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Protein

PCTP-like protein

Gene

STARD10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:STARD10
Synonyms:SDCCAG28
ORF Names:CGI-52
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:10666. STARD10.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35596.

Polymorphism and mutation databases

BioMutaiSTARD10.
DMDMi25090873.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 291291PCTP-like proteinPRO_0000220661Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei94 – 941N6-succinyllysineBy similarity
Modified residuei197 – 1971N6-succinyllysineBy similarity
Modified residuei202 – 2021N6-succinyllysineBy similarity
Modified residuei253 – 2531Phosphoserine1 Publication
Modified residuei259 – 2591Phosphoserine1 Publication
Modified residuei284 – 2841Phosphoserine; by CK22 Publications

Post-translational modificationi

Phosphorylation at Ser-284 by CK2 negatively regulates lipid transfer activity, possibly by decreasing membrane association.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Y365.
PaxDbiQ9Y365.
PRIDEiQ9Y365.

PTM databases

PhosphoSiteiQ9Y365.

Expressioni

Gene expression databases

BgeeiQ9Y365.
CleanExiHS_STARD10.
ExpressionAtlasiQ9Y365. baseline and differential.
GenevisibleiQ9Y365. HS.

Organism-specific databases

HPAiHPA026661.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
PRMT6Q96LA82EBI-4289836,EBI-912440

Protein-protein interaction databases

BioGridi116023. 3 interactions.
IntActiQ9Y365. 1 interaction.
MINTiMINT-5000159.
STRINGi9606.ENSP00000335247.

Structurei

3D structure databases

ProteinModelPortaliQ9Y365.
SMRiQ9Y365. Positions 42-198.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 224211STARTPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 START domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG292439.
GeneTreeiENSGT00510000047611.
HOGENOMiHOG000019919.
HOVERGENiHBG031807.
InParanoidiQ9Y365.
PhylomeDBiQ9Y365.
TreeFamiTF354285.

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]

Sequencei

Sequence statusi: Complete.

Q9Y365-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKLAASTEP QGPRPVLGRE SVQVPDDQDF RSFRSECEAE VGWNLTYSRA
60 70 80 90 100
GVSVWVQAVE MDRTLHKIKC RMECCDVPAE TLYDVLHDIE YRKKWDSNVI
110 120 130 140 150
ETFDIARLTV NADVGYYSWR CPKPLKNRDV ITLRSWLPMG ADYIIMNYSV
160 170 180 190 200
KHPKYPPRKD LVRAVSIQTG YLIQSTGPKS CVITYLAQVD PKGSLPKWVV
210 220 230 240 250
NKSSQFLAPK AMKKMYKACL KYPEWKQKHL PHFKPWLHPE QSPLPSLALS
260 270 280 290
ELSVQHADSL ENIDESAVAE SREERMGGAG GEGSDDDTSL T
Length:291
Mass (Da):33,049
Last modified:November 15, 2002 - v2
Checksum:i26D6D3AF8C300EA6
GO

Sequence cautioni

The sequence AAC18045.1 differs from that shown.Various sequencing problems as well as a translation in a wrong frame.Curated
The sequence AAD34047.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151810 mRNA. Translation: AAD34047.1. Different initiation.
BC007919 mRNA. Translation: AAH07919.1.
BC014033 mRNA. Translation: AAH14033.1.
AF039696 mRNA. Translation: AAC18045.1. Sequence problems.
CCDSiCCDS41688.1.
RefSeqiNP_006636.2. NM_006645.2.
UniGeneiHs.188606.

Genome annotation databases

EnsembliENST00000334805; ENSP00000335247; ENSG00000214530.
ENST00000543304; ENSP00000438792; ENSG00000214530.
GeneIDi10809.
KEGGihsa:10809.
UCSCiuc001osy.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151810 mRNA. Translation: AAD34047.1. Different initiation.
BC007919 mRNA. Translation: AAH07919.1.
BC014033 mRNA. Translation: AAH14033.1.
AF039696 mRNA. Translation: AAC18045.1. Sequence problems.
CCDSiCCDS41688.1.
RefSeqiNP_006636.2. NM_006645.2.
UniGeneiHs.188606.

3D structure databases

ProteinModelPortaliQ9Y365.
SMRiQ9Y365. Positions 42-198.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116023. 3 interactions.
IntActiQ9Y365. 1 interaction.
MINTiMINT-5000159.
STRINGi9606.ENSP00000335247.

PTM databases

PhosphoSiteiQ9Y365.

Polymorphism and mutation databases

BioMutaiSTARD10.
DMDMi25090873.

Proteomic databases

MaxQBiQ9Y365.
PaxDbiQ9Y365.
PRIDEiQ9Y365.

Protocols and materials databases

DNASUi10809.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000334805; ENSP00000335247; ENSG00000214530.
ENST00000543304; ENSP00000438792; ENSG00000214530.
GeneIDi10809.
KEGGihsa:10809.
UCSCiuc001osy.3. human.

Organism-specific databases

CTDi10809.
GeneCardsiGC11M072465.
HGNCiHGNC:10666. STARD10.
HPAiHPA026661.
neXtProtiNX_Q9Y365.
PharmGKBiPA35596.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG292439.
GeneTreeiENSGT00510000047611.
HOGENOMiHOG000019919.
HOVERGENiHBG031807.
InParanoidiQ9Y365.
PhylomeDBiQ9Y365.
TreeFamiTF354285.

Miscellaneous databases

GeneWikiiSTARD10.
GenomeRNAii10809.
NextBioi41063.
PROiQ9Y365.

Gene expression databases

BgeeiQ9Y365.
CleanExiHS_STARD10.
ExpressionAtlasiQ9Y365. baseline and differential.
GenevisibleiQ9Y365. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253; SER-259 AND SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPCTL_HUMAN
AccessioniPrimary (citable) accession number: Q9Y365
Secondary accession number(s): O60532
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: July 22, 2015
This is version 114 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.