BNIP2_HUMAN
ID BNIP2_HUMAN Reviewed; 314 AA.
AC Q12982; B4DS94;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=BCL2/adenovirus E1B 19 kDa protein-interacting protein 2;
GN Name=BNIP2; Synonyms=NIP2;
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).
RX PubMed=7954800; DOI=10.1016/0092-8674(94)90202-x;
RA Boyd J.M., Malstrom S., Subramanian T., Venkatesh L.K., Schaeper U.,
RA Elangovan B., D'Sa-Eipper C., Chinnadurai G.;
RT "Adenovirus E1B 19 kDa and Bcl-2 proteins interact with a common set of
RT cellular proteins.";
RL Cell 79:341-351(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [GENOMIC DNA], AND VARIANT THR-24.
RG NIEHS SNPs program;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(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-114, 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=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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41; SER-77; THR-87; SER-89;
RP SER-92 AND SER-114, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: Implicated in the suppression of cell death. Interacts with
CC the BCL-2 and adenovirus E1B 19 kDa proteins.
CC -!- INTERACTION:
CC Q12982; Q8TB40: ABHD4; NbExp=3; IntAct=EBI-752094, EBI-7131019;
CC Q12982; Q9NRZ7: AGPAT3; NbExp=3; IntAct=EBI-752094, EBI-2803601;
CC Q12982; Q9UH17-2: APOBEC3B; NbExp=3; IntAct=EBI-752094, EBI-17624977;
CC Q12982; Q12983: BNIP3; NbExp=3; IntAct=EBI-752094, EBI-749464;
CC Q12982; P0C671: BNIP5; NbExp=3; IntAct=EBI-752094, EBI-12806802;
CC Q12982; Q9H9P2: CHODL; NbExp=3; IntAct=EBI-752094, EBI-17447707;
CC Q12982; Q7Z7G2: CPLX4; NbExp=3; IntAct=EBI-752094, EBI-18013275;
CC Q12982; P00387: CYB5R3; NbExp=3; IntAct=EBI-752094, EBI-1046040;
CC Q12982; Q9BSY9: DESI2; NbExp=3; IntAct=EBI-752094, EBI-12878374;
CC Q12982; Q6ZPD8: DGAT2L6; NbExp=3; IntAct=EBI-752094, EBI-12831978;
CC Q12982; Q96LJ7: DHRS1; NbExp=3; IntAct=EBI-752094, EBI-746300;
CC Q12982; O14681: EI24; NbExp=3; IntAct=EBI-752094, EBI-2339413;
CC Q12982; O75477: ERLIN1; NbExp=3; IntAct=EBI-752094, EBI-359299;
CC Q12982; Q6P587-2: FAHD1; NbExp=3; IntAct=EBI-752094, EBI-12902289;
CC Q12982; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-752094, EBI-18304435;
CC Q12982; Q92520: FAM3C; NbExp=3; IntAct=EBI-752094, EBI-2876774;
CC Q12982; Q969F0: FATE1; NbExp=6; IntAct=EBI-752094, EBI-743099;
CC Q12982; P42685: FRK; NbExp=8; IntAct=EBI-752094, EBI-1383583;
CC Q12982; Q5T7V8: GORAB; NbExp=3; IntAct=EBI-752094, EBI-3917143;
CC Q12982; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-752094, EBI-13345167;
CC Q12982; Q8TED1: GPX8; NbExp=3; IntAct=EBI-752094, EBI-11721746;
CC Q12982; Q8IUY3: GRAMD2A; NbExp=3; IntAct=EBI-752094, EBI-11984319;
CC Q12982; O15499: GSC2; NbExp=3; IntAct=EBI-752094, EBI-19954058;
CC Q12982; O95279: KCNK5; NbExp=3; IntAct=EBI-752094, EBI-3934936;
CC Q12982; Q07866: KLC1; NbExp=3; IntAct=EBI-752094, EBI-721019;
CC Q12982; Q07866-2: KLC1; NbExp=3; IntAct=EBI-752094, EBI-11979975;
