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Q00169 (PIPNA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylinositol transfer protein alpha isoform

Short name=PI-TP-alpha
Short name=PtdIns transfer protein alpha
Short name=PtdInsTP alpha
Gene names
Name:PITPNA
Synonyms:PITPN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length270 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes.

Subcellular location

Cytoplasm.

Tissue specificity

Expressed in a wide range of tissues.

Sequence similarities

Belongs to the PtdIns transfer protein family. PI transfer class I subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 270269Phosphatidylinositol transfer protein alpha isoform
PRO_0000191639

Sites

Binding site581Phosphatidylinositol lipid headgroup
Binding site601Phosphatidylinositol lipid headgroup
Binding site851Phosphatidylinositol lipid headgroup
Binding site891Phosphatidylinositol lipid headgroup
Binding site961Phosphatidylinositol lipid headgroup
Binding site1941Phosphatidylinositol lipid headgroup

Amino acid modifications

Modified residue2151N6-acetyllysine Ref.5

Experimental info

Sequence conflict451N → P in BAA06276. Ref.2

Secondary structure

.............................................. 270
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q00169 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 4531E6E38697C93B

FASTA27031,806
        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 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of a human cDNA encoding phosphatidylinositol transfer protein and occurrence of a related sequence in widely divergent eukaryotes."
Dickeson S.K., Helmkamp G.M. Jr., Yarbrough L.R.
Gene 142:301-305(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]Tanaka S., Yamashita S., Hosaka K.
Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Ovary.
[4]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 135-146, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[5]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Structure-function analysis of human phosphatidylinositol transfer protein alpha bound to phosphatidylinositol."
Tilley S.J., Skippen A., Murray-Rust J., Swigart P.M., Stewart A., Morgan C.P., Cockcroft S., McDonald N.Q.
Structure 12:317-326(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH PHOSPHATIDYLINOSITOL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M73704 mRNA. Translation: AAA36441.1.
D30036 mRNA. Translation: BAA06276.1.
BC082976 mRNA. Translation: AAH82976.1.
BC045108 mRNA. Translation: AAH45108.1.
PIRI53775.
RefSeqNP_006215.1. NM_006224.3.
UniGeneHs.429819.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UW5X-ray2.90A/B/C/D1-270[»]
ProteinModelPortalQ00169.
SMRQ00169. Positions 1-269.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111323. 6 interactions.
IntActQ00169. 3 interactions.
STRING9606.ENSP00000316809.

PTM databases

PhosphoSiteQ00169.

Proteomic databases

PaxDbQ00169.
PRIDEQ00169.

Protocols and materials databases

DNASU5306.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000313486; ENSP00000316809; ENSG00000174238.
GeneID5306.
KEGGhsa:5306.
UCSCuc010cjt.3. human.

Organism-specific databases

CTD5306.
GeneCardsGC17M001421.
HGNCHGNC:9001. PITPNA.
HPAHPA000528.
MIM600174. gene.
neXtProtNX_Q00169.
PharmGKBPA33335.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG250489.
HOVERGENHBG058915.
InParanoidQ00169.
OMAMVLLKEY.
OrthoDBEOG7PGDRB.
PhylomeDBQ00169.
TreeFamTF313279.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.

Gene expression databases

ArrayExpressQ00169.
BgeeQ00169.
CleanExHS_PITPNA.
GenevestigatorQ00169.

Family and domain databases

Gene3D3.30.530.20. 1 hit.
InterProIPR001666. PI_transfer.
IPR023393. START-like_dom.
[Graphical view]
PANTHERPTHR10658. PTHR10658. 1 hit.
PfamPF02121. IP_trans. 1 hit.
[Graphical view]
PRINTSPR00391. PITRANSFER.
ProtoNetSearch...

Other

ChiTaRSPITPNA. human.
EvolutionaryTraceQ00169.
GeneWikiPhosphatidylinositol_transfer_protein,_alpha.
GenomeRNAi5306.
NextBio20510.
PROQ00169.
SOURCESearch...

Entry information

Entry namePIPNA_HUMAN
AccessionPrimary (citable) accession number: Q00169
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM