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Oxysterol-binding protein-related protein 1 (ORP-1) (OSBP-related protein 1)

 OSBL1_HUMAN             Reviewed;         950 AA.
Q9BXW6; B7Z7D3; Q9BZF5; Q9NW87;
11-FEB-2002, integrated into UniProtKB/Swiss-Prot.
27-MAR-2002, sequence version 2.
13-FEB-2019, entry version 170.
RecName: Full=Oxysterol-binding protein-related protein 1;
Short=ORP-1;
Short=OSBP-related protein 1;
Name=OSBPL1A; Synonyms=ORP1, OSBP8, OSBPL1, OSBPL1B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B), AND VARIANT PRO-810.
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 [MRNA] (ISOFORM A).
PubMed=11279184; DOI=10.1074/jbc.M101204200;
Xu Y., Liu Y., Ridgway N.D., McMaster C.R.;
"Novel members of the human oxysterol-binding protein family bind
phospholipids and regulate vesicle transport.";
J. Biol. Chem. 276:18407-18414(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND GENE FAMILY.
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 514-790 (ISOFORM A).
TISSUE=Embryo;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RAB7A.
PubMed=16176980; DOI=10.1091/mbc.E05-03-0189;
Johansson M., Lehto M., Tanhuanpaeae K., Cover T.L., Olkkonen V.M.;
"The oxysterol-binding protein homologue ORP1L interacts with Rab7 and
alters functional properties of late endocytic compartments.";
Mol. Biol. Cell 16:5480-5492(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
FUNCTION.
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, 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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, 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).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, 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).
-!- FUNCTION: Binds phospholipids; exhibits strong binding to
phosphatidic acid and weak binding to phosphatidylinositol 3-
phosphate (By similarity). Stabilizes GTP-bound RAB7A on late
endosomes/lysosomes and alters functional properties of late
endocytic compartments via its interaction with RAB7A
(PubMed:16176980). Binds 25-hydroxycholesterol and cholesterol
(PubMed:17428193). {ECO:0000250, ECO:0000269|PubMed:16176980,
ECO:0000269|PubMed:17428193}.
-!- SUBUNIT: Interacts with VAPA (By similarity). Interacts with the
GTP-bound form of RAB7A. Interacts with OAS1B (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Late endosome {ECO:0000269|PubMed:16176980}.
Note=Colocalizes with RAB7A, RAB9A and LAMP1 in late endosomes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=B; Synonyms=OSBPL1B, OSBP8L, ORP1L;
IsoId=Q9BXW6-1; Sequence=Displayed;
Name=A; Synonyms=OSBPL1A, OSBP8S;
IsoId=Q9BXW6-2; Sequence=VSP_003779;
Name=4;
IsoId=Q9BXW6-4; Sequence=VSP_045443;
-!- SIMILARITY: Belongs to the OSBP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG53407.2; Type=Miscellaneous discrepancy; Note=Unlikely isoform. Aberrant splice sites.; Evidence={ECO:0000305};
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EMBL; AF392449; AAL40662.1; -; mRNA.
EMBL; AF392450; AAL40663.1; -; mRNA.
EMBL; AF274714; AAK15154.1; -; mRNA.
EMBL; AF323726; AAG53407.2; ALT_SEQ; mRNA.
EMBL; AK001079; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AK301862; BAH13569.1; -; mRNA.
EMBL; AC023983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC090772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS11884.1; -. [Q9BXW6-1]
CCDS; CCDS11885.1; -. [Q9BXW6-2]
CCDS; CCDS56056.1; -. [Q9BXW6-4]
RefSeq; NP_001229437.1; NM_001242508.1. [Q9BXW6-4]
RefSeq; NP_060500.3; NM_018030.4. [Q9BXW6-2]
RefSeq; NP_542164.2; NM_080597.3. [Q9BXW6-1]
RefSeq; XP_016881022.1; XM_017025533.1. [Q9BXW6-2]
RefSeq; XP_016881023.1; XM_017025534.1.
UniGene; Hs.370725; -.
ProteinModelPortal; Q9BXW6; -.
SMR; Q9BXW6; -.
BioGrid; 125379; 25.
IntAct; Q9BXW6; 13.
STRING; 9606.ENSP00000320291; -.
SwissLipids; SLP:000001534; -.
iPTMnet; Q9BXW6; -.
PhosphoSitePlus; Q9BXW6; -.
BioMuta; OSBPL1A; -.
DMDM; 20143880; -.
EPD; Q9BXW6; -.
jPOST; Q9BXW6; -.
MaxQB; Q9BXW6; -.
PaxDb; Q9BXW6; -.
PeptideAtlas; Q9BXW6; -.
PRIDE; Q9BXW6; -.
ProteomicsDB; 79527; -.
ProteomicsDB; 79528; -. [Q9BXW6-2]
Ensembl; ENST00000319481; ENSP00000320291; ENSG00000141447. [Q9BXW6-1]
Ensembl; ENST00000357041; ENSP00000349545; ENSG00000141447. [Q9BXW6-4]
Ensembl; ENST00000399443; ENSP00000382372; ENSG00000141447. [Q9BXW6-2]
GeneID; 114876; -.
KEGG; hsa:114876; -.
UCSC; uc002kvd.5; human. [Q9BXW6-1]
CTD; 114876; -.
DisGeNET; 114876; -.
EuPathDB; HostDB:ENSG00000141447.16; -.
GeneCards; OSBPL1A; -.
H-InvDB; HIX0014371; -.
HGNC; HGNC:16398; OSBPL1A.
HPA; HPA040959; -.
HPA; HPA043401; -.
MIM; 606730; gene.
neXtProt; NX_Q9BXW6; -.
OpenTargets; ENSG00000141447; -.
PharmGKB; PA32826; -.
eggNOG; KOG1737; Eukaryota.
eggNOG; ENOG410XP9E; LUCA.
GeneTree; ENSGT00940000155295; -.
HOGENOM; HOG000048711; -.
HOVERGEN; HBG082087; -.
InParanoid; Q9BXW6; -.
KO; K20174; -.
OMA; IEDHSAY; -.
OrthoDB; 863978at2759; -.
PhylomeDB; Q9BXW6; -.
TreeFam; TF320922; -.
Reactome; R-HSA-192105; Synthesis of bile acids and bile salts.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
ChiTaRS; OSBPL1A; human.
GeneWiki; OSBPL1A; -.
GenomeRNAi; 114876; -.
PRO; PR:Q9BXW6; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000141447; Expressed in 230 organ(s), highest expression level in corpus callosum.
ExpressionAtlas; Q9BXW6; baseline and differential.
Genevisible; Q9BXW6; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IBA:GO_Central.
GO; GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
GO; GO:0008289; F:lipid binding; IBA:GO_Central.
GO; GO:0005543; F:phospholipid binding; NAS:UniProtKB.
GO; GO:0032934; F:sterol binding; IBA:GO_Central.
GO; GO:0015248; F:sterol transporter activity; IBA:GO_Central.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0006699; P:bile acid biosynthetic process; TAS:Reactome.
GO; GO:0008203; P:cholesterol metabolic process; NAS:UniProtKB.
GO; GO:0016192; P:vesicle-mediated transport; NAS:UniProtKB.
CDD; cd00204; ANK; 1.
Gene3D; 1.25.40.20; -; 2.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR002110; Ankyrin_rpt.
InterPro; IPR020683; Ankyrin_rpt-contain_dom.
InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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; 3.
Pfam; PF12796; Ank_2; 1.
Pfam; PF01237; Oxysterol_BP; 1.
PRINTS; PR01415; ANKYRIN.
SMART; SM00248; ANK; 3.
SMART; SM00233; PH; 1.
SUPFAM; SSF144000; SSF144000; 1.
SUPFAM; SSF48403; SSF48403; 1.
PROSITE; PS50297; ANK_REP_REGION; 1.
PROSITE; PS50088; ANK_REPEAT; 3.
PROSITE; PS01013; OSBP; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
1: Evidence at protein level;
Alternative splicing; ANK repeat; Coiled coil; Complete proteome;
Endosome; Lipid transport; Lipid-binding; Phosphoprotein;
Polymorphism; Reference proteome; Repeat; Transport.
