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Q9Y4L1 (HYOU1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length999 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.8

Subunit structure

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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 By similarity
Chain33 – 999967Hypoxia up-regulated protein 1
PRO_0000013538

Regions

Motif996 – 9994Prevents secretion from ER Potential
Compositional bias603 – 6064Poly-Glu
Compositional bias636 – 6416Poly-Pro

Amino acid modifications

Modified residue8831N6-acetyllysine By similarity
Glycosylation1551N-linked (GlcNAc...) Ref.10
Glycosylation2221N-linked (GlcNAc...) Potential
Glycosylation5151N-linked (GlcNAc...) Ref.10 Ref.11 Ref.12 Ref.13 Ref.14
Glycosylation5961N-linked (GlcNAc...) Ref.10 Ref.13
Glycosylation8301N-linked (GlcNAc...) Ref.10 Ref.11 Ref.13
Glycosylation8621N-linked (GlcNAc...) Ref.10 Ref.13
Glycosylation8691N-linked (GlcNAc...) Ref.11
Glycosylation9221N-linked (GlcNAc...) Potential
Glycosylation9311N-linked (GlcNAc...) Ref.10 Ref.11 Ref.13

Experimental info

Sequence conflict751K → E in BAD96476. Ref.5
Sequence conflict921N → D in BAD96476. Ref.5
Sequence conflict2551M → T in BAD96476. Ref.5
Sequence conflict4421V → A in BAD96476. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9Y4L1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: FCE0F292466AFAB9

FASTA999111,335
        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 

« Hide

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Astrocytoma.
[2]"Production of three distinct mRNAs of 150 kDa oxygen-regulated protein (ORP150) by alternative promoters: preferential induction of one species under stress conditions."
Kaneda S., Yura T., Yanagi H.
J. Biochem. 128:529-538(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Cerebellum.
[5]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.
[6]NHLBI resequencing and genotyping service (RS&G)
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[8]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"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] [Europe PMC] [Abstract]
Cited for: COMPONENT OF A CHAPERONE COMPLEX.
[10]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-155; ASN-515; ASN-596; ASN-830; ASN-862 AND ASN-931.
[11]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515; ASN-830; ASN-869 AND ASN-931.
Tissue: Plasma.
[12]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515.
Tissue: Platelet.
[13]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515; ASN-596; ASN-830; ASN-862 AND ASN-931.
Tissue: Liver.
[14]"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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-515.
Tissue: Leukemic T-cell.
[15]"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] [Europe PMC] [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.
AB009979 Genomic DNA. Translation: BAF80348.1.
DQ350134 mRNA. Translation: ABC75106.1.
DQ372932 mRNA. Translation: ABD14370.1.
AK314178 mRNA. Translation: BAG36860.1.
AK222756 mRNA. Translation: BAD96476.1.
EF444986 Genomic DNA. Translation: ACA06002.1.
CCDSCCDS8408.1.
PIRJC5278.
RefSeqNP_001124463.1. NM_001130991.2.
NP_006380.1. NM_006389.4.
UniGeneHs.277704.

3D structure databases

ProteinModelPortalQ9Y4L1.
SMRQ9Y4L1. Positions 35-613, 711-817.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115780. 27 interactions.
IntActQ9Y4L1. 8 interactions.
MINTMINT-4105974.
STRING9606.ENSP00000278752.

Chemistry

ChEMBLCHEMBL2216741.

PTM databases

PhosphoSiteQ9Y4L1.

Polymorphism databases

DMDM10720185.

2D gel databases

REPRODUCTION-2DPAGEIPI00000877.

Proteomic databases

MaxQBQ9Y4L1.
PaxDbQ9Y4L1.
PeptideAtlasQ9Y4L1.
PRIDEQ9Y4L1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000404233; ENSP00000384144; ENSG00000149428.
ENST00000571646; ENSP00000458419; ENSG00000262812.
GeneID10525.
KEGGhsa:10525.
UCSCuc001put.2. human.

Organism-specific databases

CTD10525.
GeneCardsGC11M118914.
HGNCHGNC:16931. HYOU1.
HPAHPA049296.
MIM601746. gene.
neXtProtNX_Q9Y4L1.
PharmGKBPA38427.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0443.
HOGENOMHOG000007865.
HOVERGENHBG106402.
InParanoidQ9Y4L1.
KOK09486.
OMADTKENGT.
PhylomeDBQ9Y4L1.
TreeFamTF105048.

Enzyme and pathway databases

ReactomeREACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.
REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ9Y4L1.
BgeeQ9Y4L1.
CleanExHS_HYOU1.
GenevestigatorQ9Y4L1.

Family and domain databases

Gene3D1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
SUPFAMSSF100934. SSF100934. 1 hit.
PROSITEPS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHYOU1. human.
GeneWikiHYOU1.
GenomeRNAi10525.
NextBio39930.
PMAP-CutDBQ9Y4L1.
PROQ9Y4L1.
SOURCESearch...

Entry information

Entry nameHYOU1_HUMAN
AccessionPrimary (citable) accession number: Q9Y4L1
Secondary accession number(s): A8C1Z0, Q2I204, Q53H25
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM