ID PITM1_HUMAN Reviewed; 1244 AA. AC O00562; A6NME4; Q6T7X3; Q8TBN3; Q9BZ73; DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 31-OCT-2006, sequence version 4. DT 27-MAR-2024, entry version 174. DE RecName: Full=Membrane-associated phosphatidylinositol transfer protein 1; DE AltName: Full=Drosophila retinal degeneration B homolog; DE AltName: Full=Phosphatidylinositol transfer protein, membrane-associated 1; DE Short=PITPnm 1; DE AltName: Full=Pyk2 N-terminal domain-interacting receptor 2; DE Short=NIR-2; GN Name=PITPNM1; Synonyms=DRES9, NIR2, PITPNM; 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=9680295; DOI=10.1046/j.1365-4624.1997.00015.x; RA Rubboli F., Bulfone A., Bogni S., Marchitiello A., Zollo M., Borsani G., RA Ballabio A., Banfi S.; RT "A mammalian homologue of the Drosophila retinal degeneration B gene: RT implications for the evolution of phototransduction mechanisms."; RL Genes Funct. 1:205-213(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CALCIUM-BINDING, RP INTERACTION WITH PTK2B, PHOSPHORYLATION, AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=10022914; DOI=10.1128/mcb.19.3.2278; RA Lev S., Hernandez J., Martinez R., Chen A., Plowman G., Schlessinger J.; RT "Identification of a novel family of targets of PYK2 related to Drosophila RT retinal degeneration B (rdgB) protein."; RL Mol. Cell. Biol. 19:2278-2288(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=15627748; DOI=10.1159/000081519; RA Ocaka L., Spalluto C., Wilson D.I., Hunt D.M., Halford S.; RT "Chromosomal localization, genomic organization and evolution of the genes RT encoding human phosphatidylinositol transfer protein membrane-associated RT (PITPNM) 1, 2 and 3."; RL Cytogenet. Genome Res. 108:293-302(2005). 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 2). RC TISSUE=Duodenum; 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 FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=10531358; DOI=10.1074/jbc.274.44.31553; RA Fullwood Y., dos Santos M., Hsuan J.J.; RT "Cloning and characterization of a novel human phosphatidylinositol RT transfer protein, rdgBbeta."; RL J. Biol. Chem. 274:31553-31558(1999). RN [8] RP SUBCELLULAR LOCATION, MUTAGENESIS OF THR-59, AND PHOSPHORYLATION AT THR-59. RX PubMed=12225667; DOI=10.1016/s0960-9822(02)01107-7; RA Litvak V., Shaul Y.D., Shulewitz M., Amarilio R., Carmon S., Lev S.; RT "Targeting of Nir2 to lipid droplets is regulated by a specific threonine RT residue within its PI-transfer domain."; RL Curr. Biol. 12:1513-1518(2002). RN [9] RP FUNCTION, AND INTERACTION WITH RHOA. RX PubMed=11909959; DOI=10.1128/mcb.22.8.2650-2662.2002; RA Tian D., Litvak V., Toledo-Rodriguez M., Carmon S., Lev S.; RT "Nir2, a novel regulator of cell morphogenesis."; RL Mol. Cell. Biol. 22:2650-2662(2002). RN [10] RP PHOSPHORYLATION AT THR-287; SER-382 AND SER-896, IDENTIFICATION BY MASS RP SPECTROMETRY, MUTAGENESIS OF THR-287; SER-300; SER-326; SER-382; THR-389; RP THR-794; SER-896 AND THR-1223, INTERACTION WITH CDK1 AND PLK1, AND RP SUBCELLULAR LOCATION. RX PubMed=15125835; DOI=10.1016/s1097-2765(04)00214-x; RA Litvak V., Argov R., Dahan N., Ramachandran S., Amarilio R., Shainskaya A., RA Lev S.; RT "Mitotic phosphorylation of the peripheral Golgi protein Nir2 by Cdk1 RT provides a docking mechanism for Plk1 and affects cytokinesis completion."; RL Mol. Cell 14:319-330(2004). RN [11] RP FUNCTION, INTERACTION WITH VAPB, AND MUTAGENESIS OF 349-GLU--ALA-353. RX PubMed=15545272; DOI=10.1074/jbc.m409566200; RA Amarilio R., Ramachandran S., Sabanay H., Lev S.; RT "Differential regulation of endoplasmic reticulum structure through VAP-Nir