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Q9NZD2

- GLTP_HUMAN

UniProt

Q9NZD2 - GLTP_HUMAN

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Protein
Glycolipid transfer protein
Gene
GLTP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 1401Glycolipid
Binding sitei207 – 2071Glycolipid

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
Complete GO annotation...

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
Complete GO annotation...

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 – 11Removed By similarity
Chaini2 – 209208Glycolipid transfer protein
PRO_0000148915Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By 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.1 Publication

Protein-protein interaction databases

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

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ9NZD2.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Belongs to the GLTP family.

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 113 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

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