PPME1_HUMAN
ID PPME1_HUMAN Reviewed; 386 AA.
AC Q9Y570; B3KMU6; B5MEE7; J3QT22; Q8WYG8; Q9NVT5; Q9UI18;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Protein phosphatase methylesterase 1;
DE Short=PME-1;
DE EC=3.1.1.89;
GN Name=PPME1; Synonyms=PME1; ORFNames=PP2593, PRO0750;
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, CATALYTIC ACTIVITY, AND
RP INTERACTION WITH PPP2CB.
RC TISSUE=Cervix carcinoma;
RX PubMed=10318862; DOI=10.1074/jbc.274.20.14382;
RA Ogris E., Du X., Nelson K.C., Mak E.K., Yu X.X., Lane W.S., Pallas D.C.;
RT "A protein phosphatase methylesterase (PME-1) is one of several novel
RT proteins stably associating with two inactive mutants of protein
RT phosphatase 2A.";
RL J. Biol. Chem. 274:14382-14391(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Fetal liver;
RA Zhang C., Yu Y., Zhang S., Ouyang S., Luo L., Wei H., Zhou G., Zhang Y.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 9 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Amygdala;
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].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, 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 [7]
RP PROTEIN SEQUENCE OF 2-12.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 257-386 (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [9]
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, 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].
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 [12]
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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, AND IDENTIFICATION BY
RP 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, 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).
RN [16]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-16, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 39-386 ALONE AND IN COMPLEX WITH
RP PPP2CA AND PPP2R1A, ACTIVE SITE, AND CATALYTIC ACTIVITY.
RX PubMed=18394995; DOI=10.1016/j.cell.2008.02.041;
RA Xing Y., Li Z., Chen Y., Stock J.B., Jeffrey P.D., Shi Y.;
RT "Structural mechanism of demethylation and inactivation of protein
RT phosphatase 2A.";
RL Cell 133:154-163(2008).
CC -!- FUNCTION: Demethylates proteins that have been reversibly
CC carboxymethylated. Demethylates PPP2CB (in vitro) and PPP2CA. Binding
CC to PPP2CA displaces the manganese ion and inactivates the enzyme.
CC {ECO:0000269|PubMed:10318862}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphatase 2A protein]-C-terminal L-leucine methyl ester +
CC H2O = [phosphatase 2A protein]-C-terminal L-leucine + H(+) +
CC methanol; Xref=Rhea:RHEA:48548, Rhea:RHEA-COMP:12134, Rhea:RHEA-
CC COMP:12135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:90516, ChEBI:CHEBI:90517; EC=3.1.1.89;
CC Evidence={ECO:0000269|PubMed:10318862, ECO:0000269|PubMed:18394995};
CC -!- SUBUNIT: Binds PPP2CA and PPP2CB. {ECO:0000269|PubMed:18394995}.
CC -!- INTERACTION:
CC Q9Y570; P67775-1: PPP2CA; NbExp=2; IntAct=EBI-1772895, EBI-16765970;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9Y570-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y570-2; Sequence=VSP_010336;
CC Name=3;
CC IsoId=Q9Y570-3; Sequence=VSP_010335, VSP_010337;
CC Name=4;
CC IsoId=Q9Y570-4; Sequence=VSP_054818;
CC -!- PTM: Phosphorylated by SIK1 following increases in intracellular
CC sodium, leading to dissociation from the protein phosphatase 2A (PP2A)
CC complex and subsequent dephosphorylation of sodium/potassium-
CC transporting ATPase ATP1A1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG22477.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AF157028; AAD44976.1; -; mRNA.
DR EMBL; AF111853; AAF16692.1; -; mRNA.
DR EMBL; AK001381; BAA91661.1; -; mRNA.
DR EMBL; AK022725; BAG51108.1; -; mRNA.
DR EMBL; AK123288; BAC85574.1; -; mRNA.
DR EMBL; AP000577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74932.1; -; Genomic_DNA.
DR EMBL; BC003046; AAH03046.1; -; mRNA.
DR EMBL; BC050705; AAH50705.1; -; mRNA.
DR EMBL; AF193049; AAG22477.1; ALT_SEQ; mRNA.
DR CCDS; CCDS44678.1; -. [Q9Y570-1]
DR CCDS; CCDS60891.1; -. [Q9Y570-4]
DR RefSeq; NP_001258522.1; NM_001271593.1. [Q9Y570-4]
DR RefSeq; NP_057231.1; NM_016147.2. [Q9Y570-1]
DR PDB; 3C5V; X-ray; 2.00 A; A=39-386.
DR PDB; 3C5W; X-ray; 2.80 A; P=284-386, P=39-238.
DR PDBsum; 3C5V; -.
DR PDBsum; 3C5W; -.
DR AlphaFoldDB; Q9Y570; -.
DR SMR; Q9Y570; -.
DR BioGRID; 119524; 158.
DR CORUM; Q9Y570; -.
DR IntAct; Q9Y570; 30.
DR MINT; Q9Y570; -.
DR STRING; 9606.ENSP00000381461; -.
DR BindingDB; Q9Y570; -.
DR ChEMBL; CHEMBL1293320; -.
DR GuidetoPHARMACOLOGY; 2875; -.
DR ESTHER; human-PPME1; PPase_methylesterase_euk.
DR MEROPS; S33.984; -.
DR GlyGen; Q9Y570; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y570; -.
DR MetOSite; Q9Y570; -.
DR PhosphoSitePlus; Q9Y570; -.
DR SwissPalm; Q9Y570; -.
DR BioMuta; PPME1; -.
DR DMDM; 47606055; -.
DR REPRODUCTION-2DPAGE; IPI00007694; -.
DR EPD; Q9Y570; -.
DR jPOST; Q9Y570; -.
DR MassIVE; Q9Y570; -.
DR MaxQB; Q9Y570; -.
DR PaxDb; Q9Y570; -.
DR PeptideAtlas; Q9Y570; -.
DR PRIDE; Q9Y570; -.
DR ProteomicsDB; 86296; -. [Q9Y570-1]
DR ProteomicsDB; 86297; -. [Q9Y570-2]
DR ProteomicsDB; 86298; -. [Q9Y570-3]
DR Antibodypedia; 3870; 338 antibodies from 32 providers.
DR DNASU; 51400; -.
DR Ensembl; ENST00000328257.13; ENSP00000329867.8; ENSG00000214517.10. [Q9Y570-1]
DR Ensembl; ENST00000398427.6; ENSP00000381461.4; ENSG00000214517.10. [Q9Y570-4]
DR GeneID; 51400; -.
DR KEGG; hsa:51400; -.
DR MANE-Select; ENST00000328257.13; ENSP00000329867.8; NM_016147.3; NP_057231.1.
DR UCSC; uc001ouw.5; human. [Q9Y570-1]
DR CTD; 51400; -.
DR DisGeNET; 51400; -.
DR GeneCards; PPME1; -.
DR HGNC; HGNC:30178; PPME1.
DR HPA; ENSG00000214517; Low tissue specificity.
DR MIM; 611117; gene.
DR neXtProt; NX_Q9Y570; -.
DR OpenTargets; ENSG00000214517; -.
DR PharmGKB; PA142671152; -.
DR VEuPathDB; HostDB:ENSG00000214517; -.
DR eggNOG; KOG2564; Eukaryota.
DR GeneTree; ENSGT00390000004396; -.
DR HOGENOM; CLU_024818_0_1_1; -.
DR InParanoid; Q9Y570; -.
DR OMA; WHIRSRT; -.
DR OrthoDB; 911863at2759; -.
DR PhylomeDB; Q9Y570; -.
DR TreeFam; TF314697; -.
DR BioCyc; MetaCyc:MON-16514; -.
DR BRENDA; 3.1.1.89; 2681.
DR PathwayCommons; Q9Y570; -.
DR Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR SignaLink; Q9Y570; -.
DR SIGNOR; Q9Y570; -.
DR BioGRID-ORCS; 51400; 177 hits in 1081 CRISPR screens.
DR ChiTaRS; PPME1; human.
DR EvolutionaryTrace; Q9Y570; -.
DR GenomeRNAi; 51400; -.
DR Pharos; Q9Y570; Tchem.
DR PRO; PR:Q9Y570; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9Y570; protein.
DR Bgee; ENSG00000214517; Expressed in prefrontal cortex and 200 other tissues.
DR ExpressionAtlas; Q9Y570; baseline and differential.
DR Genevisible; Q9Y570; HS.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0106222; F:lncRNA binding; IEA:Ensembl.
DR GO; GO:0051722; F:protein C-terminal methylesterase activity; IDA:HGNC-UCL.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0051723; F:protein methylesterase activity; IBA:GO_Central.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IDA:HGNC-UCL.
