Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q00169

- PIPNA_HUMAN

UniProt

Q00169 - PIPNA_HUMAN

Protein

Phosphatidylinositol transfer protein alpha isoform

Gene

PITPNA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei58 – 581Phosphatidylinositol lipid headgroup1 Publication
    Binding sitei60 – 601Phosphatidylinositol lipid headgroup1 Publication
    Binding sitei85 – 851Phosphatidylinositol lipid headgroup1 Publication
    Binding sitei89 – 891Phosphatidylinositol lipid headgroup1 Publication
    Binding sitei96 – 961Phosphatidylinositol lipid headgroup1 Publication
    Binding sitei194 – 1941Phosphatidylinositol lipid headgroup1 Publication

    GO - Molecular functioni

    1. lipid binding Source: UniProtKB-KW
    2. phosphatidylcholine transporter activity Source: ProtInc
    3. phosphatidylinositol transporter activity Source: ProtInc

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. lipid metabolic process Source: ProtInc
    3. phospholipid transport Source: GOC
    4. visual perception Source: ProtInc

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    ReactomeiREACT_22228. Role of second messengers in netrin-1 signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylinositol transfer protein alpha isoform
    Short name:
    PI-TP-alpha
    Short name:
    PtdIns transfer protein alpha
    Short name:
    PtdInsTP alpha
    Gene namesi
    Name:PITPNA
    Synonyms:PITPN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9001. PITPNA.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33335.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 270269Phosphatidylinositol transfer protein alpha isoformPRO_0000191639Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei215 – 2151N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ00169.
    PaxDbiQ00169.
    PRIDEiQ00169.

    PTM databases

    PhosphoSiteiQ00169.

    Expressioni

    Tissue specificityi

    Expressed in a wide range of tissues.

    Gene expression databases

    ArrayExpressiQ00169.
    BgeeiQ00169.
    CleanExiHS_PITPNA.
    GenevestigatoriQ00169.

    Organism-specific databases

    HPAiHPA000528.

    Interactioni

    Protein-protein interaction databases

    BioGridi111323. 6 interactions.
    IntActiQ00169. 3 interactions.
    STRINGi9606.ENSP00000316809.

    Structurei

    Secondary structure

    1
    270
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 1311
    Helixi15 – 3319
    Beta strandi38 – 4912
    Beta strandi54 – 6512
    Helixi70 – 734
    Beta strandi81 – 9010
    Beta strandi93 – 997
    Helixi101 – 1033
    Beta strandi106 – 12015
    Turni123 – 1264
    Helixi130 – 1334
    Beta strandi137 – 1415
    Helixi146 – 1483
    Helixi151 – 1533
    Helixi156 – 1583
    Helixi160 – 1623
    Turni166 – 1683
    Helixi177 – 1826
    Beta strandi190 – 20011
    Turni203 – 2053
    Helixi206 – 23025
    Helixi232 – 2354
    Helixi240 – 26021

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UW5X-ray2.90A/B/C/D1-270[»]
    ProteinModelPortaliQ00169.
    SMRiQ00169. Positions 1-269.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ00169.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG250489.
    HOVERGENiHBG058915.
    InParanoidiQ00169.
    OMAiMVLLKEY.
    OrthoDBiEOG7PGDRB.
    PhylomeDBiQ00169.
    TreeFamiTF313279.

