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Protein

Hypoxia up-regulated protein 1

Gene

Hyou1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • cellular response to hypoxia Source: MGI
  • negative regulation of apoptotic process Source: ParkinsonsUK-UCL
  • negative regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
  • negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway Source: MGI
  • response to ischemia Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_280759. Scavenging by Class F Receptors.

Names & Taxonomyi

Protein namesi
Recommended name:
Hypoxia up-regulated protein 1
Short name:
GRP-170
Alternative name(s):
140 kDa Ca(2+)-binding protein
Short name:
CBP-140
Gene namesi
Name:Hyou1
Synonyms:Grp170
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:108030. Hyou1.

Subcellular locationi

  • Endoplasmic reticulum lumen 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232By similarityAdd
BLAST
Chaini33 – 999967Hypoxia up-regulated protein 1PRO_5000057827Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi155 – 1551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi222 – 2221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi515 – 5151N-linked (GlcNAc...)1 Publication
Modified residuei567 – 5671PhosphoserineBy similarity
Glycosylationi596 – 5961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi830 – 8301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi862 – 8621N-linked (GlcNAc...)Sequence Analysis
Glycosylationi869 – 8691N-linked (GlcNAc...)Sequence Analysis
Modified residuei883 – 8831N6-acetyllysine1 Publication
Glycosylationi922 – 9221N-linked (GlcNAc...)Sequence Analysis
Glycosylationi931 – 9311N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9JKR6.
PaxDbiQ9JKR6.
PRIDEiQ9JKR6.

2D gel databases

REPRODUCTION-2DPAGEIPI00123342.
Q3TZD0.
Q64139.
Q9JKR6.

PTM databases

PhosphoSiteiQ9JKR6.

Expressioni

Gene expression databases

BgeeiQ9JKR6.
CleanExiMM_HYOU1.
ExpressionAtlasiQ9JKR6. baseline and differential.
GenevestigatoriQ9JKR6.

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

BioGridi198427. 8 interactions.
IntActiQ9JKR6. 6 interactions.
MINTiMINT-4130117.
STRINGi10090.ENSMUSP00000068594.

Structurei

3D structure databases

ProteinModelPortaliQ9JKR6.
SMRiQ9JKR6. Positions 35-613.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi996 – 9994Prevents secretion from ERSequence Analysis

Compositional bias

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

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG0443.
GeneTreeiENSGT00390000016919.
HOGENOMiHOG000007865.
HOVERGENiHBG106402.
InParanoidiQ9JKR6.
KOiK09486.
OMAiDTKENGT.
OrthoDBiEOG72RMXD.
PhylomeDBiQ9JKR6.
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. 2 hits.
[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.

Q9JKR6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATVRRQRP RRLLCWALVA VLLADLLALS DTLAVMSVDL GSESMKVAIV
60 70 80 90 100
KPGVPMEIVL NKESRRKTPV TVTLKENERF LGDSAAGMAI KNPKATLRYF
110 120 130 140 150
QHLLGKQADN PHVALYRSRF PEHELIVDPQ RQTVRFQISP QLQFSPEEVL
160 170 180 190 200
GMVLNYSRSL AEDFAEQPIK DAVITVPAFF NQAERRAVLQ AARMAGLKVL
210 220 230 240 250
QLINDNTATA LSYGVFRRKD INSTAQNVMF YDMGSGSTVC TIVTYQTVKT
260 270 280 290 300
KEAGMQPQLQ IRGVGFDRTL GGLEMELRLR EHLAKLFNEQ RKGQKAKDVR
310 320 330 340 350
ENPRAMAKLL REANRLKTVL SANADHMAQI EGLMDDVDFK AKVTRVEFEE
360 370 380 390 400
LCADLFDRVP GPVQQALQSA EMSLDQIEQV ILVGGATRVP KVQEVLLKAV
410 420 430 440 450
GKEELGKNIN ADEAAAMGAV YQAAALSKAF KVKPFVVRDA VIYPILVEFT
460 470 480 490 500
REVEEEPGLR SLKHNKRVLF SRMGPYPQRK VITFNRYSHD FNFHINYGDL
510 520 530 540 550
GFLGPEDLRV FGSQNLTTVK LKGVGESFKK YPDYESKGIK AHFNLDESGV
560 570 580 590 600
LSLDRVESVF ETLVEDSPEE ESTLTKLGNT ISSLFGGGTS SDAKENGTDA
610 620 630 640 650
VQEEEESPAE GSKDEPAEQG ELKEEAEPPA EETSQPPPSE PKGDAAREGE
660 670 680 690 700
KPDEKESGDK PEAQKPNEKG QAGPEGAAPA PEEDKKPKPA RKQKMVEEIG
710 720 730 740 750
VELAVLDLPD LPEDELARSV QKLEELTLRD LEKQEREKAA NSLEAFIFET
760 770 780 790 800
QDKLYQPEYQ EVSTEEQREE ISGKLSATST WLEDEGFGAT TVMLKDKLAE
810 820 830 840 850
LRKLCQGLFF RVEERRKWPE RLSALDNLLN HSSIFLKGAR LIPEMDQVFT
860 870 880 890 900
EVEMTTLEKV INDTWAWKNA TLAEQAKLPA TEKPVLLSKD IEAKMMALDR
910 920 930 940 950
EVQYLLNKAK FTKPRPRPKD KNGTRAEPPL NASAGDQEEK VIPPAGQTEE
960 970 980 990
AKPILEPDKE ETGTEPADSE PLELGGPGAG PEQEEQSAGQ KRPSKNDEL
Length:999
Mass (Da):111,181
Last modified:October 1, 2000 - v1
Checksum:i2951482D1EE2EF36
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1371Q → L in AAH50107 (PubMed:15489334).Curated
Sequence conflicti227 – 2271N → D in AAH50107 (PubMed:15489334).Curated
Sequence conflicti247 – 2471T → A in BAE34279 (PubMed:16141072).Curated
Sequence conflicti290 – 2901Q → R in BAE42657 (PubMed:16141072).Curated
Sequence conflicti467 – 4671R → G in AAB35051 (PubMed:7641295).Curated
Sequence conflicti540 – 5401K → R in AAH50107 (PubMed:15489334).Curated
Sequence conflicti615 – 6151E → K in AAH50107 (PubMed:15489334).Curated
Sequence conflicti665 – 6651Missing in AAB35051 (PubMed:7641295).Curated
Sequence conflicti687 – 6871P → L in AAB35051 (PubMed:7641295).Curated
Sequence conflicti710 – 7101D → N in AAB35051 (PubMed:7641295).Curated
Sequence conflicti734 – 7341Q → R in AAH50107 (PubMed:15489334).Curated
Sequence conflicti744 – 7441E → K in AAH50107 (PubMed:15489334).Curated
Sequence conflicti772 – 7721S → P in AAH50107 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF228709 mRNA. Translation: AAF65544.1.
AK171769 mRNA. Translation: BAE42657.1.
AK145857 mRNA. Translation: BAE26702.1.
AK155721 mRNA. Translation: BAE33401.1.
AK157949 mRNA. Translation: BAE34279.1.
BC050107 mRNA. Translation: AAH50107.1.
S78797 mRNA. Translation: AAB35051.1.
CCDSiCCDS23107.1.
RefSeqiNP_067370.3. NM_021395.4.
XP_006510022.1. XM_006509959.1.
XP_006510023.1. XM_006509960.1.
XP_006510024.1. XM_006509961.1.
UniGeneiMm.116721.

Genome annotation databases

EnsembliENSMUST00000066601; ENSMUSP00000068594; ENSMUSG00000032115.
ENSMUST00000160902; ENSMUSP00000125594; ENSMUSG00000032115.
ENSMUST00000161318; ENSMUSP00000123700; ENSMUSG00000032115.
GeneIDi12282.
KEGGimmu:12282.
UCSCiuc009pdf.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF228709 mRNA. Translation: AAF65544.1.
AK171769 mRNA. Translation: BAE42657.1.
AK145857 mRNA. Translation: BAE26702.1.
AK155721 mRNA. Translation: BAE33401.1.
AK157949 mRNA. Translation: BAE34279.1.
BC050107 mRNA. Translation: AAH50107.1.
S78797 mRNA. Translation: AAB35051.1.
CCDSiCCDS23107.1.
RefSeqiNP_067370.3. NM_021395.4.
XP_006510022.1. XM_006509959.1.
XP_006510023.1. XM_006509960.1.
XP_006510024.1. XM_006509961.1.
UniGeneiMm.116721.

3D structure databases

ProteinModelPortaliQ9JKR6.
SMRiQ9JKR6. Positions 35-613.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198427. 8 interactions.
IntActiQ9JKR6. 6 interactions.
MINTiMINT-4130117.
STRINGi10090.ENSMUSP00000068594.

PTM databases

PhosphoSiteiQ9JKR6.

2D gel databases

REPRODUCTION-2DPAGEIPI00123342.
Q3TZD0.
Q64139.
Q9JKR6.

Proteomic databases

MaxQBiQ9JKR6.
PaxDbiQ9JKR6.
PRIDEiQ9JKR6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000066601; ENSMUSP00000068594; ENSMUSG00000032115.
ENSMUST00000160902; ENSMUSP00000125594; ENSMUSG00000032115.
ENSMUST00000161318; ENSMUSP00000123700; ENSMUSG00000032115.
GeneIDi12282.
KEGGimmu:12282.
UCSCiuc009pdf.2. mouse.

Organism-specific databases

CTDi10525.
MGIiMGI:108030. Hyou1.

Phylogenomic databases

eggNOGiCOG0443.
GeneTreeiENSGT00390000016919.
HOGENOMiHOG000007865.
HOVERGENiHBG106402.
InParanoidiQ9JKR6.
KOiK09486.
OMAiDTKENGT.
OrthoDBiEOG72RMXD.
PhylomeDBiQ9JKR6.
TreeFamiTF105048.

Enzyme and pathway databases

ReactomeiREACT_280759. Scavenging by Class F Receptors.

Miscellaneous databases

NextBioi280746.
PROiQ9JKR6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JKR6.
CleanExiMM_HYOU1.
ExpressionAtlasiQ9JKR6. baseline and differential.
GenevestigatoriQ9JKR6.

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. 2 hits.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100934. SSF100934. 1 hit.
PROSITEiPS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The 170 kDa glucose regulated protein of mouse."
    Chen X., Easton D.P., Subjeck J.R.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Inner ear, Placenta and Spleen.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo.
  4. "CBP-140, a novel endoplasmic reticulum resident Ca(2+)-binding protein with a carboxy-terminal NDEL sequence showed partial homology with 70-kDa heat shock protein (hsp70)."
    Naved A.F., Ozawa M., Yu S., Miyauchi T., Muramatsu H., Muramatsu T.
    Cell Struct. Funct. 20:133-141(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 347-999, SUBCELLULAR LOCATION.
  5. Lubec G., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 439-451.
    Tissue: Brain.
  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] [Europe PMC] [Abstract]
    Cited for: COMPONENT OF A CHAPERONE COMPLEX.
  7. "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.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-883, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiHYOU1_MOUSE
AccessioniPrimary (citable) accession number: Q9JKR6
Secondary accession number(s): Q3TAL1
, Q3TZD0, Q3U1U2, Q64139, Q80X75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 1, 2000
Last modified: May 27, 2015
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.