PPM1E_HUMAN
ID PPM1E_HUMAN Reviewed; 755 AA.
AC Q8WY54; A7E2X1; Q68DW1; Q7LAF3; Q9UPT0;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Protein phosphatase 1E;
DE EC=3.1.3.16;
DE AltName: Full=Ca(2+)/calmodulin-dependent protein kinase phosphatase N;
DE Short=CaMKP-N;
DE AltName: Full=CaMKP-nucleus;
DE Short=CaMKN;
DE AltName: Full=Partner of PIX 1;
DE AltName: Full=Partner of PIX-alpha;
DE Short=Partner of PIXA;
GN Name=PPM1E; Synonyms=CAMKN, KIAA1072, POPX1;
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 2), FUNCTION, INTERACTION WITH ARHGEF,
RP AND VARIANT PRO-GLU-44 INS.
RX PubMed=11864573; DOI=10.1016/s0960-9822(02)00652-8;
RA Koh C.-G., Tan E.-J., Manser E., Lim L.;
RT "The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a
RT pair of serine/threonine phosphatases of the PP2C family.";
RL Curr. Biol. 12:317-321(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT PRO-GLU-44 INS.
RA Wu G., Couch F.J.;
RT "Five novel genes from 17q23 amplicon have different amplification and
RT overexpression frequency in breast cancer.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT PRO-GLU-44
RP INS.
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT PRO-GLU-44
RP INS.
RC TISSUE=Hippocampus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-GLU-44 INS.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT PRO-GLU-44
RP INS.
RC TISSUE=Brain;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-112 (ISOFORM 2).
RX PubMed=16344560; DOI=10.1101/gr.4039406;
RA Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T., Yamashita R.,
RA Yamamoto J., Sekine M., Tsuritani K., Wakaguri H., Ishii S., Sugiyama T.,
RA Saito K., Isono Y., Irie R., Kushida N., Yoneyama T., Otsuka R., Kanda K.,
RA Yokoi T., Kondo H., Wagatsuma M., Murakawa K., Ishida S., Ishibashi T.,
RA Takahashi-Fujii A., Tanase T., Nagai K., Kikuchi H., Nakai K., Isogai T.,
RA Sugano S.;
RT "Diversification of transcriptional modulation: large-scale identification
RT and characterization of putative alternative promoters of human genes.";
RL Genome Res. 16:55-65(2006).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=15496589; DOI=10.1093/jb/mvh109;
RA Takeuchi M., Taniguchi T., Fujisawa H.;
RT "Identification and characterization of nuclear localization signals of
RT CaMKP-N.";
RL J. Biochem. 136:183-188(2004).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=16269004; DOI=10.1111/j.1471-4159.2005.03540.x;
RA Kitani T., Okuno S., Nakamura Y., Tokuno H., Takeuchi M., Fujisawa H.;
RT "Post-translational excision of the carboxyl-terminal segment of CaM kinase
RT phosphatase N and its cytosolic occurrence in the brain.";
RL J. Neurochem. 96:374-384(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 VARIANTS [LARGE SCALE ANALYSIS] SER-222 AND GLY-311.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Protein phosphatase that inactivates multifunctional CaM
CC kinases such as CAMK4 and CAMK2 (By similarity). Dephosphorylates and
CC inactivates PAK. May play a role in the inhibition of actin fiber
CC stress breakdown and in morphological changes driven by TNK2/CDC42.
CC Dephosphorylates PRKAA2 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11864573}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium or manganese ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Heterotrimer. Interacts with PAX1 and ARHGEF6 (or ARHGEF7).
CC {ECO:0000269|PubMed:11864573}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15496589,
CC ECO:0000269|PubMed:16269004}. Cytoplasm {ECO:0000269|PubMed:15496589,
CC ECO:0000269|PubMed:16269004}. Note=A truncated form, major form, with
CC the C-terminal part missing, is mostly found in the cytoplasm and a
CC little in the nucleus. The full-length, minor form, is found in the
CC nucleus. {ECO:0000269|PubMed:15496589, ECO:0000269|PubMed:16269004}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q8WY54-2; Sequence=Displayed;
CC Name=3;
CC IsoId=Q8WY54-3; Sequence=VSP_025198;
CC -!- POLYMORPHISM: The poly-Pro-Glu stretch is polymorphic.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF70325.1; Type=Miscellaneous discrepancy; Note=Contains a 27 bp insertion which does not match the genome.; Evidence={ECO:0000305};
CC Sequence=BAA83024.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF520614; AAM76058.1; -; mRNA.
