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Membrane-associated phosphatidylinositol transfer protein 1 (Drosophila retinal degeneration B homolog) (Phosphatidylinositol transfer protein, membrane-associated 1) (PITPnm 1) (Pyk2 N-terminal domain-interacting receptor 2) (NIR-2)

 PITM1_HUMAN             Reviewed;        1244 AA.
O00562; A6NME4; Q6T7X3; Q8TBN3; Q9BZ73;
18-APR-2006, integrated into UniProtKB/Swiss-Prot.
31-OCT-2006, sequence version 4.
27-SEP-2017, entry version 136.
RecName: Full=Membrane-associated phosphatidylinositol transfer protein 1;
AltName: Full=Drosophila retinal degeneration B homolog;
AltName: Full=Phosphatidylinositol transfer protein, membrane-associated 1;
Short=PITPnm 1;
AltName: Full=Pyk2 N-terminal domain-interacting receptor 2;
Short=NIR-2;
Name=PITPNM1; Synonyms=DRES9, NIR2, PITPNM;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9680295;
Rubboli F., Bulfone A., Bogni S., Marchitiello A., Zollo M.,
Borsani G., Ballabio A., Banfi S.;
"A mammalian homologue of the Drosophila retinal degeneration B gene:
implications for the evolution of phototransduction mechanisms.";
Genes Funct. 1:205-213(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CALCIUM-BINDING,
INTERACTION WITH PTK2B, PHOSPHORYLATION, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=10022914; DOI=10.1128/MCB.19.3.2278;
Lev S., Hernandez J., Martinez R., Chen A., Plowman G.,
Schlessinger J.;
"Identification of a novel family of targets of PYK2 related to
Drosophila retinal degeneration B (rdgB) protein.";
Mol. Cell. Biol. 19:2278-2288(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=15627748; DOI=10.1159/000081519;
Ocaka L., Spalluto C., Wilson D.I., Hunt D.M., Halford S.;
"Chromosomal localization, genomic organization and evolution of the
genes encoding human phosphatidylinositol transfer protein membrane-
associated (PITPNM) 1, 2 and 3.";
Cytogenet. Genome Res. 108:293-302(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Duodenum;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
SUBCELLULAR LOCATION, MUTAGENESIS OF THR-59, AND PHOSPHORYLATION AT
THR-59.
PubMed=12225667; DOI=10.1016/S0960-9822(02)01107-7;
Litvak V., Shaul Y.D., Shulewitz M., Amarilio R., Carmon S., Lev S.;
"Targeting of Nir2 to lipid droplets is regulated by a specific
threonine residue within its PI-transfer domain.";
Curr. Biol. 12:1513-1518(2002).
[8]
FUNCTION, AND INTERACTION WITH RHOA.
PubMed=11909959; DOI=10.1128/MCB.22.8.2650-2662.2002;
Tian D., Litvak V., Toledo-Rodriguez M., Carmon S., Lev S.;
"Nir2, a novel regulator of cell morphogenesis.";
Mol. Cell. Biol. 22:2650-2662(2002).
[9]
PHOSPHORYLATION AT THR-287; SER-382 AND SER-896, IDENTIFICATION BY
MASS SPECTROMETRY, MUTAGENESIS OF THR-287; SER-300; SER-326; SER-382;
THR-389; THR-794; SER-896 AND THR-1223, INTERACTION WITH CDK1 AND
PLK1, AND SUBCELLULAR LOCATION.
PubMed=15125835; DOI=10.1016/S1097-2765(04)00214-X;
Litvak V., Argov R., Dahan N., Ramachandran S., Amarilio R.,
Shainskaya A., Lev S.;
"Mitotic phosphorylation of the peripheral Golgi protein Nir2 by Cdk1
provides a docking mechanism for Plk1 and affects cytokinesis
completion.";
Mol. Cell 14:319-330(2004).
[10]
FUNCTION, INTERACTION WITH VAPB, AND MUTAGENESIS OF 349-GLU--ALA-353.
PubMed=15545272; DOI=10.1074/jbc.M409566200;
Amarilio R., Ramachandran S., Sabanay H., Lev S.;
"Differential regulation of endoplasmic reticulum structure through
VAP-Nir protein interaction.";
J. Biol. Chem. 280:5934-5944(2005).
[11]
FUNCTION.
