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UniProtKB/Swiss-Prot entry Q00169


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PIPNA_HUMAN
Primary accession number Q00169
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 82)
Name and origin of the protein
Protein name Phosphatidylinositol transfer protein alpha isoform
Synonyms PtdIns transfer protein alpha
PtdInsTP
PI-TP-alpha
Gene name
Name: PITPNA
Synonyms: PITPN
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
DOI=10.1016/0378-1119(94)90279-8; PubMed=8194769 [NCBI, ExPASy, EBI, Israel, Japan]
Dickeson S.K., Helmkamp G.M. Jr., Yarbrough L.R.;
"Sequence of a human cDNA encoding phosphatidylinositol transfer protein and occurrence of a related sequence in widely divergent eukaryotes.";
Gene 142:301-305(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Tanaka S., Yamashita S., Hosaka K.;
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Ovary;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
PROTEIN SEQUENCE OF 135-146, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Afjehi-Sadat L.;
Submitted (MAR-2007) to UniProtKB.
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-57, AND MASS SPECTROMETRY.
TISSUE=Lung;
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[6]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M73704; AAA36441.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D30036; BAA06276.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC082976; AAH82976.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC045108; AAH45108.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00216048; -.
PIR I53775; I53775.
RefSeq NP_006215.1; -.
UniGene Hs.429819
3D structure databases
PDB
1UW5; X-ray; 2.90 A; A/B/C/D=1-270.[ExPASy / RCSB / EBI]
PDBsum 1UW5; -.
ModBase Q00169.
Protein-protein interaction databases
IntAct Q00169; 4.
PTM databases
PhosphoSite Q00169; -.
Organism-specific databases
GeneCards GC17M001368; -.
H-InvDB HIX0013400; -.
HGNC HGNC:9001; PITPNA.
GenAtlas PITPNA.
HPA HPA000528; -.
MIM 600174; gene. [NCBI / EBI]
PharmGKB PA33335; -.
Gene expression databases
ArrayExpress Q00169; -.
Bgee Q00169; -.
CleanEx HS_PITPNA; -.
GermOnline ENSG00000174238; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0005634; Cellular component: nucleus (inferred from direct assay from HPA).
GO:0008525; Molecular function: phosphatidylcholine transmembrane transporter activity (traceable author statement from ProtInc).
GO:0008526; Molecular function: phosphatidylinositol transporter activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006629; Biological process: lipid metabolic process (non-traceable author statement from ProtInc).
GO:0006810; Biological process: transport (inferred from electronic annotation from UniProtKB-KW).
GO:0007601; Biological process: visual perception (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR001666; PI_transfer.
Graphical view of domain structure.
PANTHER PTHR10658; PI_transfer; 1.
Pfam PF02121; IP_trans; 1.
Pfam graphical view of domain structure.
PRINTS PR00391; PITRANSFER.
Proteomic databases
PRIDE Q00169; -.
Genome annotation databases
Ensembl ENSG00000174238; Homo sapiens. [Contig view]
GeneID 5306; -.
KEGG hsa:5306; -.
Phylogenomic databases
HOVERGEN Q00169; -.
Other
NextBio 20510; -.
SOURCE PITPNA; Homo sapiens.
ProtoNet Q00169.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cytoplasm; Direct protein sequencing; Lipid-binding; Phosphoprotein; Transport.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   270  269     Phosphatidylinositol transfer protein alpha isoform. PRO_0000191639
MOD_RES   57    57        Phosphotyrosine. 
CONFLICT   45    45        N -> P (in Ref. 2; BAA06276). 
STRAND   3    13  11      
HELIX   15    33  19      
STRAND   38    49  12      
STRAND   54    65  12      
HELIX   70    73  4      
STRAND   81    90  10      
STRAND   93    99  7      
HELIX   101   103  3      
STRAND   106   120  15      
TURN   123   126  4      
HELIX   130   133  4      
STRAND   137   141  5      
HELIX   146   148  3      
HELIX   151   153  3      
HELIX   156   158  3      
HELIX   160   162  3      
TURN   166   168  3      
HELIX   177   182  6      
STRAND   190   200  11      
TURN   203   205  3      
HELIX   206   230  25      
HELIX   232   235  4      
HELIX   240   260  21      
Sequence information
Length: 270 AA [This is the length of the unprocessed precursor] Molecular weight: 31806 Da [This is the MW of the unprocessed precursor] CRC64: 4531E6E38697C93B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVLLKEYRVI LPVSVDEYQV GQLYSVAEAS KNETGGGEGV EVLVNEPYEK DGEKGQYTHK 

        70         80         90        100        110        120 
IYHLQSKVPT FVRMLAPEGA LNIHEKAWNA YPYCRTVITN EYMKEDFLIK IETWHKPDLG 

       130        140        150        160        170        180 
TQENVHKLEP EAWKHVEAVY IDIADRSQVL SKDYKAEEDP AKFKSIKTGR GPLGPNWKQE 

       190        200        210        220        230        240 
LVNQKDCPYM CAYKLVTVKF KWWGLQNKVE NFIHKQERRL FTNFHRQLFC WLDKWVDLTM 

       250        260        270 
DDIRRMEEET KRQLDEMRQK DPVKGMTADD 

Q00169 in FASTA format

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