PP6R2_HUMAN
ID PP6R2_HUMAN Reviewed; 966 AA.
AC O75170; A6PVG3; B7Z7T3; Q5U5P3; Q7Z2L2; Q7Z5G5; Q7Z731; Q9UGB9;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Serine/threonine-protein phosphatase 6 regulatory subunit 2;
DE AltName: Full=SAPS domain family member 2;
GN Name=PPP6R2; Synonyms=KIAA0685, PP6R2, SAPS2;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 6).
RC TISSUE=Brain, Lymph, Muscle, Placenta, and Skin;
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 [5]
RP FUNCTION, INTERACTION WITH PPP6C AND NFKBIE, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=16769727; DOI=10.1074/jbc.m601772200;
RA Stefansson B., Brautigan D.L.;
RT "Protein phosphatase 6 subunit with conserved Sit4-associated protein
RT domain targets IkappaBepsilon.";
RL J. Biol. Chem. 281:22624-22634(2006).
RN [6]
RP INTERACTION WITH PPP6C AND ANKRD28.
RX PubMed=18186651; DOI=10.1021/bi7022877;
RA Stefansson B., Ohama T., Daugherty A.E., Brautigan D.L.;
RT "Protein phosphatase 6 regulatory subunits composed of ankyrin repeat
RT domains.";
RL Biochemistry 47:1442-1451(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND IDENTIFICATION BY
RP 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND IDENTIFICATION BY
RP 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND SER-828, 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).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Regulatory subunit of protein phosphatase 6 (PP6). May
CC function as a scaffolding PP6 subunit. Involved in the PP6-mediated
CC dephosphorylation of NFKBIE opposing its degradation in response to
CC TNF-alpha. {ECO:0000269|PubMed:16769727}.
CC -!- SUBUNIT: Protein phosphatase 6 (PP6) holoenzyme is proposed to be a
CC heterotrimeric complex formed by the catalytic subunit, a SAPS domain-
CC containing subunit (PP6R) and an ankyrin repeat-domain containing
CC regulatory subunit (ARS). Interacts with PPP6C and NFKBIE. Interacts
CC with ANKRD28. {ECO:0000269|PubMed:16769727,
CC ECO:0000269|PubMed:18186651}.
CC -!- INTERACTION:
CC O75170; O15084: ANKRD28; NbExp=7; IntAct=EBI-359739, EBI-359567;
CC O75170; O00221: NFKBIE; NbExp=2; IntAct=EBI-359739, EBI-355098;
CC O75170; O00743: PPP6C; NbExp=9; IntAct=EBI-359739, EBI-359751;
CC O75170-4; P42858: HTT; NbExp=3; IntAct=EBI-11079164, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16769727}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=O75170-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75170-2; Sequence=VSP_030758, VSP_030759, VSP_030760,
CC VSP_030761;
CC Name=3;
CC IsoId=O75170-3; Sequence=VSP_037768, VSP_030758, VSP_030760;
CC Name=4;
CC IsoId=O75170-4; Sequence=VSP_030758, VSP_030760;
CC Name=5;
CC IsoId=O75170-5; Sequence=VSP_030760;
CC Name=6;
CC IsoId=O75170-6; Sequence=VSP_037767, VSP_030758, VSP_030760;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with strongest expression in
CC the testis followed by liver, heart, kidney, brain and placenta.
CC {ECO:0000269|PubMed:16769727}.
CC -!- SIMILARITY: Belongs to the SAPS family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31660.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB014585; BAA31660.2; ALT_INIT; mRNA.
DR EMBL; AK302472; BAH13719.1; -; mRNA.
DR EMBL; AL096767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL671545; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL954743; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000976; AAH00976.2; -; mRNA.
DR EMBL; BC006568; AAH06568.1; -; mRNA.
DR EMBL; BC032664; AAH32664.1; -; mRNA.
DR EMBL; BC041698; AAH41698.1; -; mRNA.
DR EMBL; BC052995; AAH52995.1; -; mRNA.
DR CCDS; CCDS33681.1; -. [O75170-4]
DR CCDS; CCDS56235.1; -. [O75170-3]
DR CCDS; CCDS56236.1; -. [O75170-2]
DR CCDS; CCDS74881.1; -. [O75170-5]
DR PIR; T00357; T00357.