CHAIN 1 950 Oxysterol-binding protein-related protein
1.
/FTId=PRO_0000100367.
REPEAT 47 76 ANK 1.
REPEAT 80 109 ANK 2.
REPEAT 175 204 ANK 3.
DOMAIN 235 334 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
REGION 1 237 Interaction with RAB7A.
{ECO:0000269|PubMed:16176980}.
COILED 430 463 {ECO:0000255}.
COILED 877 913 {ECO:0000255}.
MOD_RES 499 499 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 513 Missing (in isoform A).
{ECO:0000303|PubMed:11279184,
ECO:0000303|PubMed:11735225,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_003779.
VAR_SEQ 1 382 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045443.
VARIANT 810 810 S -> P (in dbSNP:rs35693789).
{ECO:0000269|PubMed:11735225}.
/FTId=VAR_053547.
CONFLICT 735 735 T -> A (in Ref. 4; AK001079).
{ECO:0000305}.
CONFLICT 841 841 P -> S (in Ref. 1; AAL40662).
{ECO:0000305}.
CONFLICT 844 844 A -> G (in Ref. 1; AAL40662).
{ECO:0000305}.
SEQUENCE 950 AA; 108470 MW; CDDA26CA27B65F63 CRC64;
MNTEAEQQLL HHARNGNAEE VRQLLETMAR NEVIADINCK GRSKSNLGWT PLHLACYFGH
RQVVQDLLKA GAEVNVLNDM GDTPLHRAAF TGRKELVMLL LEYNADTTIV NGSGQTAKEV
THAEEIRSML EAVERTQQRK LEELLLAAAR EGKTTELTAL LNRPNPPDVN CSDQLGNTPL
HCAAYRAHKQ CALKLLRSGA DPNLKNKNDQ KPLDLAQGAE MKHILVGNKV IYKALKRYEG
PLWKSSRFFG WRLFWVVLEH GVLSWYRKQP DAVHNIYRQG CKHLTQAVCT VKSTDSCLFF
IKCFDDTIHG FRVPKNSLQQ SREDWLEAIE EHSAYSTHYC SQDQLTDEEE EDTVSAADLK
KSLEKAQSCQ QRLDREISNF LKMIKECDMA KEMLPSFLQK VEVVSEASRE TCVALTDCLN
LFTKQEGVRN FKLEQEQEKN KILSEALETL ATEHHELEQS LVKGSPPASI LSEDEFYDAL
SDSESERSLS RLEAVTARSF EEEGEHLGSR KHRMSEEKDC GGGDALSNGI KKHRTSLPSP
MFSRNDFSIW SILRKCIGME LSKITMPVIF NEPLSFLQRL TEYMEHTYLI HKASSLSDPV
ERMQCVAAFA VSAVASQWER TGKPFNPLLG ETYELVRDDL GFRLISEQVS HHPPISAFHA
EGLNNDFIFH GSIYPKLKFW GKSVEAEPKG TITLELLEHN EAYTWTNPTC CVHNIIVGKL
WIEQYGNVEI INHKTGDKCV LNFKPCGLFG KELHKVEGYI QDKSKKKLCA LYGKWTECLY
SVDPATFDAY KKNDKKNTEE KKNSKQMSTS EELDEMPVPD SESVFIIPGS VLLWRIAPRP
PNSAQMYNFT SFAMVLNEVD KDMESVIPKT DCRLRPDIRA MENGEIDQAS EEKKRLEEKQ
RAARKNRSKS EEDWKTRWFH QGPNPYNGAQ DWIYSGSYWD RNYFNLPDIY


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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

Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP731: Sterol regulatory element binding protein related
WP2199: Seed Development
WP2272: Pathogenic Escherichia coli infection
WP1531: Vitamin D synthesis
WP1616: ABC transporters
WP2292: Chemokine signaling pathway
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair

Related Genes :
[OSBPL3 KIAA0704 ORP3 OSBP3] Oxysterol-binding protein-related protein 3 (ORP-3) (OSBP-related protein 3)
[Osbpl8 Kiaa1451 Orp8] Oxysterol-binding protein-related protein 8 (ORP-8) (OSBP-related protein 8)
[OSBPL2 KIAA0772 ORP2] Oxysterol-binding protein-related protein 2 (ORP-2) (OSBP-related protein 2)
[OSBP OSBP1] Oxysterol-binding protein 1
[Osbpl3 Orp3] Oxysterol-binding protein-related protein 3 (ORP-3) (OSBP-related protein 3)
[gag-pol] Gag-Pol polyprotein (Pr180gag-pol) [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10 (NC-pol); Protease p14 (PR) (EC 3.4.23.-); Reverse transcriptase/ribonuclease H p80 (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase p46 (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr180gag-pol) [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10 (NC-pol); Protease p14 (PR) (EC 3.4.23.-); Reverse transcriptase/ribonuclease H p80 (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase p46 (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[gag-pol] Gag-Pol polyprotein (Pr180gag-pol) [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10 (NC-pol); Protease p14 (PR) (EC 3.4.23.-); Reverse transcriptase/ribonuclease H p80 (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase p46 (IN) (EC 2.7.7.-) (EC 3.1.-.-)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO) (SARS coronavirus main proteinase); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[Osbp Kiaa4220] Oxysterol-binding protein 1
[OSBP] Oxysterol-binding protein 1
[S 2] Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
[AURKA AIK AIRK1 ARK1 AURA AYK1 BTAK IAK1 STK15 STK6] Aurora kinase A (EC 2.7.11.1) (Aurora 2) (Aurora/IPL1-related kinase 1) (ARK-1) (Aurora-related kinase 1) (hARK1) (Breast tumor-amplified kinase) (Serine/threonine-protein kinase 15) (Serine/threonine-protein kinase 6) (Serine/threonine-protein kinase aurora-A)
[Ceacam1 Bgp Bgp1] Carcinoembryonic antigen-related cell adhesion molecule 1 (Biliary glycoprotein 1) (BGP-1) (Biliary glycoprotein D) (MHVR1) (Murine hepatitis virus receptor) (MHV-R) (CD antigen CD66a)
[Rorc Nr1f3 Rorg Thor] Nuclear receptor ROR-gamma (Nuclear receptor RZR-gamma) (Nuclear receptor subfamily 1 group F member 3) (RAR-related orphan receptor C) (Retinoid-related orphan receptor-gamma) (Thymus orphan receptor) (TOR)
[S 3] Spike glycoprotein (S glycoprotein) (E2) (Peplomer protein) [Cleaved into: Spike protein S1; Spike protein S2; Spike protein S2']
[Rora Nr1f1 Rzra] Nuclear receptor ROR-alpha (Nuclear receptor RZR-alpha) (Nuclear receptor subfamily 1 group F member 1) (RAR-related orphan receptor A) (Retinoid-related orphan receptor-alpha)
[Aurka Aik Airk Ark1 Aura Ayk1 Btak Iak1 Stk15 Stk6] Aurora kinase A (EC 2.7.11.1) (Aurora 2) (Aurora family kinase 1) (Aurora/IPL1-related kinase 1) (ARK-1) (Aurora-related kinase 1) (Ipl1- and aurora-related kinase 1) (Serine/threonine-protein kinase 6) (Serine/threonine-protein kinase Ayk1) (Serine/threonine-protein kinase aurora-A)
[Atk TK] Tachykinins (AmTRP) (Tachykinin-related peptide) [Cleaved into: APTGHQEMQ-amide (AmTRP1) (Tachykinin-related peptide 1) (TRP1); ALMGFQGVR-amide (AmTRP2) (Tachykinin-related peptide 2) (TRP2); Brain peptide NSIINDVKNELFPEDIN; APMGFQGMR-amide 1 (AmTRP3) (Tachykinin-related peptide 3-1) (TRP3-1); Brain peptide ASFDDEYY; APMGFQGMR-amide 2 (AmTRP3) (Tachykinin-related peptide 3-2) (TRP3-2); Brain peptide SLEEILDEIK; Brain peptide SLEEILDEI; Brain peptide EILDEI; TTRFQDSRSKDVYLIDYPEDY-amide (AmTAP1) (Tachykinin-associated peptide 1); Brain peptide VLSMDGYQNILDKKDELLGEWE; Brain peptide APMGFYGT; APMGFYGTR-amide (AmTRP4) (Tachykinin-related peptide 4) (TRP4); Brain peptide IILDALEELD; Brain peptide ILDALEELD; Brain peptide GVMDFQIGLQ; ARMGFHGMR-amide (AmTRP5) (Tachykinin-related peptide 5) (TRP5); SPFRYLGAR-amide (AmTRP6) (Tachykinin-related peptide 6) (TRP6); NPRWEFRGKFVGVR-amide (AmTRP7) (Tachykinin-related peptide 7) (TRP7)]
[KIN10 AK21 AKIN10 SKIN10 SNR2 SNRK1.1 At3g01090 T4P13.22] SNF1-related protein kinase catalytic subunit alpha KIN10 (AKIN10) (EC 2.7.11.1) (AKIN alpha-2) (AKINalpha2) (SNF1-related kinase 1.1) (SnRK1.1)
[HEY1 BHLHB31 CHF2 HERP2 HESR1 HRT1] Hairy/enhancer-of-split related with YRPW motif protein 1 (Cardiovascular helix-loop-helix factor 2) (CHF-2) (Class B basic helix-loop-helix protein 31) (bHLHb31) (HES-related repressor protein 1) (Hairy and enhancer of split-related protein 1) (HESR-1) (Hairy-related transcription factor 1) (HRT-1) (hHRT1)
[KIN11 AKIN11 SNR1 SNRK1.2 At3g29160 MXE2.16] SNF1-related protein kinase catalytic subunit alpha KIN11 (AKIN11) (EC 2.7.11.1) (AKIN alpha-1) (AKINalpha1) (SNF1-related kinase 1.2) (SnRK1.2)
[RORA NR1F1 RZRA] Nuclear receptor ROR-alpha (Nuclear receptor RZR-alpha) (Nuclear receptor subfamily 1 group F member 1) (RAR-related orphan receptor A) (Retinoid-related orphan receptor-alpha)
[hey1 bc8 hrt1] Hairy/enhancer-of-split related with YRPW motif protein 1 (XHey-1) (Hairy and enhancer of split-related protein 1) (Hesr-1) (Hairy-related transcription factor 1) (HRT-1) (XHRT1) (xHRT-1) (Protein xbc8)
[KCNH2 ERG ERG1 HERG] Potassium voltage-gated channel subfamily H member 2 (Eag homolog) (Ether-a-go-go-related gene potassium channel 1) (ERG-1) (Eag-related protein 1) (Ether-a-go-go-related protein 1) (H-ERG) (hERG-1) (hERG1) (Voltage-gated potassium channel subunit Kv11.1)
[RTM1 JAL1 At1g05760 T20M3.2] Protein RESTRICTED TEV MOVEMENT 1 (Jacalin-related lectin 1) (Restricted tobacco etch virus movement protein 1)
[RUNX1 AML1 CBFA2] Runt-related transcription factor 1 (Acute myeloid leukemia 1 protein) (Core-binding factor subunit alpha-2) (CBF-alpha-2) (Oncogene AML-1) (Polyomavirus enhancer-binding protein 2 alpha B subunit) (PEA2-alpha B) (PEBP2-alpha B) (SL3-3 enhancer factor 1 alpha B subunit) (SL3/AKV core-binding factor alpha B subunit)
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[1a] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Non-structural protein 1 (nsp1) (Leader protein); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.69) (PL2-PRO) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (nsp5); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[Nfe2l1 Nrf1] Endoplasmic reticulum membrane sensor NFE2L1 (Locus control region-factor 1) (LCR-F1) (Nuclear factor erythroid 2-related factor 1) (NF-E2-related factor 1) (NFE2-related factor 1) (Nuclear factor, erythroid derived 2, like 1) [Cleaved into: Transcription factor NRF1]

Bibliography :
[12631712] The two variants of oxysterol binding protein-related protein-1 display different tissue expression patterns, have different intracellular localization, and are functionally distinct.