Q8IXW5 (RPAP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	612 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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. 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.

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 mutant phenotype Ref.8. Source: UniProtKB snRNA transcription Inferred from mutant phenotype Ref.8. Source: UniProtKB
Cellular_component	DNA-directed RNA polymerase II, holoenzyme Inferred from direct assay Ref.8Ref.7. Source: UniProtKB cytoplasm Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	CTD phosphatase activity Inferred from mutant phenotype Ref.8. 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: 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 612	612	Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2		PRO_0000250648
Regions
	Zinc finger	77 – 160	84	RTR1-type
	Coiled coil	33 – 68	36	Potential
Amino acid modifications
	Modified residue	433	1	Phosphoserine Ref.5
	Modified residue	480	1	Phosphoserine Ref.6
Natural variations
	Alternative sequence	563 – 596	34	LLTPI…HLKNE → FLLNVKTRIKTFMMIYFHLM NS in isoform 2.		VSP_020680
	Alternative sequence	597 – 612	16	Missing in isoform 2.		VSP_020681
Experimental info
	Mutagenesis	100	1	C → A: Abolishes interaction with RNA polymerase II complex subunits; when associated with A-105. Ref.8
	Mutagenesis	105	1	C → A: Abolishes interaction with RNA polymerase II complex subunits; when associated with A-100. Ref.8
	Mutagenesis	136	1	C → A: Abolishes interaction with RNA polymerase II complex subunits; when associated with A-140. Ref.8
	Mutagenesis	140	1	C → A: Abolishes interaction with RNA polymerase II complex subunits; when associated with A-136. Ref.8
	Sequence conflict	421	1	P → R in AAH31070. Ref.3
	Sequence conflict	467	1	Y → C in BAB14465. Ref.1
Isoform 2:
	Sequence conflict	584	1	S → N in AAH31070. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 43D6DE7C30BB5C96	FASTA	612	69,509
	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
	Isoform 2 [UniParc]. Checksum: C01259C16617931A	FASTA	584	66,473
	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 LTNRNIIHKP AEWTLIAMVL LSFLLNVKTR IKTFMMIYFH LMNS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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.

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.
IPI	IPI00293375. IPI00787580.
RefSeq	NP_079089.2. NM_024813.2.
UniGene	Hs.444421.
3D structure databases
ProteinModelPortal	Q8IXW5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8IXW5. 3 interactions.
STRING	9606.ENSP00000359368.
PTM databases
PhosphoSite	Q8IXW5.
Polymorphism databases
DMDM	74750745.
Proteomic databases
PaxDb	Q8IXW5.
PRIDE	Q8IXW5.
Protocols and materials databases
DNASU	79871.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000370343; ENSP00000359368; ENSG00000122484.
GeneID	79871.
KEGG	hsa:79871.
UCSC	uc001dot.2. human.
Organism-specific databases
CTD	79871.
GeneCards	GC01P092764.
HGNC	HGNC:25791. RPAP2.
HPA	HPA046443.
MIM	611476. gene.
neXtProt	NX_Q8IXW5.
PharmGKB	PA162401981.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG241465.
HOGENOM	HOG000253960.
HOVERGEN	HBG080953.
InParanoid	Q8IXW5.
OMA	ECGKFIT.
OrthoDB	EOG44F69F.
PhylomeDB	Q8IXW5.
Gene expression databases
Bgee	Q8IXW5.
CleanEx	HS_RPAP2.
Genevestigator	Q8IXW5.
GermOnline	ENSG00000122484. Homo sapiens.
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
GenomeRNAi	79871.
NextBio	69637.
SOURCE	Search...

Entry information

Entry name

RPAP2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 83 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.