BIN2_HUMAN
ID BIN2_HUMAN Reviewed; 565 AA.
AC Q9UBW5; B7Z6F3; F5H0W4; Q86VV0; Q9NWK4; Q9UKN4;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Bridging integrator 2;
DE AltName: Full=Breast cancer-associated protein 1;
GN Name=BIN2; Synonyms=BRAP1;
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), VARIANT ASP-529, INDUCTION,
RP INTERACTION WITH BIN2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10903846; DOI=10.1006/geno.2000.6216;
RA Ge K., Prendergast G.C.;
RT "Bin2, a functionally nonredundant member of the BAR adaptor gene family.";
RL Genomics 67:210-220(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND VARIANTS ASN-48
RP AND ASP-529.
RC TISSUE=Mammary gland;
RA Miki Y., Saito H.;
RT "Genomic structure and chromosome location of the BRAP1 gene.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP ASP-529.
RC TISSUE=Colon, and Placenta;
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=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASP-529.
RC TISSUE=Ovary;
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=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-273; SER-357; SER-436;
RP THR-438; SER-444; SER-447 AND SER-458, AND IDENTIFICATION BY MASS
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395; SER-444 AND SER-451, AND
RP IDENTIFICATION BY 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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS) OF 1-238, FUNCTION, DOMAIN, SUBUNIT,
RP INTERACTION WITH ARHGEF6; ARHGEF7; SH3GL1; SH3GL2; SH3GL3, IDENTIFICATION
RP IN A COMPLEX WITH GIT2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP MUTAGENESIS OF PHE-13; PHE-21; VAL-81 AND SER-214.
RX PubMed=23285027; DOI=10.1371/journal.pone.0052401;
RA Sanchez-Barrena M.J., Vallis Y., Clatworthy M.R., Doherty G.J.,
RA Veprintsev D.B., Evans P.R., McMahon H.T.;
RT "Bin2 is a membrane sculpting N-BAR protein that influences leucocyte
RT podosomes, motility and phagocytosis.";
RL PLoS ONE 7:E52401-E52401(2012).
CC -!- FUNCTION: Promotes cell motility and migration, probably via its
CC interaction with the cell membrane and with podosome proteins that
CC mediate interaction with the cytoskeleton. Modulates membrane curvature
CC and mediates membrane tubulation. Plays a role in podosome formation.
CC Inhibits phagocytosis. {ECO:0000269|PubMed:23285027}.
CC -!- SUBUNIT: Homodimer. Interacts with BIN1. Interacts with ARHGEF6 (via
CC SH3 domain), ARHGEF7 (via SH3 domain), SH3GL1, SH3GL2 and SH3GL3.
CC Identified in a complex with ARHGEF6 and GIT2.
CC {ECO:0000269|PubMed:10903846, ECO:0000269|PubMed:23285027}.
CC -!- INTERACTION:
CC Q9UBW5; Q92624: APPBP2; NbExp=3; IntAct=EBI-2042570, EBI-743771;
CC Q9UBW5; O00499: BIN1; NbExp=2; IntAct=EBI-2042570, EBI-719094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23285027}. Cell
CC projection, podosome membrane {ECO:0000269|PubMed:23285027}; Peripheral
CC membrane protein {ECO:0000269|PubMed:23285027}; Cytoplasmic side
CC {ECO:0000269|PubMed:23285027}. Cytoplasm, cell cortex
CC {ECO:0000269|PubMed:23285027}. Cell projection, phagocytic cup
CC {ECO:0000269|PubMed:23285027}. Note=Associates with membranes enriched
CC in phosphoinositides. Detected in the actin-rich cell cortex at the
CC leading edge of migrating cells. Detected at podosomes, at an actin-
CC rich ring-like structure. {ECO:0000269|PubMed:23285027}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UBW5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBW5-2; Sequence=VSP_021328;
CC Name=3;
CC IsoId=Q9UBW5-3; Sequence=VSP_059731;
CC -!- TISSUE SPECIFICITY: Detected in natural killer cells (at protein
CC level). Highest level expression seen in spleen and peripheral blood
CC leukocytes and is also expressed at high levels in thymus, colon and
CC placenta, suggesting preferential expression in hematopoietic tissues.
CC {ECO:0000269|PubMed:10903846, ECO:0000269|PubMed:23285027}.
CC -!- INDUCTION: Up-regulated during monocytic differentiation.
CC {ECO:0000269|PubMed:10903846}.
CC -!- DOMAIN: The BAR domain mediates dimerization and interaction with
CC membranes enriched in phosphatidylinositides.
CC {ECO:0000269|PubMed:23285027}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91376.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA91376.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF146531; AAD54227.1; -; mRNA.
DR EMBL; AB032698; BAA88108.1; -; mRNA.
DR EMBL; AB032710; BAA88125.1; -; Genomic_DNA.
DR EMBL; AK000783; BAA91376.1; ALT_SEQ; mRNA.
DR EMBL; AK300211; BAH13239.1; -; mRNA.
DR EMBL; AC046135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047686; AAH47686.1; -; mRNA.
DR CCDS; CCDS76561.1; -. [Q9UBW5-3]
DR CCDS; CCDS8811.2; -. [Q9UBW5-1]
DR RefSeq; NP_001276936.1; NM_001290007.1. [Q9UBW5-3]
DR RefSeq; NP_001276937.1; NM_001290008.1. [Q9UBW5-2]
DR RefSeq; NP_001276938.1; NM_001290009.1.
DR RefSeq; NP_057377.3; NM_016293.3. [Q9UBW5-1]
DR PDB; 4AVM; X-ray; 1.91 A; A=11-245.
DR PDB; 4I1Q; X-ray; 2.53 A; A/B=20-238.
DR PDBsum; 4AVM; -.
DR PDBsum; 4I1Q; -.
DR AlphaFoldDB; Q9UBW5; -.
DR SMR; Q9UBW5; -.
DR BioGRID; 119528; 8.
DR IntAct; Q9UBW5; 10.
DR STRING; 9606.ENSP00000267012; -.
DR iPTMnet; Q9UBW5; -.
DR PhosphoSitePlus; Q9UBW5; -.
DR SwissPalm; Q9UBW5; -.
DR BioMuta; BIN2; -.
DR DMDM; 143811367; -.
DR OGP; Q9UBW5; -.
DR EPD; Q9UBW5; -.
DR jPOST; Q9UBW5; -.
DR MassIVE; Q9UBW5; -.
DR MaxQB; Q9UBW5; -.
DR PaxDb; Q9UBW5; -.
DR PeptideAtlas; Q9UBW5; -.
DR PRIDE; Q9UBW5; -.
DR ProteomicsDB; 25466; -.
DR ProteomicsDB; 84083; -. [Q9UBW5-1]
DR ProteomicsDB; 84084; -. [Q9UBW5-2]
DR Antibodypedia; 26379; 189 antibodies from 21 providers.
DR DNASU; 51411; -.
DR Ensembl; ENST00000452142.7; ENSP00000410217.3; ENSG00000110934.13. [Q9UBW5-2]
DR Ensembl; ENST00000544402.5; ENSP00000445874.1; ENSG00000110934.13. [Q9UBW5-3]
DR Ensembl; ENST00000615107.6; ENSP00000483983.2; ENSG00000110934.13. [Q9UBW5-1]
DR GeneID; 51411; -.
DR KEGG; hsa:51411; -.
DR MANE-Select; ENST00000615107.6; ENSP00000483983.2; NM_016293.4; NP_057377.4.
DR UCSC; uc058ocp.1; human. [Q9UBW5-1]
DR CTD; 51411; -.
DR DisGeNET; 51411; -.
DR GeneCards; BIN2; -.
DR HGNC; HGNC:1053; BIN2.
DR HPA; ENSG00000110934; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 605936; gene.
DR neXtProt; NX_Q9UBW5; -.
DR OpenTargets; ENSG00000110934; -.
DR PharmGKB; PA25356; -.
DR VEuPathDB; HostDB:ENSG00000110934; -.
DR eggNOG; KOG3771; Eukaryota.
DR GeneTree; ENSGT00950000182882; -.
DR InParanoid; Q9UBW5; -.
DR OMA; STMQNTH; -.
DR OrthoDB; 1366218at2759; -.
DR PhylomeDB; Q9UBW5; -.
DR TreeFam; TF313542; -.
DR PathwayCommons; Q9UBW5; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-9673768; Signaling by membrane-tethered fusions of PDGFRA or PDGFRB.
DR SignaLink; Q9UBW5; -.
DR BioGRID-ORCS; 51411; 11 hits in 1061 CRISPR screens.
DR ChiTaRS; BIN2; human.
DR GenomeRNAi; 51411; -.
DR Pharos; Q9UBW5; Tbio.
DR PRO; PR:Q9UBW5; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9UBW5; protein.
DR Bgee; ENSG00000110934; Expressed in granulocyte and 129 other tissues.
DR ExpressionAtlas; Q9UBW5; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0002102; C:podosome; IDA:UniProtKB.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0005543; F:phospholipid binding; IDA:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; IMP:UniProtKB.
DR GO; GO:0097320; P:plasma membrane tubulation; IDA:UniProtKB.
DR GO; GO:0071800; P:podosome assembly; IMP:UniProtKB.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR003005; Amphiphysin.
DR InterPro; IPR004148; BAR_dom.
DR InterPro; IPR028827; BIN2.
DR PANTHER; PTHR46514:SF1; PTHR46514:SF1; 1.
DR Pfam; PF03114; BAR; 1.
DR PRINTS; PR01251; AMPHIPHYSIN.
DR SMART; SM00721; BAR; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR PROSITE; PS51021; BAR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell junction; Cell membrane;
KW Cell projection; Coiled coil; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..565
FT /note="Bridging integrator 2"
FT /id="PRO_0000256140"
FT DOMAIN 28..244
FT /note="BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00361"
FT REGION 267..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 304..329
FT /evidence="ECO:0000255"
FT COMPBIAS 267..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..331
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..489
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 273
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3Z6Q9"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 438
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3Z6Q9"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 451
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:D3Z6Q9"
FT VAR_SEQ 1..27
FT /note="MAEGKAGGAAGLFAKQVQKKFSRAQEK -> M (in isoform 3)"
FT /id="VSP_059731"
FT VAR_SEQ 105..136
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021328"
FT VARIANT 48
FT /note="S -> N (in dbSNP:rs7312857)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_028883"
FT VARIANT 529
FT /note="N -> D (in dbSNP:rs7954976)"
FT /evidence="ECO:0000269|PubMed:10903846,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.2"
FT /id="VAR_028884"
FT MUTAGEN 13
FT /note="F->A: Strongly reduces binding to membranes."
FT /evidence="ECO:0000269|PubMed:23285027"
FT MUTAGEN 21
FT /note="F->A: Strongly reduces binding to membranes."
FT /evidence="ECO:0000269|PubMed:23285027"
FT MUTAGEN 81
FT /note="V->R: Abolishes dimerization and membrane binding;
FT when associated with E-214."
FT /evidence="ECO:0000269|PubMed:23285027"
FT MUTAGEN 214
FT /note="S->E: Abolishes dimerization and membrane binding;
FT when associated with R-81."
FT /evidence="ECO:0000269|PubMed:23285027"
FT CONFLICT 163
FT /note="Missing (in Ref. 1; AAD54227)"
FT /evidence="ECO:0000305"
FT HELIX 16..31
FT /evidence="ECO:0007829|PDB:4AVM"
FT HELIX 41..88
FT /evidence="ECO:0007829|PDB:4AVM"
FT HELIX 96..120
FT /evidence="ECO:0007829|PDB:4AVM"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:4AVM"
FT HELIX 132..160
FT /evidence="ECO:0007829|PDB:4AVM"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:4I1Q"
FT HELIX 167..200
FT /evidence="ECO:0007829|PDB:4AVM"
FT HELIX 202..241
FT /evidence="ECO:0007829|PDB:4AVM"
SQ SEQUENCE 565 AA; 61874 MW; B1D1FB89A97E9E43 CRC64;
MAEGKAGGAA GLFAKQVQKK FSRAQEKVLQ KLGKAVETKD ERFEQSASNF YQQQAEGHKL
YKDLKNFLSA VKVMHESSKR VSETLQEIYS SEWDGHEELK AIVWNNDLLW EDYEEKLADQ
AVRTMEIYVA QFSEIKERIA KRGRKLVDYD SARHHLEAVQ NAKKKDEAKT AKAEEEFNKA
QTVFEDLNQE LLEELPILYN SRIGCYVTIF QNISNLRDVF YREMSKLNHN LYEVMSKLEK
QHSNKVFVVK GLSSSSRRSL VISPPVRTAT VSSPLTSPTS PSTLSLKSES ESVSATEDLA
PDAAQGEDNS EIKELLEEEE IEKEGSEASS SEEDEPLPAC NGPAQAQPSP TTERAKSQEE
VLPSSTTPSP GGALSPSGQP SSSATEVVLR TRTASEGSEQ PKKRASIQRT SAPPSRPPPP
RATASPRPSS GNIPSSPTAS GGGSPTSPRA SLGTGTASPR TSLEVSPNPE PPEKPVRTPE
AKENENIHNQ NPEELCTSPT LMTSQVASEP GEAKKMEDKE KDNKLISANS SEGQDQLQVS
MVPENNNLTA PEPQEEVSTS ENPQL
