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Q8VC34 (RPAP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative RNA polymerase II subunit B1 CTD phosphatase Rpap2

EC=3.1.3.16
Alternative name(s):
RNA polymerase II-associated protein 2
Gene names
Name:Rpap2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length614 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + 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.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8VC34-1)

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: Q8VC34-2)

The sequence of this isoform differs from the canonical sequence as follows:
     569-570: LT → IL
     571-614: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8VC34-3)

The sequence of this isoform differs from the canonical sequence as follows:
     569-614: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q8VC34-4)

The sequence of this isoform differs from the canonical sequence as follows:
     2-79: Missing.
     569-614: Missing.
Note: No experimental confirmation available.
Isoform 5 (identifier: Q8VC34-5)

The sequence of this isoform differs from the canonical sequence as follows:
     2-77: Missing.
     78-78: C → M
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 614613Putative RNA polymerase II subunit B1 CTD phosphatase Rpap2
PRO_0000250649

Regions

Zinc finger77 – 16084RTR1-type
Coiled coil41 – 6828 Potential

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue4811Phosphoserine By similarity

Natural variations

Alternative sequence2 – 7978Missing in isoform 4.
VSP_020682
Alternative sequence2 – 7776Missing in isoform 5.
VSP_020683
Alternative sequence781C → M in isoform 5.
VSP_020684
Alternative sequence569 – 61446Missing in isoform 3 and isoform 4.
VSP_020685
Alternative sequence569 – 5702LT → IL in isoform 2.
VSP_020686
Alternative sequence571 – 61444Missing in isoform 2.
VSP_020687

Experimental info

Sequence conflict2011E → D in AAH21895. Ref.2
Sequence conflict3181K → T in AAH21895. Ref.2
Sequence conflict4441I → V in BAE26681. Ref.1
Sequence conflict5241G → V in BAE38864. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 3, 2006. Version 2.
Checksum: 3029373A246478D7

FASTA61468,530
        10         20         30         40         50         60 
MADSAVPCSL GPSTRASSTH RDATGTKQTR ALKRGDASKR QAELEAAIQR KVEFERKAVR 

        70         80         90        100        110        120 
IVEQLLEENI TEEFLKECGM FITPAHYSDV VDERSIIKLC GYPLCQKKLG VIPKQKYRIS 

       130        140        150        160        170        180 
TKTNKVYDIT ERKSFCSNFC YRASKFFETQ IPKTPVWVRE EERPPDFQLL KKGQSGSSGE 

       190        200        210        220        230        240 
VVQFFRDAVT AADVDGSGAL EAQCDPASSS SWSERASDEE EQGFVSSLLP GNRPKAVDTR 

       250        260        270        280        290        300 
PQPHTKSSIM RKKAAQNVDS KEGEQTVSEV TEQLDNCRLD SQEKVATCKR PLKKESTQIS 

       310        320        330        340        350        360 
SPGPLCDRFN TSAISEHKHG VSQVTLVGIS KKSAEHFRSK FAKSNPGSGS ASGLVHVRPE 

       370        380        390        400        410        420 
VAKANLLRVL SDTLTEWKTE ETLKFLYGQN HDSVCLKPSS ASEPDEELDE DDISCDPGSC 

       430        440        450        460        470        480 
GPALSQAQNT LDATLPFRGS DTAIKPLPSY ESLKKETEML NLRVREFYRG RCVLNEDTTK 

       490        500        510        520        530        540 
SQDSKESVLQ RDPSFPLIDS SSQNQIRRRI VLEKLSKVLP GLLGPLQITM GDIYTELKNL 

       550        560        570        580        590        600 
IQTFRLSNRN IIHKPVEWTL IAVVLLLLLT PILGIQKHSP KNVVFTQFIA TLLTELHLKF 

       610 
EDLEKLTMIF RTSC 

« Hide

Isoform 2 [UniParc].

Checksum: FC6E023D8CCD2587
Show »

FASTA57063,458
Isoform 3 [UniParc].

Checksum: 423D8CCD2587F3F5
Show »

FASTA56863,232
Isoform 4 [UniParc].

Checksum: 629644474A5F45AE
Show »

FASTA49054,635
Isoform 5 [UniParc].

Checksum: 69E8B18BADBDAEA4
Show »

FASTA53860,121

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3; 4 AND 5).
Strain: C57BL/6J.
Tissue: Diencephalon, Hippocampus, Medulla oblongata and Placenta.
[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).
Strain: C57BL/6J and FVB/N.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK034418 mRNA. Translation: BAC28703.1.
AK049889 mRNA. Translation: BAC33973.1.
AK145830 mRNA. Translation: BAE26681.1.
AK161901 mRNA. Translation: BAE36627.1.
AK166574 mRNA. Translation: BAE38864.1.
BC021895 mRNA. Translation: AAH21895.1.
CCDSCCDS19506.1. [Q8VC34-1]
CCDS51588.1. [Q8VC34-3]
CCDS51589.1. [Q8VC34-4]
RefSeqNP_001156933.1. NM_001163461.2. [Q8VC34-3]
NP_001156934.1. NM_001163462.2.
NP_001276498.1. NM_001289569.1.
NP_001276499.1. NM_001289570.1. [Q8VC34-2]
NP_659160.2. NM_144911.3. [Q8VC34-1]
XP_006534963.1. XM_006534900.1.
UniGeneMm.482420.

3D structure databases

ProteinModelPortalQ8VC34.
SMRQ8VC34. Positions 53-171.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8VC34.

Proteomic databases

PaxDbQ8VC34.
PRIDEQ8VC34.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000065422; ENSMUSP00000070209; ENSMUSG00000033773. [Q8VC34-1]
ENSMUST00000112650; ENSMUSP00000108269; ENSMUSG00000033773.
ENSMUST00000112651; ENSMUSP00000108270; ENSMUSG00000033773.
ENSMUST00000112654; ENSMUSP00000108273; ENSMUSG00000033773. [Q8VC34-3]
ENSMUST00000112655; ENSMUSP00000108274; ENSMUSG00000033773. [Q8VC34-2]
GeneID231571.
KEGGmmu:231571.
UCSCuc008ymn.2. mouse. [Q8VC34-1]
uc008ymq.2. mouse. [Q8VC34-5]

Organism-specific databases

CTD79871.
MGIMGI:2141142. Rpap2.

Phylogenomic databases

eggNOGNOG241465.
GeneTreeENSGT00390000017965.
HOGENOMHOG000253960.
HOVERGENHBG080953.
InParanoidQ8VC34.
OMAIIFRTSC.
OrthoDBEOG7XWPQD.
PhylomeDBQ8VC34.
TreeFamTF331431.

Gene expression databases

ArrayExpressQ8VC34.
BgeeQ8VC34.
CleanExMM_RPAP2.
GenevestigatorQ8VC34.

Family and domain databases

InterProIPR007308. DUF408.
[Graphical view]
PfamPF04181. RPAP2_Rtr1. 1 hit.
[Graphical view]
PROSITEPS51479. ZF_RTR1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPAP2. mouse.
NextBio380622.
PROQ8VC34.
SOURCESearch...

Entry information

Entry nameRPAP2_MOUSE
AccessionPrimary (citable) accession number: Q8VC34
Secondary accession number(s): Q3TLC8 expand/collapse secondary AC list , Q3TSP8, Q3UKX0, Q8C7M5, Q8CBW8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 3, 2006
Last modified: July 9, 2014
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot