Q9Y4L1 (HYOU1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hypoxia up-regulated protein 1

Alternative name(s):
150 kDa oxygen-regulated protein
Short name=ORP-150
170 kDa glucose-regulated protein
Short name=GRP-170

Gene names

Name:	HYOU1
Synonyms:	GRP170, ORP150

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	999 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.5
Subunit structure	Part 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.
Subcellular location	Endoplasmic reticulum lumen.
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.
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Biological process	Stress response
Cellular component	Endoplasmic reticulum
Domain	Signal
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Cellular component	endoplasmic reticulum lumen Traceable author statement. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 32	32	By similarity
	Chain	33 – 999	967	Hypoxia up-regulated protein 1		PRO_0000013538
Regions
	Motif	996 – 999	4	Prevents secretion from ER Potential
	Compositional bias	603 – 606	4	Poly-Glu
	Compositional bias	636 – 641	6	Poly-Pro
Amino acid modifications
	Glycosylation	155	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	222	1	N-linked (GlcNAc...) Potential
	Glycosylation	515	1	N-linked (GlcNAc...) Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
	Glycosylation	596	1	N-linked (GlcNAc...) Ref.7 Ref.10
	Glycosylation	830	1	N-linked (GlcNAc...) Ref.7 Ref.8 Ref.10
	Glycosylation	862	1	N-linked (GlcNAc...) Ref.7 Ref.10
	Glycosylation	869	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	922	1	N-linked (GlcNAc...) Potential
	Glycosylation	931	1	N-linked (GlcNAc...) Ref.7 Ref.8 Ref.10
Experimental info
	Sequence conflict	75	1	K → E in BAD96476. Ref.3
	Sequence conflict	92	1	N → D in BAD96476. Ref.3
	Sequence conflict	255	1	M → T in BAD96476. Ref.3
	Sequence conflict	442	1	V → A in BAD96476. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9Y4L1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: FCE0F292466AFAB9	FASTA	999	111,335
	10 20 30 40 50 60 MADKVRRQRP RRRVCWALVA VLLADLLALS DTLAVMSVDL GSESMKVAIV KPGVPMEIVL 70 80 90 100 110 120 NKESRRKTPV IVTLKENERF FGDSAASMAI KNPKATLRYF QHLLGKQADN PHVALYQARF 130 140 150 160 170 180 PEHELTFDPQ RQTVHFQISS QLQFSPEEVL GMVLNYSRSL AEDFAEQPIK DAVITVPVFF 190 200 210 220 230 240 NQAERRAVLQ AARMAGLKVL QLINDNTATA LSYGVFRRKD INTTAQNIMF YDMGSGSTVC 250 260 270 280 290 300 TIVTYQMVKT KEAGMQPQLQ IRGVGFDRTL GGLEMELRLR ERLAGLFNEQ RKGQRAKDVR 310 320 330 340 350 360 ENPRAMAKLL REANRLKTVL SANADHMAQI EGLMDDVDFK AKVTRVEFEE LCADLFERVP 370 380 390 400 410 420 GPVQQALQSA EMSLDEIEQV ILVGGATRVP RVQEVLLKAV GKEELGKNIN ADEAAAMGAV 430 440 450 460 470 480 YQAAALSKAF KVKPFVVRDA VVYPILVEFT REVEEEPGIH SLKHNKRVLF SRMGPYPQRK 490 500 510 520 530 540 VITFNRYSHD FNFHINYGDL GFLGPEDLRV FGSQNLTTVK LKGVGDSFKK YPDYESKGIK 550 560 570 580 590 600 AHFNLDESGV LSLDRVESVF ETLVEDSAEE ESTLTKLGNT ISSLFGGGTT PDAKENGTDT 610 620 630 640 650 660 VQEEEESPAE GSKDEPGEQV ELKEEAEAPV EDGSQPPPPE PKGDATPEGE KATEKENGDK 670 680 690 700 710 720 SEAQKPSEKA EAGPEGVAPA PEGEKKQKPA RKRRMVEEIG VELVVLDLPD LPEDKLAQSV 730 740 750 760 770 780 QKLQDLTLRD LEKQEREKAA NSLEAFIFET QDKLYQPEYQ EVSTEEQREE ISGKLSAAST 790 800 810 820 830 840 WLEDEGVGAT TVMLKEKLAE LRKLCQGLFF RVEERKKWPE RLSALDNLLN HSSMFLKGAR 850 860 870 880 890 900 LIPEMDQIFT EVEMTTLEKV INETWAWKNA TLAEQAKLPA TEKPVLLSKD IEAKMMALDR 910 920 930 940 950 960 EVQYLLNKAK FTKPRPRPKD KNGTRAEPPL NASASDQGEK VIPPAGQTED AEPISEPEKV 970 980 990 ETGSEPGDTE PLELGGPGAE PEQKEQSTGQ KRPLKNDEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of cDNA encoding the human 150 kDa oxygen-regulated protein, ORP150." Ikeda J., Kaneda S., Kuwabara K., Ogawa S., Kobayashi T., Matsumoto M., Yura T., Yanagi H. Biochem. Biophys. Res. Commun. 230:94-99(1997) [PubMed: 9020069] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Astrocytoma.