DR GO; GO:0019903; F:protein phosphatase binding; IDA:HGNC-UCL.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; TAS:ProtInc.
DR GO; GO:0019888; F:protein phosphatase regulator activity; TAS:HGNC-UCL.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0006482; P:protein demethylation; IDA:HGNC-UCL.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR016812; PPase_methylesterase_euk.
DR PANTHER; PTHR14189; PTHR14189; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR PIRSF; PIRSF022950; PPase_methylesterase_euk; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing; Hydrolase;
KW Methylation; Phosphoprotein; Reference proteome; Serine esterase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801"
FT CHAIN 2..386
FT /note="Protein phosphatase methylesterase 1"
FT /id="PRO_0000090390"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..280
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /evidence="ECO:0000269|PubMed:18394995"
FT ACT_SITE 181
FT /evidence="ECO:0000269|PubMed:18394995"
FT ACT_SITE 349
FT /evidence="ECO:0000269|PubMed:18394995"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 16
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q8BVQ5"
FT MOD_RES 16
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..276
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010335"
FT VAR_SEQ 1..187
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_010336"
FT VAR_SEQ 278
FT /note="E -> EGLPSETQNLLLFLQ (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_054818"
FT VAR_SEQ 360..386
FT /note="AEAVATFLIRHRFAEPIGGFQCVFPGC -> SLVLSDCKRTTVRITLDVTED
FT KSLSLSLHCLQQLLWSLCRCSSTSSPTSPWQLLMVLVLCICAEELLTLCYFIPGPCG
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_010337"
FT CONFLICT 309
FT /note="F -> S (in Ref. 3; BAA91661)"
FT /evidence="ECO:0000305"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:3C5V"
FT STRAND 51..60
FT /evidence="ECO:0007829|PDB:3C5V"
FT STRAND 63..72
FT /evidence="ECO:0007829|PDB:3C5V"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:3C5V"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:3C5V"
FT HELIX 89..92
FT /evidence="ECO:0007829|PDB:3C5V"
FT HELIX 93..100
FT /evidence="ECO:0007829|PDB:3C5V"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:3C5V"
FT HELIX 128..143
FT /evidence="ECO:0007829|PDB:3C5V"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3C5W"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:3C5V"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:3C5V"
FT STRAND 174..181
FT /evidence="ECO:0007829|PDB:3C5V"
FT HELIX 184..200
FT /evidence="ECO:0007829|PDB:3C5V"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:3C5V"
FT HELIX 208..217
FT /evidence="ECO:0007829|PDB:3C5V"
FT HELIX 224..234
FT /evidence="ECO:0007829|PDB:3C5V"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:3C5V"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:3C5V"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:3C5V"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:3C5V"
FT HELIX 305..311
FT /evidence="ECO:0007829|PDB:3C5V"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:3C5V"
FT STRAND 316..322
FT /evidence="ECO:0007829|PDB:3C5V"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:3C5W"
FT HELIX 328..335
FT /evidence="ECO:0007829|PDB:3C5V"
FT STRAND 339..343
FT /evidence="ECO:0007829|PDB:3C5V"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:3C5V"
FT HELIX 356..369
FT /evidence="ECO:0007829|PDB:3C5V"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:3C5W"
SQ SEQUENCE 386 AA; 42315 MW; 37B25324583E8578 CRC64;
MSALEKSMHL GRLPSRPPLP GSGGSQSGAK MRMGPGRKRD FSPVPWSQYF ESMEDVEVEN
ETGKDTFRVY KSGSEGPVLL LLHGGGHSAL SWAVFTAAII SRVQCRIVAL DLRSHGETKV
KNPEDLSAET MAKDVGNVVE AMYGDLPPPI MLIGHSMGGA IAVHTASSNL VPSLLGLCMI
DVVEGTAMDA LNSMQNFLRG RPKTFKSLEN AIEWSVKSGQ IRNLESARVS MVGQVKQCEG
ITSPEGSKSI VEGIIEEEEE DEEGSESISK RKKEDDMETK KDHPYTWRIE LAKTEKYWDG
WFRGLSNLFL SCPIPKLLLL AGVDRLDKDL TIGQMQGKFQ MQVLPQCGHA VHEDAPDKVA
EAVATFLIRH RFAEPIGGFQ CVFPGC
