Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Oxysterol-binding protein-related protein 10 (ORP-10) (OSBP-related protein 10)

 OSB10_HUMAN             Reviewed;         764 AA.
Q9BXB5; B4E212; Q9BTU5;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
11-FEB-2002, sequence version 2.
12-SEP-2018, entry version 133.
RecName: Full=Oxysterol-binding protein-related protein 10;
Short=ORP-10;
Short=OSBP-related protein 10;
Name=OSBPL10; Synonyms=ORP10, OSBP9;
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).
PubMed=11735225; DOI=10.1006/geno.2001.6663;
Jaworski C.J., Moreira E., Li A., Lee R., Rodriguez I.R.;
"A family of 12 human genes containing oxysterol-binding domains.";
Genomics 78:185-196(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-251 (ISOFORM 1).
PubMed=11483621;
Lehto M., Laitinen S., Chinetti G., Johansson M., Ehnholm C.,
Staels B., Ikonen E., Olkkonen V.M.;
"The OSBP-related protein family in humans.";
J. Lipid Res. 42:1203-1213(2001).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[7]
FUNCTION, AND DOMAIN.
PubMed=17428193; DOI=10.1042/BJ20070176;
Suchanek M., Hynynen R., Wohlfahrt G., Lehto M., Johansson M.,
Saarinen H., Radzikowska A., Thiele C., Olkkonen V.M.;
"The mammalian oxysterol-binding protein-related proteins (ORPs) bind
25-hydroxycholesterol in an evolutionarily conserved pocket.";
Biochem. J. 405:473-480(2007).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-60; SER-64;
THR-196; SER-201 AND SER-223, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19554302; DOI=10.1007/s00109-009-0490-z;
Perttila J., Merikanto K., Naukkarinen J., Surakka I., Martin N.W.,
Tanhuanpaa K., Grimard V., Taskinen M.R., Thiele C., Salomaa V.,
Jula A., Perola M., Virtanen I., Peltonen L., Olkkonen V.M.;
"OSBPL10, a novel candidate gene for high triglyceride trait in
dyslipidemic Finnish subjects, regulates cellular lipid metabolism.";
J. Mol. Med. 87:825-835(2009).
[11]
POLYMORPHISM.
PubMed=20224571; DOI=10.1038/hr.2010.28;
Koriyama H., Nakagami H., Katsuya T., Akasaka H., Saitoh S.,
Shimamoto K., Ogihara T., Kaneda Y., Morishita R., Rakugi H.;
"Variation in OSBPL10 is associated with dyslipidemia.";
Hypertens. Res. 33:511-514(2010).
[12]
POLYMORPHISM.
PubMed=20610895; DOI=10.5551/jat.4291;
Koriyama H., Nakagami H., Katsuya T., Sugimoto K., Yamashita H.,
Takami Y., Maeda S., Kubo M., Takahashi A., Nakamura Y., Ogihara T.,
Rakugi H., Kaneda Y., Morishita R.;
"Identification of evidence suggestive of an association with
peripheral arterial disease at the OSBPL10 locus by genome-wide
investigation in the Japanese population.";
J. Atheroscler. Thromb. 17:1054-1062(2010).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209 AND SER-223, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
FUNCTION, INTERACTION WITH OSBPL9, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=22906437; DOI=10.1016/j.bbalip.2012.08.004;
Nissila E., Ohsaki Y., Weber-Boyvat M., Perttila J., Ikonen E.,
Olkkonen V.M.;
"ORP10, a cholesterol binding protein associated with microtubules,
regulates apolipoprotein B-100 secretion.";
Biochim. Biophys. Acta 1821:1472-1484(2012).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30; SER-64; SER-209 AND
SER-223, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
FUNCTION.
PubMed=23934110; DOI=10.1038/nature12430;
Maeda K., Anand K., Chiapparino A., Kumar A., Poletto M., Kaksonen M.,
Gavin A.C.;
"Interactome map uncovers phosphatidylserine transport by oxysterol-
binding proteins.";
Nature 501:257-261(2013).
[18]
IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH DIAPH1.
PubMed=23325789; DOI=10.1091/mbc.E12-08-0597;
Li D., Dammer E.B., Lucki N.C., Sewer M.B.;
"cAMP-stimulated phosphorylation of diaphanous 1 regulates protein
stability and interaction with binding partners in adrenocortical
cells.";
Mol. Biol. Cell 24:848-857(2013).
[19]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-38, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- FUNCTION: Probable lipid transporter involved in lipid
countertransport between the endoplasmic reticulum and the plasma
membrane. Its ability to bind phosphatidylserine, suggests that it
specifically exchanges phosphatidylserine with
phosphatidylinositol 4-phosphate (PI4P), delivering
phosphatidylserine to the plasma membrane in exchange for PI4P
(PubMed:23934110) (Probable). Plays a role in negative regulation
of lipid biosynthesis (PubMed:19554302). Negatively regulates APOB
secretion from hepatocytes (PubMed:19554302, PubMed:22906437).
Binds cholesterol and acidic phospholipids (PubMed:22906437). Also
binds 25-hydroxycholesterol (PubMed:17428193). Binds
phosphatidylserine (PubMed:23934110).
{ECO:0000269|PubMed:17428193, ECO:0000269|PubMed:19554302,
ECO:0000269|PubMed:22906437, ECO:0000269|PubMed:23934110,
ECO:0000305}.
-!- SUBUNIT: Interacts with OSBPL9 (PubMed:22906437). Interacts with
DIAPH1 (PubMed:23325789). {ECO:0000269|PubMed:22906437,
ECO:0000269|PubMed:23325789}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:19554302, ECO:0000269|PubMed:22906437}.
Note=Associates with microtubules. {ECO:0000269|PubMed:19554302,
ECO:0000269|PubMed:22906437}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BXB5-1; Sequence=Displayed;
Name=2;
IsoId=Q9BXB5-2; Sequence=VSP_042930;
Note=No experimental confirmation available.;
-!- DOMAIN: The C-terminal region binds cholesterol, 25-hydroxysterol
and acidic phospholipids and is required for localization to
microtubules. {ECO:0000269|PubMed:17428193,
ECO:0000269|PubMed:22906437}.
-!- DOMAIN: The PH domain selectively interacts with
phosphatidylinositol-4-phosphate. {ECO:0000269|PubMed:22906437}.
-!- POLYMORPHISM: Polymorphisms are associated with dyslipidemia.
Variant Asn-254 is associated with LDL-cholesterol levels in
Japanese population (PubMed:20224571). Association with peripheral
arterial disease has also been oberved (PubMed:20610895).
{ECO:0000269|PubMed:20224571, ECO:0000269|PubMed:20610895}.
-!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF392451; AAL40664.1; -; mRNA.
EMBL; AK304067; BAG64974.1; -; mRNA.
EMBL; AC092024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC094019; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC107620; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC108485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC003168; AAH03168.2; -; mRNA.
EMBL; AF346291; AAK31140.1; -; mRNA.
CCDS; CCDS2651.1; -. [Q9BXB5-1]
CCDS; CCDS54559.1; -. [Q9BXB5-2]
RefSeq; NP_001167531.1; NM_001174060.1. [Q9BXB5-2]
RefSeq; NP_060254.2; NM_017784.4. [Q9BXB5-1]
UniGene; Hs.150122; -.
ProteinModelPortal; Q9BXB5; -.
SMR; Q9BXB5; -.
BioGrid; 125385; 20.
IntAct; Q9BXB5; 21.
STRING; 9606.ENSP00000379804; -.
SwissLipids; SLP:000000528; -.
iPTMnet; Q9BXB5; -.
PhosphoSitePlus; Q9BXB5; -.
BioMuta; OSBPL10; -.
DMDM; 20139128; -.
EPD; Q9BXB5; -.
MaxQB; Q9BXB5; -.
PaxDb; Q9BXB5; -.
PeptideAtlas; Q9BXB5; -.
PRIDE; Q9BXB5; -.
ProteomicsDB; 79399; -.
ProteomicsDB; 79400; -. [Q9BXB5-2]
Ensembl; ENST00000396556; ENSP00000379804; ENSG00000144645. [Q9BXB5-1]
Ensembl; ENST00000438237; ENSP00000406124; ENSG00000144645. [Q9BXB5-2]
GeneID; 114884; -.
KEGG; hsa:114884; -.
UCSC; uc011axf.3; human. [Q9BXB5-1]
CTD; 114884; -.
DisGeNET; 114884; -.
EuPathDB; HostDB:ENSG00000144645.13; -.
GeneCards; OSBPL10; -.
HGNC; HGNC:16395; OSBPL10.
HPA; HPA003636; -.
MIM; 606738; gene.
neXtProt; NX_Q9BXB5; -.
OpenTargets; ENSG00000144645; -.
PharmGKB; PA32824; -.
eggNOG; KOG2210; Eukaryota.
eggNOG; ENOG410XRW6; LUCA.
GeneTree; ENSGT00550000074515; -.
HOGENOM; HOG000233871; -.
HOVERGEN; HBG053376; -.
InParanoid; Q9BXB5; -.
KO; K20465; -.
OMA; REMMNQV; -.
OrthoDB; EOG091G0FV2; -.
PhylomeDB; Q9BXB5; -.
TreeFam; TF312807; -.
Reactome; R-HSA-1482801; Acyl chain remodelling of PS.
ChiTaRS; OSBPL10; human.
GenomeRNAi; 114884; -.
PRO; PR:Q9BXB5; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000144645; Expressed in 215 organ(s), highest expression level in cauda epididymis.
CleanEx; HS_OSBPL10; -.
ExpressionAtlas; Q9BXB5; baseline and differential.
Genevisible; Q9BXB5; HS.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
GO; GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB.
GO; GO:0005548; F:phospholipid transporter activity; TAS:Reactome.
GO; GO:0036150; P:phosphatidylserine acyl-chain remodeling; TAS:Reactome.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR037239; OSBP_sf.
InterPro; IPR000648; Oxysterol-bd.
InterPro; IPR018494; Oxysterol-bd_CS.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
PANTHER; PTHR10972; PTHR10972; 1.
Pfam; PF01237; Oxysterol_BP; 2.
SMART; SM00233; PH; 1.
SUPFAM; SSF144000; SSF144000; 1.
PROSITE; PS01013; OSBP; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Lipid biosynthesis; Lipid metabolism; Lipid transport;
Lipid-binding; Methylation; Phosphoprotein; Polymorphism;
Reference proteome; Transport.
CHAIN 1 764 Oxysterol-binding protein-related protein
10.
/FTId=PRO_0000100380.
DOMAIN 74 171 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
REGION 413 418 Phosphatidylinositol 4-phosphate binding.
{ECO:0000250|UniProtKB:Q02201}.
REGION 413 418 Phosphatidylserine binding.
{ECO:0000250|UniProtKB:Q02201}.
REGION 477 480 Phosphatidylinositol 4-phosphate binding.
{ECO:0000250|UniProtKB:Q02201}.
REGION 535 536 Phosphatidylinositol 4-phosphate binding.
{ECO:0000250|UniProtKB:Q02201}.
COILED 713 740 {ECO:0000255}.
COMPBIAS 14 66 Ser-rich. {ECO:0000255|PROSITE-
ProRule:PRU00016}.
BINDING 480 480 Phosphatidylserine.
{ECO:0000250|UniProtKB:Q02201}.
BINDING 561 561 Phosphatidylserine.
{ECO:0000250|UniProtKB:Q02201}.
BINDING 721 721 Phosphatidylinositol 4-phosphate.
{ECO:0000250|UniProtKB:Q02201}.
BINDING 725 725 Phosphatidylinositol 4-phosphate.
{ECO:0000250|UniProtKB:Q02201}.
BINDING 729 729 Phosphatidylinositol 4-phosphate.
{ECO:0000250|UniProtKB:Q02201}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000250|UniProtKB:S4R1M9}.
MOD_RES 30 30 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 38 38 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 57 57 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 64 64 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 196 196 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 201 201 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 209 209 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 223 223 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 180 243 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042930.
VARIANT 254 254 N -> D (in dbSNP:rs2290532).
/FTId=VAR_022100.
SEQUENCE 764 AA; 83970 MW; 62B1DF599C7C15FC CRC64;
MERAVQGTDG GGGSNSSSRS SSRATSAGSS PSCSLAGRGV SSRSAAAGLG GGGSRSSPGS
VAASPSGGGG RRREPALEGV LSKYTNLLQG WQNRYFVLDF EAGILQYFVN EQSKHQKPRG
VLSLSGAIVS LSDEAPHMLV VYSANGEMFK LRAADAKEKQ FWVTQLRACA KYHMEMNSKS
APSSRSRSLT LLPHGTPNSA SPCSQRHLSV GAPGVVTITH HKSPAAARRA KSQYSGQLHE
VREMMNQVEG QQKNLVHAIE SLPGSGPLTA LDQDLLLLKA TSAATLSCLG ECLNLLQQSV
HQAGQPSQKP GASENILGWH GSKSHSTEQL KNGTLGSLPS ASANITWAIL PNSAEDEQTS
QPEPEPNSGS ELVLSEDEKS DNEDKEETEL GVMEDQRSII LHLISQLKLG MDLTKVVLPT
FILEKRSLLE MYADFMAHPD LLLAITAGAT PEERVICFVE YYLTAFHEGR KGALAKKPYN
PIIGETFHCS WEVPKDRVKP KRTASRSPAS CHEHPMADDP SKSYKLRFVA EQVSHHPPIS
CFYCECEEKR LCVNTHVWTK SKFMGMSVGV SMIGEGVLRL LEHGEEYVFT LPSAYARSIL
TIPWVELGGK VSINCAKTGY SATVIFHTKP FYGGKVHRVT AEVKHNPTNT IVCKAHGEWN
GTLEFTYNNG ETKVIDTTTL PVYPKKIRPL EKQGPMESRN LWREVTRYLR LGDIDAATEQ
KRHLEEKQRV EERKRENLRT PWKPKYFIQE GDGWVYFNPL WKAH


Related products :

Catalog number Product name Quantity
EIAAB29238 Homo sapiens,Human,KIAA1534,OBPH1,ORP5,ORP-5,OSBPL5,OSBP-related protein 5,Oxysterol-binding protein homolog 1;,Oxysterol-binding protein-related protein 5
EIAAB29249 Homo sapiens,Human,KIAA1664,ORP4,ORP-4,OSBP2,OSBPL4,OSBP-related protein 4,Oxysterol-binding protein 2,Oxysterol-binding protein-related protein 4
EIAAB29237 Mouse,Mus musculus,Obph1,ORP-5,Osbp2,Osbpl5,OSBP-related protein 5,Oxysterol-binding protein homolog 1,Oxysterol-binding protein-related protein 5
EIAAB29227 Homo sapiens,Human,ORP10,ORP-10,OSBP9,OSBPL10,OSBP-related protein 10,Oxysterol-binding protein-related protein 10
EIAAB29228 Homo sapiens,Human,ORP11,ORP-11,OSBP12,OSBPL11,OSBP-related protein 11,Oxysterol-binding protein-related protein 11
EIAAB29234 Homo sapiens,Human,KIAA0772,ORP2,ORP-2,OSBPL2,OSBP-related protein 2,Oxysterol-binding protein-related protein 2
EIAAB29244 Homo sapiens,Human,ORP9,ORP-9,OSBP4,OSBPL9,OSBP-related protein 9,Oxysterol-binding protein-related protein 9
EIAAB29236 Homo sapiens,Human,KIAA0704,ORP3,ORP-3,OSBP3,OSBPL3,OSBP-related protein 3,Oxysterol-binding protein-related protein 3
EIAAB29242 Homo sapiens,Human,KIAA1451,ORP8,ORP-8,OSBP10,OSBPL8,OSBP-related protein 8,Oxysterol-binding protein-related protein 8
EIAAB29231 Homo sapiens,Human,ORP1,ORP-1,OSBP8,OSBPL1,OSBPL1A,OSBPL1B,OSBP-related protein 1,Oxysterol-binding protein-related protein 1
EIAAB29230 Mouse,Mus musculus,Orp1,ORP-1,Orp1a,Osbpl1a,OSBP-related protein 1,Oxysterol-binding protein-related protein 1
EIAAB29240 Homo sapiens,Human,ORP6,ORP-6,OSBPL6,OSBP-related protein 6,Oxysterol-binding protein-related protein 6
EIAAB29241 Homo sapiens,Human,ORP7,ORP-7,OSBPL7,OSBP-related protein 7,Oxysterol-binding protein-related protein 7
EIAAB29232 Orp1,ORP-1,Osbpl1a,OSBP-related protein 1,Oxysterol-binding protein-related protein 1,Rat,Rattus norvegicus
EIAAB29243 Mouse,Mus musculus,Orp9,ORP-9,Osbpl9,OSBP-related protein 9,Oxysterol-binding protein-related protein 9
EIAAB29235 Mouse,Mus musculus,Orp3,ORP-3,Osbpl3,OSBP-related protein 3,Oxysterol-binding protein-related protein 3
EIAAB29233 Mouse,Mus musculus,ORP-2,Osbpl2,OSBP-related protein 2,Oxysterol-binding protein-related protein 2
EIAAB29229 Mouse,Mus musculus,ORP-11,Osbpl11,OSBP-related protein 11,Oxysterol-binding protein-related protein 11
EIAAB29239 Mouse,Mus musculus,ORP-6,Osbpl6,OSBP-related protein 6,Oxysterol-binding protein-related protein 6
CSB-EL017253HU Human Oxysterol-binding protein-related protein 8(OSBPL8) ELISA kit 96T
CSB-EL017254MO Mouse Oxysterol-binding protein-related protein 9(OSBPL9) ELISA kit 96T
CSB-EL017251MO Mouse Oxysterol-binding protein-related protein 6(OSBPL6) ELISA kit 96T
CSB-EL017252HU Human Oxysterol-binding protein-related protein 7(OSBPL7) ELISA kit 96T
CSB-EL017254HU Human Oxysterol-binding protein-related protein 9(OSBPL9) ELISA kit 96T
CSB-EL017250MO Mouse Oxysterol-binding protein-related protein 5(OSBPL5) ELISA kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur