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Q8IXW5 (RPAP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
Synonyms:C1orf82
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length612 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Ref.4 Ref.8

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. Ref.4 Ref.7

Subcellular location

Cytoplasm. Nucleus. Note: Shuttles between the cytoplasm and the nucleus in a CRM1-dependent manner. Ref.8

Domain

The RTR1-type zinc finger mediates interactions with RNA polymerase II complex subunits (Ref.8).

Sequence similarities

Belongs to the RPAP2 family.

Contains 1 RTR1-type zinc finger.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IXW5-1)

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: Q8IXW5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     563-596: LLTPILGIQKHSQEGMVFTRFLDTLLEELHLKNE → FLLNVKTRIKTFMMIYFHLMNS
     597-612: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 612611Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2
PRO_0000250648

Regions

Zinc finger77 – 16084RTR1-type
Coiled coil33 – 6836 Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.9
Modified residue4331Phosphoserine Ref.5
Modified residue4801Phosphoserine Ref.6

Natural variations

Alternative sequence563 – 59634LLTPI…HLKNE → FLLNVKTRIKTFMMIYFHLM NS in isoform 2.
VSP_020680
Alternative sequence597 – 61216Missing in isoform 2.
VSP_020681

Experimental info

Mutagenesis1001C → A: Abolishes interaction with RNA polymerase II complex subunits; when associated with A-105. Ref.8
Mutagenesis1051C → A: Abolishes interaction with RNA polymerase II complex subunits; when associated with A-100. Ref.8
Mutagenesis1361C → A: Abolishes interaction with RNA polymerase II complex subunits; when associated with A-140. Ref.8
Mutagenesis1401C → A: Abolishes interaction with RNA polymerase II complex subunits; when associated with A-136. Ref.8
Sequence conflict4211P → R in AAH31070. Ref.3
Sequence conflict4671Y → C in BAB14465. Ref.1
Isoform 2:
Sequence conflict5841S → N in AAH31070. Ref.3

Sequences

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

Last modified March 1, 2003. Version 1.
Checksum: 43D6DE7C30BB5C96

FASTA61269,509
        10         20         30         40         50         60 
MADFAGPSSA GRKAGAPRCS RKAAGTKQTS TLKQEDASKR KAELEAAVRK KIEFERKALH 

        70         80         90        100        110        120 
IVEQLLEENI TEEFLMECGR FITPAHYSDV VDERSIVKLC GYPLCQKKLG IVPKQKYKIS 

       130        140        150        160        170        180 
TKTNKVYDIT ERKSFCSNFC YQASKFFEAQ IPKTPVWVRE EERHPDFQLL KEEQSGHSGE 

       190        200        210        220        230        240 
EVQLCSKAIK TSDIDNPSHF EKQYESSSSS THSDSSSDNE QDFVSSILPG NRPNSTNIRP 

       250        260        270        280        290        300 
QLHQKSIMKK KAGHKANSKH KDKEQTVVDV TEQLGDCKLD SQEKDATCEL PLQKVNTQSS 

       310        320        330        340        350        360 
SNSTLPERLK ASENSESEYS RSEITLVGIS KKSAEHFKRK FAKSNQVSRS VSSSVQVCPE 

       370        380        390        400        410        420 
VGKRNLLKVL KETLIEWKTE ETLRFLYGQN YASVCLKPEA SLVKEELDED DIISDPDSHF 

       430        440        450        460        470        480 
PAWRESQNSL DESLPFRGSG TAIKPLPSYE NLKKETEKLN LRIREFYRGR YVLGEETTKS 

       490        500        510        520        530        540 
QDSEEHDSTF PLIDSSSQNQ IRKRIVLEKL SKVLPGLLVP LQITLGDIYT QLKNLVRTFR 

       550        560        570        580        590        600 
LTNRNIIHKP AEWTLIAMVL LSLLTPILGI QKHSQEGMVF TRFLDTLLEE LHLKNEDLES 

       610 
LTIIFRTSCL PE 

« Hide

Isoform 2 [UniParc].

Checksum: C01259C16617931A
Show »

FASTA58466,473

References

« Hide 'large scale' references
[1]"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] (ISOFORM 1).
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] (ISOFORMS 1 AND 2).
Tissue: Brain.
[4]"Systematic analysis of the protein interaction network for the human transcription machinery reveals the identity of the 7SK capping enzyme."
Jeronimo C., Forget D., Bouchard A., Li Q., Chua G., Poitras C., Therien C., Bergeron D., Bourassa S., Greenblatt J., Chabot B., Poirier G.G., Hughes T.R., Blanchette M., Price D.H., Coulombe B.
Mol. Cell 27:262-274(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE RNA POLYMERASE II COMPLEX.
[5]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Control of the RNA polymerase II phosphorylation state in promoter regions by CTD interaction domain-containing proteins RPRD1A and RPRD1B."
Ni Z., Olsen J.B., Guo X., Zhong G., Ruan E.D., Marcon E., Young P., Guo H., Li J., Moffat J., Emili A., Greenblatt J.F.
Transcription 2:237-242(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE RNA POLYMERASE II COMPLEX.
[8]"Ser7 phosphorylation of the CTD recruits the RPAP2 Ser5 phosphatase to snRNA genes."
Egloff S., Zaborowska J., Laitem C., Kiss T., Murphy S.
Mol. Cell 45:111-122(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-100; CYS-105; CYS-136 AND CYS-140.
[9]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK023212 mRNA. Translation: BAB14465.1.
AL451010 Genomic DNA. Translation: CAH70763.1.
BC031070 mRNA. Translation: AAH31070.1.
BC039014 mRNA. Translation: AAH39014.1.
CCDSCCDS740.1. [Q8IXW5-1]
RefSeqNP_079089.2. NM_024813.2. [Q8IXW5-1]
UniGeneHs.444421.

3D structure databases

ProteinModelPortalQ8IXW5.
SMRQ8IXW5. Positions 53-174.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122959. 47 interactions.
IntActQ8IXW5. 3 interactions.
STRING9606.ENSP00000359368.

PTM databases

PhosphoSiteQ8IXW5.

Polymorphism databases

DMDM74750745.

Proteomic databases

MaxQBQ8IXW5.
PaxDbQ8IXW5.
PRIDEQ8IXW5.

Protocols and materials databases

DNASU79871.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000610020; ENSP00000476948; ENSG00000122484. [Q8IXW5-1]
GeneID79871.
KEGGhsa:79871.
UCSCuc001dot.2. human. [Q8IXW5-1]

Organism-specific databases

CTD79871.
GeneCardsGC01P092764.
HGNCHGNC:25791. RPAP2.
HPAHPA046443.
MIM611476. gene.
neXtProtNX_Q8IXW5.
PharmGKBPA162401981.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG241465.
HOGENOMHOG000253960.
HOVERGENHBG080953.
InParanoidQ8IXW5.
OMAIIFRTSC.
OrthoDBEOG7XWPQD.
PhylomeDBQ8IXW5.
TreeFamTF331431.

Gene expression databases

BgeeQ8IXW5.
CleanExHS_RPAP2.
GenevestigatorQ8IXW5.

Family and domain databases

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

Other

GeneWikiRPAP2.
GenomeRNAi79871.
NextBio69637.
PROQ8IXW5.
SOURCESearch...

Entry information

Entry nameRPAP2_HUMAN
AccessionPrimary (citable) accession number: Q8IXW5
Secondary accession number(s): C9JKB5, Q49AS7, Q9H8Y2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 93 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

Uncharacterized protein families (UPF)

List of uncharacterized protein family (UPF) entries

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 1

Human chromosome 1: entries, gene names and cross-references to MIM