PP4R2_HUMAN
ID PP4R2_HUMAN Reviewed; 417 AA.
AC Q9NY27; A8K1I6; Q2TAJ9; Q498B8; Q8WXX6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 2;
GN Name=PPP4R2; ORFNames=SBBI57;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10769191; DOI=10.1042/bj3470845;
RA Hastie C.J., Carnegie G.K., Morrice N., Cohen P.T.W.;
RT "A novel 50 kDa protein forms complexes with protein phosphatase 4 and is
RT located at centrosomal microtubule organizing centres.";
RL Biochem. J. 347:845-855(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Zhang W., Li N., Wan T., Cao X.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Corpus callosum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH PPP4C; DDX20 AND GEMIN4.
RX PubMed=12668731; DOI=10.1242/jcs.00409;
RA Carnegie G.K., Sleeman J.E., Morrice N., Hastie C.J., Peggie M.W.,
RA Philp A., Lamond A.I., Cohen P.T.W.;
RT "Protein phosphatase 4 interacts with the survival of motor neurons complex
RT and enhances the temporal localisation of snRNPs.";
RL J. Cell Sci. 116:1905-1913(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP IDENTIFICATION IN THE PPP4C-PPP4R2-PPP4R3A COMPLEX, IDENTIFICATION IN THE
RP PPP4C-PPP4R2-PPP4R3B COMPLEX, AND FUNCTION OF THE PPP4C-PPP4R2-PPP4R3A
RP COMPLEX.
RX PubMed=18614045; DOI=10.1016/j.molcel.2008.05.016;
RA Chowdhury D., Xu X., Zhong X., Ahmed F., Zhong J., Liao J., Dykxhoorn D.M.,
RA Weinstock D.M., Pfeifer G.P., Lieberman J.;
RT "A PP4-phosphatase complex dephosphorylates gamma-H2AX generated during DNA
RT replication.";
RL Mol. Cell 31:33-46(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-226, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-226, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP FUNCTION, INTERACTION WITH RPA2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP PHE-99; ARG-103 AND GLU-106.
RX PubMed=20154705; DOI=10.1038/nsmb.1769;
RA Lee D.H., Pan Y., Kanner S., Sung P., Borowiec J.A., Chowdhury D.;
RT "A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair
RT via homologous recombination.";
RL Nat. Struct. Mol. Biol. 17:365-372(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-226, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-226, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-226, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Regulatory subunit of serine/threonine-protein phosphatase 4
CC (PP4). May regulate the activity of PPP4C at centrosomal microtubule
CC organizing centers. Its interaction with the SMN complex leads to
CC enhance the temporal localization of snRNPs, suggesting a role of PPP4C
CC in maturation of spliceosomal snRNPs. The PPP4C-PPP4R2-PPP4R3A PP4
CC complex specifically dephosphorylates H2AX phosphorylated on 'Ser-140'
CC (gamma-H2AX) generated during DNA replication and required for DNA
CC double strand break repair. Mediates RPA2 dephosphorylation by
CC recruiting PPP4C to RPA2 in a DNA damage-dependent manner. RPA2
CC dephosphorylation is required for the efficient RPA2-mediated
CC recruitment of RAD51 to chromatin following double strand breaks, an
CC essential step for DNA repair. {ECO:0000269|PubMed:10769191,
CC ECO:0000269|PubMed:12668731, ECO:0000269|PubMed:18614045,
CC ECO:0000269|PubMed:20154705}.
CC -!- SUBUNIT: Serine/threonine-protein phosphatase 4 (PP4) occurs in
CC different assemblies of the catalytic and one or more regulatory
CC subunits. Component of the PP4 complexes PPP4C-PPP4R2, PPP4C-PPP4R2-
CC PPP4R3A and PPP4C-PPP4R2-PPP4R3B. The PPP4C-PPP4R2 complex appears to
CC be a tetramer composed of 2 molecules of PPP4C and 2 molecules of
CC PPP4R2. Interacts with DDX20/GEMIN3 and GEMIN4. Interacts with RPA2;
CC this DNA damage-dependent interaction recruits PPP4C leading to RPA2
CC dephosphorylation. {ECO:0000269|PubMed:12668731,
CC ECO:0000269|PubMed:18614045, ECO:0000269|PubMed:20154705}.
CC -!- INTERACTION:
CC Q9NY27; P60510: PPP4C; NbExp=14; IntAct=EBI-1048740, EBI-1046072;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome. Nucleus. Note=Ionizing radiation induces
CC relocalization to nuclear foci and colocalization with RPA2.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9NY27-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NY27-2; Sequence=VSP_027613;
CC Name=3;
CC IsoId=Q9NY27-3; Sequence=VSP_027612;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12668731}.
CC -!- SIMILARITY: Belongs to the PPP4R2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI00282.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=CAB93534.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ271448; CAB93534.2; ALT_INIT; mRNA.
DR EMBL; AF327345; AAL56006.1; -; mRNA.
DR EMBL; AK289901; BAF82590.1; -; mRNA.
DR EMBL; CH471055; EAW65530.1; -; Genomic_DNA.
DR EMBL; BC100281; AAI00282.1; ALT_SEQ; mRNA.
DR EMBL; BC110889; AAI10890.1; -; mRNA.
DR EMBL; BC128136; AAI28137.1; -; mRNA.
DR EMBL; BC128137; AAI28138.1; -; mRNA.
DR CCDS; CCDS2917.1; -. [Q9NY27-1]
DR RefSeq; NP_001304954.1; NM_001318025.1. [Q9NY27-2]
DR RefSeq; NP_001304955.1; NM_001318026.1.
DR RefSeq; NP_001304956.1; NM_001318027.1.
DR RefSeq; NP_777567.1; NM_174907.3. [Q9NY27-1]
DR AlphaFoldDB; Q9NY27; -.
DR BioGRID; 127414; 93.
DR ComplexPortal; CPX-156; PPP4C-PPP4R2 protein phosphatase 4 complex.
DR ComplexPortal; CPX-1843; PPP4C-PPP4R2-PPP4R3A protein phosphatase 4 complex.
DR ComplexPortal; CPX-1844; PPP4C-PPP4R2-PPP4R3B protein phosphatase 4 complex.
DR CORUM; Q9NY27; -.
DR IntAct; Q9NY27; 43.
DR MINT; Q9NY27; -.
DR STRING; 9606.ENSP00000349124; -.
DR GlyGen; Q9NY27; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NY27; -.
DR MetOSite; Q9NY27; -.
DR PhosphoSitePlus; Q9NY27; -.
DR SwissPalm; Q9NY27; -.
DR BioMuta; PPP4R2; -.
DR DMDM; 158564082; -.
DR EPD; Q9NY27; -.
DR jPOST; Q9NY27; -.
DR MassIVE; Q9NY27; -.
DR MaxQB; Q9NY27; -.
DR PaxDb; Q9NY27; -.
DR PeptideAtlas; Q9NY27; -.
DR PRIDE; Q9NY27; -.
DR ProteomicsDB; 83154; -. [Q9NY27-1]
DR ProteomicsDB; 83155; -. [Q9NY27-2]
DR ProteomicsDB; 83156; -. [Q9NY27-3]
DR Antibodypedia; 35014; 170 antibodies from 25 providers.
DR DNASU; 151987; -.
DR Ensembl; ENST00000356692.10; ENSP00000349124.5; ENSG00000163605.15. [Q9NY27-1]
DR GeneID; 151987; -.
DR KEGG; hsa:151987; -.
DR MANE-Select; ENST00000356692.10; ENSP00000349124.5; NM_174907.4; NP_777567.1.
DR UCSC; uc003dph.2; human. [Q9NY27-1]
DR CTD; 151987; -.
DR DisGeNET; 151987; -.
DR GeneCards; PPP4R2; -.
DR HGNC; HGNC:18296; PPP4R2.
DR HPA; ENSG00000163605; Low tissue specificity.
DR MIM; 613822; gene.
DR neXtProt; NX_Q9NY27; -.
DR OpenTargets; ENSG00000163605; -.
DR PharmGKB; PA38520; -.
DR VEuPathDB; HostDB:ENSG00000163605; -.
DR eggNOG; KOG3175; Eukaryota.
DR GeneTree; ENSGT00940000160975; -.
DR HOGENOM; CLU_043908_1_1_1; -.
DR InParanoid; Q9NY27; -.
DR OMA; PMEDTPV; -.
DR OrthoDB; 774806at2759; -.
DR PhylomeDB; Q9NY27; -.
DR TreeFam; TF105561; -.
DR PathwayCommons; Q9NY27; -.
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR SignaLink; Q9NY27; -.
DR BioGRID-ORCS; 151987; 399 hits in 1052 CRISPR screens.
DR ChiTaRS; PPP4R2; human.
DR GenomeRNAi; 151987; -.
DR Pharos; Q9NY27; Tbio.
DR PRO; PR:Q9NY27; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9NY27; protein.
DR Bgee; ENSG00000163605; Expressed in secondary oocyte and 189 other tissues.
DR ExpressionAtlas; Q9NY27; baseline and differential.
DR Genevisible; Q9NY27; HS.
DR GO; GO:0005813; C:centrosome; TAS:ProtInc.
DR GO; GO:0000785; C:chromatin; IDA:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0030289; C:protein phosphatase 4 complex; IDA:UniProtKB.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IMP:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IMP:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0033128; P:negative regulation of histone phosphorylation; IMP:ComplexPortal.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
DR GO; GO:2000779; P:regulation of double-strand break repair; IMP:ComplexPortal.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR015267; PPP4R2.
DR PANTHER; PTHR16487; PTHR16487; 1.
DR Pfam; PF09184; PPP4R2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..417
FT /note="Serine/threonine-protein phosphatase 4 regulatory
FT subunit 2"
FT /id="PRO_0000299365"
FT REGION 140..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..312
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..363
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..396
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..417
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027612"
FT VAR_SEQ 39..96
FT /note="MIQWSQFKGYFIFKLEKVMDDFRTSAPEPRGPPNPNVEYIPFDEMKERILKI
FT VTGFNG -> I (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027613"
FT VARIANT 174
FT /note="P -> L (in dbSNP:rs2306983)"
FT /id="VAR_051749"
FT VARIANT 282
FT /note="S -> C (in dbSNP:rs34742137)"
FT /id="VAR_034811"
FT MUTAGEN 99
FT /note="F->A: No effect on RPA2-binding; decrease in PPP4C-
FT binding."
FT /evidence="ECO:0000269|PubMed:20154705"
FT MUTAGEN 103
FT /note="R->A: No effect on RPA2-binding; loss of PPP4C-
FT binding."
FT /evidence="ECO:0000269|PubMed:20154705"
FT MUTAGEN 106
FT /note="E->A: No effect on RPA2-binding, nor on PPP4C-
FT binding."
FT /evidence="ECO:0000269|PubMed:20154705"
SQ SEQUENCE 417 AA; 46898 MW; 75298CD34A202F40 CRC64;
MDVERLQEAL KDFEKRGKKE VCPVLDQFLC HVAKTGETMI QWSQFKGYFI FKLEKVMDDF
RTSAPEPRGP PNPNVEYIPF DEMKERILKI VTGFNGIPFT IQRLCELLTD PRRNYTGTDK
FLRGVEKNVM VVSCVYPSSE KNNSNSLNRM NGVMFPGNSP SYTERSNING PGTPRPLNRP
KVSLSAPMTT NGLPESTDSK EANLQQNEEK NHSDSSTSES EVSSVSPLKN KHPDEDAVEA
EGHEVKRLRF DKEGEVRETA SQTTSSEISS VMVGETEASS SSQDKDKDSR CTRQHCTEED
EEEDEEEEEE SFMTSREMIP ERKNQEKESD DALTVNEETS EENNQMEESD VSQAEKDLLH
SEGSENEGPV SSSSSDCRET EELVGSNSSK TGEILSESSM ENDDEATEVT DEPMEQD
