ID   JMY_HUMAN               Reviewed;         988 AA.
AC   Q8N9B5; A1L4P5; B5MDS2; B5MDT0;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Junction-mediating and -regulatory protein;
GN   Name=JMY;
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 GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-364.
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 345-988 (ISOFORM 2).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 351-988 (ISOFORM 1), AND VARIANT
RP   LEU-364.
RC   TISSUE=Substantia nigra;
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   INDUCTION.
RX   PubMed=15706352; DOI=10.1038/sj.cdd.4401575;
RA   Hershko T., Chaussepied M., Oren M., Ginsberg D.;
RT   "Novel link between E2F and p53: proapoptotic cofactors of p53 are
RT   transcriptionally upregulated by E2F.";
RL   Cell Death Differ. 12:377-383(2005).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-974, 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   [7]
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   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=19287377; DOI=10.1038/ncb1852;
RA   Zuchero J.B., Coutts A.S., Quinlan M.E., Thangue N.B., Mullins R.D.;
RT   "p53-cofactor JMY is a multifunctional actin nucleation factor.";
RL   Nat. Cell Biol. 11:451-459(2009).
RN   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115; SER-121 AND SER-713, 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   [11]
RP   FUNCTION, INTERACTION WITH TTC5 AND MAP1LC3B, SUBCELLULAR LOCATION, AND
RP   DOMAIN.
RX   PubMed=30420355; DOI=10.1083/jcb.201802157;
RA   Hu X., Mullins R.D.;
RT   "LC3 and STRAP regulate actin filament assembly by JMY during autophagosome
RT   formation.";
RL   J. Cell Biol. 218:251-266(2019).
CC   -!- FUNCTION: Acts both as a nuclear p53/TP53-cofactor and a cytoplasmic
CC       regulator of actin dynamics depending on conditions (PubMed:30420355).
CC       In nucleus, acts as a cofactor that increases p53/TP53 response via its
CC       interaction with p300/EP300. Increases p53/TP53-dependent transcription
CC       and apoptosis, suggesting an important role in p53/TP53 stress response
CC       such as DNA damage. In cytoplasm, acts as a nucleation-promoting factor
CC       for both branched and unbranched actin filaments (PubMed:30420355).
CC       Activates the Arp2/3 complex to induce branched actin filament
CC       networks. Also catalyzes actin polymerization in the absence of Arp2/3,
CC       creating unbranched filaments (PubMed:30420355). Contributes to cell
CC       motility by controlling actin dynamics. May promote the rapid formation
CC       of a branched actin network by first nucleating new mother filaments
CC       and then activating Arp2/3 to branch off these filaments. Upon nutrient
CC       stress, directly recruited by MAP1LC3B to the phagophore membrane
CC       surfaces to promote actin assembly during autophagy (PubMed:30420355).
CC       The p53/TP53-cofactor and actin activator activities are regulated via
CC       its subcellular location (By similarity).
CC       {ECO:0000250|UniProtKB:Q9QXM1, ECO:0000269|PubMed:30420355}.
CC   -!- SUBUNIT: Interacts with p300/EP300, the complex activates p53/TP53
CC       transcriptional activity. Interacts with TTC5; the interaction
CC       facilitates the association between JMY and p300/EP300 (By similarity).
CC       Interacts with MAP1LC3B; the interaction results in the activation of
CC       JYM's nucleation activity in the cytoplasm (PubMed:30420355). Interacts
CC       with TTC5/STRAP; the interaction results in the inhibition of JYM's
CC       nucleation activity in the cytoplasm due to competition with MAP1LC3B
CC       binding (PubMed:30420355). {ECO:0000250|UniProtKB:Q9QXM1,
CC       ECO:0000269|PubMed:30420355}.
CC   -!- INTERACTION:
CC       Q8N9B5; Q00987: MDM2; NbExp=2; IntAct=EBI-866435, EBI-389668;
CC       Q8N9B5-2; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-10268138, EBI-10171416;
CC       Q8N9B5-2; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-10268138, EBI-5916454;
CC       Q8N9B5-2; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-10268138, EBI-11522433;
CC       Q8N9B5-2; Q5RL73: RBM48; NbExp=3; IntAct=EBI-10268138, EBI-473821;
CC       Q8N9B5-2; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-10268138, EBI-726876;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9QXM1}.
CC       Cytoplasmic vesicle {ECO:0000269|PubMed:30420355}. Cytoplasm,
CC       cytoskeleton {ECO:0000269|PubMed:19287377,
CC       ECO:0000269|PubMed:30420355}. Endomembrane system; Lipid-anchor.
CC       Cytoplasmic vesicle, autophagosome membrane
CC       {ECO:0000269|PubMed:30420355}. Note=Localizes to the nucleus in most
CC       cell types. Accumulates in nucleus under DNA damage conditions,
CC       increasing p53/TP53 transcription response and reducing its influence
CC       on cell motility (By similarity). In primary neutrophils, it
CC       colocalizes with actin filaments at the leading edge and is excluded
CC       from the nucleus. Localization correlates with motility, because it
CC       moves from the nucleus to the cytoplasmic compartment when cells are
CC       differentiated from nonmotile cells into highly motile neutrophil-like
CC       cells. Localizes to cytoplasmic vesicles which associate with actin
CC       filament and autophagosomal membranes upon starvation-induced autophagy
CC       (PubMed:30420355). {ECO:0000250, ECO:0000269|PubMed:30420355}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8N9B5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8N9B5-2; Sequence=VSP_032310;
CC   -!- INDUCTION: By E2F. {ECO:0000269|PubMed:15706352}.
CC   -!- DOMAIN: The N-terminal region is involved in actin binding and actin
CC       nucleation activity. {ECO:0000269|PubMed:30420355}.
CC   -!- PTM: Ubiquitinated by MDM2, leading to its subsequent degradation by
CC       the proteasome. In case of DNA damage, the interaction with MDM2 is
CC       altered, preventing degradation and allowing interaction with
CC       p300/EP300 and its function in p53/TP53 stress response (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the JMY family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI30625.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC04495.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=EAW95834.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC016559; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC020898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471084; EAW95834.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC130624; AAI30625.1; ALT_INIT; mRNA.
DR   EMBL; AK095189; BAC04495.1; ALT_INIT; mRNA.
DR   CCDS; CCDS4047.3; -. [Q8N9B5-1]
DR   RefSeq; NP_689618.4; NM_152405.4. [Q8N9B5-1]
DR   AlphaFoldDB; Q8N9B5; -.
DR   BioGRID; 126372; 42.
DR   IntAct; Q8N9B5; 18.
DR   MINT; Q8N9B5; -.
DR   STRING; 9606.ENSP00000379441; -.
DR   GlyGen; Q8N9B5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8N9B5; -.
DR   PhosphoSitePlus; Q8N9B5; -.
DR   BioMuta; JMY; -.
DR   DMDM; 172045777; -.
DR   EPD; Q8N9B5; -.
DR   jPOST; Q8N9B5; -.
DR   MassIVE; Q8N9B5; -.
DR   MaxQB; Q8N9B5; -.
DR   PaxDb; 9606-ENSP00000379441; -.
DR   PeptideAtlas; Q8N9B5; -.
DR   ProteomicsDB; 72518; -. [Q8N9B5-1]
DR   ProteomicsDB; 72519; -. [Q8N9B5-2]
DR   Pumba; Q8N9B5; -.
DR   Antibodypedia; 24555; 283 antibodies from 30 providers.
DR   DNASU; 133746; -.
DR   Ensembl; ENST00000396137.5; ENSP00000379441.4; ENSG00000152409.9. [Q8N9B5-1]
DR   GeneID; 133746; -.
DR   KEGG; hsa:133746; -.
DR   MANE-Select; ENST00000396137.5; ENSP00000379441.4; NM_152405.5; NP_689618.4.
DR   UCSC; uc003kfx.5; human. [Q8N9B5-1]
DR   AGR; HGNC:28916; -.
DR   CTD; 133746; -.
DR   DisGeNET; 133746; -.
DR   GeneCards; JMY; -.
DR   HGNC; HGNC:28916; JMY.
DR   HPA; ENSG00000152409; Low tissue specificity.
DR   MIM; 604279; gene.
DR   neXtProt; NX_Q8N9B5; -.
DR   OpenTargets; ENSG00000152409; -.
DR   PharmGKB; PA164721124; -.
DR   VEuPathDB; HostDB:ENSG00000152409; -.
DR   eggNOG; ENOG502QRHU; Eukaryota.
DR   GeneTree; ENSGT00510000046704; -.
DR   HOGENOM; CLU_012316_0_0_1; -.
DR   InParanoid; Q8N9B5; -.
DR   OMA; PGEECSW; -.
DR   OrthoDB; 5354952at2759; -.
DR   PhylomeDB; Q8N9B5; -.
DR   TreeFam; TF331023; -.
DR   PathwayCommons; Q8N9B5; -.
DR   Reactome; R-HSA-6804760; Regulation of TP53 Activity through Methylation.
DR   SignaLink; Q8N9B5; -.
DR   SIGNOR; Q8N9B5; -.
DR   BioGRID-ORCS; 133746; 13 hits in 1157 CRISPR screens.
DR   ChiTaRS; JMY; human.
DR   GenomeRNAi; 133746; -.
DR   Pharos; Q8N9B5; Tbio.
DR   PRO; PR:Q8N9B5; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q8N9B5; Protein.
DR   Bgee; ENSG00000152409; Expressed in endothelial cell and 193 other cell types or tissues.
DR   GO; GO:0000421; C:autophagosome membrane; IDA:UniProtKB.
DR   GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0071933; F:Arp2/3 complex binding; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:HGNC-UCL.
DR   GO; GO:0070060; P:'de novo' actin filament nucleation; ISS:UniProtKB.
DR   GO; GO:0070358; P:actin polymerization-dependent cell motility; ISS:UniProtKB.
DR   GO; GO:0034314; P:Arp2/3 complex-mediated actin nucleation; ISS:UniProtKB.
DR   GO; GO:0009267; P:cellular response to starvation; IMP:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IBA:GO_Central.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:HGNC-UCL.
DR   InterPro; IPR031738; JMY/WHAMM.
DR   InterPro; IPR031808; JMY/WHAMM_N.
DR   InterPro; IPR003124; WH2_dom.
DR   PANTHER; PTHR23330:SF8; JUNCTION-MEDIATING AND -REGULATORY PROTEIN; 1.
DR   PANTHER; PTHR23330; P300 TRANSCRIPTIONAL COFACTOR JMY-RELATED; 1.
DR   Pfam; PF15871; JMY; 1.
DR   Pfam; PF15920; WHAMM-JMY_N; 2.
DR   SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR   PROSITE; PS51082; WH2; 1.
DR   Genevisible; Q8N9B5; HS.
PE   1: Evidence at protein level;
KW   Actin-binding; Alternative splicing; Coiled coil; Cytoplasm;
KW   Cytoplasmic vesicle; Cytoskeleton; DNA damage; DNA repair; Lipoprotein;
KW   Membrane; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..988
FT                   /note="Junction-mediating and -regulatory protein"
FT                   /id="PRO_0000324611"
FT   DOMAIN          921..938
FT                   /note="WH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00406"
FT   REGION          1..126
FT                   /note="Interaction with p300/EP300"
FT                   /evidence="ECO:0000250"
FT   REGION          51..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          478..567
FT                   /note="Interaction with p300/EP300"
FT                   /evidence="ECO:0000250"
FT   REGION          731..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          800..865
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          967..988
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          324..360
FT                   /evidence="ECO:0000255"
FT   COILED          489..541
FT                   /evidence="ECO:0000255"
FT   COILED          590..621
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        801..830
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        833..851
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        974..988
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         115
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         121
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         713
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         888
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QXM1"
FT   MOD_RES         974
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   VAR_SEQ         814..825
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032310"
FT   VARIANT         364
FT                   /note="M -> L (in dbSNP:rs13182512)"
FT                   /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2"
FT                   /id="VAR_039846"
FT   VARIANT         592
FT                   /note="A -> V (in dbSNP:rs12109475)"
FT                   /id="VAR_039847"
FT   VARIANT         720
FT                   /note="H -> R (in dbSNP:rs16876657)"
FT                   /id="VAR_039848"
SQ   SEQUENCE   988 AA;  111445 MW;  7166FF8AE325F37A CRC64;
     MSFALEETLE SDWVAVRPHV FDEREKHKFV FIVAWNEIEG KFAITCHNRT AQRQRSGSRE
     QAGARGGAEA GGAASDGSRG PGSPAGRGRP EATASATLVR SPGPRRSSAW AEGGSPRSTR
     SLLGDPRLRS PGSKGAESRL RSPVRAKPIP GQKTSEADDA AGAAAAAARP APREAQVSSV
     RIVSASGTVS EEIEVLEMVK EDEAPLALSD AEQPPPATEL ESPAEECSWA GLFSFQDLRA
     VHQQLCSVNS QLEPCLPVFP EEPSGMWTVL FGGAPEMTEQ EIDTLCYQLQ VYLGHGLDTC
     GWKILSQVLF TETDDPEEYY ESLSELRQKG YEEVLQRARK RIQELLDKHK NTESMVELLD
     LYQMEDEAYS SLAEATTELY QYLLQPFRDM RELAMLRRQQ IKISMENDYL GPRRIESLQK
     EDADWQRKAH MAVLSIQDLT VKYFEITAKA QKAVYDRMRA DQKKFGKASW AAAAERMEKL
     QYAVSKETLQ MMRAKEICLE QRKHALKEEM QSLRGGTEAI ARLDQLEADY YDLQLQLYEV
     QFEILKCEEL LLTAQLESIK RLISEKRDEV VYYDTYESME AMLEKEEMAA SAYLQREELQ
     KLQQKARQLE ARRGRVSAKK SYLRNKKEIC IAKHNEKIQQ RTRIEDEYRT HHTVQLKREK
     LHDEEERKSA WVSQERQRTL DRLRTFKQRY PGQVILKSTR LRLAHARRKG AASPVLQEDH
     CDSLPSVLQV EEKTEEVGEG RVKRGPSQTT EPQSLVQLED TSLTQLEATS LPLSGVTSEL
     PPTISLPLLN NNLEPCSVTI NPLPSPLPPT PPPPPPPPPP PPPPPLPVAK DSGPETLEKD
     LPRKEGNEKR IPKSASAPSA HLFDSSQLVS ARKKLRKTAE GLQRRRVSSP MDEVLASLKR
     GSFHLKKVEQ RTLPPFPDED DSNNILAQIR KGVKLKKVQK DVLRESFTLL PDTDPLTRSI
     HEALRRIKEA SPESEDEEEA LPCTDWEN
//