[2]	"Molecular cloning, sequence, function and structural basis of human heart 150 kDa oxygen-regulated protein, an ER chaperone." Takeuchi S. Protein J. 25:517-528(2006) [PubMed: 17131193] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[3]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[4]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 241-256; 541-555; 577-594 AND 754-768, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[5]	"150-kDa oxygen-regulated protein (ORP150) suppresses hypoxia-induced apoptotic cell death." 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. J. Biol. Chem. 274:6397-6404(1999) [PubMed: 10037731] [Abstract] Cited for: FUNCTION.
[6]	"A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins." Meunier L., Usherwood Y.-K., Chung K.T., Hendershot L.M. Mol. Biol. Cell 13:4456-4469(2002) [PubMed: 12475965] [Abstract] Cited for: COMPONENT OF A CHAPERONE COMPLEX.
[7]	"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry." Zhang H., Li X.-J., Martin D.B., Aebersold R. Nat. Biotechnol. 21:660-666(2003) [PubMed: 12754519] [Abstract] Cited for: GLYCOSYLATION AT ASN-155; ASN-515; ASN-596; ASN-830; ASN-862 AND ASN-931.
[8]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515; ASN-830; ASN-869 AND ASN-931, MASS SPECTROMETRY. Tissue: Plasma.
[9]	"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach." Lewandrowski U., Moebius J., Walter U., Sickmann A. Mol. Cell. Proteomics 5:226-233(2006) [PubMed: 16263699] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515, MASS SPECTROMETRY. Tissue: Platelet.
[10]	"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry." Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H. J. Proteome Res. 8:651-661(2009) [PubMed: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515; ASN-596; ASN-830; ASN-862 AND ASN-931, MASS SPECTROMETRY. Tissue: Liver.
[11]	"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins." Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D. Nat. Biotechnol. 27:378-386(2009) [PubMed: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U65785 mRNA. Translation: AAC50947.1. DQ350134 mRNA. Translation: ABC75106.1. DQ372932 mRNA. Translation: ABD14370.1. AK222756 mRNA. Translation: BAD96476.1.
IPI	IPI00000877.
PIR	JC5278.
RefSeq	NP_001124463.1. NM_001130991.1. NP_006380.1. NM_006389.3.
UniGene	Hs.277704.
3D structure databases
ProteinModelPortal	Q9Y4L1.
SMR	Q9Y4L1. Positions 32-811.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y4L1. 4 interactions.
STRING	Q9Y4L1.
PTM databases
PhosphoSite	Q9Y4L1.
Polymorphism databases
DMDM	10720185.
2D gel databases
REPRODUCTION-2DPAGE	IPI00000877.
Proteomic databases
PeptideAtlas	Q9Y4L1.
PRIDE	Q9Y4L1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000353883; ENSP00000278752; ENSG00000149428. ENST00000404233; ENSP00000384144; ENSG00000149428.
GeneID	10525.
KEGG	hsa:10525.
UCSC	uc001puu.2. human.
Organism-specific databases
CTD	10525.
GeneCards	GC11M118948.
H-InvDB	HIX0201658.
HGNC	HGNC:16931. HYOU1.
MIM	601746. gene.
neXtProt	NX_Q9Y4L1.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00390000016919.
HOGENOM	HBG379834.
HOVERGEN	HBG106402.
InParanoid	Q9Y4L1.
OMA	FKVKPFV.
OrthoDB	EOG4R5021.
PhylomeDB	Q9Y4L1.
Enzyme and pathway databases
Reactome	REACT_15380. Diabetes pathways.
Gene expression databases
ArrayExpress	Q9Y4L1.
Bgee	Q9Y4L1.
CleanEx	HS_HYOU1.
Genevestigator	Q9Y4L1.
GermOnline	ENSG00000149428. Homo sapiens.
Family and domain databases
InterPro	IPR018181. Heat_shock_70_CS. IPR001023. Hsp70. IPR013126. Hsp_70. [Graphical view]
KO	K09486.
PANTHER	PTHR19375. Hsp70. 1 hit.
Pfam	PF00012. HSP70. 1 hit. [Graphical view]
PRINTS	PR00301. HEATSHOCK70.
PROSITE	PS00297. HSP70_1. False negative. PS00329. HSP70_2. 1 hit. PS01036. HSP70_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	39930.
PMAP-CutDB	Q9Y4L1.
SOURCE	Search...

Entry information

Entry name

HYOU1_HUMAN

Accession

Primary (citable) accession number: Q9Y4L1
Secondary accession number(s): Q2I204, Q53H25

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1999
Last modified:	January 25, 2012
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.