PI5PA_HUMAN
ID PI5PA_HUMAN Reviewed; 1006 AA.
AC Q15735; B3KS54; Q32M61; Q6ZTH6; Q8N902; Q9UDT9;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A;
DE EC=3.1.3.56;
DE AltName: Full=Inositol polyphosphate 5-phosphatase J;
GN Name=INPP5J; Synonyms=PIB5PA, PIPP;
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] (ISOFORMS 2 AND 3).
RC TISSUE=Cerebellum, Heart, and Spleen;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
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 [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 NUCLEOTIDE SEQUENCE [MRNA] OF 610-1006.
RC TISSUE=Brain;
RA Nussbaum R.L.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-903 AND SER-990, 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: Inositol 5-phosphatase, which converts inositol 1,4,5-
CC trisphosphate to inositol 1,4-bisphosphate. Also converts
CC phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4-
CC phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-
CC trisphosphate in vitro. May be involved in modulation of the function
CC of inositol and phosphatidylinositol polyphosphate-binding proteins
CC that are present at membranes ruffles (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,4,5-trisphosphate + H2O = 1D-myo-inositol
CC 1,4-bisphosphate + phosphate; Xref=Rhea:RHEA:19797,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58282,
CC ChEBI:CHEBI:203600; EC=3.1.3.56;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-
CC inositol 1,3,4-trisphosphate + phosphate; Xref=Rhea:RHEA:11392,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57895,
CC ChEBI:CHEBI:58414; EC=3.1.3.56;
CC -!- INTERACTION:
CC Q15735; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-10236940, EBI-396137;
CC Q15735; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-10236940, EBI-739624;
CC Q15735; Q96EY1-2: DNAJA3; NbExp=3; IntAct=EBI-10236940, EBI-3952284;
CC Q15735; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-10236940, EBI-2349927;
CC Q15735; Q12929: EPS8; NbExp=3; IntAct=EBI-10236940, EBI-375576;
CC Q15735; P51116: FXR2; NbExp=3; IntAct=EBI-10236940, EBI-740459;
CC Q15735; Q08379: GOLGA2; NbExp=6; IntAct=EBI-10236940, EBI-618309;
CC Q15735; O75031: HSF2BP; NbExp=3; IntAct=EBI-10236940, EBI-7116203;
CC Q15735; P50221: MEOX1; NbExp=3; IntAct=EBI-10236940, EBI-2864512;
CC Q15735; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-10236940, EBI-16439278;
CC Q15735; Q96FA3: PELI1; NbExp=3; IntAct=EBI-10236940, EBI-448369;
CC Q15735; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-10236940, EBI-79165;
CC Q15735; P31321: PRKAR1B; NbExp=3; IntAct=EBI-10236940, EBI-2805516;
CC Q15735; P61289: PSME3; NbExp=3; IntAct=EBI-10236940, EBI-355546;
CC Q15735; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-10236940, EBI-726876;
CC Q15735; Q08117-2: TLE5; NbExp=3; IntAct=EBI-10236940, EBI-11741437;
CC Q15735; P14373: TRIM27; NbExp=3; IntAct=EBI-10236940, EBI-719493;
CC Q15735; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-10236940, EBI-2130429;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Note=Predominantly
CC localized to membrane ruffles. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q15735-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15735-2; Sequence=VSP_007296;
CC Name=3;
CC IsoId=Q15735-3; Sequence=VSP_021017;
CC -!- DOMAIN: The 5 Arg-Ser-Xaa-Ser-Xaa-Xaa (RSXSXX) motifs may constitute
CC binding sites for the 14-3-3 protein.
CC -!- SIMILARITY: Belongs to the inositol 1,4,5-trisphosphate 5-phosphatase
CC type II family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD15618.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK092859; BAG52616.1; -; mRNA.
DR EMBL; AK095944; BAC04657.1; -; mRNA.
DR EMBL; AK126610; BAC86611.1; -; mRNA.
DR EMBL; AC005005; AAD15618.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471095; EAW59936.1; -; Genomic_DNA.
DR EMBL; BC109288; AAI09289.1; -; mRNA.
DR EMBL; U45975; AAB03216.1; -; mRNA.
DR CCDS; CCDS46687.1; -. [Q15735-3]
DR CCDS; CCDS63453.1; -. [Q15735-1]
DR CCDS; CCDS63455.1; -. [Q15735-2]
DR RefSeq; NP_001002837.1; NM_001002837.2. [Q15735-3]
DR RefSeq; NP_001271214.1; NM_001284285.1. [Q15735-1]
DR RefSeq; NP_001271217.1; NM_001284288.1. [Q15735-2]
DR RefSeq; NP_001271218.1; NM_001284289.1. [Q15735-2]
DR RefSeq; XP_016884260.1; XM_017028771.1.
DR AlphaFoldDB; Q15735; -.
DR SMR; Q15735; -.
DR BioGRID; 118015; 18.
DR IntAct; Q15735; 18.
DR STRING; 9606.ENSP00000333262; -.
DR DEPOD; INPP5J; -.
DR GlyGen; Q15735; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q15735; -.
DR PhosphoSitePlus; Q15735; -.
DR BioMuta; INPP5J; -.
DR DMDM; 116242713; -.
DR EPD; Q15735; -.
DR jPOST; Q15735; -.
DR MassIVE; Q15735; -.
DR MaxQB; Q15735; -.
DR PaxDb; Q15735; -.
DR PeptideAtlas; Q15735; -.
DR PRIDE; Q15735; -.
DR ProteomicsDB; 60724; -. [Q15735-1]
DR ProteomicsDB; 60725; -. [Q15735-2]
DR ProteomicsDB; 60726; -. [Q15735-3]
DR Antibodypedia; 5745; 207 antibodies from 30 providers.
DR DNASU; 27124; -.
DR Ensembl; ENST00000331075.10; ENSP00000333262.5; ENSG00000185133.14. [Q15735-1]
DR Ensembl; ENST00000400294.6; ENSP00000383150.2; ENSG00000185133.14. [Q15735-2]
DR Ensembl; ENST00000404390.7; ENSP00000384534.3; ENSG00000185133.14. [Q15735-3]
DR Ensembl; ENST00000405300.5; ENSP00000384596.1; ENSG00000185133.14. [Q15735-2]
DR GeneID; 27124; -.
DR KEGG; hsa:27124; -.
DR MANE-Select; ENST00000331075.10; ENSP00000333262.5; NM_001284285.2; NP_001271214.1.
DR UCSC; uc003ajs.5; human. [Q15735-1]
DR CTD; 27124; -.
DR DisGeNET; 27124; -.
DR GeneCards; INPP5J; -.
DR HGNC; HGNC:8956; INPP5J.
DR HPA; ENSG00000185133; Group enriched (parathyroid gland, thyroid gland).
DR MIM; 606481; gene.
DR neXtProt; NX_Q15735; -.
DR OpenTargets; ENSG00000185133; -.
DR PharmGKB; PA164720918; -.
DR VEuPathDB; HostDB:ENSG00000185133; -.
DR eggNOG; KOG0565; Eukaryota.
DR GeneTree; ENSGT00940000156855; -.
DR InParanoid; Q15735; -.
DR OMA; EWLRPEQ; -.
DR PhylomeDB; Q15735; -.
DR TreeFam; TF317034; -.
DR BioCyc; MetaCyc:HS11950-MON; -.
DR BRENDA; 3.1.3.56; 2681.
DR PathwayCommons; Q15735; -.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-HSA-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR Reactome; R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol.
DR SignaLink; Q15735; -.
DR BioGRID-ORCS; 27124; 9 hits in 1079 CRISPR screens.
DR ChiTaRS; INPP5J; human.
DR GeneWiki; PIB5PA; -.
DR GenomeRNAi; 27124; -.
DR Pharos; Q15735; Tbio.
DR PRO; PR:Q15735; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q15735; protein.
DR Bgee; ENSG00000185133; Expressed in right lobe of thyroid gland and 106 other tissues.
DR ExpressionAtlas; Q15735; baseline and differential.
DR Genevisible; Q15735; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043198; C:dendritic shaft; IEA:Ensembl.
DR GO; GO:0019898; C:extrinsic component of membrane; IEA:Ensembl.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0001726; C:ruffle; IDA:MGI.
DR GO; GO:0052659; F:inositol-1,3,4,5-tetrakisphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052658; F:inositol-1,4,5-trisphosphate 5-phosphatase activity; TAS:Reactome.
DR GO; GO:0004445; F:inositol-polyphosphate 5-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0034485; F:phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase activity; IBA:GO_Central.
DR GO; GO:0004439; F:phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity; IBA:GO_Central.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; IEA:Ensembl.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR000300; IPPc.
DR InterPro; IPR041611; SKICH.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF17751; SKICH; 1.
DR SMART; SM00128; IPPc; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; SH3-binding.
FT CHAIN 1..1006
FT /note="Phosphatidylinositol 4,5-bisphosphate 5-phosphatase
FT A"
FT /id="PRO_0000209738"
FT REGION 1..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..728
FT /note="Catalytic"
FT /evidence="ECO:0000255"
FT REGION 729..840
FT /note="Required for ruffle localization"
FT /evidence="ECO:0000250"
FT REGION 844..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 102..107
FT /note="RSXSXX motif 1"
FT MOTIF 345..350
FT /note="SH3-binding"
FT /evidence="ECO:0000255"
FT MOTIF 350..355
FT /note="RSXSXX motif 2"
FT MOTIF 874..879
FT /note="RSXSXX motif 3"
FT MOTIF 885..890
FT /note="RSXSXX motif 4"
FT MOTIF 911..916
FT /note="RSXSXX motif 5"
FT COMPBIAS 96..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..367
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..939
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 56
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59644"
FT MOD_RES 56
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59644"
FT MOD_RES 65
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P59644"
FT MOD_RES 76
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P59644"
FT MOD_RES 83
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59644"
FT MOD_RES 83
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P59644"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59644"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P59644"
FT MOD_RES 903
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 990
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..367
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007296"
FT VAR_SEQ 56..423
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021017"
FT VARIANT 333
FT /note="S -> I (in dbSNP:rs12485025)"
FT /id="VAR_028107"
FT CONFLICT 610..612
FT /note="SYD -> ARG (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 662
FT /note="V -> A (in Ref. 1; BAC86611)"
FT /evidence="ECO:0000305"
FT CONFLICT 791
FT /note="W -> R (in Ref. 4; AAI09289)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1006 AA; 107197 MW; ADB6382AA33E15AC CRC64;
MEGQSSRGSR RPGTRAGLGS LPMPQGVAQT GAPSKVDSSF QLPAKKNAAL GPSEPRLALA
PVGPRAAMSA SSEGPRLALA SPRPILAPLC TPEGQKTATA HRSSSLAPTS VGQLVMSASA
GPKPPPATTG SVLAPTSLGL VMPASAGPRS PPVTLGPNLA PTSRDQKQEP PASVGPKPTL
AASGLSLALA SEEQPPELPS TPSPVPSPVL SPTQEQALAP ASTASGAASV GQTSARKRDA
PAPRPLPASE GHLQPPAQTS GPTGSPPCIQ TSPDPRLSPS FRARPEALHS SPEDPVLPRP
PQTLPLDVGQ GPSEPGTHSP GLLSPTFRPG APSGQTVPPP LPKPPRSPSR SPSHSPNRSP
CVPPAPDMAL PRLGTQSTGP GRCLSPNLQA QEAPAPVTTS SSTSTLSSSP WSAQPTWKSD
PGFRITVVTW NVGTAMPPDD VTSLLHLGGG DDSDGADMIA IGLQEVNSML NKRLKDALFT
DQWSELFMDA LGPFNFVLVS SVRMQGVILL LFAKYYHLPF LRDVQTDCTR TGLGGYWGNK
GGVSVRLAAF GHMLCFLNCH LPAHMDKAEQ RKDNFQTILS LQQFQGPGAQ GILDHDLVFW
FGDLNFRIES YDLHFVKFAI DSDQLHQLWE KDQLNMAKNT WPILKGFQEG PLNFAPTFKF
DVGTNKYDTS AKKRKPAWTD RILWKVKAPG GGPSPSGRKS HRLQVTQHSY RSHMEYTVSD
HKPVAAQFLL QFAFRDDMPL VRLEVADEWV RPEQAVVRYR METVFARSSW DWIGLYRVGF
RHCKDYVAYV WAKHEDVDGN TYQVTFSEES LPKGHGDFIL GYYSHNHSIL IGITEPFQIS
LPSSELASSS TDSSGTSSEG EDDSTLELLA PKSRSPSPGK SKRHRSRSPG LARFPGLALR
PSSRERRGAS RSPSPQSRRL SRVAPDRSSN GSSRGSSEEG PSGLPGPWAF PPAVPRSLGL
LPALRLETVD PGGGGSWGPD REALAPNSLS PSPQGHRGLE EGGLGP
