PITM1_HUMAN
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 03-AUG-2022, entry version 165.
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; 14.
DR ELM; O00562; -.
DR IntAct; O00562; 8.
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 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; O00562; -.
DR PeptideAtlas; O00562; -.
DR PRIDE; O00562; -.
DR ProteomicsDB; 47977; -. [O00562-1]
DR ProteomicsDB; 47978; -. [O00562-2]
DR Antibodypedia; 30438; 231 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 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; DPLGHKA; -.
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 1079 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 141 other tissues.
DR ExpressionAtlas; O00562; baseline and differential.
DR Genevisible; O00562; HS.
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 Gene3D; 3.30.530.20; -; 1.
DR Gene3D; 3.40.50.1000; -; 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; PTHR10658; 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; SSF56784; SSF56784; 1.
DR PROSITE; PS51043; DDHD; 1.
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 A-
FT 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; A-
FT 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; A-
FT 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 A-
FT 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