    Family and domain databases

    Gene3Di3.30.530.20. 1 hit.
    InterProiIPR001666. PI_transfer.
    IPR023393. START-like_dom.
    [Graphical view]
    PANTHERiPTHR10658. PTHR10658. 1 hit.
    PfamiPF02121. IP_trans. 1 hit.
    [Graphical view]
    PRINTSiPR00391. PITRANSFER.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q00169-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVLLKEYRVI LPVSVDEYQV GQLYSVAEAS KNETGGGEGV EVLVNEPYEK    50
    DGEKGQYTHK IYHLQSKVPT FVRMLAPEGA LNIHEKAWNA YPYCRTVITN 100
    EYMKEDFLIK IETWHKPDLG TQENVHKLEP EAWKHVEAVY IDIADRSQVL 150
    SKDYKAEEDP AKFKSIKTGR GPLGPNWKQE LVNQKDCPYM CAYKLVTVKF 200
    KWWGLQNKVE NFIHKQERRL FTNFHRQLFC WLDKWVDLTM DDIRRMEEET 250
    KRQLDEMRQK DPVKGMTADD 270
    Length:270
    Mass (Da):31,806
    Last modified:January 23, 2007 - v2
    Checksum:i4531E6E38697C93B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 451N → P in BAA06276. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73704 mRNA. Translation: AAA36441.1.
    D30036 mRNA. Translation: BAA06276.1.
    BC082976 mRNA. Translation: AAH82976.1.
    BC045108 mRNA. Translation: AAH45108.1.
    CCDSiCCDS45563.1.
    PIRiI53775.
    RefSeqiNP_006215.1. NM_006224.3.
    UniGeneiHs.429819.

    Genome annotation databases

    EnsembliENST00000313486; ENSP00000316809; ENSG00000174238.
    GeneIDi5306.
    KEGGihsa:5306.
    UCSCiuc010cjt.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M73704 mRNA. Translation: AAA36441.1 .
    D30036 mRNA. Translation: BAA06276.1 .
    BC082976 mRNA. Translation: AAH82976.1 .
    BC045108 mRNA. Translation: AAH45108.1 .
    CCDSi CCDS45563.1.
    PIRi I53775.
    RefSeqi NP_006215.1. NM_006224.3.
    UniGenei Hs.429819.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UW5 X-ray 2.90 A/B/C/D 1-270 [» ]
    ProteinModelPortali Q00169.
    SMRi Q00169. Positions 1-269.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111323. 6 interactions.
    IntActi Q00169. 3 interactions.
    STRINGi 9606.ENSP00000316809.

    PTM databases

    PhosphoSitei Q00169.

    Proteomic databases

    MaxQBi Q00169.
    PaxDbi Q00169.
    PRIDEi Q00169.

    Protocols and materials databases

    DNASUi 5306.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313486 ; ENSP00000316809 ; ENSG00000174238 .
    GeneIDi 5306.
    KEGGi hsa:5306.
    UCSCi uc010cjt.3. human.

    Organism-specific databases

    CTDi 5306.
    GeneCardsi GC17M001421.
    HGNCi HGNC:9001. PITPNA.
    HPAi HPA000528.
    MIMi 600174. gene.
    neXtProti NX_Q00169.
    PharmGKBi PA33335.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG250489.
    HOVERGENi HBG058915.
    InParanoidi Q00169.
    OMAi MVLLKEY.
    OrthoDBi EOG7PGDRB.
    PhylomeDBi Q00169.
    TreeFami TF313279.

    Enzyme and pathway databases

    Reactomei REACT_22228. Role of second messengers in netrin-1 signaling.

    Miscellaneous databases

    ChiTaRSi PITPNA. human.
    EvolutionaryTracei Q00169.
    GeneWikii Phosphatidylinositol_transfer_protein,_alpha.
    GenomeRNAii 5306.
    NextBioi 20510.
    PROi Q00169.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q00169.
    Bgeei Q00169.
    CleanExi HS_PITPNA.
    Genevestigatori Q00169.

    Family and domain databases

    Gene3Di 3.30.530.20. 1 hit.
    InterProi IPR001666. PI_transfer.
    IPR023393. START-like_dom.
    [Graphical view ]
    PANTHERi PTHR10658. PTHR10658. 1 hit.
    Pfami PF02121. IP_trans. 1 hit.
    [Graphical view ]
    PRINTSi PR00391. PITRANSFER.
    ProtoNeti Search...

    Publicationsi

    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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. 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.

    Entry informationi

    Entry nameiPIPNA_HUMAN
    AccessioniPrimary (citable) accession number: Q00169
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 137 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3