Full text data of PITPNB
PITPNB
[Confidence: low (only semi-automatic identification from reviews)]
Phosphatidylinositol transfer protein beta isoform; PI-TP-beta; PtdIns transfer protein beta; PtdInsTP beta
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Phosphatidylinositol transfer protein beta isoform; PI-TP-beta; PtdIns transfer protein beta; PtdInsTP beta
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P48739
ID PIPNB_HUMAN Reviewed; 271 AA.
AC P48739; B3KYB8; Q8N5W1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Phosphatidylinositol transfer protein beta isoform;
DE Short=PI-TP-beta;
DE Short=PtdIns transfer protein beta;
DE Short=PtdInsTP beta;
GN Name=PITPNB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8541325; DOI=10.1016/0005-2760(95)00192-1;
RA Tanaka S., Yamashita S., Hosaka K.;
RT "Cloning and expression of human cDNA encoding phosphatidylinositol
RT transfer protein beta.";
RL Biochim. Biophys. Acta 1259:199-202(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lymph, and Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalyzes the transfer of PtdIns and phosphatidylcholine
CC between membranes.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P48739-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48739-2; Sequence=VSP_012762;
CC -!- TISSUE SPECIFICITY: Widely expressed in various tissues including
CC brain.
CC -!- PTM: Constitutive phosphorylation of Ser-262 has no effect on
CC phospholipid transfer activity but is required for Golgi targeting
CC (By similarity).
CC -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI
CC transfer class I subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D30037; BAA06277.1; -; mRNA.
DR EMBL; CR456541; CAG30427.1; -; mRNA.
DR EMBL; AL031591; CAB63033.1; -; Genomic_DNA.
DR EMBL; AL031591; CAQ68296.1; -; Genomic_DNA.
DR EMBL; BC018704; AAH18704.1; -; mRNA.
DR EMBL; BC031427; AAH31427.1; -; mRNA.
DR RefSeq; NP_001271206.1; NM_001284277.1.
DR RefSeq; NP_001271207.1; NM_001284278.1.
DR RefSeq; NP_036531.1; NM_012399.4.
DR UniGene; Hs.705323; -.
DR ProteinModelPortal; P48739; -.
DR SMR; P48739; 2-270.
DR IntAct; P48739; 1.
DR MINT; MINT-5002601; -.
DR STRING; 9606.ENSP00000334738; -.
DR PhosphoSite; P48739; -.
DR DMDM; 1346772; -.
DR PaxDb; P48739; -.
DR PRIDE; P48739; -.
DR DNASU; 23760; -.
DR Ensembl; ENST00000320996; ENSP00000321266; ENSG00000180957.
DR Ensembl; ENST00000335272; ENSP00000334738; ENSG00000180957.
DR GeneID; 23760; -.
DR KEGG; hsa:23760; -.
DR UCSC; uc003adk.3; human.
DR CTD; 23760; -.
DR GeneCards; GC22M028202; -.
DR HGNC; HGNC:9002; PITPNB.
DR HPA; HPA000528; -.
DR MIM; 606876; gene.
DR neXtProt; NX_P48739; -.
DR PharmGKB; PA33336; -.
DR eggNOG; NOG250489; -.
DR HOVERGEN; HBG058915; -.
DR OrthoDB; EOG7PGDRB; -.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; PITPNB; human.
DR GeneWiki; PITPNB; -.
DR GenomeRNAi; 23760; -.
DR NextBio; 46707; -.
DR PRO; PR:P48739; -.
DR ArrayExpress; P48739; -.
DR Bgee; P48739; -.
DR CleanEx; HS_PITPNB; -.
DR Genevestigator; P48739; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; TAS:Reactome.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0015914; P:phospholipid transport; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR001666; PI_transfer.
DR InterPro; IPR023393; START-like_dom.
DR PANTHER; PTHR10658; PTHR10658; 1.
DR Pfam; PF02121; IP_trans; 1.
DR PRINTS; PR00391; PITRANSFER.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Golgi apparatus; Lipid-binding; Phosphoprotein; Reference proteome;
KW Transport.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 271 Phosphatidylinositol transfer protein
FT beta isoform.
FT /FTId=PRO_0000191643.
FT MOD_RES 215 215 N6-acetyllysine.
FT MOD_RES 262 262 Phosphoserine (By similarity).
FT VAR_SEQ 257 271 MRKRGSVRGTSAADV -> LRNQGQVRGTSAASDE (in
FT isoform 2).
FT /FTId=VSP_012762.
