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Q9NZD2

- GLTP_HUMAN

UniProt

Q9NZD2 - GLTP_HUMAN

Protein

Glycolipid transfer protein

Gene

GLTP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides.4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei140 – 1401Glycolipid1 Publication
    Binding sitei207 – 2071Glycolipid1 Publication

    GO - Molecular functioni

    1. glycolipid binding Source: HGNC
    2. glycolipid transporter activity Source: HGNC
    3. lipid binding Source: HGNC

    GO - Biological processi

    1. glycolipid transport Source: HGNC

    Keywords - Biological processi

    Lipid transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glycolipid transfer protein
    Short name:
    GLTP
    Gene namesi
    Name:GLTP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:24867. GLTP.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi45 – 451I → N: 18% decrease in activity. 1 Publication
    Mutagenesisi48 – 481D → V: Significant inactivation; 15% residual activity. 1 Publication
    Mutagenesisi52 – 521N → I: Significant inactivation; 15% residual activity. 1 Publication
    Mutagenesisi55 – 551K → I: No loss of activity; 90-97% residual activity. 1 Publication
    Mutagenesisi96 – 961W → A: Almost complete inactivation; 1-3% residual activity. 1 Publication
    Mutagenesisi96 – 961W → F: Partial inactivation; 63% residual activity. 1 Publication
    Mutagenesisi103 – 1031F → S: About 25% decrease in activity. 1 Publication
    Mutagenesisi136 – 1361L → R: Significant inactivation; 5% residual activity. 1 Publication
    Mutagenesisi140 – 1401H → L: Almost complete inactivation; 1-3% residual activity. 1 Publication
    Mutagenesisi148 – 1481F → S: About 50% decrease in activity. 1 Publication
    Mutagenesisi165 – 1651L → R: 46% decrease in activity. 1 Publication
    Mutagenesisi183 – 1831F → S: No loss of activity; 90% residual activity. 1 Publication
    Mutagenesisi207 – 2071Y → L: No loss of activity; 90-97% residual activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA142671729.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 209208Glycolipid transfer proteinPRO_0000148915Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9NZD2.
    PaxDbiQ9NZD2.
    PRIDEiQ9NZD2.

    PTM databases

    PhosphoSiteiQ9NZD2.

    Expressioni

    Tissue specificityi

    Detected in fibroblasts (at protein level). Detected in fibroblasts and in various cancer cell lines.2 Publications

    Gene expression databases

    ArrayExpressiQ9NZD2.
    BgeeiQ9NZD2.
    CleanExiHS_GLTP.
    GenevestigatoriQ9NZD2.

    Organism-specific databases

    HPAiHPA056461.

    Interactioni

    Subunit structurei

    Monomer.2 Publications

    Protein-protein interaction databases

    BioGridi119392. 2 interactions.
    DIPiDIP-59418N.
    IntActiQ9NZD2. 1 interaction.
    STRINGi9606.ENSP00000315263.

    Structurei

    Secondary structure

    1
    209
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 63
    Helixi20 – 278
    Turni28 – 303
    Helixi31 – 366
    Helixi40 – 423
    Helixi43 – 6220
    Turni64 – 674
    Helixi70 – 8112
    Helixi82 – 843
    Helixi89 – 11224
    Beta strandi118 – 1203
    Helixi125 – 13511
    Helixi137 – 1393
    Helixi142 – 15110
    Helixi152 – 1543
    Helixi158 – 1658
    Turni166 – 1683
    Helixi173 – 20028

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1SWXX-ray1.65A1-209[»]
    1SX6X-ray1.95A1-209[»]
    2EUKX-ray1.85A1-209[»]
    2EUMX-ray2.30A1-209[»]
    2EVDX-ray2.00A1-209[»]
    2EVLX-ray2.20A1-209[»]
    2EVSX-ray2.20A/E1-209[»]
    2EVTX-ray1.99A1-209[»]
    3RICX-ray2.10A1-209[»]
    3RWVX-ray1.50A/B1-209[»]
    3RZNX-ray1.10A1-209[»]
    3S0IX-ray1.50A1-209[»]
    3S0KX-ray1.40A1-209[»]
    4GH0X-ray1.35A1-209[»]
    4GHPX-ray1.90A1-209[»]
    4GHSX-ray3.20A/B1-209[»]
    4GIXX-ray1.80A1-209[»]
    4GJQX-ray2.00A/B1-209[»]
    4GVTX-ray2.90A1-209[»]
    4GXDX-ray2.10A1-209[»]
    4GXGX-ray2.40A/B/D/E1-209[»]
    4H2ZX-ray1.45A1-209[»]
    ProteinModelPortaliQ9NZD2.
    SMRiQ9NZD2. Positions 4-209.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NZD2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati45 – 55111Add
    BLAST
    Repeati56 – 66112Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni45 – 66222 X 12 AA approximate tandem repeatsAdd
    BLAST
    Regioni48 – 558Glycolipid binding

    Sequence similaritiesi

    Belongs to the GLTP family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG302244.
    HOGENOMiHOG000199421.
    HOVERGENiHBG019001.
    InParanoidiQ9NZD2.
    OMAiKFHNFVV.
    OrthoDBiEOG7FJH25.
    PhylomeDBiQ9NZD2.
    TreeFamiTF317467.

    Family and domain databases

    Gene3Di1.10.3520.10. 1 hit.
    InterProiIPR014830. Glycolipid_transfer_prot_dom.
    [Graphical view]
    PfamiPF08718. GLTP. 1 hit.
    [Graphical view]
    SUPFAMiSSF110004. SSF110004. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    Q9NZD2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALLAEHLLK PLPADKQIET GPFLEAVSHL PPFFDCLGSP VFTPIKADIS    50
    GNITKIKAVY DTNPAKFRTL QNILEVEKEM YGAEWPKVGA TLALMWLKRG 100
    LRFIQVFLQS ICDGERDENH PNLIRVNATK AYEMALKKYH GWIVQKIFQA 150
    ALYAAPYKSD FLKALSKGQN VTEEECLEKI RLFLVNYTAT IDVIYEMYTQ 200
    MNAELNYKV 209
    Length:209
    Mass (Da):23,850
    Last modified:January 23, 2007 - v3
    Checksum:iF3DD96D702AE22CF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF209704 mRNA. Translation: AAF33210.1.
    AY372530 mRNA. Translation: AAR85984.1.
    AY372531 mRNA. Translation: AAR85985.1.
    AY372532 mRNA. Translation: AAR87373.1.
    AK313457 mRNA. Translation: BAG36244.1.
    CH471054 Genomic DNA. Translation: EAW97880.1.
    BC009932 mRNA. Translation: AAH09932.1.
    CCDSiCCDS9136.1.
    RefSeqiNP_057517.1. NM_016433.3.
    UniGeneiHs.381256.

    Genome annotation databases

    EnsembliENST00000318348; ENSP00000315263; ENSG00000139433.
    GeneIDi51228.
    KEGGihsa:51228.
    UCSCiuc001tpm.3. human.

    Polymorphism databases

    DMDMi20138399.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF209704 mRNA. Translation: AAF33210.1 .
    AY372530 mRNA. Translation: AAR85984.1 .
    AY372531 mRNA. Translation: AAR85985.1 .
    AY372532 mRNA. Translation: AAR87373.1 .
    AK313457 mRNA. Translation: BAG36244.1 .
    CH471054 Genomic DNA. Translation: EAW97880.1 .
    BC009932 mRNA. Translation: AAH09932.1 .
    CCDSi CCDS9136.1.
    RefSeqi NP_057517.1. NM_016433.3.
    UniGenei Hs.381256.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SWX X-ray 1.65 A 1-209 [» ]
    1SX6 X-ray 1.95 A 1-209 [» ]
    2EUK X-ray 1.85 A 1-209 [» ]
    2EUM X-ray 2.30 A 1-209 [» ]
    2EVD X-ray 2.00 A 1-209 [» ]
    2EVL X-ray 2.20 A 1-209 [» ]
    2EVS X-ray 2.20 A/E 1-209 [» ]
    2EVT X-ray 1.99 A 1-209 [» ]
    3RIC X-ray 2.10 A 1-209 [» ]
    3RWV X-ray 1.50 A/B 1-209 [» ]
    3RZN X-ray 1.10 A 1-209 [» ]
    3S0I X-ray 1.50 A 1-209 [» ]
    3S0K X-ray 1.40 A 1-209 [» ]
    4GH0 X-ray 1.35 A 1-209 [» ]
    4GHP X-ray 1.90 A 1-209 [» ]
    4GHS X-ray 3.20 A/B 1-209 [» ]
    4GIX X-ray 1.80 A 1-209 [» ]
    4GJQ X-ray 2.00 A/B 1-209 [» ]
    4GVT X-ray 2.90 A 1-209 [» ]
    4GXD X-ray 2.10 A 1-209 [» ]
    4GXG X-ray 2.40 A/B/D/E 1-209 [» ]
    4H2Z X-ray 1.45 A 1-209 [» ]
    ProteinModelPortali Q9NZD2.
    SMRi Q9NZD2. Positions 4-209.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119392. 2 interactions.
    DIPi DIP-59418N.
    IntActi Q9NZD2. 1 interaction.
    STRINGi 9606.ENSP00000315263.