CC Q12982; Q5T700: LDLRAD1; NbExp=3; IntAct=EBI-752094, EBI-10173166;
CC Q12982; Q9H400: LIME1; NbExp=3; IntAct=EBI-752094, EBI-2830566;
CC Q12982; P50221: MEOX1; NbExp=3; IntAct=EBI-752094, EBI-2864512;
CC Q12982; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-752094, EBI-16439278;
CC Q12982; Q9ULV0: MYO5B; NbExp=5; IntAct=EBI-752094, EBI-311356;
CC Q12982; Q9ULV0-2: MYO5B; NbExp=3; IntAct=EBI-752094, EBI-14093244;
CC Q12982; P32243-2: OTX2; NbExp=3; IntAct=EBI-752094, EBI-9087860;
CC Q12982; O00623: PEX12; NbExp=3; IntAct=EBI-752094, EBI-594836;
CC Q12982; Q53GL0: PLEKHO1; NbExp=3; IntAct=EBI-752094, EBI-949945;
CC Q12982; Q8TDF6-2: RASGRP4; NbExp=3; IntAct=EBI-752094, EBI-12816371;
CC Q12982; O95562: SFT2D2; NbExp=3; IntAct=EBI-752094, EBI-4402330;
CC Q12982; H3BQL7: SIN3A; NbExp=3; IntAct=EBI-752094, EBI-13384308;
CC Q12982; Q7Z769: SLC35E3; NbExp=3; IntAct=EBI-752094, EBI-13389236;
CC Q12982; Q9NUM3: SLC39A9; NbExp=3; IntAct=EBI-752094, EBI-2823239;
CC Q12982; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-752094, EBI-5235586;
CC Q12982; P21579: SYT1; NbExp=3; IntAct=EBI-752094, EBI-524909;
CC Q12982; Q8N9I0: SYT2; NbExp=3; IntAct=EBI-752094, EBI-8032987;
CC Q12982; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-752094, EBI-10982110;
CC Q12982; O15393-2: TMPRSS2; NbExp=3; IntAct=EBI-752094, EBI-12345267;
CC Q12982; Q9Y320: TMX2; NbExp=3; IntAct=EBI-752094, EBI-6447886;
CC Q12982; O95070: YIF1A; NbExp=3; IntAct=EBI-752094, EBI-2799703;
CC Q12982; B2R9H7; NbExp=3; IntAct=EBI-752094, EBI-10175711;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, perinuclear region.
CC Note=Localizes to the nuclear envelope region and to other cytoplasmic
CC structures.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q12982-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12982-2; Sequence=VSP_038964;
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/bnip2/";
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DR EMBL; U15173; AAC00021.1; -; mRNA.
DR EMBL; AK299628; BAG61556.1; -; mRNA.
DR EMBL; AY268590; AAP03429.1; -; Genomic_DNA.
DR EMBL; AC092755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002461; AAH02461.1; -; mRNA.
DR CCDS; CCDS10174.2; -. [Q12982-1]
DR CCDS; CCDS81889.1; -. [Q12982-1]
DR PIR; I38864; I38864.
DR RefSeq; NP_001307604.1; NM_001320675.1. [Q12982-1]
DR RefSeq; NP_004321.2; NM_004330.3. [Q12982-1]
DR AlphaFoldDB; Q12982; -.
DR BioGRID; 107131; 69.
DR CORUM; Q12982; -.
DR ELM; Q12982; -.
DR IntAct; Q12982; 53.
DR MINT; Q12982; -.
DR STRING; 9606.ENSP00000267859; -.
DR SwissLipids; SLP:000001512; -.
DR GlyGen; Q12982; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12982; -.
DR PhosphoSitePlus; Q12982; -.
DR BioMuta; BNIP2; -.
DR DMDM; 6093506; -.
DR EPD; Q12982; -.
DR jPOST; Q12982; -.
DR MassIVE; Q12982; -.
DR MaxQB; Q12982; -.
DR PaxDb; Q12982; -.
DR PeptideAtlas; Q12982; -.
DR PRIDE; Q12982; -.