RT protein interaction."; RL J. Biol. Chem. 280:5934-5944(2005). RN [12] RP FUNCTION. RX PubMed=15723057; DOI=10.1038/ncb1221; RA Litvak V., Dahan N., Ramachandran S., Sabanay H., Lev S.; RT "Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 RT protein is critical for Golgi secretory function."; RL Nat. Cell Biol. 7:225-234(2005). RN [13] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=22822086; DOI=10.1074/jbc.m112.375840; RA Garner K., Hunt A.N., Koster G., Somerharju P., Groves E., Li M., Raghu P., RA Holic R., Cockcroft S.; RT "Phosphatidylinositol transfer protein, cytoplasmic 1 (PITPNC1) binds and RT transfers phosphatidic acid."; RL J. Biol. Chem. 287:32263-32276(2012). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621 AND SER-1237, 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600 AND SER-621, 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). CC -!- FUNCTION: Catalyzes the transfer of phosphatidylinositol (PI) between CC membranes (PubMed:22822086, PubMed:10531358). Binds PI, CC phosphatidylcholine (PC) and phosphatidic acid (PA) with the binding CC affinity order of PI > PA > PC (PubMed:22822086). Regulates RHOA CC activity, and plays a role in cytoskeleton remodeling CC (PubMed:11909959). Necessary for normal completion of cytokinesis CC (PubMed:15125835). Plays a role in maintaining normal diacylglycerol CC levels in the Golgi apparatus (PubMed:15723057). Necessary for CC maintaining the normal structure of the endoplasmic reticulum and the CC Golgi apparatus (PubMed:15545272). Required for protein export from the CC endoplasmic reticulum and the Golgi (PubMed:15723057). Binds calcium CC ions (PubMed:10022914). {ECO:0000269|PubMed:10022914, CC ECO:0000269|PubMed:10531358, ECO:0000269|PubMed:11909959, CC ECO:0000269|PubMed:15545272, ECO:0000269|PubMed:15723057, CC ECO:0000269|PubMed:22822086}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out); CC Xref=Rhea:RHEA:38691, ChEBI:CHEBI:57880; CC Evidence={ECO:0000269|PubMed:10531358, ECO:0000269|PubMed:22822086}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692; CC Evidence={ECO:0000305|PubMed:22822086}; CC -!- SUBUNIT: Interacts with PIK4CA (By similarity). Interacts with PTK2B CC via its C-terminus. Interacts with RHOA. Has higher affinity for the CC inactive, GDP-bound form of RHOA. The CDK1-phosphorylated form CC interacts with PLK1. Interacts with VAPB. {ECO:0000250, CC ECO:0000269|PubMed:10022914, ECO:0000269|PubMed:11909959, CC ECO:0000269|PubMed:15125835, ECO:0000269|PubMed:15545272}. CC -!- INTERACTION: CC O00562; Q12800: TFCP2; NbExp=3; IntAct=EBI-2861268, EBI-717422; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, Golgi stack membrane CC {ECO:0000269|PubMed:12225667}; Peripheral membrane protein. Endoplasmic CC reticulum membrane {ECO:0000269|PubMed:12225667}; Peripheral membrane CC protein. Lipid droplet {ECO:0000269|PubMed:12225667}. Cleavage furrow CC {ECO:0000269|PubMed:15125835}. Midbody {ECO:0000269|PubMed:15125835}. CC Note=Peripheral membrane protein associated with Golgi stacks in CC interphase cells. A minor proportion is associated with the endoplasmic CC reticulum. Associated with lipid droplets (PubMed:12225667). CC Dissociates from the Golgi early on in mitosis and localizes to the CC cleavage furrow and midbody during cytokinesis (PubMed:15125835). CC {ECO:0000269|PubMed:12225667, ECO:0000269|PubMed:15125835}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O00562-1; Sequence=Displayed; CC Name=2; CC IsoId=O00562-2; Sequence=VSP_021157; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10022914}. CC -!