DR EMBL; AF260269; AAF70325.1; ALT_SEQ; mRNA.
DR EMBL; AB028995; BAA83024.2; ALT_INIT; mRNA.
DR EMBL; AK289966; BAF82655.1; -; mRNA.
DR EMBL; CR749253; CAH18109.1; -; mRNA.
DR EMBL; AC025521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC100832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471109; EAW94429.1; -; Genomic_DNA.
DR EMBL; BC136290; AAI36291.1; -; mRNA.
DR EMBL; BC151228; AAI51229.1; -; mRNA.
DR EMBL; DA497512; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; DA791319; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS11613.1; -. [Q8WY54-2]
DR RefSeq; NP_055721.3; NM_014906.4. [Q8WY54-2]
DR RefSeq; XP_005257226.1; XM_005257169.4.
DR RefSeq; XP_011522836.1; XM_011524534.2.
DR AlphaFoldDB; Q8WY54; -.
DR SMR; Q8WY54; -.
DR BioGRID; 116515; 47.
DR IntAct; Q8WY54; 24.
DR MINT; Q8WY54; -.
DR STRING; 9606.ENSP00000312411; -.
DR DEPOD; PPM1E; -.
DR GlyGen; Q8WY54; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WY54; -.
DR PhosphoSitePlus; Q8WY54; -.
DR BioMuta; PPM1E; -.
DR DMDM; 311033412; -.
DR EPD; Q8WY54; -.
DR jPOST; Q8WY54; -.
DR MassIVE; Q8WY54; -.
DR MaxQB; Q8WY54; -.
DR PaxDb; Q8WY54; -.
DR PeptideAtlas; Q8WY54; -.
DR PRIDE; Q8WY54; -.
DR ProteomicsDB; 75129; -. [Q8WY54-2]
DR ProteomicsDB; 75130; -. [Q8WY54-3]
DR Antibodypedia; 18444; 67 antibodies from 16 providers.
DR DNASU; 22843; -.
DR Ensembl; ENST00000308249.4; ENSP00000312411.2; ENSG00000175175.6. [Q8WY54-2]
DR GeneID; 22843; -.
DR KEGG; hsa:22843; -.
DR MANE-Select; ENST00000308249.4; ENSP00000312411.2; NM_014906.5; NP_055721.3.
DR UCSC; uc002iwx.5; human. [Q8WY54-2]
DR CTD; 22843; -.
DR DisGeNET; 22843; -.
DR GeneCards; PPM1E; -.
DR HGNC; HGNC:19322; PPM1E.
DR HPA; ENSG00000175175; Group enriched (brain, retina).
DR MIM; 619308; gene.
DR neXtProt; NX_Q8WY54; -.
DR OpenTargets; ENSG00000175175; -.
DR PharmGKB; PA134943567; -.
DR VEuPathDB; HostDB:ENSG00000175175; -.
DR eggNOG; KOG0698; Eukaryota.
DR GeneTree; ENSGT00940000157884; -.
DR HOGENOM; CLU_013173_15_1_1; -.
DR InParanoid; Q8WY54; -.
DR OMA; SHLRYHY; -.
DR OrthoDB; 1044139at2759; -.
DR PhylomeDB; Q8WY54; -.
DR TreeFam; TF317617; -.
DR PathwayCommons; Q8WY54; -.
DR Reactome; R-HSA-9617324; Negative regulation of NMDA receptor-mediated neuronal transmission.
DR SignaLink; Q8WY54; -.
DR SIGNOR; Q8WY54; -.
DR BioGRID-ORCS; 22843; 209 hits in 1077 CRISPR screens.
DR ChiTaRS; PPM1E; human.
DR GenomeRNAi; 22843; -.
DR Pharos; Q8WY54; Tbio.
DR PRO; PR:Q8WY54; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8WY54; protein.
DR Bgee; ENSG00000175175; Expressed in endothelial cell and 124 other tissues.
DR Genevisible; Q8WY54; HS.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
DR GO; GO:0035970; P:peptidyl-threonine dephosphorylation; IDA:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IDA:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Nucleus; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Repeat.