DR ProteomicsDB; 59079; -. [Q12982-1]
DR ProteomicsDB; 59080; -. [Q12982-2]
DR Antibodypedia; 12947; 333 antibodies from 29 providers.
DR DNASU; 663; -.
DR Ensembl; ENST00000267859.8; ENSP00000267859.4; ENSG00000140299.13. [Q12982-1]
DR Ensembl; ENST00000415213.7; ENSP00000412767.3; ENSG00000140299.13. [Q12982-1]
DR Ensembl; ENST00000607373.6; ENSP00000475320.1; ENSG00000140299.13. [Q12982-1]
DR GeneID; 663; -.
DR KEGG; hsa:663; -.
DR MANE-Select; ENST00000607373.6; ENSP00000475320.1; NM_004330.4; NP_004321.3.
DR UCSC; uc010uhb.3; human. [Q12982-1]
DR CTD; 663; -.
DR DisGeNET; 663; -.
DR GeneCards; BNIP2; -.
DR HGNC; HGNC:1083; BNIP2.
DR HPA; ENSG00000140299; Tissue enhanced (bone).
DR MIM; 603292; gene.
DR neXtProt; NX_Q12982; -.
DR OpenTargets; ENSG00000140299; -.
DR PharmGKB; PA25393; -.
DR VEuPathDB; HostDB:ENSG00000140299; -.
DR eggNOG; ENOG502QUXY; Eukaryota.
DR GeneTree; ENSGT00940000158531; -.
DR HOGENOM; CLU_039135_1_0_1; -.
DR InParanoid; Q12982; -.
DR OrthoDB; 755773at2759; -.
DR PhylomeDB; Q12982; -.
DR PathwayCommons; Q12982; -.
DR Reactome; R-HSA-525793; Myogenesis.
DR SignaLink; Q12982; -.
DR SIGNOR; Q12982; -.
DR BioGRID-ORCS; 663; 14 hits in 1077 CRISPR screens.
DR ChiTaRS; BNIP2; human.
DR GeneWiki; BNIP2; -.
DR GenomeRNAi; 663; -.
DR Pharos; Q12982; Tbio.
DR PRO; PR:Q12982; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q12982; protein.
DR Bgee; ENSG00000140299; Expressed in calcaneal tendon and 192 other tissues.
DR ExpressionAtlas; Q12982; baseline and differential.
DR Genevisible; Q12982; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; TAS:ProtInc.
DR GO; GO:0006915; P:apoptotic process; IPI:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0090649; P:response to oxygen-glucose deprivation; IEA:Ensembl.
DR CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; -; 1.
DR InterPro; IPR022181; Bcl2-/adenovirus-E1B.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR Pfam; PF12496; BNIP2; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; SSF52087; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cytoplasm; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..314
FT /note="BCL2/adenovirus E1B 19 kDa protein-interacting
FT protein 2"
FT /id="PRO_0000064961"
FT DOMAIN 147..304
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00056"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 87
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1
FT /note="M -> MEPCPSSAPPPFYPGVGEVAGLRWFSIYDQRPSWYRTKKLGLLDIGS
FT LDYQEFVVDIESRLRM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_038964"
FT VARIANT 24
FT /note="S -> T (in dbSNP:rs6151509)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_018837"
FT CONFLICT 175
FT /note="M -> T (in Ref. 2; BAG61556)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 36018 MW; 0A3CEC636569DD2F CRC64;
MEGVELKEEW QDEDFPIPLP EDDSIEADIL AITGPEDQPG SLEVNGNKVR KKLMAPDISL
TLDPSDGSVL SDDLDESGEI DLDGLDTPSE NSNEFEWEDD LPKPKTTEVI RKGSITEYTA
AEEKEDGRRW RMFRIGEQDH RVDMKAIEPY KKVISHGGYY GDGLNAIVVF AVCFMPESSQ
PNYRYLMDNL FKYVIGTLEL LVAENYMIVY LNGATTRRKM PSLGWLRKCY QQIDRRLRKN
LKSLIIVHPS WFIRTLLAVT RPFISSKFSQ KIRYVFNLAE LAELVPMEYV GIPECIKQVD
QELNGKQDEP KNEQ
