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Hypoxia up-regulated protein 1 (150 kDa oxygen-regulated protein) (ORP-150) (170 kDa glucose-regulated protein) (GRP-170)

 HYOU1_HUMAN             Reviewed;         999 AA.
Q9Y4L1; A8C1Z0; B7Z909; Q2I204; Q53H25;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
13-FEB-2019, entry version 183.
RecName: Full=Hypoxia up-regulated protein 1;
AltName: Full=150 kDa oxygen-regulated protein;
Short=ORP-150;
AltName: Full=170 kDa glucose-regulated protein;
Short=GRP-170;
Flags: Precursor;
Name=HYOU1; Synonyms=GRP170, ORP150;
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=Astrocytoma;
PubMed=9020069; DOI=10.1006/bbrc.1996.5890;
Ikeda J., Kaneda S., Kuwabara K., Ogawa S., Kobayashi T.,
Matsumoto M., Yura T., Yanagi H.;
"Cloning and expression of cDNA encoding the human 150 kDa oxygen-
regulated protein, ORP150.";
Biochem. Biophys. Res. Commun. 230:94-99(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10965054; DOI=10.1093/oxfordjournals.jbchem.a022783;
Kaneda S., Yura T., Yanagi H.;
"Production of three distinct mRNAs of 150 kDa oxygen-regulated
protein (ORP150) by alternative promoters: preferential induction of
one species under stress conditions.";
J. Biochem. 128:529-538(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Heart;
PubMed=17131193; DOI=10.1007/s10930-006-9038-z;
Takeuchi S.;
"Molecular cloning, sequence, function and structural basis of human
heart 150 kDa oxygen-regulated protein, an ER chaperone.";
Protein J. 25:517-528(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Cerebellum, and 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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Liver;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[8]
PROTEIN SEQUENCE OF 241-256; 541-555; 577-594 AND 754-768, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[9]
FUNCTION.
PubMed=10037731; DOI=10.1074/jbc.274.10.6397;
Ozawa K., Kuwabara K., Tamatani M., Takatsuji K., Tsukamoto Y.,
Kaneda S., Yanagi H., Stern D.M., Eguchi Y., Tsujimoto Y., Ogawa S.,
Tohyama M.;
"150-kDa oxygen-regulated protein (ORP150) suppresses hypoxia-induced
apoptotic cell death.";
J. Biol. Chem. 274:6397-6404(1999).
[10]
COMPONENT OF A CHAPERONE COMPLEX.
PubMed=12475965; DOI=10.1091/mbc.E02-05-0311;
Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M.;
"A subset of chaperones and folding enzymes form multiprotein
complexes in endoplasmic reticulum to bind nascent proteins.";
Mol. Biol. Cell 13:4456-4469(2002).
[11]
GLYCOSYLATION AT ASN-155; ASN-515; ASN-596; ASN-830; ASN-862 AND
ASN-931.
PubMed=12754519; DOI=10.1038/nbt827;
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
"Identification and quantification of N-linked glycoproteins using
hydrazide chemistry, stable isotope labeling and mass spectrometry.";
Nat. Biotechnol. 21:660-666(2003).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515; ASN-830; ASN-869 AND
ASN-931.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515; ASN-596; ASN-830;
ASN-862 AND ASN-931.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[16]
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).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
CLEAVAGE OF SIGNAL PEPTIDE [LARGE SCALE ANALYSIS] AFTER THR-32, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Has a pivotal role in cytoprotective cellular mechanisms
triggered by oxygen deprivation. May play a role as a molecular
chaperone and participate in protein folding.
{ECO:0000269|PubMed:10037731}.
-!- SUBUNIT: Part of a large chaperone multiprotein complex comprising
DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PDIA6, PPIB, SDF2L1,
UGT1A1 and very small amounts of ERP29, but not, or at very low
levels, CALR nor CANX.
-!- INTERACTION:
P11021:HSPA5; NbExp=2; IntAct=EBI-1054186, EBI-354921;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y4L1-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y4L1-2; Sequence=VSP_056364, VSP_056365, VSP_056366;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in tissues that contain well-
developed endoplasmic reticulum and synthesize large amounts of
secretory proteins. Highly expressed in liver and pancreas and
lower expression in brain and kidney. Also expressed in
macrophages within aortic atherosclerotic plaques, and in breast
cancers.
-!- INDUCTION: By hypoxia and also by 2-deoxyglucose or tunicamycin.
-!- SIMILARITY: Belongs to the heat shock protein 70 family.
{ECO:0000305}.
