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Q5TA50

- CPTP_HUMAN

UniProt

Q5TA50 - CPTP_HUMAN

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Protein
Ceramide-1-phosphate transfer protein
Gene
CPTP, GLTPD1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

GO - Cellular componenti

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

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 protein
PRO_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. 7 interactions.
STRINGi9606.ENSP00000343890.

Structurei

Secondary structure

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.

Family & Domainsi

Sequence similaritiesi

Belongs to the GLTP family.

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. 7 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 73 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

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