    PTM databases

    PhosphoSitei Q9NZD2.

    Polymorphism databases

    DMDMi 20138399.

    Proteomic databases

    MaxQBi Q9NZD2.
    PaxDbi Q9NZD2.
    PRIDEi Q9NZD2.

    Protocols and materials databases

    DNASUi 51228.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000318348 ; ENSP00000315263 ; ENSG00000139433 .
    GeneIDi 51228.
    KEGGi hsa:51228.
    UCSCi uc001tpm.3. human.

    Organism-specific databases

    CTDi 51228.
    GeneCardsi GC12M110288.
    HGNCi HGNC:24867. GLTP.
    HPAi HPA056461.
    MIMi 608949. gene.
    neXtProti NX_Q9NZD2.
    PharmGKBi PA142671729.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG302244.
    HOGENOMi HOG000199421.
    HOVERGENi HBG019001.
    InParanoidi Q9NZD2.
    OMAi KFHNFVV.
    OrthoDBi EOG7FJH25.
    PhylomeDBi Q9NZD2.
    TreeFami TF317467.

    Miscellaneous databases

    ChiTaRSi GLTP. human.
    EvolutionaryTracei Q9NZD2.
    GeneWikii GLTP.
    GenomeRNAii 51228.
    NextBioi 54324.
    PROi Q9NZD2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NZD2.
    Bgeei Q9NZD2.
    CleanExi HS_GLTP.
    Genevestigatori Q9NZD2.

    Family and domain databases

    Gene3Di 1.10.3520.10. 1 hit.
    InterProi IPR014830. Glycolipid_transfer_prot_dom.
    [Graphical view ]
    Pfami PF08718. GLTP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF110004. SSF110004. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Human glycolipid transfer protein: probing conformation using fluorescence spectroscopy."
      Li X.-M., Malakhova M.L., Lin X., Pike H.M., Chung T., Molotkovsky J.G., Brown R.E.
      Biochemistry 43:10285-10294(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Skin fibroblast.
    2. "Human glycolipid transfer protein (GLTP) genes: organization, transcriptional status and evolution."
      Zou X., Chung T., Lin X., Malakhova M.L., Pike H.M., Brown R.E.
      BMC Genomics 9:72-72(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Brain.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Caudate nucleus.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Placenta.
    6. "Glycolipid transfer protein mediated transfer of glycosphingolipids between membranes: a model for action based on kinetic and thermodynamic analyses."
      Rao C.S., Lin X., Pike H.M., Molotkovsky J.G., Brown R.E.
      Biochemistry 43:13805-13815(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Human glycolipid transfer protein -- intracellular localization and effects on the sphingolipid synthesis."
      Tuuf J., Mattjus P.
      Biochim. Biophys. Acta 1771:1353-1363(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Structural basis for glycosphingolipid transfer specificity."
      Malinina L., Malakhova M.L., Teplov A., Brown R.E., Patel D.J.
      Nature 430:1048-1053(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH GLYCOLIPID, FUNCTION, MUTAGENESIS OF ILE-45; ASP-48; ASN-52; LYS-55; TRP-96; PHE-103; LEU-136; HIS-140; PHE-148; LEU-165; PHE-183 AND TYR-207.
    10. "The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure."
      Malinina L., Malakhova M.L., Kanack A.T., Lu M., Abagyan R., Brown R.E., Patel D.J.
      PLoS Biol. 4:1996-2011(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEXES WITH GLYCOSPHINGOLIPIDS, SUBUNIT.

    Entry informationi

    Entry nameiGLTP_HUMAN
    AccessioniPrimary (citable) accession number: Q9NZD2
    Secondary accession number(s): Q53Z13, Q96J68
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 114 of the entry and version 3 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, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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