SQ SEQUENCE 271 AA; 31540 MW; AC5333FBC0F6CA06 CRC64;
MVLIKEFRVV LPCSVQEYQV GQLYSVAEAS KNETGGGEGI EVLKNEPYEK DGEKGQYTHK
IYHLKSKVPA FVRMIAPEGS LVFHEKAWNA YPYCRTIVTN EYMKDDFFIK IETWHKPDLG
TLENVHGLDP NTWKTVEIVH IDIADRSQVE PADYKADEDP ALFQSVKTKR GPLGPNWKKE
LANSPDCPQM CAYKLVTIKF KWWGLQSKVE NFIQKQEKRI FTNFHRQLFC WIDKWIDLTM
EDIRRMEDET QKELETMRKR GSVRGTSAAD V
//
ID PIPNB_HUMAN Reviewed; 271 AA.
AC P48739; B3KYB8; Q8N5W1;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 120.
DE RecName: Full=Phosphatidylinositol transfer protein beta isoform;
DE Short=PI-TP-beta;
DE Short=PtdIns transfer protein beta;
DE Short=PtdInsTP beta;
GN Name=PITPNB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=8541325; DOI=10.1016/0005-2760(95)00192-1;
RA Tanaka S., Yamashita S., Hosaka K.;
RT "Cloning and expression of human cDNA encoding phosphatidylinositol
RT transfer protein beta.";
RL Biochim. Biophys. Acta 1259:199-202(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
RA Khan A.S., Lane L., Tilahun Y., Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lymph, and Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Catalyzes the transfer of PtdIns and phosphatidylcholine
CC between membranes.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Golgi apparatus
CC (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P48739-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P48739-2; Sequence=VSP_012762;
CC -!- TISSUE SPECIFICITY: Widely expressed in various tissues including
CC brain.
CC -!- PTM: Constitutive phosphorylation of Ser-262 has no effect on
CC phospholipid transfer activity but is required for Golgi targeting
CC (By similarity).
CC -!- SIMILARITY: Belongs to the PtdIns transfer protein family. PI
CC transfer class I subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; D30037; BAA06277.1; -; mRNA.
DR EMBL; CR456541; CAG30427.1; -; mRNA.
DR EMBL; AL031591; CAB63033.1; -; Genomic_DNA.
DR EMBL; AL031591; CAQ68296.1; -; Genomic_DNA.
DR EMBL; BC018704; AAH18704.1; -; mRNA.
DR EMBL; BC031427; AAH31427.1; -; mRNA.
DR RefSeq; NP_001271206.1; NM_001284277.1.
DR RefSeq; NP_001271207.1; NM_001284278.1.
DR RefSeq; NP_036531.1; NM_012399.4.
DR UniGene; Hs.705323; -.
DR ProteinModelPortal; P48739; -.
DR SMR; P48739; 2-270.
DR IntAct; P48739; 1.
DR MINT; MINT-5002601; -.
DR STRING; 9606.ENSP00000334738; -.
DR PhosphoSite; P48739; -.
DR DMDM; 1346772; -.
DR PaxDb; P48739; -.
DR PRIDE; P48739; -.
DR DNASU; 23760; -.
DR Ensembl; ENST00000320996; ENSP00000321266; ENSG00000180957.
DR Ensembl; ENST00000335272; ENSP00000334738; ENSG00000180957.
DR GeneID; 23760; -.
DR KEGG; hsa:23760; -.
DR UCSC; uc003adk.3; human.
DR CTD; 23760; -.
DR GeneCards; GC22M028202; -.
DR HGNC; HGNC:9002; PITPNB.
DR HPA; HPA000528; -.
DR MIM; 606876; gene.
DR neXtProt; NX_P48739; -.
DR PharmGKB; PA33336; -.
DR eggNOG; NOG250489; -.
DR HOVERGEN; HBG058915; -.
DR OrthoDB; EOG7PGDRB; -.
DR Reactome; REACT_111217; Metabolism.
DR ChiTaRS; PITPNB; human.
DR GeneWiki; PITPNB; -.
DR GenomeRNAi; 23760; -.
DR NextBio; 46707; -.
DR PRO; PR:P48739; -.
DR ArrayExpress; P48739; -.
DR Bgee; P48739; -.
DR CleanEx; HS_PITPNB; -.
DR Genevestigator; P48739; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; TAS:Reactome.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0015914; P:phospholipid transport; TAS:Reactome.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR Gene3D; 3.30.530.20; -; 1.
DR InterPro; IPR001666; PI_transfer.
DR InterPro; IPR023393; START-like_dom.
DR PANTHER; PTHR10658; PTHR10658; 1.
DR Pfam; PF02121; IP_trans; 1.
DR PRINTS; PR00391; PITRANSFER.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Golgi apparatus; Lipid-binding; Phosphoprotein; Reference proteome;
KW Transport.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 271 Phosphatidylinositol transfer protein
FT beta isoform.
FT /FTId=PRO_0000191643.
FT MOD_RES 215 215 N6-acetyllysine.
FT MOD_RES 262 262 Phosphoserine (By similarity).
FT VAR_SEQ 257 271 MRKRGSVRGTSAADV -> LRNQGQVRGTSAASDE (in
FT isoform 2).
FT /FTId=VSP_012762.
SQ SEQUENCE 271 AA; 31540 MW; AC5333FBC0F6CA06 CRC64;
MVLIKEFRVV LPCSVQEYQV GQLYSVAEAS KNETGGGEGI EVLKNEPYEK DGEKGQYTHK
IYHLKSKVPA FVRMIAPEGS LVFHEKAWNA YPYCRTIVTN EYMKDDFFIK IETWHKPDLG
TLENVHGLDP NTWKTVEIVH IDIADRSQVE PADYKADEDP ALFQSVKTKR GPLGPNWKKE
LANSPDCPQM CAYKLVTIKF KWWGLQSKVE NFIQKQEKRI FTNFHRQLFC WIDKWIDLTM
EDIRRMEDET QKELETMRKR GSVRGTSAAD V
//
MIM
606876
*RECORD*
*FIELD* NO
606876
*FIELD* TI
*606876 PHOSPHATIDYLINOSITOL TRANSFER PROTEIN, BETA; PITPNB
*FIELD* TX
DESCRIPTION
read more
Phosphatidylinositol transfer protein is a member of a diverse set of
cytosolic phospholipid transfer proteins that are distinguished by their
ability to transfer phospholipids between membranes in vitro (Wirtz,
1991).
CLONING
Tanaka et al. (1995) cloned PITPNB cDNA by screening a human brain cDNA
library with the rat brain cDNA homolog as probe. The deduced 271-amino
acid protein has a calculated molecular mass of 31.5 kD and shows 98.1%
sequence identity with the rat protein. Northern blot analysis detected
ubiquitous expression of a 3.4-kb transcript, with highest expression in
liver and lowest in skeletal muscle. Expression was found in all regions
of the brain examined, with highest expression in amygdala.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PITPNB
gene to chromosome 22 (TMAP stSG2906).
*FIELD* RF
1. Tanaka, S.; Yamashita, S.; Hosaka, K.: Cloning and expression
of human cDNA encoding phosphatidylinositol transfer protein beta. Biochim.
Biophys. Acta 1259: 199-202, 1995.
2. Wirtz, K. W. A.: Phospholipid transfer proteins. Annu. Rev. Biochem. 60:
73-99, 1991.
*FIELD* CD
Patricia A. Hartz: 4/24/2002
*FIELD* ED
carol: 04/24/2002
*RECORD*
*FIELD* NO
606876
*FIELD* TI
*606876 PHOSPHATIDYLINOSITOL TRANSFER PROTEIN, BETA; PITPNB
*FIELD* TX
DESCRIPTION
read more
Phosphatidylinositol transfer protein is a member of a diverse set of
cytosolic phospholipid transfer proteins that are distinguished by their
ability to transfer phospholipids between membranes in vitro (Wirtz,
1991).
CLONING
Tanaka et al. (1995) cloned PITPNB cDNA by screening a human brain cDNA
library with the rat brain cDNA homolog as probe. The deduced 271-amino
acid protein has a calculated molecular mass of 31.5 kD and shows 98.1%
sequence identity with the rat protein. Northern blot analysis detected
ubiquitous expression of a 3.4-kb transcript, with highest expression in
liver and lowest in skeletal muscle. Expression was found in all regions
of the brain examined, with highest expression in amygdala.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PITPNB
gene to chromosome 22 (TMAP stSG2906).
*FIELD* RF
1. Tanaka, S.; Yamashita, S.; Hosaka, K.: Cloning and expression
of human cDNA encoding phosphatidylinositol transfer protein beta. Biochim.
Biophys. Acta 1259: 199-202, 1995.
2. Wirtz, K. W. A.: Phospholipid transfer proteins. Annu. Rev. Biochem. 60:
73-99, 1991.
*FIELD* CD
Patricia A. Hartz: 4/24/2002
*FIELD* ED
carol: 04/24/2002