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Q9NY27

- PP4R2_HUMAN

UniProt

Q9NY27 - PP4R2_HUMAN

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Protein

Serine/threonine-protein phosphatase 4 regulatory subunit 2

Gene

PPP4R2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  1. protein binding, bridging Source: UniProtKB
  2. protein phosphatase type 4 regulator activity Source: UniProtKB

GO - Biological processi

  1. cellular protein modification process Source: ProtInc
  2. hematopoietic progenitor cell differentiation Source: Ensembl
  3. mRNA processing Source: UniProtKB-KW
  4. regulation of catalytic activity Source: GOC
  5. regulation of double-strand break repair via homologous recombination Source: UniProtKB
  6. RNA splicing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 4 regulatory subunit 2
Gene namesi
Name:PPP4R2
ORF Names:SBBI57
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:18296. PPP4R2.

Subcellular locationi

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

GO - Cellular componenti

  1. centrosome Source: ProtInc
  2. cytoplasm Source: UniProtKB-KW
  3. nucleus Source: UniProtKB
  4. protein phosphatase 4 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi99 – 991F → A: No effect on RPA2-binding; decrease in PPP4C-binding. 1 Publication
Mutagenesisi103 – 1031R → A: No effect on RPA2-binding; loss of PPP4C-binding. 1 Publication
Mutagenesisi106 – 1061E → A: No effect on RPA2-binding, nor on PPP4C-binding. 1 Publication

Organism-specific databases

PharmGKBiPA38520.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 417417Serine/threonine-protein phosphatase 4 regulatory subunit 2PRO_0000299365Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei159 – 1591Phosphoserine4 Publications
Modified residuei226 – 2261Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NY27.
PaxDbiQ9NY27.
PRIDEiQ9NY27.

PTM databases

PhosphoSiteiQ9NY27.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ9NY27.
CleanExiHS_PPP4R2.
ExpressionAtlasiQ9NY27. baseline and differential.
GenevestigatoriQ9NY27.

Organism-specific databases

HPAiHPA034695.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PPP4CP605108EBI-1048740,EBI-1046072

Protein-protein interaction databases

BioGridi127414. 30 interactions.
IntActiQ9NY27. 4 interactions.
MINTiMINT-8214437.
STRINGi9606.ENSP00000349124.

Structurei

3D structure databases

ProteinModelPortaliQ9NY27.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi298 – 415118Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the PPP4R2 family.Curated

Phylogenomic databases

eggNOGiNOG240518.
GeneTreeiENSGT00390000007637.
HOGENOMiHOG000060339.
HOVERGENiHBG101227.
InParanoidiQ9NY27.
KOiK15425.
OMAiPVKNKHS.
OrthoDBiEOG74XS92.
PhylomeDBiQ9NY27.
TreeFamiTF105561.

Family and domain databases

InterProiIPR015267. PPP4R2.
[Graphical view]
PfamiPF09184. PPP4R2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NY27-1) [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
MDVERLQEAL KDFEKRGKKE VCPVLDQFLC HVAKTGETMI QWSQFKGYFI
60 70 80 90 100
FKLEKVMDDF RTSAPEPRGP PNPNVEYIPF DEMKERILKI VTGFNGIPFT
110 120 130 140 150
IQRLCELLTD PRRNYTGTDK FLRGVEKNVM VVSCVYPSSE KNNSNSLNRM
160 170 180 190 200
NGVMFPGNSP SYTERSNING PGTPRPLNRP KVSLSAPMTT NGLPESTDSK
210 220 230 240 250
EANLQQNEEK NHSDSSTSES EVSSVSPLKN KHPDEDAVEA EGHEVKRLRF
260 270 280 290 300
DKEGEVRETA SQTTSSEISS VMVGETEASS SSQDKDKDSR CTRQHCTEED
310 320 330 340 350
EEEDEEEEEE SFMTSREMIP ERKNQEKESD DALTVNEETS EENNQMEESD
360 370 380 390 400
VSQAEKDLLH SEGSENEGPV SSSSSDCRET EELVGSNSSK TGEILSESSM
410
ENDDEATEVT DEPMEQD
Length:417
Mass (Da):46,898
Last modified:September 11, 2007 - v3
Checksum:i75298CD34A202F40
GO
Isoform 2 (identifier: Q9NY27-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     39-96: MIQWSQFKGYFIFKLEKVMDDFRTSAPEPRGPPNPNVEYIPFDEMKERILKIVTGFNG → I

Note: No experimental confirmation available.