PubMed=15723057; DOI=10.1038/ncb1221;
Litvak V., Dahan N., Ramachandran S., Sabanay H., Lev S.;
"Maintenance of the diacylglycerol level in the Golgi apparatus by the
Nir2 protein is critical for Golgi secretory function.";
Nat. Cell Biol. 7:225-234(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-621 AND SER-1237, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-600 AND SER-621, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Regulates RHOA activity, and plays a role in
cytoskeleton remodeling. Necessary for normal completion of
cytokinesis. Plays a role in maintaining normal diacylglycerol
levels in the Golgi apparatus. Binds phosphatidyl inositol
phosphates (in vitro). May catalyze the transfer of
phosphatidylinositol and phosphatidylcholine between membranes (By
similarity). Necessary for maintaining the normal structure of the
endoplasmic reticulum and the Golgi apparatus. Required for
protein export from the endoplasmic reticulum and the Golgi. Binds
calcium ions. {ECO:0000250, ECO:0000269|PubMed:10022914,
ECO:0000269|PubMed:11909959, ECO:0000269|PubMed:15545272,
ECO:0000269|PubMed:15723057}.
-!- SUBUNIT: Interacts with PIK4CA (By similarity). Interacts with
PTK2B via its C-terminus. Interacts with RHOA. Has higher affinity
for the inactive, GDP-bound form of RHOA. The CDK1-phosphorylated
form interacts with PLK1. Interacts with VAPB. {ECO:0000250,
ECO:0000269|PubMed:10022914, ECO:0000269|PubMed:11909959,
ECO:0000269|PubMed:15125835, ECO:0000269|PubMed:15545272}.
-!- INTERACTION:
Q12800:TFCP2; NbExp=3; IntAct=EBI-2861268, EBI-717422;
-!- SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, Golgi stack
membrane {ECO:0000269|PubMed:12225667}; Peripheral membrane
protein. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:12225667}; Peripheral membrane protein. Lipid
droplet {ECO:0000269|PubMed:12225667}. Cleavage furrow
{ECO:0000269|PubMed:15125835}. Midbody
{ECO:0000269|PubMed:15125835}. Note=Peripheral membrane protein
associated with Golgi stacks in interphase cells. A minor
proportion is associated with the endoplasmic reticulum.
Associated with lipid droplets (PubMed:12225667). Dissociates from
the Golgi early on in mitosis and localizes to the cleavage furrow
and midbody during cytokinesis (PubMed:15125835).
{ECO:0000269|PubMed:12225667, ECO:0000269|PubMed:15125835}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O00562-1; Sequence=Displayed;
Name=2;
IsoId=O00562-2; Sequence=VSP_021157;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10022914}.
-!- PTM: Phosphorylated on multiple sites by CDK1 at the onset of
mitosis. Phosphorylation facilitates dissociation from the Golgi
complex and is required for interaction with PLK1.
-!- PTM: Phosphorylated on threonine residues upon treatment with
oleic acid.
-!- PTM: Phosphorylated on tyrosine residues by PTK2B.
-!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI
transfer class IIA subfamily. {ECO:0000305}.
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EMBL; X98654; CAA67224.1; -; mRNA.
EMBL; AF334584; AAK01444.1; -; mRNA.
EMBL; AY429102; AAR06909.1; -; mRNA.
EMBL; AP001184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471076; EAW74638.1; -; Genomic_DNA.
EMBL; BC022230; AAH22230.1; -; mRNA.
CCDS; CCDS31620.1; -. [O00562-1]
CCDS; CCDS44659.1; -. [O00562-2]
RefSeq; NP_001124320.1; NM_001130848.1. [O00562-2]
RefSeq; NP_004901.2; NM_004910.2. [O00562-1]
RefSeq; XP_016874075.1; XM_017018586.1. [O00562-1]
UniGene; Hs.372295; -.
ProteinModelPortal; O00562; -.
SMR; O00562; -.
BioGrid; 114965; 7.
ELM; O00562; -.
IntAct; O00562; 8.
STRING; 9606.ENSP00000348772; -.
ChEMBL; CHEMBL1764937; -.
SwissLipids; SLP:000000414; -.
iPTMnet; O00562; -.
PhosphoSitePlus; O00562; -.
BioMuta; PITPNM1; -.
EPD; O00562; -.
MaxQB; O00562; -.
PaxDb; O00562; -.
PeptideAtlas; O00562; -.
PRIDE; O00562; -.
DNASU; 9600; -.
Ensembl; ENST00000356404; ENSP00000348772; ENSG00000110697. [O00562-1]
Ensembl; ENST00000436757; ENSP00000398787; ENSG00000110697. [O00562-2]
Ensembl; ENST00000534749; ENSP00000437286; ENSG00000110697. [O00562-1]
GeneID; 9600; -.
KEGG; hsa:9600; -.
UCSC; uc001olx.3; human. [O00562-1]
CTD; 9600; -.
DisGeNET; 9600; -.
EuPathDB; HostDB:ENSG00000110697.12; -.
GeneCards; PITPNM1; -.
HGNC; HGNC:9003; PITPNM1.
HPA; HPA060227; -.
HPA; HPA062757; -.
MIM; 608794; gene.
neXtProt; NX_O00562; -.
OpenTargets; ENSG00000110697; -.
PharmGKB; PA33337; -.
eggNOG; KOG3668; Eukaryota.
eggNOG; COG5083; LUCA.
GeneTree; ENSGT00760000119216; -.
HOGENOM; HOG000294231; -.
HOVERGEN; HBG052733; -.
InParanoid; O00562; -.
OMA; MQNIARD; -.
OrthoDB; EOG091G0BMT; -.
PhylomeDB; O00562; -.
TreeFam; TF312967; -.
Reactome; R-HSA-1483226; Synthesis of PI.
SIGNOR; O00562; -.
ChiTaRS; PITPNM1; human.
GeneWiki; PITPNM1; -.
GenomeRNAi; 9600; -.
PRO; PR:O00562; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000110697; -.
CleanEx; HS_PITPNM1; -.
ExpressionAtlas; O00562; baseline and differential.
Genevisible; O00562; HS.
GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
GO; GO:0000932; C:P-body; IDA:HPA.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070300; F:phosphatidic acid binding; IDA:BHF-UCL.
GO; GO:0031210; F:phosphatidylcholine binding; IDA:BHF-UCL.
GO; GO:0035091; F:phosphatidylinositol binding; IDA:BHF-UCL.
GO; GO:0008526; F:phosphatidylinositol transporter activity; IDA:BHF-UCL.
GO; GO:0007420; P:brain development; TAS:ProtInc.
GO; GO:0006629; P:lipid metabolic process; NAS:ProtInc.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0015914; P:phospholipid transport; IDA:BHF-UCL.
GO; GO:0007602; P:phototransduction; TAS:ProtInc.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
Gene3D; 3.30.530.20; -; 1.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR004177; DDHD_dom.
InterPro; IPR023214; HAD-like_dom.
InterPro; IPR031315; LNS2/PITP.
InterPro; IPR001666; PI_transfer.
InterPro; IPR023393; START-like_dom.
PANTHER; PTHR10658; PTHR10658; 1.
Pfam; PF02862; DDHD; 1.
Pfam; PF02121; IP_trans; 1.
PRINTS; PR00391; PITRANSFER.
SMART; SM01127; DDHD; 1.
SMART; SM00775; LNS2; 1.
SUPFAM; SSF56784; SSF56784; 1.
PROSITE; PS51043; DDHD; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Complete proteome; Cytoplasm;
Endoplasmic reticulum; Golgi apparatus; Lipid droplet; Membrane;
Metal-binding; Methylation; Phosphoprotein; Protein transport;
Reference proteome; Transport.
CHAIN 1 1244 Membrane-associated phosphatidylinositol
transfer protein 1.
/FTId=PRO_0000232738.
DOMAIN 686 880 DDHD. {ECO:0000255|PROSITE-
ProRule:PRU00378}.
COMPBIAS 310 319 Poly-Ser.
MOD_RES 59 59 Phosphothreonine.
{ECO:0000305|PubMed:12225667}.
MOD_RES 287 287 Phosphothreonine; by CDK1.
{ECO:0000269|PubMed:15125835}.
MOD_RES 300 300 Phosphoserine.
{ECO:0000250|UniProtKB:O35954}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000250|UniProtKB:O35954}.
MOD_RES 319 319 Phosphoserine.
{ECO:0000250|UniProtKB:O35954}.
MOD_RES 326 326 Phosphoserine.
{ECO:0000250|UniProtKB:O35954}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000250|UniProtKB:O35954}.
MOD_RES 342 342 Phosphoserine.
{ECO:0000250|UniProtKB:Q5U2N3}.
MOD_RES 345 345 Phosphoserine.
{ECO:0000250|UniProtKB:Q5U2N3}.
MOD_RES 346 346 Phosphoserine.
{ECO:0000250|UniProtKB:Q5U2N3}.
MOD_RES 373 373 Phosphoserine.
{ECO:0000250|UniProtKB:O35954}.
MOD_RES 382 382 Phosphoserine; by CDK1.
{ECO:0000269|PubMed:15125835}.
MOD_RES 593 593 Phosphoserine.
{ECO:0000250|UniProtKB:O35954}.
MOD_RES 600 600 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 621 621 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 896 896 Phosphoserine.
{ECO:0000269|PubMed:15125835}.
MOD_RES 1211 1211 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:O35954}.
MOD_RES 1218 1218 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:O35954}.
MOD_RES 1237 1237 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 716 716 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15627748}.
/FTId=VSP_021157.
MUTAGEN 59 59 T->A: Prevents association with lipid
droplets. {ECO:0000269|PubMed:12225667}.
MUTAGEN 59 59 T->E: Causes association with lipid
droplets. {ECO:0000269|PubMed:12225667}.
MUTAGEN 287 287 T->A: Slightly reduced phosphorylation.
Strongly reduced phosphorylation; when
associated with A-794 or A-389. Loss of
threonine phosphorylation; when
associated with A-389; A-793 and A-1222.
{ECO:0000269|PubMed:15125835}.
MUTAGEN 300 300 S->A: No effect on phosphorylation.
{ECO:0000269|PubMed:15125835}.
MUTAGEN 326 326 S->A: No effect on phosphorylation.
{ECO:0000269|PubMed:15125835}.
MUTAGEN 349 353 EFFDA->ALLAG: Loss of interaction with
VAPB. {ECO:0000269|PubMed:15545272}.
MUTAGEN 382 382 S->A: Strongly reduced phosphorylation.
{ECO:0000269|PubMed:15125835}.
MUTAGEN 389 389 T->A: No detectable effect on
phosphorylation; when associated with A-
793 and A-1222. Strongly reduced
phosphorylation; when associated with A-
287. Loss of threonine phosphorylation;
when associated with A-287; A-794 and A-
1222. {ECO:0000269|PubMed:15125835}.
MUTAGEN 794 794 T->A: No detectable effect on
phosphorylation; when associated with A-
389 and A-1222. Strongly reduced
phosphorylation; when associated with A-
287. Loss of threonine phosphorylation;
when associated with A-287; A-389 and A-
1222. {ECO:0000269|PubMed:15125835}.
MUTAGEN 896 896 S->A: Reduced phosphorylation.
{ECO:0000269|PubMed:15125835}.
MUTAGEN 1223 1223 T->A: No detectable effect on
phosphorylation; when associated with A-
389 and A-793. Loss of threonine
phosphorylation; when associated with A-
287; A-389 and A-794.
{ECO:0000269|PubMed:15125835}.
CONFLICT 931 931 R -> P (in Ref. 2; AAK01444).
{ECO:0000305}.
CONFLICT 1034 1034 S -> G (in Ref. 3; AAR06909).
{ECO:0000305}.
CONFLICT 1116 1116 E -> G (in Ref. 1; CAA67224).
{ECO:0000305}.
CONFLICT 1133 1133 A -> T (in Ref. 1; CAA67224).
{ECO:0000305}.
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


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E1550Rb Mouse ELISA Kit FOR Membrane-associated phosphatidylinositol transfer protein 2 96T
PITRM1 PITPNM2 Gene phosphatidylinositol transfer protein, membrane-associated 2
BRDT_HUMAN Mouse ELISA Kit FOR Membrane-associated phosphatidylinositol transfer protein 3 96T
VPS11_HUMAN Mouse ELISA Kit FOR Membrane-associated phosphatidylinositol transfer protein 3 96T
E0134Ge Mouse ELISA Kit FOR Membrane-associated phosphatidylinositol transfer protein 3 96T
PITM3_HUMAN Human ELISA Kit FOR Membrane-associated phosphatidylinositol transfer protein 3 96T
CSB-EL018038RA Rat Membrane-associated phosphatidylinositol transfer protein 1(PITPNM1) ELISA kit SpeciesRat 96T
CSB-EL018039HU Human Membrane-associated phosphatidylinositol transfer protein 2(PITPNM2) ELISA kit 96T
CSB-EL018040MO Mouse Membrane-associated phosphatidylinositol transfer protein 3(PITPNM3) ELISA kit 96T
CSB-EL018038MO Mouse Membrane-associated phosphatidylinositol transfer protein 1(PITPNM1) ELISA kit 96T
CSB-EL018040HU Human Membrane-associated phosphatidylinositol transfer protein 3(PITPNM3) ELISA kit 96T
CSB-EL018038HU Human Membrane-associated phosphatidylinositol transfer protein 1(PITPNM1) ELISA kit 96T
CSB-EL018039MO Mouse Membrane-associated phosphatidylinositol transfer protein 2(PITPNM2) ELISA kit 96T


 

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