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Q9NY27 (PP4R2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase 4 regulatory subunit 2
Gene names
Name:PPP4R2
ORF Names:SBBI57
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). May regulate the activity of PPP4C at centrosomal microtubule organizing centers. Its interaction with the SMN complex leads to enhance the temporal localization of snRNPs, suggesting a role of PPP4C in maturation of spliceosomal snRNPs. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on 'Ser-140' (gamma-H2AFX) generated during DNA replication and required for DNA double strand break repair. Mediates RPA2 dephosphorylation by recruiting PPP4C to RPA2 in a DNA damage-dependent manner. RPA2 dephosphorylation is required for the efficient RPA2-mediated recruitment of RAD51 to chromatin following double strand breaks, an essential step for DNA repair. Ref.1 Ref.6 Ref.8 Ref.12

Subunit structure

Serine/threonine-protein phosphatase 4 (PP4) occurs in different assemblies of the catalytic and one or more regulatory subunits. Component of the PP4 complexes PPP4C-PPP4R2, PPP4C-PPP4R2-PPP4R3A and PPP4C-PPP4R2-PPP4R3B. The PPP4C-PPP4R2 complex appears to be a tetramer composed of 2 molecules of PPP4C and 2 molecules of PPP4R2. Interacts with DDX20/GEMIN3 and GEMIN4. Interacts with RPA2; this DNA damage-dependent interaction recruits PPP4C leading to RPA2 dephosphorylation. Ref.6 Ref.8 Ref.12

Subcellular location

Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Nucleus. Note: Ionizing radiation induces relocalization to nuclear foci and colocalization with RPA2. Ref.1 Ref.12

Tissue specificity

Widely expressed. Ref.6

Sequence similarities

Belongs to the PPP4R2 family.

Sequence caution

The sequence AAI00282.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence CAB93534.2 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PPP4CP605108EBI-1048740,EBI-1046072

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NY27-1)

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: Q9NY27-2)

The sequence of this isoform differs from the canonical sequence as follows:
     39-96: MIQWSQFKGYFIFKLEKVMDDFRTSAPEPRGPPNPNVEYIPFDEMKERILKIVTGFNG → I
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9NY27-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 417417Serine/threonine-protein phosphatase 4 regulatory subunit 2
PRO_0000299365

Regions

Compositional bias298 – 415118Glu-rich

Amino acid modifications

Modified residue1591Phosphoserine Ref.9 Ref.11 Ref.13 Ref.15
Modified residue2261Phosphoserine Ref.9 Ref.11 Ref.13 Ref.15

Natural variations

Alternative sequence1 – 5656Missing in isoform 3.
VSP_027612
Alternative sequence39 – 9658MIQWS…TGFNG → I in isoform 2.
VSP_027613
Natural variant1741P → L.
Corresponds to variant rs2306983 [ dbSNP | Ensembl ].
VAR_051749
Natural variant2821S → C.
Corresponds to variant rs34742137 [ dbSNP | Ensembl ].
VAR_034811

Experimental info

Mutagenesis991F → A: No effect on RPA2-binding; decrease in PPP4C-binding. Ref.12
Mutagenesis1031R → A: No effect on RPA2-binding; loss of PPP4C-binding. Ref.12
Mutagenesis1061E → A: No effect on RPA2-binding, nor on PPP4C-binding. Ref.12

Sequences

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

Last modified September 11, 2007. Version 3.
Checksum: 75298CD34A202F40

FASTA41746,898
        10         20         30         40         50         60 
MDVERLQEAL KDFEKRGKKE VCPVLDQFLC HVAKTGETMI QWSQFKGYFI FKLEKVMDDF 

        70         80         90        100        110        120 
RTSAPEPRGP PNPNVEYIPF DEMKERILKI VTGFNGIPFT IQRLCELLTD PRRNYTGTDK 

       130        140        150        160        170        180 
FLRGVEKNVM VVSCVYPSSE KNNSNSLNRM NGVMFPGNSP SYTERSNING PGTPRPLNRP 

       190        200        210        220        230        240 
KVSLSAPMTT NGLPESTDSK EANLQQNEEK NHSDSSTSES EVSSVSPLKN KHPDEDAVEA 

       250        260        270        280        290        300 
EGHEVKRLRF DKEGEVRETA SQTTSSEISS VMVGETEASS SSQDKDKDSR CTRQHCTEED 

       310        320        330        340        350        360 
EEEDEEEEEE SFMTSREMIP ERKNQEKESD DALTVNEETS EENNQMEESD VSQAEKDLLH 

       370        380        390        400        410 
SEGSENEGPV SSSSSDCRET EELVGSNSSK TGEILSESSM ENDDEATEVT DEPMEQD 

« Hide

Isoform 2 [UniParc].

Checksum: 8008773931775213
Show »

FASTA36040,175
Isoform 3 [UniParc].

Checksum: 3B1868993A26757A
Show »

FASTA36140,249

References

« Hide 'large scale' references
[1]"A novel 50 kDa protein forms complexes with protein phosphatase 4 and is located at centrosomal microtubule organizing centres."
Hastie C.J., Carnegie G.K., Morrice N., Cohen P.T.W.
Biochem. J. 347:845-855(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
[2]Zhang W., Li N., Wan T., Cao X.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"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).
Tissue: Corpus callosum.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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; 2 AND 3).
Tissue: Uterus.
[6]"Protein phosphatase 4 interacts with the survival of motor neurons complex and enhances the temporal localisation of snRNPs."
Carnegie G.K., Sleeman J.E., Morrice N., Hastie C.J., Peggie M.W., Philp A., Lamond A.I., Cohen P.T.W.
J. Cell Sci. 116:1905-1913(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH PPP4C; DDX20 AND GEMIN4.
[7]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"A PP4-phosphatase complex dephosphorylates gamma-H2AX generated during DNA replication."
Chowdhury D., Xu X., Zhong X., Ahmed F., Zhong J., Liao J., Dykxhoorn D.M., Weinstock D.M., Pfeifer G.P., Lieberman J.
Mol. Cell 31:33-46(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE PPP4C-PPP4R2-PPP4R3A COMPLEX, IDENTIFICATION IN THE PPP4C-PPP4R2-PPP4R3B COMPLEX, FUNCTION OF THE PPP4C-PPP4R2-PPP4R3A COMPLEX.
[9]"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-159 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination."
Lee D.H., Pan Y., Kanner S., Sung P., Borowiec J.A., Chowdhury D.
Nat. Struct. Mol. Biol. 17:365-372(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RPA2, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-99; ARG-103 AND GLU-106.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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-159 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ271448 mRNA. Translation: CAB93534.2. Different initiation.
AF327345 mRNA. Translation: AAL56006.1.
AK289901 mRNA. Translation: BAF82590.1.
CH471055 Genomic DNA. Translation: EAW65530.1.
BC100281 mRNA. Translation: AAI00282.1. Sequence problems.
BC110889 mRNA. Translation: AAI10890.1.
BC128136 mRNA. Translation: AAI28137.1.
BC128137 mRNA. Translation: AAI28138.1.
RefSeqNP_777567.1. NM_174907.2.
UniGeneHs.431092.

3D structure databases

ProteinModelPortalQ9NY27.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127414. 25 interactions.
IntActQ9NY27. 4 interactions.
MINTMINT-8214437.
STRING9606.ENSP00000349124.

PTM databases

PhosphoSiteQ9NY27.

Polymorphism databases

DMDM158564082.

Proteomic databases

PaxDbQ9NY27.
PRIDEQ9NY27.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295862; ENSP00000295862; ENSG00000163605. [Q9NY27-3]
ENST00000356692; ENSP00000349124; ENSG00000163605. [Q9NY27-1]
ENST00000394284; ENSP00000377825; ENSG00000163605. [Q9NY27-2]
GeneID151987.
KEGGhsa:151987.
UCSCuc003dph.1. human. [Q9NY27-1]
uc003dpi.1. human. [Q9NY27-2]

Organism-specific databases

CTD151987.
GeneCardsGC03P073045.
HGNCHGNC:18296. PPP4R2.
HPAHPA034695.
MIM613822. gene.
neXtProtNX_Q9NY27.
PharmGKBPA38520.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG240518.
HOGENOMHOG000060339.
HOVERGENHBG101227.
InParanoidQ9NY27.
KOK15425.
OMANEDKNHS.
OrthoDBEOG74XS92.
PhylomeDBQ9NY27.
TreeFamTF105561.

Gene expression databases

ArrayExpressQ9NY27.
BgeeQ9NY27.
CleanExHS_PPP4R2.
GenevestigatorQ9NY27.

Family and domain databases

InterProIPR015267. PPP4R2.
[Graphical view]
PfamPF09184. PPP4R2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPP4R2. human.
GenomeRNAi151987.
NextBio86831.
PROQ9NY27.
SOURCESearch...

Entry information

Entry namePP4R2_HUMAN
AccessionPrimary (citable) accession number: Q9NY27
Secondary accession number(s): A8K1I6 expand/collapse secondary AC list , Q2TAJ9, Q498B8, Q8WXX6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: April 16, 2014
This is version 86 of the entry and version 3 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

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM