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StAR-related lipid transfer protein 13 (46H23.2) (Deleted in liver cancer 2 protein) (DLC-2) (Rho GTPase-activating protein) (START domain-containing protein 13) (StARD13)

 STA13_HUMAN             Reviewed;        1113 AA.
Q9Y3M8; A2A309; A2A310; Q5HYH1; Q5TAE3; Q6UN61; Q86TP6; Q86WQ3;
Q86XT1;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
07-MAR-2006, sequence version 2.
22-NOV-2017, entry version 146.
RecName: Full=StAR-related lipid transfer protein 13;
AltName: Full=46H23.2;
AltName: Full=Deleted in liver cancer 2 protein;
Short=DLC-2;
AltName: Full=Rho GTPase-activating protein;
AltName: Full=START domain-containing protein 13;
Short=StARD13;
Name=STARD13; Synonyms=DLC2, GT650;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
MUTAGENESIS OF ARG-699.
PubMed=12531887; DOI=10.1074/jbc.M208310200;
Ching Y.-P., Wong C.-M., Chan S.-F., Leung T.H.-Y., Ng D.-C.,
Jin D.-Y., Ng I.O.;
"Deleted in liver cancer (DLC) 2 encodes a RhoGAP protein with growth
suppressor function and is underexpressed in hepatocellular
carcinoma.";
J. Biol. Chem. 278:10824-10830(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND INTERACTION WITH TAX1BP1.
PubMed=14697242; DOI=10.1016/j.bbrc.2003.12.001;
Nagaraja G.M., Kandpal R.P.;
"Chromosome 13q12 encoded Rho GTPase activating protein suppresses
growth of breast carcinoma cells, and yeast two-hybrid screen shows
its interaction with several proteins.";
Biochem. Biophys. Res. Commun. 313:654-665(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-736 AND ARG-740.
PubMed=16217026; DOI=10.1073/pnas.0504501102;
Leung T.H.-Y., Ching Y.-P., Yam J.W.P., Wong C.-M., Yau T.-O.,
Jin D.-Y., Ng I.O.;
"Deleted in liver cancer 2 (DLC2) suppresses cell transformation by
means of inhibition of RhoA activity.";
Proc. Natl. Acad. Sci. U.S.A. 102:15207-15212(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Rhodes S.;
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
SUBCELLULAR LOCATION.
PubMed=16364308; DOI=10.1016/j.febslet.2005.11.073;
Ng D.C.-H., Chan S.-F., Kok K.H., Yam J.W.P., Ching Y.-P., Ng I.O.,
Jin D.-Y.;
"Mitochondrial targeting of growth suppressor protein DLC2 through the
START domain.";
FEBS Lett. 580:191-198(2006).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
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.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[10]
STRUCTURE BY NMR OF 56-120, SUBUNIT, AND INTERACTION WITH MEMBRANE
PHOSPHOLIPIDS.
PubMed=17380510; DOI=10.1002/prot.21361;
Li H., Fung K.-L., Jin D.-Y., Chung S.S.M., Ching Y.-P., Ng I.O.,
Sze K.-H., Ko B.C.B., Sun H.;
"Solution structures, dynamics, and lipid-binding of the sterile
alpha-motif domain of the deleted in liver cancer 2.";
Proteins 67:1154-1166(2007).
[11]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 900-1113.
Structural genomics consortium (SGC);
"The crystal structure of human STARD13 (DLC2) lipid transfer and
protein localization domain.";
Submitted (MAY-2007) to the PDB data bank.
-!- FUNCTION: GTPase-activating protein for RhoA, and perhaps for
Cdc42. May be involved in regulation of cytoskeletal
reorganization, cell proliferation and cell motility. Acts a tumor
suppressor in hepatocellular carcinoma cells.
{ECO:0000269|PubMed:14697242, ECO:0000269|PubMed:16217026}.
-!- SUBUNIT: Homodimer. Interacts with TAX1BP1.
{ECO:0000269|PubMed:14697242, ECO:0000269|PubMed:17380510}.
-!- INTERACTION:
Q86VP1:TAX1BP1; NbExp=2; IntAct=EBI-465487, EBI-529518;
-!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
protein; Cytoplasmic side. Mitochondrion membrane; Peripheral
membrane protein; Cytoplasmic side. Lipid droplet.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=DLC2alpha;
IsoId=Q9Y3M8-1; Sequence=Displayed;
Name=2; Synonyms=DLC2beta;
IsoId=Q9Y3M8-2; Sequence=VSP_017354;
Name=3; Synonyms=DLC2gamma;
IsoId=Q9Y3M8-3; Sequence=VSP_017353;
Name=4;
IsoId=Q9Y3M8-4; Sequence=VSP_017355;
Name=5;
IsoId=Q9Y3M8-5; Sequence=VSP_017354, VSP_017356, VSP_017357;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Underexpressed in
hepatocellular carcinoma cells and some breast cancer cell lines.
{ECO:0000269|PubMed:12531887, ECO:0000269|PubMed:14697242}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/STARD13ID44051ch13q13.html";
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EMBL; AY082589; AAL91648.1; -; mRNA.
EMBL; AY366448; AAQ72791.1; -; mRNA.
EMBL; AY082590; AAL91649.1; -; mRNA.
EMBL; AY082591; AAL91650.1; -; mRNA.
EMBL; AL049801; CAB42562.1; -; mRNA.
EMBL; BX647695; CAI46026.1; -; mRNA.
EMBL; Z84483; CAC94774.1; -; Genomic_DNA.
EMBL; AL627232; CAM17900.1; -; Genomic_DNA.
EMBL; AL139187; CAM17900.1; JOINED; Genomic_DNA.
EMBL; AL139187; CAM23625.1; -; Genomic_DNA.
EMBL; AL627232; CAM23625.1; JOINED; Genomic_DNA.
EMBL; AL139187; CAM23626.1; -; Genomic_DNA.
EMBL; BC046563; AAH46563.1; -; mRNA.
CCDS; CCDS9348.1; -. [Q9Y3M8-1]
CCDS; CCDS9349.1; -. [Q9Y3M8-2]
CCDS; CCDS9350.1; -. [Q9Y3M8-3]
PIR; H59432; H59432.
RefSeq; NP_001230395.1; NM_001243466.1. [Q9Y3M8-5]
RefSeq; NP_001230403.1; NM_001243474.1.
RefSeq; NP_001230405.1; NM_001243476.2.
RefSeq; NP_443083.1; NM_052851.2. [Q9Y3M8-3]
RefSeq; NP_821074.1; NM_178006.3. [Q9Y3M8-1]
RefSeq; NP_821075.1; NM_178007.2. [Q9Y3M8-2]
UniGene; Hs.156551; -.
UniGene; Hs.507704; -.
UniGene; Hs.721224; -.
PDB; 2H80; NMR; -; A=56-120.
PDB; 2JW2; NMR; -; A=56-120.
PDB; 2PSO; X-ray; 2.80 A; A/B/C=903-1113.
PDBsum; 2H80; -.
PDBsum; 2JW2; -.
PDBsum; 2PSO; -.
ProteinModelPortal; Q9Y3M8; -.
SMR; Q9Y3M8; -.
BioGrid; 124744; 38.
IntAct; Q9Y3M8; 11.
MINT; MINT-1194865; -.
STRING; 9606.ENSP00000338785; -.
iPTMnet; Q9Y3M8; -.
PhosphoSitePlus; Q9Y3M8; -.
BioMuta; STARD13; -.
DMDM; 90185285; -.
EPD; Q9Y3M8; -.
PaxDb; Q9Y3M8; -.
PeptideAtlas; Q9Y3M8; -.
PRIDE; Q9Y3M8; -.
Ensembl; ENST00000255486; ENSP00000255486; ENSG00000133121. [Q9Y3M8-2]
Ensembl; ENST00000336934; ENSP00000338785; ENSG00000133121. [Q9Y3M8-1]
Ensembl; ENST00000399365; ENSP00000382300; ENSG00000133121. [Q9Y3M8-3]
GeneID; 90627; -.
KEGG; hsa:90627; -.
UCSC; uc001uuu.4; human. [Q9Y3M8-1]
CTD; 90627; -.
DisGeNET; 90627; -.
EuPathDB; HostDB:ENSG00000133121.20; -.
GeneCards; STARD13; -.
H-InvDB; HIX0171887; -.
HGNC; HGNC:19164; STARD13.
HPA; HPA039535; -.
HPA; HPA058867; -.
MIM; 609866; gene.
neXtProt; NX_Q9Y3M8; -.
OpenTargets; ENSG00000133121; -.
PharmGKB; PA38806; -.
eggNOG; KOG2200; Eukaryota.
eggNOG; ENOG410XQ10; LUCA.
GeneTree; ENSGT00760000119123; -.
HOVERGEN; HBG055955; -.
InParanoid; Q9Y3M8; -.
KO; K20632; -.
OMA; DEDFVQW; -.
OrthoDB; EOG091G00OE; -.
PhylomeDB; Q9Y3M8; -.
TreeFam; TF314044; -.
Reactome; R-HSA-194840; Rho GTPase cycle.
ChiTaRS; STARD13; human.
EvolutionaryTrace; Q9Y3M8; -.
GeneWiki; STARD13; -.
GenomeRNAi; 90627; -.
PRO; PR:Q9Y3M8; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000133121; -.
ExpressionAtlas; Q9Y3M8; baseline and differential.
Genevisible; Q9Y3M8; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
GO; GO:0005096; F:GTPase activator activity; TAS:Reactome.
GO; GO:0008289; F:lipid binding; IEA:InterPro.
GO; GO:0043542; P:endothelial cell migration; IMP:MGI.
GO; GO:0097498; P:endothelial tube lumen extension; IMP:MGI.
GO; GO:0090051; P:negative regulation of cell migration involved in sprouting angiogenesis; IMP:MGI.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
Gene3D; 1.10.555.10; -; 1.
Gene3D; 3.30.530.20; -; 1.
InterPro; IPR008936; Rho_GTPase_activation_prot.
InterPro; IPR000198; RhoGAP_dom.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR023393; START-like_dom_sf.
InterPro; IPR002913; START_lipid-bd_dom.
Pfam; PF00620; RhoGAP; 1.
Pfam; PF07647; SAM_2; 1.
Pfam; PF01852; START; 1.
SMART; SM00324; RhoGAP; 1.
SMART; SM00234; START; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF48350; SSF48350; 1.
PROSITE; PS50238; RHOGAP; 1.
PROSITE; PS50848; START; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; GTPase activation; Lipid droplet; Membrane; Mitochondrion;
Phosphoprotein; Polymorphism; Reference proteome; Tumor suppressor.
CHAIN 1 1113 StAR-related lipid transfer protein 13.
/FTId=PRO_0000220679.
DOMAIN 55 122 SAM.
DOMAIN 663 868 Rho-GAP. {ECO:0000255|PROSITE-
ProRule:PRU00172}.
DOMAIN 899 1107 START. {ECO:0000255|PROSITE-
ProRule:PRU00197}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 411 411 Phosphoserine.
{ECO:0000250|UniProtKB:Q923Q2}.
VAR_SEQ 1 118 Missing (in isoform 3).
{ECO:0000303|PubMed:16217026,
ECO:0000303|Ref.4}.
/FTId=VSP_017353.
VAR_SEQ 1 56 MFSQVPRTPASGCYYLNSMTPEGQEMYLRFDQTTRRSPYRM
SRILARHQLVTKIQQ -> MLEPSSVLHANVNQAPLWCLVL
RWCRECKDTVCGGKQKSRVNHTFQRR (in isoform 2
and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16217026}.
/FTId=VSP_017354.
VAR_SEQ 1 56 MFSQVPRTPASGCYYLNSMTPEGQEMYLRFDQTTRRSPYRM
SRILARHQLVTKIQQ -> MSTGTQPKTKVLSDKRPKERV
(in isoform 4).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_017355.
VAR_SEQ 695 695 V -> E (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017356.
VAR_SEQ 696 1113 Missing (in isoform 5).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017357.
VARIANT 175 175 T -> M (in dbSNP:rs9568878).
/FTId=VAR_037494.
VARIANT 250 250 K -> R (in dbSNP:rs3742321).
/FTId=VAR_022098.
VARIANT 383 383 R -> P (in dbSNP:rs34425674).
