:609
Mass (Da):67,892
Last modified:February 15, 2005 - v1
Checksum:iAB4E505B6037636D
GO
Isoform 2 (identifier: Q5I0E6-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:604
Mass (Da):67,334
Checksum:i6DC2B969BA54B3CD
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei214 – 2185Missing in isoform 2. CuratedVSP_042584

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC088426 mRNA. Translation: AAH88426.1.
RefSeqiNP_001014009.1. NM_001013987.1. [Q5I0E6-1]
UniGeneiRn.49042.

Genome annotation databases

EnsembliENSRNOT00000002815; ENSRNOP00000002815; ENSRNOG00000023484. [Q5I0E6-1]
GeneIDi305120.
KEGGirno:305120.
UCSCiRGD:1309034. rat. [Q5I0E6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC088426 mRNA. Translation: AAH88426.1 .
RefSeqi NP_001014009.1. NM_001013987.1. [Q5I0E6-1 ]
UniGenei Rn.49042.

3D structure databases

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000002815.

Proteomic databases

PaxDbi Q5I0E6.
PRIDEi Q5I0E6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000002815 ; ENSRNOP00000002815 ; ENSRNOG00000023484 . [Q5I0E6-1 ]
GeneIDi 305120.
KEGGi rno:305120.
UCSCi RGD:1309034. rat. [Q5I0E6-1 ]

Organism-specific databases

CTDi 79871.
RGDi 1309034. Rpap2.

Phylogenomic databases

eggNOGi NOG241465.
GeneTreei ENSGT00390000017965.
HOGENOMi HOG000253960.
HOVERGENi HBG080953.
InParanoidi Q5I0E6.
OMAi IIFRTSC.
OrthoDBi EOG7XWPQD.
PhylomeDBi Q5I0E6.
TreeFami TF331431.

Miscellaneous databases

NextBioi 654102.
PROi Q5I0E6.

Gene expression databases

Genevestigatori Q5I0E6.

Family and domain databases

InterProi IPR007308. DUF408.
[Graphical view ]
Pfami PF04181. RPAP2_Rtr1. 1 hit.
[Graphical view ]
PROSITEi PS51479. ZF_RTR1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiRPAP2_RAT
AccessioniPrimary (citable) accession number: Q5I0E6
Secondary accession number(s): D4A5J9, D4A672
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: February 15, 2005
Last modified: October 29, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3