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Q9Y4L1

- HYOU1_HUMAN

UniProt

Q9Y4L1 - HYOU1_HUMAN

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Protein
Hypoxia up-regulated protein 1
Gene
HYOU1, GRP170, ORP150
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. cellular protein metabolic process Source: Reactome
  3. endoplasmic reticulum unfolded protein response Source: Reactome
  4. response to ischemia Source: Ensembl
  5. response to stress Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_163813. Scavenging by Class F Receptors.
REACT_18273. XBP1(S) activates chaperone genes.

Names & Taxonomyi

Protein namesi
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 namesi
Name:HYOU1
Synonyms:GRP170, ORP150
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:16931. HYOU1.

Subcellular locationi

GO - Cellular componenti

  1. endocytic vesicle lumen Source: Reactome
  2. endoplasmic reticulum Source: ProtInc
  3. endoplasmic reticulum lumen Source: Reactome
  4. extracellular region Source: Reactome
  5. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38427.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232 By similarity
Add
BLAST
Chaini33 – 999967Hypoxia up-regulated protein 1
PRO_0000013538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi155 – 1551N-linked (GlcNAc...)1 Publication
Glycosylationi222 – 2221N-linked (GlcNAc...) Reviewed prediction
Glycosylationi515 – 5151N-linked (GlcNAc...)5 Publications
Glycosylationi596 – 5961N-linked (GlcNAc...)2 Publications
Glycosylationi830 – 8301N-linked (GlcNAc...)3 Publications
Glycosylationi862 – 8621N-linked (GlcNAc...)2 Publications
Glycosylationi869 – 8691N-linked (GlcNAc...)1 Publication
Modified residuei883 – 8831N6-acetyllysine By similarity
Glycosylationi922 – 9221N-linked (GlcNAc...) Reviewed prediction
Glycosylationi931 – 9311N-linked (GlcNAc...)3 Publications

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQBiQ9Y4L1.
PaxDbiQ9Y4L1.
PeptideAtlasiQ9Y4L1.
PRIDEiQ9Y4L1.

2D gel databases

REPRODUCTION-2DPAGEIPI00000877.

PTM databases

PhosphoSiteiQ9Y4L1.

Miscellaneous databases

PMAP-CutDBQ9Y4L1.

Expressioni

Tissue specificityi

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.

Inductioni

By hypoxia and also by 2-deoxyglucose or tunicamycin.

Gene expression databases

ArrayExpressiQ9Y4L1.
BgeeiQ9Y4L1.
CleanExiHS_HYOU1.
GenevestigatoriQ9Y4L1.

Organism-specific databases

HPAiHPA049296.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi115780. 28 interactions.
IntActiQ9Y4L1. 8 interactions.
MINTiMINT-4105974.
STRINGi9606.ENSP00000278752.

Structurei

3D structure databases

ProteinModelPortaliQ9Y4L1.
SMRiQ9Y4L1. Positions 35-613, 711-817.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi996 – 9994Prevents secretion from ER Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi603 – 6064Poly-Glu
Compositional biasi636 – 6416Poly-Pro

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0443.
HOGENOMiHOG000007865.
HOVERGENiHBG106402.
InParanoidiQ9Y4L1.
KOiK09486.
OMAiDTKENGT.
PhylomeDBiQ9Y4L1.
TreeFamiTF105048.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100934. SSF100934. 1 hit.
PROSITEiPS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Y4L1-1 [UniParc]FASTAAdd to Basket

« Hide

MADKVRRQRP RRRVCWALVA VLLADLLALS DTLAVMSVDL GSESMKVAIV    50
KPGVPMEIVL NKESRRKTPV IVTLKENERF FGDSAASMAI KNPKATLRYF 100
QHLLGKQADN PHVALYQARF PEHELTFDPQ RQTVHFQISS QLQFSPEEVL 150
GMVLNYSRSL AEDFAEQPIK DAVITVPVFF NQAERRAVLQ AARMAGLKVL 200
QLINDNTATA LSYGVFRRKD INTTAQNIMF YDMGSGSTVC TIVTYQMVKT 250
KEAGMQPQLQ IRGVGFDRTL GGLEMELRLR ERLAGLFNEQ RKGQRAKDVR 300
ENPRAMAKLL REANRLKTVL SANADHMAQI EGLMDDVDFK AKVTRVEFEE 350
LCADLFERVP GPVQQALQSA EMSLDEIEQV ILVGGATRVP RVQEVLLKAV 400
GKEELGKNIN ADEAAAMGAV YQAAALSKAF KVKPFVVRDA VVYPILVEFT 450
REVEEEPGIH SLKHNKRVLF SRMGPYPQRK VITFNRYSHD FNFHINYGDL 500
GFLGPEDLRV FGSQNLTTVK LKGVGDSFKK YPDYESKGIK AHFNLDESGV 550
LSLDRVESVF ETLVEDSAEE ESTLTKLGNT ISSLFGGGTT PDAKENGTDT 600
VQEEEESPAE GSKDEPGEQV ELKEEAEAPV EDGSQPPPPE PKGDATPEGE 650
KATEKENGDK SEAQKPSEKA EAGPEGVAPA PEGEKKQKPA RKRRMVEEIG 700
VELVVLDLPD LPEDKLAQSV QKLQDLTLRD LEKQEREKAA NSLEAFIFET 750
QDKLYQPEYQ EVSTEEQREE ISGKLSAAST WLEDEGVGAT TVMLKEKLAE 800
LRKLCQGLFF RVEERKKWPE RLSALDNLLN HSSMFLKGAR LIPEMDQIFT 850
EVEMTTLEKV INETWAWKNA TLAEQAKLPA TEKPVLLSKD IEAKMMALDR 900
EVQYLLNKAK FTKPRPRPKD KNGTRAEPPL NASASDQGEK VIPPAGQTED 950
AEPISEPEKV ETGSEPGDTE PLELGGPGAE PEQKEQSTGQ KRPLKNDEL 999
Length:999
Mass (Da):111,335
Last modified:November 1, 1999 - v1
Checksum:iFCE0F292466AFAB9
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751K → E in BAD96476. 1 Publication
Sequence conflicti92 – 921N → D in BAD96476. 1 Publication
Sequence conflicti255 – 2551M → T in BAD96476. 1 Publication
Sequence conflicti442 – 4421V → A in BAD96476. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS8408.1.
PIRiJC5278.
RefSeqiNP_001124463.1. NM_001130991.2.
NP_006380.1. NM_006389.4.
UniGeneiHs.277704.

Genome annotation databases

EnsembliENST00000404233; ENSP00000384144; ENSG00000149428.
ENST00000571646; ENSP00000458419; ENSG00000262812.
GeneIDi10525.
KEGGihsa:10525.
UCSCiuc001put.2. human.

Polymorphism databases

DMDMi10720185.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS8408.1.
PIRi JC5278.
RefSeqi NP_001124463.1. NM_001130991.2.
NP_006380.1. NM_006389.4.
UniGenei Hs.277704.

3D structure databases

ProteinModelPortali Q9Y4L1.
SMRi Q9Y4L1. Positions 35-613, 711-817.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115780. 28 interactions.
IntActi Q9Y4L1. 8 interactions.
MINTi MINT-4105974.
STRINGi 9606.ENSP00000278752.

Chemistry

ChEMBLi CHEMBL2216741.

PTM databases

PhosphoSitei Q9Y4L1.

Polymorphism databases

DMDMi 10720185.

2D gel databases

REPRODUCTION-2DPAGE IPI00000877.

Proteomic databases

MaxQBi Q9Y4L1.
PaxDbi Q9Y4L1.
PeptideAtlasi Q9Y4L1.
PRIDEi Q9Y4L1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000404233 ; ENSP00000384144 ; ENSG00000149428 .
ENST00000571646 ; ENSP00000458419 ; ENSG00000262812 .
GeneIDi 10525.
KEGGi hsa:10525.
UCSCi uc001put.2. human.

Organism-specific databases

CTDi 10525.
GeneCardsi GC11M118914.
HGNCi HGNC:16931. HYOU1.
HPAi HPA049296.
MIMi 601746. gene.
neXtProti NX_Q9Y4L1.
PharmGKBi PA38427.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0443.
HOGENOMi HOG000007865.
HOVERGENi HBG106402.
InParanoidi Q9Y4L1.
KOi K09486.
OMAi DTKENGT.
PhylomeDBi Q9Y4L1.
TreeFami TF105048.

Enzyme and pathway databases

Reactomei REACT_163813. Scavenging by Class F Receptors.
REACT_18273. XBP1(S) activates chaperone genes.

Miscellaneous databases

ChiTaRSi HYOU1. human.
GeneWikii HYOU1.
GenomeRNAii 10525.
NextBioi 39930.
PMAP-CutDB Q9Y4L1.
PROi Q9Y4L1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y4L1.
Bgeei Q9Y4L1.
CleanExi HS_HYOU1.
Genevestigatori Q9Y4L1.

Family and domain databases

Gene3Di 1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProi IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view ]
Pfami PF00012. HSP70. 1 hit.
[Graphical view ]
PRINTSi PR00301. HEATSHOCK70.
SUPFAMi SSF100934. SSF100934. 1 hit.
PROSITEi PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiHYOU1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y4L1
Secondary accession number(s): A8C1Z0, Q2I204, Q53H25
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: September 3, 2014
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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