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EMBL; U65785; AAC50947.1; -; mRNA.
EMBL; AB009979; BAF80348.1; -; Genomic_DNA.
EMBL; DQ350134; ABC75106.1; -; mRNA.
EMBL; DQ372932; ABD14370.1; -; mRNA.
EMBL; AK304264; BAH14145.1; -; mRNA.
EMBL; AK314178; BAG36860.1; -; mRNA.
EMBL; AK222756; BAD96476.1; -; mRNA.
EMBL; EF444986; ACA06002.1; -; Genomic_DNA.
EMBL; AP003392; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS8408.1; -. [Q9Y4L1-1]
PIR; JC5278; JC5278.
RefSeq; NP_001124463.1; NM_001130991.2. [Q9Y4L1-1]
RefSeq; NP_006380.1; NM_006389.4. [Q9Y4L1-1]
RefSeq; XP_016872585.1; XM_017017096.1. [Q9Y4L1-1]
RefSeq; XP_016872586.1; XM_017017097.1. [Q9Y4L1-1]
UniGene; Hs.277704; -.
ProteinModelPortal; Q9Y4L1; -.
SMR; Q9Y4L1; -.
BioGrid; 115780; 120.
IntAct; Q9Y4L1; 56.
MINT; Q9Y4L1; -.
STRING; 9606.ENSP00000384144; -.
ChEMBL; CHEMBL2216741; -.
TCDB; 3.A.16.1.4; the endoplasmic reticular retrotranslocon (er-rt) family.
CarbonylDB; Q9Y4L1; -.
GlyConnect; 1383; -.
iPTMnet; Q9Y4L1; -.
PhosphoSitePlus; Q9Y4L1; -.
SwissPalm; Q9Y4L1; -.
BioMuta; HYOU1; -.
DMDM; 10720185; -.
REPRODUCTION-2DPAGE; IPI00000877; -.
EPD; Q9Y4L1; -.
jPOST; Q9Y4L1; -.
PaxDb; Q9Y4L1; -.
PeptideAtlas; Q9Y4L1; -.
PRIDE; Q9Y4L1; -.
ProteomicsDB; 86227; -.
Ensembl; ENST00000617285; ENSP00000480150; ENSG00000149428. [Q9Y4L1-1]
Ensembl; ENST00000630669; ENSP00000486825; ENSG00000280682. [Q9Y4L1-1]
GeneID; 10525; -.
KEGG; hsa:10525; -.
UCSC; uc031yhc.2; human. [Q9Y4L1-1]
CTD; 10525; -.
DisGeNET; 10525; -.
EuPathDB; HostDB:ENSG00000149428.18; -.
GeneCards; HYOU1; -.
HGNC; HGNC:16931; HYOU1.
HPA; HPA049296; -.
MIM; 601746; gene.
neXtProt; NX_Q9Y4L1; -.
OpenTargets; ENSG00000149428; -.
PharmGKB; PA38427; -.
eggNOG; KOG0104; Eukaryota.
eggNOG; COG0443; LUCA.
GeneTree; ENSGT00940000157686; -.
HOGENOM; HOG000007865; -.
HOVERGEN; HBG106402; -.
InParanoid; Q9Y4L1; -.
KO; K09486; -.
OMA; YFNQAER; -.
OrthoDB; 708294at2759; -.
PhylomeDB; Q9Y4L1; -.
TreeFam; TF105048; -.
Reactome; R-HSA-3000484; Scavenging by Class F Receptors.
Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
SIGNOR; Q9Y4L1; -.
ChiTaRS; HYOU1; human.
GeneWiki; HYOU1; -.
GenomeRNAi; 10525; -.
PMAP-CutDB; Q9Y4L1; -.
PRO; PR:Q9Y4L1; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000149428; Expressed in 230 organ(s), highest expression level in islet of Langerhans.
ExpressionAtlas; Q9Y4L1; baseline and differential.
Genevisible; Q9Y4L1; HS.
GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
GO; GO:0034663; C:endoplasmic reticulum chaperone complex; IBA:GO_Central.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005790; C:smooth endoplasmic reticulum; ISS:ParkinsonsUK-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0051087; F:chaperone binding; ISS:ParkinsonsUK-UCL.
GO; GO:0071456; P:cellular response to hypoxia; IDA:ParkinsonsUK-UCL.
GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IDA:ParkinsonsUK-UCL.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
GO; GO:1903382; P:negative regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:1903298; P:negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IEP:ParkinsonsUK-UCL.
GO; GO:0002931; P:response to ischemia; ISS:ParkinsonsUK-UCL.
Gene3D; 1.20.1270.10; -; 1.
Gene3D; 2.60.34.10; -; 1.
InterPro; IPR018181; Heat_shock_70_CS.
InterPro; IPR029048; HSP70_C_sf.
InterPro; IPR029047; HSP70_peptide-bd_sf.
InterPro; IPR013126; Hsp_70_fam.
PANTHER; PTHR19375; PTHR19375; 1.
Pfam; PF00012; HSP70; 1.
PRINTS; PR00301; HEATSHOCK70.
SUPFAM; SSF100934; SSF100934; 1.
PROSITE; PS00329; HSP70_2; 1.
PROSITE; PS01036; HSP70_3; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; ATP-binding; Chaperone;
Complete proteome; Direct protein sequencing; Endoplasmic reticulum;
Glycoprotein; Nucleotide-binding; Phosphoprotein; Reference proteome;
Signal; Stress response.
SIGNAL 1 32 {ECO:0000244|PubMed:25944712}.
CHAIN 33 999 Hypoxia up-regulated protein 1.
/FTId=PRO_0000013538.
MOTIF 996 999 Prevents secretion from ER.
{ECO:0000255}.
COMPBIAS 603 606 Poly-Glu.
COMPBIAS 636 641 Poly-Pro.
MOD_RES 567 567 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 883 883 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9JKR6}.
CARBOHYD 155 155 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519}.
CARBOHYD 222 222 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 515 515 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 596 596 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218}.
CARBOHYD 830 830 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
CARBOHYD 862 862 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:19159218}.
CARBOHYD 869 869 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 922 922 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 931 931 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:12754519,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
VAR_SEQ 1 87 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056364.
VAR_SEQ 603 646 EEEESPAEGSKDEPGEQVELKEEAEAPVEDGSQPPPPEPKG
DAT -> MLFLCPARLPQSKQAIDRFHTAVTCMEPPWGRRC
RARPAWRLCS (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056365.
VAR_SEQ 647 999 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056366.
CONFLICT 75 75 K -> E (in Ref. 5; BAD96476).
{ECO:0000305}.
CONFLICT 92 92 N -> D (in Ref. 5; BAD96476).
{ECO:0000305}.
CONFLICT 255 255 M -> T (in Ref. 5; BAD96476).
{ECO:0000305}.
CONFLICT 442 442 V -> A (in Ref. 5; BAD96476).
{ECO:0000305}.
SEQUENCE 999 AA; 111335 MW; FCE0F292466AFAB9 CRC64;
MADKVRRQRP RRRVCWALVA VLLADLLALS DTLAVMSVDL GSESMKVAIV KPGVPMEIVL
NKESRRKTPV IVTLKENERF FGDSAASMAI KNPKATLRYF QHLLGKQADN PHVALYQARF
PEHELTFDPQ RQTVHFQISS QLQFSPEEVL GMVLNYSRSL AEDFAEQPIK DAVITVPVFF
NQAERRAVLQ AARMAGLKVL QLINDNTATA LSYGVFRRKD INTTAQNIMF YDMGSGSTVC
TIVTYQMVKT KEAGMQPQLQ IRGVGFDRTL GGLEMELRLR ERLAGLFNEQ RKGQRAKDVR
ENPRAMAKLL REANRLKTVL SANADHMAQI EGLMDDVDFK AKVTRVEFEE LCADLFERVP
GPVQQALQSA EMSLDEIEQV ILVGGATRVP RVQEVLLKAV GKEELGKNIN ADEAAAMGAV
YQAAALSKAF KVKPFVVRDA VVYPILVEFT REVEEEPGIH SLKHNKRVLF SRMGPYPQRK
VITFNRYSHD FNFHINYGDL GFLGPEDLRV FGSQNLTTVK LKGVGDSFKK YPDYESKGIK
AHFNLDESGV LSLDRVESVF ETLVEDSAEE ESTLTKLGNT ISSLFGGGTT PDAKENGTDT
VQEEEESPAE GSKDEPGEQV ELKEEAEAPV EDGSQPPPPE PKGDATPEGE KATEKENGDK
SEAQKPSEKA EAGPEGVAPA PEGEKKQKPA RKRRMVEEIG VELVVLDLPD LPEDKLAQSV
QKLQDLTLRD LEKQEREKAA NSLEAFIFET QDKLYQPEYQ EVSTEEQREE ISGKLSAAST
WLEDEGVGAT TVMLKEKLAE LRKLCQGLFF RVEERKKWPE RLSALDNLLN HSSMFLKGAR
LIPEMDQIFT EVEMTTLEKV INETWAWKNA TLAEQAKLPA TEKPVLLSKD IEAKMMALDR
EVQYLLNKAK FTKPRPRPKD KNGTRAEPPL NASASDQGEK VIPPAGQTED AEPISEPEKV
ETGSEPGDTE PLELGGPGAE PEQKEQSTGQ KRPLKNDEL


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EIAAB35726 Mouse,Mus musculus,Orp1,Oxygen-regulated protein 1,Retinitis pigmentosa RP1 protein homolog,Rp1,Rp1h
CSB-EL020073DO Dog Oxygen-regulated protein 1(RP1) ELISA kit 96T
EIAAB28223 Androgen-regulated protein RP2,D7Rp2e,Mouse,Mus musculus,Nucleoside diphosphate-linked moiety X motif 19, mitochondrial,Nudix motif 19,Nudt19,RP2p,Testosterone-regulated RP2 protein
EIAAB45422 Bos taurus,Bovine,HBV X protein up-regulated gene 4 protein homolog,HBxAg up-regulated gene 4 protein homolog,Up-regulator of cell proliferation,URG4,URGCP
EIAAB45421 HBV X protein up-regulated gene 4 protein homolog,HBxAg up-regulated gene 4 protein homolog,Mouse,Mus musculus,Up-regulator of cell proliferation,Urg4,Urgcp
CSB-EL020073BO Bovine Oxygen-regulated protein 1(RP1) ELISA kit 96T
CSB-EL020073DO Dog Oxygen-regulated protein 1(RP1) ELISA kit SpeciesDog 96T
CSB-EL020073HU Human Oxygen-regulated protein 1(RP1) ELISA kit 96T
CSB-EL020073MO Mouse Oxygen-regulated protein 1(RP1) ELISA kit 96T
EIAAB05237 Calmodulin-regulated spectrin-associated protein 1-like protein 1,Calmodulin-regulated spectrin-associated protein 2,CAMSAP1L1,CAMSAP2,Homo sapiens,Human,KIAA1078
CSB-EL020073BO Bovine Oxygen-regulated protein 1(RP1) ELISA kit SpeciesBovine 96T
CSB-EL020073MO Mouse Oxygen-regulated protein 1(RP1) ELISA kit SpeciesMouse 96T
CSB-EL020073HU Human Oxygen-regulated protein 1(RP1) ELISA kit SpeciesHuman 96T
HSPA5-332H Protein Recombinant Human Heat Shock 70kDa Protein 5 (Glucose-regulated Protein, 78kDa), His-tagged 20ug
HSPA5-332H Protein: Recombinant Human Heat Shock 70kDa Protein 5 (Glucose-regulated Protein, 78kDa), His-tagged 20ug
EIAAB05236 Calmodulin-regulated spectrin-associated protein 1-like protein 1,Calmodulin-regulated spectrin-associated protein 2,Camsap1l1,Camsap2,Kiaa1078,Mouse,Mus musculus
bs-11030R Rabbit Anti-Oxygen-regulated protein 1 Polyclonal Antibody 100ul
RP1_MOUSE ELISA Kit FOR Oxygen-regulated protein 1; organism: Mouse; gene name: Rp1 96T
HYOU1_HUMAN Human ELISA Kit FOR Hypoxia up-regulated protein 1 96T

Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1049: G Protein Signaling Pathways
WP1059: Diurnally regulated genes with circadian orthologs
WP1165: G Protein Signaling Pathways
WP1175: Diurnally regulated genes with circadian orthologs
WP1268: Diurnally regulated genes with circadian orthologs
WP1306: Diurnally regulated genes with circadian orthologs
WP1371: G Protein Signaling Pathways
WP1379: Diurnally regulated genes with circadian orthologs
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
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

Related Genes :
[HYOU1 GRP170 ORP150] Hypoxia up-regulated protein 1 (150 kDa oxygen-regulated protein) (ORP-150) (170 kDa glucose-regulated protein) (GRP-170)
[Hyou1 Orp150] Hypoxia up-regulated protein 1 (150 kDa oxygen-regulated protein) (ORP-150)
[Hyou1 Grp170] Hypoxia up-regulated protein 1 (GRP-170) (140 kDa Ca(2+)-binding protein) (CBP-140)
[Hsp90b1 Grp94 Tra-1 Tra1] Endoplasmin (94 kDa glucose-regulated protein) (GRP-94) (Endoplasmic reticulum resident protein 99) (ERp99) (Heat shock protein 90 kDa beta member 1) (Polymorphic tumor rejection antigen 1) (Tumor rejection antigen gp96)
[MED14 ARC150 CRSP2 CXorf4 DRIP150 EXLM1 RGR1 TRAP170] Mediator of RNA polymerase II transcription subunit 14 (Activator-recruited cofactor 150 kDa component) (ARC150) (Cofactor required for Sp1 transcriptional activation subunit 2) (CRSP complex subunit 2) (Mediator complex subunit 14) (RGR1 homolog) (hRGR1) (Thyroid hormone receptor-associated protein complex 170 kDa component) (Trap170) (Transcriptional coactivator CRSP150) (Vitamin D3 receptor-interacting protein complex 150 kDa component) (DRIP150)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[HSP90B1 GRP94 TRA1] Endoplasmin (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1) (Tumor rejection antigen 1) (gp96 homolog)
[Hspa5 Grp78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein) (Steroidogenesis-activator polypeptide)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[HYOU1 GRP170 ORP150] Hypoxia up-regulated protein 1 (150 kDa oxygen-regulated protein) (ORP-150) (170 kDa glucose-regulated protein) (GRP-170)
[Hspa5 Grp78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[HSP90B1 GRP94 TRA1] Endoplasmin (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[DCTN1] Dynactin subunit 1 (150 kDa dynein-associated polypeptide) (DAP-150) (DP-150) (p135) (p150-glued)
[PDIA3 ERP57 ERP60 GRP58] Protein disulfide-isomerase A3 (EC 5.3.4.1) (58 kDa glucose-regulated protein) (58 kDa microsomal protein) (p58) (Disulfide isomerase ER-60) (Endoplasmic reticulum resident protein 57) (ER protein 57) (ERp57) (Endoplasmic reticulum resident protein 60) (ER protein 60) (ERp60)
[HSPB1 HSP27 HSP28] Heat shock protein beta-1 (HspB1) (28 kDa heat shock protein) (Estrogen-regulated 24 kDa protein) (Heat shock 27 kDa protein) (HSP 27) (Stress-responsive protein 27) (SRP27)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[Hspa9 Grp75 Hsp74 Hspa9a] Stress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9) (Mortalin) (Peptide-binding protein 74) (PBP74) (p66 MOT)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein) (Fragment)
[HSP150 CCW7 ORE1 PIR2 YJL159W J0558] Cell wall mannoprotein HSP150 (150 kDa heat shock glycoprotein) (Covalently-linked cell wall protein 7) (Protein with internal repeats 2)
[Hspa9 Grp75 Hspa9a] Stress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9) (Mortalin) (Peptide-binding protein 74) (PBP74) (mtHSP70)
[HSPA5 GRP78 I79_019946] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[Dctn1] Dynactin subunit 1 (150 kDa dynein-associated polypeptide) (DAP-150) (DP-150) (p150-glued)
[HSP90B1 GRP94 TRA1] Endoplasmin (94 kDa glucose-regulated protein) (GRP-94) (Heat shock protein 90 kDa beta member 1)
[Dctn1] Dynactin subunit 1 (150 kDa dynein-associated polypeptide) (DAP-150) (DP-150) (p150-glued)
[HSPA9 GRP75 HSPA9B mt-HSP70] Stress-70 protein, mitochondrial (75 kDa glucose-regulated protein) (GRP-75) (Heat shock 70 kDa protein 9) (Mortalin) (MOT) (Peptide-binding protein 74) (PBP74)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[HSPA5 GRP78] Endoplasmic reticulum chaperone BiP (EC 3.6.4.10) (78 kDa glucose-regulated protein) (GRP-78) (Binding-immunoglobulin protein) (BiP) (Heat shock protein 70 family protein 5) (HSP70 family protein 5) (Heat shock protein family A member 5) (Immunoglobulin heavy chain-binding protein)
[Inpp5d 7a33 Ship Ship1] Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1 (EC 3.1.3.86) (Inositol polyphosphate-5-phosphatase of 145 kDa) (SIP-145) (SH2 domain-containing inositol 5'-phosphatase 1) (SH2 domain-containing inositol phosphatase 1) (SHIP-1) (p150Ship)
[PRA1 FBP1 CAALFM_C406980WA CaO19.10623 CaO19.3111] pH-regulated antigen PRA1 (58 kDa fibrinogen-binding mannoprotein)

Bibliography :
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