DR RefSeq; NP_001229827.1; NM_001242898.1. [O75170-5]
DR RefSeq; NP_001229828.1; NM_001242899.1. [O75170-3]
DR RefSeq; NP_001229829.1; NM_001242900.1. [O75170-2]
DR RefSeq; NP_055493.2; NM_014678.4. [O75170-4]
DR RefSeq; XP_006724497.1; XM_006724434.1.
DR RefSeq; XP_016884612.1; XM_017029123.1. [O75170-1]
DR RefSeq; XP_016884613.1; XM_017029124.1. [O75170-1]
DR RefSeq; XP_016884617.1; XM_017029128.1.
DR RefSeq; XP_016884620.1; XM_017029131.1.
DR RefSeq; XP_016884621.1; XM_017029132.1. [O75170-4]
DR AlphaFoldDB; O75170; -.
DR SMR; O75170; -.
DR BioGRID; 115053; 111.
DR CORUM; O75170; -.
DR DIP; DIP-27539N; -.
DR IntAct; O75170; 63.
DR MINT; O75170; -.
DR STRING; 9606.ENSP00000478417; -.
DR ChEMBL; CHEMBL4105960; -.
DR GlyGen; O75170; 7 sites, 2 O-linked glycans (7 sites).
DR iPTMnet; O75170; -.
DR PhosphoSitePlus; O75170; -.
DR BioMuta; PPP6R2; -.
DR EPD; O75170; -.
DR jPOST; O75170; -.
DR MassIVE; O75170; -.
DR MaxQB; O75170; -.
DR PaxDb; O75170; -.
DR PeptideAtlas; O75170; -.
DR PRIDE; O75170; -.
DR ProteomicsDB; 49835; -. [O75170-1]
DR ProteomicsDB; 49836; -. [O75170-2]
DR ProteomicsDB; 49837; -. [O75170-3]
DR ProteomicsDB; 49838; -. [O75170-4]
DR ProteomicsDB; 49839; -. [O75170-5]
DR ProteomicsDB; 49840; -. [O75170-6]
DR Antibodypedia; 28539; 83 antibodies from 20 providers.
DR DNASU; 9701; -.
DR Ensembl; ENST00000216061.9; ENSP00000216061.5; ENSG00000100239.16. [O75170-1]
DR Ensembl; ENST00000359139.7; ENSP00000352051.3; ENSG00000100239.16. [O75170-2]
DR Ensembl; ENST00000395741.7; ENSP00000379090.3; ENSG00000100239.16. [O75170-3]
DR Ensembl; ENST00000395744.7; ENSP00000379093.3; ENSG00000100239.16. [O75170-4]
DR Ensembl; ENST00000612753.5; ENSP00000478417.1; ENSG00000100239.16. [O75170-5]
DR GeneID; 9701; -.
DR KEGG; hsa:9701; -.
DR MANE-Select; ENST00000612753.5; ENSP00000478417.1; NM_001242898.2; NP_001229827.1. [O75170-5]
DR UCSC; uc003bky.3; human. [O75170-1]
DR CTD; 9701; -.
DR DisGeNET; 9701; -.
DR GeneCards; PPP6R2; -.
DR HGNC; HGNC:19253; PPP6R2.
DR HPA; ENSG00000100239; Low tissue specificity.
DR MIM; 610877; gene.
DR neXtProt; NX_O75170; -.
DR OpenTargets; ENSG00000100239; -.
DR PharmGKB; PA165378360; -.
DR VEuPathDB; HostDB:ENSG00000100239; -.
DR eggNOG; KOG2073; Eukaryota.
DR GeneTree; ENSGT00390000009899; -.
DR HOGENOM; CLU_012598_0_0_1; -.
DR InParanoid; O75170; -.
DR OMA; SDTGPGW; -.
DR PhylomeDB; O75170; -.
DR TreeFam; TF313227; -.
DR PathwayCommons; O75170; -.
DR SignaLink; O75170; -.
DR BioGRID-ORCS; 9701; 10 hits in 1073 CRISPR screens.
DR ChiTaRS; PPP6R2; human.
DR GenomeRNAi; 9701; -.
DR Pharos; O75170; Tbio.
DR PRO; PR:O75170; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; O75170; protein.
DR Bgee; ENSG00000100239; Expressed in right hemisphere of cerebellum and 185 other tissues.
DR ExpressionAtlas; O75170; baseline and differential.
DR Genevisible; O75170; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019903; F:protein phosphatase binding; IEA:InterPro.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR007587; SAPS.
DR PANTHER; PTHR12634; PTHR12634; 1.
DR Pfam; PF04499; SAPS; 2.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..966
FT /note="Serine/threonine-protein phosphatase 6 regulatory
FT subunit 2"
FT /id="PRO_0000046098"
FT REGION 408..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 771
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R3Q2"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 58..84
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037767"
FT VAR_SEQ 244
FT /note="S -> SR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037768"
FT VAR_SEQ 535..561
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9734811"
FT /id="VSP_030758"
FT VAR_SEQ 709
FT /note="E -> EA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9734811"
FT /id="VSP_030759"
FT VAR_SEQ 792..799
FT /note="SQASYFAV -> F (in isoform 2, isoform 3, isoform 4,
FT isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:9734811"
FT /id="VSP_030760"
FT VAR_SEQ 952..966
FT /note="KTDAPPEGAALNGPV -> QMPRQKELP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9734811"
FT /id="VSP_030761"
FT VARIANT 633
FT /note="D -> E (in dbSNP:rs11555194)"
FT /id="VAR_058402"
FT VARIANT 732
FT /note="R -> K (in dbSNP:rs13057311)"
FT /id="VAR_058403"
FT CONFLICT 224
FT /note="D -> G (in Ref. 2; BAH13719)"
FT /evidence="ECO:0000305"
FT CONFLICT 806
FT /note="A -> T (in Ref. 2; BAH13719)"
FT /evidence="ECO:0000305"
FT CONFLICT 835
FT /note="Q -> H (in Ref. 4; AAH52995)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 966 AA; 104942 MW; D3BC10EADB98FB62 CRC64;
MFWKFDLNTT SHVDKLLDKE HVTLQELMDE DDILQECKAQ NQKLLDFLCR QQCMEELVSL
ITQDPPLDME EKVRFKYPNT ACELLTCDVP QISDRLGGDE SLLSLLYDFL DHEPPLNPLL
ASFFSKTIGN LIARKTEQVI TFLKKKDKFI SLVLKHIGTS ALMDLLLRLV SCVEPAGLRQ
DVLHWLNEEK VIQRLVELIH PSQDEDRQSN ASQTLCDIVR LGRDQGSQLQ EALEPDPLLT
ALESQDCVEQ LLKNMFDGDR TESCLVSGTQ VLLTLLETRR VGTEGLVDSF SQGLERSYAV
SSSVLHGIEP RLKDFHQLLL NPPKKKAILT TIGVLEEPLG NARLHGARLM AALLHTNTPS
INQELCRLNT MDLLLDLFFK YTWNNFLHFQ VELCIAAILS HAAREERTEA SGSESRVEPP
HENGNRSLET PQPAASLPDN TMVTHLFQKC CLVQRILEAW EANDHTQAAG GMRRGNMGHL
TRIANAVVQN LERGPVQTHI SEVIRGLPAD CRGRWESFVE ETLTETNRRN TVDLVSTHHL
HSSSEDEDIE GAFPNELSLQ QAFSDYQIQQ MTANFVDQFG FNDEEFADQD DNINAPFDRI
AEINFNIDAD EDSPSAALFE ACCSDRIQPF DDDEDEDIWE DSDTRCAARV MARPRFGAPH
ASESCSKNGP ERGGQDGKAS LEAHRDAPGA GAPPAPGKKE APPVEGDSEG AMWTAVFDEP
ANSTPTAPGV VRDVGSSVWA AGTSAPEEKG WAKFTDFQPF CCSESGPRCS SPVDTECSHA
EGSRSQGPEK ASQASYFAVS PASPCAWNVC VTRKAPLLAS DSSSSGGSHS EDGDQKAASA
MDAVSRGPGR EAPPLPTVAR TEEAVGRVGC ADSRLLSPAC PAPKEVTAAP AVAVPPEATV
AITTALSKAG PAIPTPAVSS ALAVAVPLGP IMAVTAAPAM VATLGTVTKD GKTDAPPEGA
ALNGPV