- PTM: Phosphorylated on multiple sites by CDK1 at the onset of mitosis. CC Phosphorylation facilitates dissociation from the Golgi complex and is CC required for interaction with PLK1. CC -!- PTM: Phosphorylated on threonine residues upon treatment with oleic CC acid. CC -!- PTM: Phosphorylated on tyrosine residues by PTK2B. CC -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI transfer CC class IIA subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X98654; CAA67224.1; -; mRNA. DR EMBL; AF334584; AAK01444.1; -; mRNA. DR EMBL; AY429102; AAR06909.1; -; mRNA. DR EMBL; AP001184; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471076; EAW74638.1; -; Genomic_DNA. DR EMBL; BC022230; AAH22230.1; -; mRNA. DR CCDS; CCDS31620.1; -. [O00562-1] DR CCDS; CCDS44659.1; -. [O00562-2] DR RefSeq; NP_001124320.1; NM_001130848.1. [O00562-2] DR RefSeq; NP_004901.2; NM_004910.2. [O00562-1] DR RefSeq; XP_016874075.1; XM_017018586.1. [O00562-1] DR AlphaFoldDB; O00562; -. DR SMR; O00562; -. DR BioGRID; 114965; 17. DR ELM; O00562; -. DR IntAct; O00562; 9. DR MINT; O00562; -. DR STRING; 9606.ENSP00000348772; -. DR ChEMBL; CHEMBL1764937; -. DR SwissLipids; SLP:000000414; -. DR TCDB; 9.A.78.1.1; the retinal degeneration b protein (rdgb) family. DR GlyCosmos; O00562; 2 sites, 1 glycan. DR GlyGen; O00562; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; O00562; -. DR PhosphoSitePlus; O00562; -. DR BioMuta; PITPNM1; -. DR EPD; O00562; -. DR jPOST; O00562; -. DR MassIVE; O00562; -. DR MaxQB; O00562; -. DR PaxDb; 9606-ENSP00000348772; -. DR PeptideAtlas; O00562; -. DR ProteomicsDB; 47977; -. [O00562-1] DR ProteomicsDB; 47978; -. [O00562-2] DR Pumba; O00562; -. DR Antibodypedia; 30438; 242 antibodies from 28 providers. DR DNASU; 9600; -. DR Ensembl; ENST00000356404.8; ENSP00000348772.3; ENSG00000110697.13. [O00562-1] DR Ensembl; ENST00000436757.6; ENSP00000398787.2; ENSG00000110697.13. [O00562-2] DR Ensembl; ENST00000534749.5; ENSP00000437286.1; ENSG00000110697.13. [O00562-1] DR GeneID; 9600; -. DR KEGG; hsa:9600; -. DR MANE-Select; ENST00000356404.8; ENSP00000348772.3; NM_004910.3; NP_004901.2. DR UCSC; uc001olx.3; human. [O00562-1] DR AGR; HGNC:9003; -. DR CTD; 9600; -. DR DisGeNET; 9600; -. DR GeneCards; PITPNM1; -. DR HGNC; HGNC:9003; PITPNM1. DR HPA; ENSG00000110697; Low tissue specificity. DR MIM; 608794; gene. DR neXtProt; NX_O00562; -. DR OpenTargets; ENSG00000110697; -. DR PharmGKB; PA33337; -. DR VEuPathDB; HostDB:ENSG00000110697; -. DR eggNOG; KOG3668; Eukaryota. DR GeneTree; ENSGT00940000161522; -. DR HOGENOM; CLU_007179_0_0_1; -. DR InParanoid; O00562; -. DR OMA; PQRGDWY; -. DR OrthoDB; 3946034at2759; -. DR PhylomeDB; O00562; -. DR TreeFam; TF312967; -. DR PathwayCommons; O00562; -. DR Reactome; R-HSA-1483226; Synthesis of PI. DR SignaLink; O00562; -. DR SIGNOR; O00562; -. DR BioGRID-ORCS; 9600; 22 hits in 1161 CRISPR screens. DR ChiTaRS; PITPNM1; human. DR GeneWiki; PITPNM1; -. DR GenomeRNAi; 9600; -. DR Pharos; O00562; Tbio. DR PRO; PR:O00562; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; O00562; Protein. DR Bgee; ENSG00000110697; Expressed in granulocyte and 142 other cell types or tissues. DR ExpressionAtlas; O00562; baseline and differential. DR GO; GO:0044297; C:cell body; ISS:UniProtKB. DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB. DR GO; GO:0070300; F:phosphatidic acid binding; IDA:BHF-UCL. DR GO; GO:0031210; F:phosphatidylcholine binding; IDA:BHF-UCL. DR GO; GO:0008525; F:phosphatidylcholine transporter activity; IBA:GO_Central. DR GO; GO:0035091; F:phosphatidylinositol binding; IDA:BHF-UCL. DR GO; GO:0008526; F:phosphatidylinositol transfer activity; IDA:UniProtKB. DR GO; GO:0030971; F:receptor tyrosine kinase binding; IMP:UniProtKB. DR GO; GO:0007420; P:brain development; TAS:ProtInc. DR GO; GO:0006629; P:lipid metabolic process; NAS:ProtInc. DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome. DR GO; GO:0015914; P:phospholipid transport; IDA:BHF-UCL. DR GO; GO:0007602; P:phototransduction; TAS:ProtInc. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR CDD; cd08889; SRPBCC_PITPNM1-2_like; 1. DR Gene3D; 3.30.530.20; -; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR InterPro; IPR004177; DDHD_dom. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR031315; LNS2/PITP. DR InterPro; IPR001666; PI_transfer. DR InterPro; IPR023393; START-like_dom_sf. DR PANTHER; PTHR10658:SF40; MEMBRANE-ASSOCIATED PHOSPHATIDYLINOSITOL TRANSFER PROTEIN 1; 1. DR PANTHER; PTHR10658; PHOSPHATIDYLINOSITOL TRANSFER PROTEIN; 1. DR Pfam; PF02862; DDHD; 2. DR Pfam; PF02121; IP_trans; 1. DR PRINTS; PR00391; PITRANSFER. DR SMART; SM01127; DDHD; 1. DR SMART; SM00775; LNS2; 1. DR SUPFAM; SSF55961; Bet v1-like; 1. DR SUPFAM; SSF56784; HAD-like; 1. DR PROSITE; PS51043; DDHD; 1. DR Genevisible; O00562; HS. PE 1: Evidence at protein level; KW Alternative splicing; Calcium; Cytoplasm; Endoplasmic reticulum; KW Golgi apparatus; Lipid droplet; Membrane; Metal-binding; Methylation; KW Phosphoprotein; Protein transport; Reference proteome; Transport. FT CHAIN 1..1244 FT /note="Membrane-associated phosphatidylinositol transfer FT protein 1" FT /id="PRO_0000232738" FT DOMAIN 686..880 FT /note="DDHD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00378" FT REGION 258..331 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 339..358 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 581..682 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1206..1244 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 304..331 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 341..358 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 581..596 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 639..662 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 59 FT /note="Phosphothreonine" FT /evidence="ECO:0000305|PubMed:12225667" FT MOD_RES 287 FT /note="Phosphothreonine; by CDK1" FT /evidence="ECO:0000269|PubMed:15125835" FT MOD_RES 300 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35954" FT MOD_RES 304 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35954" FT MOD_RES 319 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35954" FT MOD_RES 326 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35954" FT MOD_RES 329 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35954" FT MOD_RES 342 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5U2N3" FT MOD_RES 345 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5U2N3" FT MOD_RES 346 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5U2N3" FT MOD_RES 373 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35954" FT MOD_RES 382 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:15125835" FT MOD_RES 593 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O35954" FT MOD_RES 600 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 621 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 896 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:15125835" FT MOD_RES 1211 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:O35954" FT MOD_RES 1218 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:O35954" FT MOD_RES 1237 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 716 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:15627748" FT /id="VSP_021157" FT MUTAGEN 59 FT /note="T->A: Prevents association with lipid droplets." FT /evidence="ECO:0000269|PubMed:12225667" FT MUTAGEN 59 FT /note="T->E: Causes association with lipid droplets." FT /evidence="ECO:0000269|PubMed:12225667" FT MUTAGEN 287 FT /note="T->A: Slightly reduced phosphorylation. Strongly FT reduced phosphorylation; when associated with A-794 or FT A-389. Loss of threonine phosphorylation; when associated FT with A-389; A-793 and A-1222." FT /evidence="ECO:0000269|PubMed:15125835" FT MUTAGEN 300 FT /note="S->A: No effect on phosphorylation." FT /evidence="ECO:0000269|PubMed:15125835" FT MUTAGEN 326 FT /note="S->A: No effect on phosphorylation." FT /evidence="ECO:0000269|PubMed:15125835" FT MUTAGEN 349..353 FT /note="EFFDA->ALLAG: Loss of interaction with VAPB." FT /evidence="ECO:0000269|PubMed:15545272" FT MUTAGEN 382 FT /note="S->A: Strongly reduced phosphorylation." FT /evidence="ECO:0000269|PubMed:15125835" FT MUTAGEN 389 FT /note="T->A: No detectable effect on phosphorylation; when FT associated with A-793 and A-1222. Strongly reduced FT phosphorylation; when associated with A-287. Loss of FT threonine phosphorylation; when associated with A-287; FT A-794 and A-1222." FT /evidence="ECO:0000269|PubMed:15125835" FT MUTAGEN 794 FT /note="T->A: No detectable effect on phosphorylation; when FT associated with A-389 and A-1222. Strongly reduced FT phosphorylation; when associated with A-287. Loss of FT threonine phosphorylation; when associated with A-287; FT A-389 and A-1222." FT /evidence="ECO:0000269|PubMed:15125835" FT MUTAGEN 896 FT /note="S->A: Reduced phosphorylation." FT /evidence="ECO:0000269|PubMed:15125835" FT MUTAGEN 1223 FT /note="T->A: No detectable effect on phosphorylation; when FT associated with A-389 and A-793. Loss of threonine FT phosphorylation; when associated with A-287; A-389 and FT A-794." FT /evidence="ECO:0000269|PubMed:15125835" FT CONFLICT 931 FT /note="R -> P (in Ref. 2; AAK01444)" FT /evidence="ECO:0000305" FT CONFLICT 1034 FT /note="S -> G (in Ref. 3; AAR06909)" FT /evidence="ECO:0000305" FT CONFLICT 1116 FT /note="E -> G (in Ref. 1; CAA67224)" FT /evidence="ECO:0000305" FT CONFLICT 1133 FT /note="A -> T (in Ref. 1; CAA67224)" FT /evidence="ECO:0000305" SQ SEQUENCE 1244 AA; 134848 MW; F4B66E98B085E9C0 CRC64; MLIKEYHILL PMSLDEYQVA QLYMIQKKSR EESSGEGSGV EILANRPYTD GPGGSGQYTH KVYHVGSHIP GWFRALLPKA ALQVEEESWN AYPYTRTRYT CPFVEKFSIE IETYYLPDGG QQPNVFNLSG AERRQRILDT IDIVRDAVAP GEYKAEEDPR LYHSVKTGRG PLSDDWARTA AQTGPLMCAY KLCKVEFRYW GMQAKIEQFI HDVGLRRVML RAHRQAWCWQ DEWTELSMAD IRALEEETAR MLAQRMAKCN TGSEGSEAQP PGKPSTEARS AASNTGTPDG PEAPPGPDAS PDASFGKQWS SSSRSSYSSQ HGGAVSPQSL SEWRMQNIAR DSENSSEEEF FDAHEGFSDS EEVFPKEMTK WNSNDFIDAF ASPVEAEGTP EPGAEAAKGI EDGAQAPRDS EGLDGAGELG AEACAVHALF LILHSGNILD SGPGDANSKQ ADVQTLSSAF EAVTRIHFPE ALGHVALRLV PCPPICAAAY ALVSNLSPYS HDGDSLSRSQ DHIPLAALPL LATSSSRYQG AVATVIARTN QAYSAFLRSP EGAGFCGQVA LIGDGVGGIL GFDALCHSAN AGTGSRGSSR RGSMNNELLS PEFGPVRDPL ADGVEGLGRG SPEPSALPPQ RIPSDMASPE PEGSQNSLQA APATTSSWEP RRASTAFCPP AASSEAPDGP SSTARLDFKV SGFFLFGSPL GLVLALRKTV MPALEAAQMR PACEQIYNLF HAADPCASRL EPLLAPKFQA IAPLTVPRYQ KFPLGDGSSL LLADTLQTHS SLFLEELEML VPSTPTSTSG AFWKGSELAT DPPAQPAAPS TTSEVVKILE RWWGTKRIDY SLYCPEALTA FPTVTLPHLF HASYWESADV VAFILRQVIE KERPQLAECE EPSIYSPAFP REKWQRKRTQ VKIRNVTSNH RASDTVVCEG RPQVLSGRFM YGPLDVVTLT GEKVDVYIMT QPLSGKWIHF GTEVTNSSGR LTFPVPPERA LGIGVYPVRM VVRGDHTYAE CCLTVVARGT EAVVFSIDGS FTASVSIMGS DPKVRAGAVD VVRHWQDSGY LIVYVTGRPD MQKHRVVAWL SQHNFPHGVV SFCDGLTHDP LRQKAMFLQS LVQEVELNIV AGYGSPKDVA VYAALGLSPS QTYIVGRAVR KLQAQCQFLS DGYVAHLGQL EAGSHSHASS GPPRAALGKS SYGVAAPVDF LRKQSQLLRS RGPSQAEREG PGTPPTTLAR GKARSISLKL DSEE //