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Q9UKL6

- PPCT_HUMAN

UniProt

Q9UKL6 - PPCT_HUMAN

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Protein

Phosphatidylcholine transfer protein

Gene

PCTP

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

Functioni

Catalyzes the transfer of phosphatidylcholine between membranes. Binds a single lipid molecule.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei72 – 721Phosphatidylcholine
Binding sitei78 – 781Phosphatidylcholine
Binding sitei157 – 1571Phosphatidylcholine

GO - Molecular functioni

  1. phosphatidylcholine binding Source: UniProtKB
  2. phosphatidylcholine transporter activity Source: UniProtKB

GO - Biological processi

  1. cholesterol metabolic process Source: Ensembl
  2. lipid transport Source: UniProtKB
  3. phospholipid transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylcholine transfer protein
Short name:
PC-TP
Alternative name(s):
START domain-containing protein 2
Short name:
StARD2
StAR-related lipid transfer protein 2
Gene namesi
Name:PCTP
Synonyms:STARD2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:8752. PCTP.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi63 – 631C → A: Reduces activity by 20%. 1 Publication

Organism-specific databases

PharmGKBiPA33098.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 214214Phosphatidylcholine transfer proteinPRO_0000220658Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9UKL6.
PaxDbiQ9UKL6.
PRIDEiQ9UKL6.

PTM databases

PhosphoSiteiQ9UKL6.

Expressioni

Tissue specificityi

Highest expression in liver, placenta, testis, kidney and heart. Low levels in brain and lung. No expression detected in thymus.1 Publication

Gene expression databases

BgeeiQ9UKL6.
CleanExiHS_PCTP.
ExpressionAtlasiQ9UKL6. baseline and differential.
GenevestigatoriQ9UKL6.

Organism-specific databases

HPAiHPA022979.

Interactioni

Subunit structurei

Interacts with ACOT13/THEM2.By similarity

Protein-protein interaction databases

BioGridi121818. 3 interactions.
STRINGi9606.ENSP00000268896.

Structurei

Secondary structure

1
214
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 156Combined sources
Helixi18 – 214Combined sources
Turni26 – 294Combined sources
Beta strandi31 – 366Combined sources
Beta strandi39 – 457Combined sources
Turni47 – 493Combined sources
Beta strandi52 – 609Combined sources
Helixi65 – 739Combined sources
Helixi75 – 817Combined sources
Beta strandi85 – 939Combined sources
Beta strandi96 – 1038Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi112 – 12312Combined sources
Helixi125 – 1273Combined sources
Beta strandi130 – 1378Combined sources
Beta strandi149 – 1524Combined sources
Beta strandi155 – 1639Combined sources
Beta strandi165 – 17713Combined sources
Helixi185 – 1939Combined sources
Helixi195 – 20814Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LN1X-ray2.40A1-214[»]
1LN2X-ray2.90A/B1-214[»]
1LN3X-ray2.90A/B1-214[»]
ProteinModelPortaliQ9UKL6.
SMRiQ9UKL6. Positions 8-210.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UKL6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 212212STARTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 START domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG264966.
GeneTreeiENSGT00530000063520.
HOGENOMiHOG000261644.
HOVERGENiHBG008237.
InParanoidiQ9UKL6.
OMAiCADVYMD.
OrthoDBiEOG70KGQK.
PhylomeDBiQ9UKL6.
TreeFamiTF320705.

Family and domain databases

Gene3Di3.30.530.20. 1 hit.
InterProiIPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view]
PfamiPF01852. START. 1 hit.
[Graphical view]
SMARTiSM00234. START. 1 hit.
[Graphical view]
PROSITEiPS50848. START. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UKL6-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MELAAGSFSE EQFWEACAEL QQPALAGADW QLLVETSGIS IYRLLDKKTG
60 70 80 90 100
LYEYKVFGVL EDCSPTLLAD IYMDSDYRKQ WDQYVKELYE QECNGETVVY
110 120 130 140 150
WEVKYPFPMS NRDYVYLRQR RDLDMEGRKI HVILARSTSM PQLGERSGVI
160 170 180 190 200
RVKQYKQSLA IESDGKKGSK VFMYYFDNPG GQIPSWLINW AAKNGVPNFL
210
KDMARACQNY LKKT
Length:214
Mass (Da):24,843
Last modified:May 1, 2000 - v1
Checksum:iE40204B7C0A9AF83
GO
Isoform 2 (identifier: Q9UKL6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.

Show »
Length:142
Mass (Da):16,824
Checksum:i1BA1CE03358BAB59
GO

Sequence cautioni

The sequence AAH05112.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521Y → H in AAF08347. (PubMed:10542325)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti10 – 101E → A.
Corresponds to variant rs12941739 [ dbSNP | Ensembl ].
VAR_052070

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7272Missing in isoform 2. 1 PublicationVSP_041363Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF114436
, AF114431, AF114432, AF114433, AF114434, AF114435 Genomic DNA. Translation: AAF08347.1.
AF114430 mRNA. Translation: AAF08345.1.
AF151638 mRNA. Translation: AAF02536.1.
AC009837 Genomic DNA. No translation available.
AC091155 Genomic DNA. No translation available.
BC005112 mRNA. Translation: AAH05112.1. Different initiation.
BC012084 mRNA. Translation: AAH12084.1.
CCDSiCCDS11588.1. [Q9UKL6-1]
CCDS45741.1. [Q9UKL6-2]
RefSeqiNP_001095872.1. NM_001102402.2. [Q9UKL6-2]
NP_067036.2. NM_021213.3. [Q9UKL6-1]
UniGeneiHs.285218.

Genome annotation databases

EnsembliENST00000268896; ENSP00000268896; ENSG00000141179. [Q9UKL6-1]
ENST00000325214; ENSP00000325181; ENSG00000141179. [Q9UKL6-2]
GeneIDi58488.
KEGGihsa:58488.
UCSCiuc002iul.4. human. [Q9UKL6-1]

Polymorphism databases

DMDMi15214192.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF114436
, AF114431 , AF114432 , AF114433 , AF114434 , AF114435 Genomic DNA. Translation: AAF08347.1 .
AF114430 mRNA. Translation: AAF08345.1 .
AF151638 mRNA. Translation: AAF02536.1 .
AC009837 Genomic DNA. No translation available.
AC091155 Genomic DNA. No translation available.
BC005112 mRNA. Translation: AAH05112.1 . Different initiation.
BC012084 mRNA. Translation: AAH12084.1 .
CCDSi CCDS11588.1. [Q9UKL6-1 ]
CCDS45741.1. [Q9UKL6-2 ]
RefSeqi NP_001095872.1. NM_001102402.2. [Q9UKL6-2 ]
NP_067036.2. NM_021213.3. [Q9UKL6-1 ]
UniGenei Hs.285218.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LN1 X-ray 2.40 A 1-214 [» ]
1LN2 X-ray 2.90 A/B 1-214 [» ]
1LN3 X-ray 2.90 A/B 1-214 [» ]
ProteinModelPortali Q9UKL6.
SMRi Q9UKL6. Positions 8-210.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121818. 3 interactions.
STRINGi 9606.ENSP00000268896.

PTM databases

PhosphoSitei Q9UKL6.

Polymorphism databases

DMDMi 15214192.

Proteomic databases

MaxQBi Q9UKL6.
PaxDbi Q9UKL6.
PRIDEi Q9UKL6.

Protocols and materials databases

DNASUi 58488.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000268896 ; ENSP00000268896 ; ENSG00000141179 . [Q9UKL6-1 ]
ENST00000325214 ; ENSP00000325181 ; ENSG00000141179 . [Q9UKL6-2 ]
GeneIDi 58488.
KEGGi hsa:58488.
UCSCi uc002iul.4. human. [Q9UKL6-1 ]

Organism-specific databases

CTDi 58488.
GeneCardsi GC17P053828.
HGNCi HGNC:8752. PCTP.
HPAi HPA022979.
MIMi 606055. gene.
neXtProti NX_Q9UKL6.
PharmGKBi PA33098.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG264966.
GeneTreei ENSGT00530000063520.
HOGENOMi HOG000261644.
HOVERGENi HBG008237.
InParanoidi Q9UKL6.
OMAi CADVYMD.
OrthoDBi EOG70KGQK.
PhylomeDBi Q9UKL6.
TreeFami TF320705.

Miscellaneous databases

EvolutionaryTracei Q9UKL6.
GeneWikii Phosphatidylcholine_transfer_protein.
GenomeRNAii 58488.
NextBioi 64950.
PROi Q9UKL6.
SOURCEi Search...

Gene expression databases

Bgeei Q9UKL6.
CleanExi HS_PCTP.
ExpressionAtlasi Q9UKL6. baseline and differential.
Genevestigatori Q9UKL6.

Family and domain databases

Gene3Di 3.30.530.20. 1 hit.
InterProi IPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view ]
Pfami PF01852. START. 1 hit.
[Graphical view ]
SMARTi SM00234. START. 1 hit.
[Graphical view ]
PROSITEi PS50848. START. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, tissue-specific expression, gene structure and chromosomal localization of human phosphatidylcholine transfer protein."
    Cohen D.E., Green R.M., Wu M.K., Beier D.R.
    Biochim. Biophys. Acta 1447:265-270(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Kidney.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Uterus.
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    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] (ISOFORMS 1 AND 2).
    Tissue: B-cell.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Human phosphatidylcholine transfer protein: purification, crystallization and preliminary X-ray diffraction data."
    Chan W.W., Roderick S.L., Cohen D.E.
    Biochim. Biophys. Acta 1596:1-5(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
  7. "Structure of human phosphatidylcholine transfer protein in complex with its ligand."
    Roderick S.L., Chan W.W., Agate D.S., Olsen L.R., Vetting M.W., Rajashankar K.R., Cohen D.E.
    Nat. Struct. Biol. 9:507-511(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEXES WITH PHOSPHATIDYLCHOLINE, FUNCTION, MUTAGENESIS OF CYS-63.

Entry informationi

Entry nameiPPCT_HUMAN
AccessioniPrimary (citable) accession number: Q9UKL6
Secondary accession number(s): Q9BSC9, Q9UIT3, Q9UKW7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 14, 2001
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 122 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 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3