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Q5TA50

- CPTP_HUMAN

UniProt

Q5TA50 - CPTP_HUMAN

Protein

Ceramide-1-phosphate transfer protein

Gene

CPTP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 74 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    Functioni

    Mediates the intracellular transfer of ceramide-1-phosphate between organelle membranes and the cell membrane. Required for normal structure of the Golgi stacks. Can bind phosphoceramides with a variety of aliphatic chains, but has a preference for lipids with saturated C16:0 or monounsaturated C18:1 aliphatic chains, and is inefficient with phosphoceramides containing lignoceryl (C24:0). Plays a role in the regulation of the cellular levels of ceramide-1-phosphate, and thereby contributes to the regulation of phospholipase PLA2G4A activity and the release of arachidonic acid. Has no activity with galactosylceramide, lactosylceramide, sphingomyelin, phosphatidylcholine, phosphatidic acid and ceramide.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei56 – 561Phosphoceramide
    Binding sitei60 – 601Phosphoceramide
    Binding sitei106 – 1061Phosphoceramide
    Binding sitei110 – 1101Phosphoceramide
    Binding sitei150 – 1501Phosphoceramide

    GO - Molecular functioni

    1. ceramide 1-phosphate binding Source: UniProtKB
    2. ceramide 1-phosphate transporter activity Source: UniProtKB
    3. glycolipid binding Source: InterPro
    4. phospholipid binding Source: UniProtKB
    5. phospholipid transporter activity Source: UniProtKB

    GO - Biological processi

    1. ceramide 1-phosphate transport Source: UniProtKB

    Keywords - Biological processi

    Lipid transport, Transport

    Keywords - Ligandi

    Lipid-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ceramide-1-phosphate transfer protein
    Short name:
    CPTP
    Alternative name(s):
    Glycolipid transfer protein domain-containing protein 1
    Short name:
    GLTP domain-containing protein 1
    Gene namesi
    Name:CPTP
    Synonyms:GLTPD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:28116. CPTP.

    Subcellular locationi

    Cytoplasmcytosol 1 Publication. Golgi apparatustrans-Golgi network membrane 1 Publication; Peripheral membrane protein 1 Publication. Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication. Endosome membrane 1 Publication; Peripheral membrane protein 1 Publication. Nucleus outer membrane 1 Publication; Peripheral membrane protein 1 Publication

    GO - Cellular componenti

    1. cytosol Source: UniProtKB-SubCell
    2. endosome membrane Source: UniProtKB-SubCell
    3. Golgi apparatus Source: UniProtKB-SubCell
    4. nuclear outer membrane Source: UniProtKB-SubCell
    5. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Endosome, Golgi apparatus, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi42 – 421F → A: Increases phosphoceramide transfer. 1 Publication
    Mutagenesisi43 – 431L → R: Nearly abolishes phosphoceramide transfer. 1 Publication
    Mutagenesisi50 – 501F → R: Slightly reduces phosphoceramide transfer. 1 Publication
    Mutagenesisi53 – 531I → N: Slightly decreases phosphoceramide transfer. 1 Publication
    Mutagenesisi56 – 561D → V: Slightly decreases phosphoceramide transfer. 1 Publication
    Mutagenesisi60 – 601K → A: Nearly abolishes phosphoceramide transfer. 1 Publication
    Mutagenesisi97 – 971R → L: No effect. 1 Publication
    Mutagenesisi106 – 1061R → L: Nearly abolishes phosphoceramide transfer. 1 Publication
    Mutagenesisi110 – 1101R → L: Reduces phosphoceramide transfer. 1 Publication
    Mutagenesisi113 – 1131R → E or L: Strongly reduces phosphoceramide transfer. 1 Publication
    Mutagenesisi117 – 1171W → A: Slightly reduces phosphoceramide transfer. 1 Publication
    Mutagenesisi118 – 1181L → R: Abolishes phosphoceramide transfer. 1 Publication
    Mutagenesisi149 – 1491Y → A: Reduces phosphoceramide transfer. 1 Publication
    Mutagenesisi158 – 1581V → N: Abolishes phosphoceramide transfer. 1 Publication

    Organism-specific databases

    PharmGKBiPA162389853.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 214214Ceramide-1-phosphate transfer proteinPRO_0000317156Add
    BLAST

    Proteomic databases

    MaxQBiQ5TA50.
    PaxDbiQ5TA50.
    PeptideAtlasiQ4G0E6.
    PRIDEiQ5TA50.

    Expressioni

    Tissue specificityi

    Ubiquitous. Detected in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes.1 Publication

    Gene expression databases

    ArrayExpressiQ5TA50.
    BgeeiQ5TA50.
    CleanExiHS_GLTPD1.
    GenevestigatoriQ5TA50.

    Organism-specific databases

    HPAiHPA056832.

    Interactioni

    Protein-protein interaction databases

    BioGridi123305. 8 interactions.
    IntActiQ5TA50. 8 interactions.
    STRINGi9606.ENSP00000343890.

    Structurei

    Secondary structure

    1
    214
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 156
    Helixi16 – 205
    Helixi29 – 4618
    Helixi48 – 503
    Helixi51 – 6919
    Helixi73 – 764
    Helixi79 – 8810
    Beta strandi94 – 963
    Helixi104 – 12724
    Helixi134 – 14411
    Helixi146 – 1494
    Helixi152 – 16211
    Helixi168 – 1747
    Beta strandi177 – 1793
    Helixi180 – 20728

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4K80X-ray2.05A1-214[»]
    4K84X-ray1.90A/B1-214[»]
    4K85X-ray1.90A/B/C/D1-214[»]
    4K8NX-ray3.10A/B/C/D/E/F1-214[»]
    4KBSX-ray1.90A/B1-214[»]
    4KF6X-ray3.20A/B/C/D/E/F1-214[»]
    ProteinModelPortaliQ5TA50.
    SMRiQ5TA50. Positions 7-214.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the GLTP family.Curated

    Phylogenomic databases

    eggNOGiNOG309816.
    HOGENOMiHOG000046738.
    HOVERGENiHBG100515.
    InParanoidiQ5TA50.
    OMAiQSMVAYE.
    OrthoDBiEOG7BW0MQ.
    PhylomeDBiQ5TA50.
    TreeFamiTF316097.

    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.

    Q5TA50-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDDSETGFNL KVVLVSFKQC LDEKEEVLLD PYIASWKGLV RFLNSLGTIF    50
    SFISKDVVSK LRIMERLRGG PQSEHYRSLQ AMVAHELSNR LVDLERRSHH 100
    PESGCRTVLR LHRALHWLQL FLEGLRTSPE DARTSALCAD SYNASLAAYH 150
    PWVVRRAVTV AFCTLPTREV FLEAMNVGPP EQAVQMLGEA LPFIQRVYNV 200
    SQKLYAEHSL LDLP 214
    Length:214
    Mass (Da):24,365
    Last modified:December 21, 2004 - v1
    Checksum:iB66F4581FD9C60A0
    GO

    Sequence cautioni

    The sequence EAW56230.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR599582 mRNA. No translation available.
    AL139287 Genomic DNA. Translation: CAI23183.1.
    CH471183 Genomic DNA. Translation: EAW56230.1. Sequence problems.
    BC098429 mRNA. Translation: AAH98429.1.
    CCDSiCCDS30555.1.
    RefSeqiNP_001025056.1. NM_001029885.1.
    XP_005244858.1. XM_005244801.1.
    UniGeneiHs.515689.

    Genome annotation databases

    EnsembliENST00000343938; ENSP00000343890; ENSG00000224051.
    GeneIDi80772.
    KEGGihsa:80772.
    UCSCiuc001aeo.3. human.

    Polymorphism databases

    DMDMi74745771.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR599582 mRNA. No translation available.
    AL139287 Genomic DNA. Translation: CAI23183.1 .
    CH471183 Genomic DNA. Translation: EAW56230.1 . Sequence problems.
    BC098429 mRNA. Translation: AAH98429.1 .
    CCDSi CCDS30555.1.
    RefSeqi NP_001025056.1. NM_001029885.1.
    XP_005244858.1. XM_005244801.1.
    UniGenei Hs.515689.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4K80 X-ray 2.05 A 1-214 [» ]
    4K84 X-ray 1.90 A/B 1-214 [» ]
    4K85 X-ray 1.90 A/B/C/D 1-214 [» ]
    4K8N X-ray 3.10 A/B/C/D/E/F 1-214 [» ]
    4KBS X-ray 1.90 A/B 1-214 [» ]
    4KF6 X-ray 3.20 A/B/C/D/E/F 1-214 [» ]
    ProteinModelPortali Q5TA50.
    SMRi Q5TA50. Positions 7-214.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123305. 8 interactions.
    IntActi Q5TA50. 8 interactions.
    STRINGi 9606.ENSP00000343890.

    Polymorphism databases

    DMDMi 74745771.

    Proteomic databases

    MaxQBi Q5TA50.
    PaxDbi Q5TA50.
    PeptideAtlasi Q4G0E6.
    PRIDEi Q5TA50.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343938 ; ENSP00000343890 ; ENSG00000224051 .
    GeneIDi 80772.
    KEGGi hsa:80772.
    UCSCi uc001aeo.3. human.

    Organism-specific databases

    CTDi 80772.
    GeneCardsi GC01P001251.
    HGNCi HGNC:28116. CPTP.
    HPAi HPA056832.
    MIMi 615467. gene.
    neXtProti NX_Q5TA50.
    PharmGKBi PA162389853.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG309816.
    HOGENOMi HOG000046738.
    HOVERGENi HBG100515.
    InParanoidi Q5TA50.
    OMAi QSMVAYE.
    OrthoDBi EOG7BW0MQ.
    PhylomeDBi Q5TA50.
    TreeFami TF316097.

    Miscellaneous databases

    NextBioi 71160.
    PROi Q5TA50.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5TA50.
    Bgeei Q5TA50.
    CleanExi HS_GLTPD1.
    Genevestigatori Q5TA50.

    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. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: B-cell.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] OF 55-214.
      Tissue: Neuroblastoma.
    5. Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH CERAMIDE-1-PHOSPHATE, FUNCTION, SUBCELLULAR LOCATION, LIPID-BINDING, MUTAGENESIS OF PHE-42; LEU-43; PHE-50; ILE-53; ASP-56; LYS-60; ARG-97; ARG-106; ARG-110; ARG-113; TRP-117; LEU-118; TYR-149 AND VAL-158, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiCPTP_HUMAN
    AccessioniPrimary (citable) accession number: Q5TA50
    Secondary accession number(s): Q4G0E6, Q7L5A4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 5, 2008
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 74 of the entry and version 1 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 1
      Human chromosome 1: 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