FT CHAIN 1..755
FT /note="Protein phosphatase 1E"
FT /id="PRO_0000286820"
FT REPEAT 31..32
FT /note="1"
FT REPEAT 33..34
FT /note="2"
FT REPEAT 35..36
FT /note="3"
FT REPEAT 37..38
FT /note="4"
FT REPEAT 39..40
FT /note="5"
FT REPEAT 41..42
FT /note="6"
FT REPEAT 43..44
FT /note="7"
FT REPEAT 45..46
FT /note="8; approximate"
FT REPEAT 47..48
FT /note="9"
FT REPEAT 49..50
FT /note="10"
FT REPEAT 51..52
FT /note="11"
FT DOMAIN 231..488
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 21..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 31..52
FT /note="11 X 2 AA tandem repeats of P-E"
FT REGION 498..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..64
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..101
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..130
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..527
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 273
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 479
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 535
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80TL0"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80Z30"
FT VAR_SEQ 1..261
FT /note="MAGCIPEEKTYRRFLELFLGEFRGPCGGGEPEPEPEPEPEPEPESEPEPEPE
FT LVEAEAAEASVEEPGEEAATVAATEEGDQEQDPEPEEEAAVEGEEEEEGAATAAAAPGH
FT SAVPPPPPQLPPLPPLPRPLSERITREEVEGESLDLCLQQLYKYNCPSFLAAALARATS
FT DEVLQSDLSAHYIPKETDGTEGTVEIETVKLARSVFSKLHEICCSWVKDFPLRRRPQLY
FT YETSIHAIKNMRRKMEDKHVCIPDFNMLFNLE -> MKSFRVIFLHIISQRKRMAQKGL
FT W (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_025198"
FT VARIANT 44
FT /note="E -> EPE"
FT /evidence="ECO:0000269|PubMed:10470851,
FT ECO:0000269|PubMed:11864573, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005,
FT ECO:0000269|Ref.2, ECO:0000269|Ref.7"
FT /id="VAR_063769"
FT VARIANT 222
FT /note="L -> S (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036518"
FT VARIANT 311
FT /note="R -> G (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036519"
FT CONFLICT 53
FT /note="L -> P (in Ref. 9; DA497512)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="V -> I (in Ref. 2; AAF70325)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 755 AA; 83952 MW; C24C64A0A1BC1091 CRC64;
MAGCIPEEKT YRRFLELFLG EFRGPCGGGE PEPEPEPEPE PEPESEPEPE PELVEAEAAE
ASVEEPGEEA ATVAATEEGD QEQDPEPEEE AAVEGEEEEE GAATAAAAPG HSAVPPPPPQ
LPPLPPLPRP LSERITREEV EGESLDLCLQ QLYKYNCPSF LAAALARATS DEVLQSDLSA
HYIPKETDGT EGTVEIETVK LARSVFSKLH EICCSWVKDF PLRRRPQLYY ETSIHAIKNM
RRKMEDKHVC IPDFNMLFNL EDQEEQAYFA VFDGHGGVDA AIYASIHLHV NLVRQEMFPH
DPAEALCRAF RVTDERFVQK AARESLRCGT TGVVTFIRGN MLHVAWVGDS QVMLVRKGQA
VELMKPHKPD REDEKQRIEA LGGCVVWFGA WRVNGSLSVS RAIGDAEHKP YICGDADSAS
TVLDGTEDYL ILACDGFYDT VNPDEAVKVV SDHLKENNGD SSMVAHKLVA SARDAGSSDN
ITVIVVFLRD MNKAVNVSEE SDWTENSFQG GQEDGGDDKE NHGECKRPWP QHQCSAPADL
GYDGRVDSFT DRTSLSPGSQ INVLEDPGYL DLTQIEASKP HSAQFLLPVE MFGPGAPKKA
NLINELMMEK KSVQSSLPEW SGAGEFPTAF NLGSTGEQIY RMQSLSPVCS GLENEQFKSP
GNRVSRLSHL RHHYSKKWHR FRFNPKFYSF LSAQEPSHKI GTSLSSLTGS GKRNRIRSSL
PWRQNSWKGY SENMRKLRKT HDIPCPDLPW SYKIE
