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Q9Y365 (PCTL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
PCTP-like protein

Short name=PCTP-L
Alternative name(s):
Antigen NY-CO-28
START domain-containing protein 10
Short name=StARD10
Serologically defined colon cancer antigen 28
StAR-related lipid transfer protein 10
Gene names
Name:STARD10
Synonyms:SDCCAG28
ORF Names:CGI-52
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length291 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play metabolic roles in sperm maturation or fertilization By similarity. Phospholipid transfer protein that preferentially selects lipid species containing a palmitoyl or stearoyl chain on the sn-1 and an unsaturated fatty acyl chain (18:1 or 18:2) on the sn-2 position. Able to transfer phosphatidylcholine (PC) and phosphatidyetanolamline (PE) between membranes. Ref.4

Subcellular location

Cell projectionciliumflagellum By similarity. Cytoplasm. Membrane. Note: In testis was predominantly detected at the flagella of elongated spermatids, with a strong signal also found at the tail of epididymal sperm By similarity. Mainly cytosolic. Ref.5

Post-translational modification

Phosphorylation at Ser-284 by CK2 negatively regulates lipid transfer activity, possibly by decreasing membrane association.

Sequence similarities

Contains 1 START domain.

Sequence caution

The sequence AAC18045.1 differs from that shown. Reason: Various sequencing problems as well as a translation in a wrong frame.

The sequence AAD34047.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processLipid transport
Transport
   Cellular componentCell projection
Cytoplasm
Membrane
   LigandLipid-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipid transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcell projection

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionlipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 23455924. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRMT6Q96LA82EBI-4289836,EBI-912440

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 291291PCTP-like protein
PRO_0000220661

Regions

Domain14 – 224211START

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8
Modified residue941N6-succinyllysine By similarity
Modified residue1971N6-succinyllysine By similarity
Modified residue2021N6-succinyllysine By similarity
Modified residue2841Phosphoserine; by CK2 Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9Y365 [UniParc].

Last modified November 15, 2002. Version 2.
Checksum: 26D6D3AF8C300EA6

FASTA29133,049
        10         20         30         40         50         60 
MEKLAASTEP QGPRPVLGRE SVQVPDDQDF RSFRSECEAE VGWNLTYSRA GVSVWVQAVE 

        70         80         90        100        110        120 
MDRTLHKIKC RMECCDVPAE TLYDVLHDIE YRKKWDSNVI ETFDIARLTV NADVGYYSWR 

       130        140        150        160        170        180 
CPKPLKNRDV ITLRSWLPMG ADYIIMNYSV KHPKYPPRKD LVRAVSIQTG YLIQSTGPKS 

       190        200        210        220        230        240 
CVITYLAQVD PKGSLPKWVV NKSSQFLAPK AMKKMYKACL KYPEWKQKHL PHFKPWLHPE 

       250        260        270        280        290 
QSPLPSLALS ELSVQHADSL ENIDESAVAE SREERMGGAG GEGSDDDTSL T 

« Hide

References

« Hide 'large scale' references
[1]"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[2]"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: Uterus.
[3]"Characterization of human colon cancer antigens recognized by autologous antibodies."
Scanlan M.J., Chen Y.-T., Williamson B., Gure A.O., Stockert E., Gordan J.D., Tuereci O., Sahin U., Pfreundschuh M., Old L.J.
Int. J. Cancer 76:652-658(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Colon carcinoma.
[4]"StarD10, a START domain protein overexpressed in breast cancer, functions as a phospholipid transfer protein."
Olayioye M.A., Vehring S., Muller P., Herrmann A., Schiller J., Thiele C., Lindeman G.J., Visvader J.E., Pomorski T.
J. Biol. Chem. 280:27436-27442(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, LIPID-BINDING.
[5]"Phosphorylation of StarD10 on serine 284 by casein kinase II modulates its lipid transfer activity."
Olayioye M.A., Buchholz M., Schmid S., Schoffler P., Hoffmann P., Pomorski T.
J. Biol. Chem. 282:22492-22498(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-284, SUBCELLULAR LOCATION.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF151810 mRNA. Translation: AAD34047.1. Different initiation.
BC007919 mRNA. Translation: AAH07919.1.
BC014033 mRNA. Translation: AAH14033.1.
AF039696 mRNA. Translation: AAC18045.1. Sequence problems.
CCDSCCDS41688.1.
RefSeqNP_006636.2. NM_006645.2.
UniGeneHs.188606.

3D structure databases

ProteinModelPortalQ9Y365.
SMRQ9Y365. Positions 42-198.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116023. 4 interactions.
IntActQ9Y365. 1 interaction.
MINTMINT-5000159.

PTM databases

PhosphoSiteQ9Y365.

Polymorphism databases

DMDM25090873.

Proteomic databases

MaxQBQ9Y365.
PaxDbQ9Y365.
PRIDEQ9Y365.

Protocols and materials databases

DNASU10809.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000334805; ENSP00000335247; ENSG00000214530.
ENST00000543304; ENSP00000438792; ENSG00000214530.
GeneID10809.
KEGGhsa:10809.
UCSCuc001osy.3. human.

Organism-specific databases

CTD10809.
GeneCardsGC11M072465.
HGNCHGNC:10666. STARD10.
HPAHPA026661.
neXtProtNX_Q9Y365.
PharmGKBPA35596.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG292439.
HOGENOMHOG000019919.
HOVERGENHBG031807.
InParanoidQ9Y365.
OMAASFKAEC.
PhylomeDBQ9Y365.
TreeFamTF354285.

Gene expression databases

ArrayExpressQ9Y365.
BgeeQ9Y365.
CleanExHS_STARD10.
GenevestigatorQ9Y365.

Family and domain databases

Gene3D3.30.530.20. 1 hit.
InterProIPR023393. START-like_dom.
IPR002913. START_lipid-bd_dom.
[Graphical view]
PfamPF01852. START. 1 hit.
[Graphical view]
SMARTSM00234. START. 1 hit.
[Graphical view]
PROSITEPS50848. START. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSTARD10.
GenomeRNAi10809.
NextBio41063.
PROQ9Y365.

Entry information

Entry namePCTL_HUMAN
AccessionPrimary (citable) accession number: Q9Y365
Secondary accession number(s): O60532
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: July 9, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM