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Q9JKR6

- HYOU1_MOUSE

UniProt

Q9JKR6 - HYOU1_MOUSE

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Protein

Hypoxia up-regulated protein 1

Gene
Hyou1, Grp170
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 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.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. response to ischemia Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_106572. XBP1(S) activates chaperone genes.
REACT_196603. 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: Chromosome 9

Organism-specific databases

MGIiMGI:108030. Hyou1.

Subcellular locationi

Endoplasmic reticulum lumen 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
  2. extracellular region Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

MaxQBiQ9JKR6.
PaxDbiQ9JKR6.
PRIDEiQ9JKR6.

2D gel databases

REPRODUCTION-2DPAGEIPI00123342.
Q3TZD0.
Q64139.
Q9JKR6.

PTM databases

PhosphoSiteiQ9JKR6.

Expressioni

Gene expression databases

ArrayExpressiQ9JKR6.
BgeeiQ9JKR6.
CleanExiMM_HYOU1.
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.

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

Sequence similaritiesi

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

MAATVRRQRP RRLLCWALVA VLLADLLALS DTLAVMSVDL GSESMKVAIV    50
KPGVPMEIVL NKESRRKTPV TVTLKENERF LGDSAAGMAI KNPKATLRYF 100
QHLLGKQADN PHVALYRSRF PEHELIVDPQ RQTVRFQISP QLQFSPEEVL 150
GMVLNYSRSL AEDFAEQPIK DAVITVPAFF NQAERRAVLQ AARMAGLKVL 200
QLINDNTATA LSYGVFRRKD INSTAQNVMF YDMGSGSTVC TIVTYQTVKT 250
KEAGMQPQLQ IRGVGFDRTL GGLEMELRLR EHLAKLFNEQ RKGQKAKDVR 300
ENPRAMAKLL REANRLKTVL SANADHMAQI EGLMDDVDFK AKVTRVEFEE 350
LCADLFDRVP GPVQQALQSA EMSLDQIEQV ILVGGATRVP KVQEVLLKAV 400
GKEELGKNIN ADEAAAMGAV YQAAALSKAF KVKPFVVRDA VIYPILVEFT 450
REVEEEPGLR SLKHNKRVLF SRMGPYPQRK VITFNRYSHD FNFHINYGDL 500
GFLGPEDLRV FGSQNLTTVK LKGVGESFKK YPDYESKGIK AHFNLDESGV 550
LSLDRVESVF ETLVEDSPEE ESTLTKLGNT ISSLFGGGTS SDAKENGTDA 600
VQEEEESPAE GSKDEPAEQG ELKEEAEPPA EETSQPPPSE PKGDAAREGE 650
KPDEKESGDK PEAQKPNEKG QAGPEGAAPA PEEDKKPKPA RKQKMVEEIG 700
VELAVLDLPD LPEDELARSV QKLEELTLRD LEKQEREKAA NSLEAFIFET 750
QDKLYQPEYQ EVSTEEQREE ISGKLSATST WLEDEGFGAT TVMLKDKLAE 800
LRKLCQGLFF RVEERRKWPE RLSALDNLLN HSSIFLKGAR LIPEMDQVFT 850
EVEMTTLEKV INDTWAWKNA TLAEQAKLPA TEKPVLLSKD IEAKMMALDR 900
EVQYLLNKAK FTKPRPRPKD KNGTRAEPPL NASAGDQEEK VIPPAGQTEE 950
AKPILEPDKE ETGTEPADSE PLELGGPGAG PEQEEQSAGQ KRPSKNDEL 999
Length:999
Mass (Da):111,181
Last modified:October 1, 2000 - v1
Checksum:i2951482D1EE2EF36
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1371Q → L in AAH50107. 1 Publication
Sequence conflicti227 – 2271N → D in AAH50107. 1 Publication
Sequence conflicti247 – 2471T → A in BAE34279. 1 Publication
Sequence conflicti290 – 2901Q → R in BAE42657. 1 Publication
Sequence conflicti467 – 4671R → G in AAB35051. 1 Publication
Sequence conflicti540 – 5401K → R in AAH50107. 1 Publication
Sequence conflicti615 – 6151E → K in AAH50107. 1 Publication
Sequence conflicti665 – 6651Missing in AAB35051. 1 Publication
Sequence conflicti687 – 6871P → L in AAB35051. 1 Publication
Sequence conflicti710 – 7101D → N in AAB35051. 1 Publication
Sequence conflicti734 – 7341Q → R in AAH50107. 1 Publication
Sequence conflicti744 – 7441E → K in AAH50107. 1 Publication
Sequence conflicti772 – 7721S → P in AAH50107. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS23107.1.
RefSeqi NP_067370.3. NM_021395.4.
XP_006510022.1. XM_006509959.1.
XP_006510023.1. XM_006509960.1.
XP_006510024.1. XM_006509961.1.
UniGenei Mm.116721.

3D structure databases

ProteinModelPortali Q9JKR6.
SMRi Q9JKR6. Positions 35-613.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198427. 8 interactions.
IntActi Q9JKR6. 6 interactions.
MINTi MINT-4130117.
STRINGi 10090.ENSMUSP00000068594.

PTM databases

PhosphoSitei Q9JKR6.

2D gel databases

REPRODUCTION-2DPAGE IPI00123342.
Q3TZD0.
Q64139.
Q9JKR6.

Proteomic databases

MaxQBi Q9JKR6.
PaxDbi Q9JKR6.
PRIDEi Q9JKR6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000066601 ; ENSMUSP00000068594 ; ENSMUSG00000032115 .
ENSMUST00000160902 ; ENSMUSP00000125594 ; ENSMUSG00000032115 .
ENSMUST00000161318 ; ENSMUSP00000123700 ; ENSMUSG00000032115 .
GeneIDi 12282.
KEGGi mmu:12282.
UCSCi uc009pdf.2. mouse.

Organism-specific databases

CTDi 10525.
MGIi MGI:108030. Hyou1.

Phylogenomic databases

eggNOGi COG0443.
GeneTreei ENSGT00390000016919.
HOGENOMi HOG000007865.
HOVERGENi HBG106402.
InParanoidi Q9JKR6.
KOi K09486.
OMAi DTKENGT.
OrthoDBi EOG72RMXD.
PhylomeDBi Q9JKR6.
TreeFami TF105048.

Enzyme and pathway databases

Reactomei REACT_106572. XBP1(S) activates chaperone genes.
REACT_196603. Scavenging by Class F Receptors.

Miscellaneous databases

NextBioi 280746.
PROi Q9JKR6.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9JKR6.
Bgeei Q9JKR6.
CleanExi MM_HYOU1.
Genevestigatori Q9JKR6.

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. 2 hits.
[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. "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: September 3, 2014
This is version 111 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

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