/FTId=VAR_037495.
VARIANT 798 798 N -> S (in dbSNP:rs35144435).
/FTId=VAR_037496.
MUTAGEN 699 699 R->A: Loss of RhoGAP activity.
{ECO:0000269|PubMed:12531887}.
MUTAGEN 736 736 K->E: Loss of RhoGAP activity.
{ECO:0000269|PubMed:16217026}.
MUTAGEN 740 740 R->E: Loss of RhoGAP activity.
{ECO:0000269|PubMed:16217026}.
CONFLICT 143 143 K -> R (in Ref. 2; AAQ72791).
{ECO:0000305}.
CONFLICT 397 397 I -> V (in Ref. 2; AAQ72791).
{ECO:0000305}.
CONFLICT 1097 1097 I -> T (in Ref. 2; AAQ72791).
{ECO:0000305}.
HELIX 56 69 {ECO:0000244|PDB:2H80}.
HELIX 73 77 {ECO:0000244|PDB:2H80}.
TURN 78 82 {ECO:0000244|PDB:2H80}.
HELIX 88 92 {ECO:0000244|PDB:2H80}.
HELIX 100 102 {ECO:0000244|PDB:2JW2}.
HELIX 103 117 {ECO:0000244|PDB:2H80}.
HELIX 913 924 {ECO:0000244|PDB:2PSO}.
STRAND 929 931 {ECO:0000244|PDB:2PSO}.
STRAND 934 936 {ECO:0000244|PDB:2PSO}.
STRAND 938 942 {ECO:0000244|PDB:2PSO}.
STRAND 952 961 {ECO:0000244|PDB:2PSO}.
HELIX 963 972 {ECO:0000244|PDB:2PSO}.
HELIX 974 976 {ECO:0000244|PDB:2PSO}.
STRAND 985 991 {ECO:0000244|PDB:2PSO}.
STRAND 994 1001 {ECO:0000244|PDB:2PSO}.
STRAND 1004 1006 {ECO:0000244|PDB:2PSO}.
STRAND 1010 1020 {ECO:0000244|PDB:2PSO}.
HELIX 1023 1025 {ECO:0000244|PDB:2PSO}.
STRAND 1027 1033 {ECO:0000244|PDB:2PSO}.
STRAND 1043 1046 {ECO:0000244|PDB:2PSO}.
STRAND 1049 1058 {ECO:0000244|PDB:2PSO}.
STRAND 1064 1072 {ECO:0000244|PDB:2PSO}.
STRAND 1075 1077 {ECO:0000244|PDB:2PSO}.
TURN 1079 1084 {ECO:0000244|PDB:2PSO}.
HELIX 1085 1099 {ECO:0000244|PDB:2PSO}.
SEQUENCE 1113 AA; 124967 MW; 314F809C23E6E1E4 CRC64;
MFSQVPRTPA SGCYYLNSMT PEGQEMYLRF DQTTRRSPYR MSRILARHQL VTKIQQEIEA
KEACDWLRAA GFPQYAQLYE DSQFPINIVA VKNDHDFLEK DLVEPLCRRL NTLNKCASMK
LDVNFQRKKG DDSDEEDLCI SNKWTFQRTS RRWSRVDDLY TLLPRGDRNG SPGGTGMRNT
TSSESVLTDL SEPEVCSIHS ESSGGSDSRS QPGQCCTDNP VMLDAPLVSS SLPQPPRDVL
NHPFHPKNEK PTRARAKSFL KRMETLRGKG AHGRHKGSGR TGGLVISGPM LQQEPESFKA
MQCIQIPNGD LQNSPPPACR KGLPCSGKSS GESSPSEHSS SGVSTPCLKE RKCHEANKRG
GMYLEDLDVL AGTALPDAGD QSRMHEFHSQ ENLVVHIPKD HKPGTFPKAL SIESLSPTDS
SNGVNWRTGS ISLGREQVPG AREPRLMASC HRASRVSIYD NVPGSHLYAS TGDLLDLEKD
DLFPHLDDIL QHVNGLQEVV DDWSKDVLPE LQTHDTLVGE PGLSTFPSPN QITLDFEGNS
VSEGRTTPSD VERDVTSLNE SEPPGVRDRR DSGVGASLTR PNRRLRWNSF QLSHQPRPAP
ASPHISSQTA SQLSLLQRFS LLRLTAIMEK HSMSNKHGWT WSVPKFMKRM KVPDYKDKAV
FGVPLIVHVQ RTGQPLPQSI QQALRYLRSN CLDQVGLFRK SGVKSRIHAL RQMNENFPEN
VNYEDQSAYD VADMVKQFFR DLPEPLFTNK LSETFLHIYQ YVSKEQRLQA VQAAILLLAD
ENREVLQTLL CFLNDVVNLV EENQMTPMNL AVCLAPSLFH LNLLKKESSP RVIQKKYATG
KPDQKDLNEN LAAAQGLAHM IMECDRLFEV PHELVAQSRN SYVEAEIHVP TLEELGTQLE
ESGATFHTYL NHLIQGLQKE AKEKFKGWVT CSSTDNTDLA FKKVGDGNPL KLWKASVEVE
APPSVVLNRV LRERHLWDED FVQWKVVETL DRQTEIYQYV LNSMAPHPSR DFVVLRTWKT
DLPKGMCTLV SLSVEHEEAQ LLGGVRAVVM DSQYLIEPCG SGKSRLTHIC RIDLKGHSPE
WYSKGFGHLC AAEVARIRNS FQPLIAEGPE TKI


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EIAAB31991 Bos taurus,Bovine,PCTP,PC-TP,Phosphatidylcholine transfer protein,StARD2,STARD2,StAR-related lipid transfer protein 2,START domain-containing protein 2
EIAAB40228 Es64,Mln64,Mouse,Mus musculus,Protein ES 64,Protein MLN 64,StARD3,Stard3,StAR-related lipid transfer protein 3,START domain-containing protein 3
EIAAB34661 ARHGAP7,Canis familiaris,Canis lupus familiaris,Deleted in liver cancer 1 protein homolog,DLC1,DLC-1,Dog,Rho GTPase-activating protein 7,Rho-type GTPase-activating protein 7,StARD12,STARD12,StAR-relat
EIAAB40238 Gestational trophoblastic tumor protein 1,GTT1,Homo sapiens,Human,StARD7,STARD7,StAR-related lipid transfer protein 7, mitochondrial,START domain-containing protein 7
EIAAB30218 Mouse,Mus musculus,Pctpl,PCTP-L,PCTP-like protein,Sdccag28,Sdccagg28,Serologically defined colon cancer antigen 28 homolog,StARD10,Stard10,StAR-related lipid transfer protein 10,START domain-containin
EIAAB40229 CAB1,Homo sapiens,Human,Metastatic lymph node gene 64 protein,MLN 64,MLN64,Protein CAB1,StARD3,STARD3,StAR-related lipid transfer protein 3,START domain-containing protein 3
EIAAB30217 Antigen NY-CO-28,CGI-52,Homo sapiens,Human,PCTP-L,PCTP-like protein,SDCCAG28,Serologically defined colon cancer antigen 28,StARD10,STARD10,StAR-related lipid transfer protein 10,START domain-containin
EIAAB40233 Mouse,Mus musculus,StARD5,Stard5,StAR-related lipid transfer protein 5,START domain-containing protein 5
EIAAB40236 Mouse,Mus musculus,StARD6,Stard6,StAR-related lipid transfer protein 6,START domain-containing protein 6
EIAAB40230 Mouse,Mus musculus,StARD4,Stard4,StAR-related lipid transfer protein 4,START domain-containing protein 4
EIAAB40234 Bos taurus,Bovine,StARD5,STARD5,StAR-related lipid transfer protein 5,START domain-containing protein 5
EIAAB40237 Mouse,Mus musculus,StARD7,Stard7,StAR-related lipid transfer protein 7, mitochondrial,START domain-containing protein 7
EIAAB40240 Kiaa0189,Mouse,Mus musculus,StARD8,Stard8,StAR-related lipid transfer protein 8,START domain-containing protein 8
EIAAB40235 Homo sapiens,Human,StARD6,STARD6,StAR-related lipid transfer protein 6,START domain-containing protein 6


 

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