Show »
Length:360
Mass (Da):40,175
Checksum:i8008773931775213
GO
Isoform 3 (identifier: Q9NY27-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-56: Missing.

Note: No experimental confirmation available.

Show »
Length:361
Mass (Da):40,249
Checksum:i3B1868993A26757A
GO

Sequence cautioni

The sequence AAI00282.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated
The sequence CAB93534.2 differs from that shown. Reason: Erroneous initiation. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti174 – 1741P → L.
Corresponds to variant rs2306983 [ dbSNP | Ensembl ].
VAR_051749
Natural varianti282 – 2821S → C.
Corresponds to variant rs34742137 [ dbSNP | Ensembl ].
VAR_034811

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5656Missing in isoform 3. 1 PublicationVSP_027612Add
BLAST
Alternative sequencei39 – 9658MIQWS…TGFNG → I in isoform 2. 1 PublicationVSP_027613Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2917.1. [Q9NY27-1]
RefSeqiNP_777567.1. NM_174907.2. [Q9NY27-1]
UniGeneiHs.431092.

Genome annotation databases

EnsembliENST00000356692; ENSP00000349124; ENSG00000163605. [Q9NY27-1]
GeneIDi151987.
KEGGihsa:151987.
UCSCiuc003dph.1. human. [Q9NY27-1]
uc003dpi.1. human. [Q9NY27-2]

Polymorphism databases

DMDMi158564082.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS2917.1. [Q9NY27-1 ]
RefSeqi NP_777567.1. NM_174907.2. [Q9NY27-1 ]
UniGenei Hs.431092.

3D structure databases

ProteinModelPortali Q9NY27.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 127414. 30 interactions.
IntActi Q9NY27. 4 interactions.
MINTi MINT-8214437.
STRINGi 9606.ENSP00000349124.

PTM databases

PhosphoSitei Q9NY27.

Polymorphism databases

DMDMi 158564082.

Proteomic databases

MaxQBi Q9NY27.
PaxDbi Q9NY27.
PRIDEi Q9NY27.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356692 ; ENSP00000349124 ; ENSG00000163605 . [Q9NY27-1 ]
GeneIDi 151987.
KEGGi hsa:151987.
UCSCi uc003dph.1. human. [Q9NY27-1 ]
uc003dpi.1. human. [Q9NY27-2 ]

Organism-specific databases

CTDi 151987.
GeneCardsi GC03P073045.
HGNCi HGNC:18296. PPP4R2.
HPAi HPA034695.
MIMi 613822. gene.
neXtProti NX_Q9NY27.
PharmGKBi PA38520.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG240518.
GeneTreei ENSGT00390000007637.
HOGENOMi HOG000060339.
HOVERGENi HBG101227.
InParanoidi Q9NY27.
KOi K15425.
OMAi PVKNKHS.
OrthoDBi EOG74XS92.
PhylomeDBi Q9NY27.
TreeFami TF105561.

Miscellaneous databases

ChiTaRSi PPP4R2. human.
GenomeRNAii 151987.
NextBioi 86831.
PROi Q9NY27.
SOURCEi Search...

Gene expression databases

Bgeei Q9NY27.
CleanExi HS_PPP4R2.
ExpressionAtlasi Q9NY27. baseline and differential.
Genevestigatori Q9NY27.

Family and domain databases

InterProi IPR015267. PPP4R2.
[Graphical view ]
Pfami PF09184. PPP4R2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 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].

Entry informationi

Entry nameiPP4R2_HUMAN
AccessioniPrimary (citable) accession number: Q9NY27
Secondary accession number(s): A8K1I6
, Q2TAJ9, Q498B8, Q8WXX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: September 11, 2007
Last modified: October 29, 2014
This is version 91 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3