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Q9JKR6 (HYOU1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

Short name=GRP-170
Alternative name(s):
140 kDa Ca(2+)-binding protein
Short name=CBP-140
Gene names
Name:Hyou1
Synonyms:Grp170
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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 By similarity.

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 Ref.4.

Sequence similarities

Belongs to the heat shock protein 70 family.

Ontologies

Keywords
   Biological processStress response
   Cellular componentEndoplasmic reticulum
   DomainSignal
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMAcetylation
Glycoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processresponse to ischemia

Inferred from direct assay PubMed 9748521. Source: MGI

   Cellular_componentendoplasmic reticulum lumen

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Traceable author statement. Source: Reactome

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 By similarity
Chain33 – 999967Hypoxia up-regulated protein 1
PRO_5000057827

Regions

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

Amino acid modifications

Modified residue8831N6-acetyllysine Ref.8
Glycosylation1551N-linked (GlcNAc...) Potential
Glycosylation2221N-linked (GlcNAc...) Potential
Glycosylation5151N-linked (GlcNAc...) Ref.7
Glycosylation5961N-linked (GlcNAc...) Potential
Glycosylation8301N-linked (GlcNAc...) Potential
Glycosylation8621N-linked (GlcNAc...) Potential
Glycosylation8691N-linked (GlcNAc...) Potential
Glycosylation9221N-linked (GlcNAc...) Potential
Glycosylation9311N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1371Q → L in AAH50107. Ref.3
Sequence conflict2271N → D in AAH50107. Ref.3
Sequence conflict2471T → A in BAE34279. Ref.2
Sequence conflict2901Q → R in BAE42657. Ref.2
Sequence conflict4671R → G in AAB35051. Ref.4
Sequence conflict5401K → R in AAH50107. Ref.3
Sequence conflict6151E → K in AAH50107. Ref.3
Sequence conflict6651Missing in AAB35051. Ref.4
Sequence conflict6871P → L in AAB35051. Ref.4
Sequence conflict7101D → N in AAB35051. Ref.4
Sequence conflict7341Q → R in AAH50107. Ref.3
Sequence conflict7441E → K in AAH50107. Ref.3
Sequence conflict7721S → P in AAH50107. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9JKR6 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 2951482D1EE2EF36

FASTA999111,181
        10         20         30         40         50         60 
MAATVRRQRP RRLLCWALVA VLLADLLALS DTLAVMSVDL GSESMKVAIV KPGVPMEIVL 

        70         80         90        100        110        120 
NKESRRKTPV TVTLKENERF LGDSAAGMAI KNPKATLRYF QHLLGKQADN PHVALYRSRF 

       130        140        150        160        170        180 
PEHELIVDPQ RQTVRFQISP QLQFSPEEVL GMVLNYSRSL AEDFAEQPIK DAVITVPAFF 

       190        200        210        220        230        240 
NQAERRAVLQ AARMAGLKVL QLINDNTATA LSYGVFRRKD INSTAQNVMF YDMGSGSTVC 

       250        260        270        280        290        300 
TIVTYQTVKT KEAGMQPQLQ IRGVGFDRTL GGLEMELRLR EHLAKLFNEQ RKGQKAKDVR 

       310        320        330        340        350        360 
ENPRAMAKLL REANRLKTVL SANADHMAQI EGLMDDVDFK AKVTRVEFEE LCADLFDRVP 

       370        380        390        400        410        420 
GPVQQALQSA EMSLDQIEQV ILVGGATRVP KVQEVLLKAV GKEELGKNIN ADEAAAMGAV 

       430        440        450        460        470        480 
YQAAALSKAF KVKPFVVRDA VIYPILVEFT REVEEEPGLR SLKHNKRVLF SRMGPYPQRK 

       490        500        510        520        530        540 
VITFNRYSHD FNFHINYGDL GFLGPEDLRV FGSQNLTTVK LKGVGESFKK YPDYESKGIK 

       550        560        570        580        590        600 
AHFNLDESGV LSLDRVESVF ETLVEDSPEE ESTLTKLGNT ISSLFGGGTS SDAKENGTDA 

       610        620        630        640        650        660 
VQEEEESPAE GSKDEPAEQG ELKEEAEPPA EETSQPPPSE PKGDAAREGE KPDEKESGDK 

       670        680        690        700        710        720 
PEAQKPNEKG QAGPEGAAPA PEEDKKPKPA RKQKMVEEIG VELAVLDLPD LPEDELARSV 

       730        740        750        760        770        780 
QKLEELTLRD LEKQEREKAA NSLEAFIFET QDKLYQPEYQ EVSTEEQREE ISGKLSATST 

       790        800        810        820        830        840 
WLEDEGFGAT TVMLKDKLAE LRKLCQGLFF RVEERRKWPE RLSALDNLLN HSSIFLKGAR 

       850        860        870        880        890        900 
LIPEMDQVFT EVEMTTLEKV INDTWAWKNA TLAEQAKLPA TEKPVLLSKD IEAKMMALDR 

       910        920        930        940        950        960 
EVQYLLNKAK FTKPRPRPKD KNGTRAEPPL NASAGDQEEK VIPPAGQTEE AKPILEPDKE 

       970        980        990 
ETGTEPADSE PLELGGPGAG PEQEEQSAGQ KRPSKNDEL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS23107.1.
RefSeqNP_067370.3. NM_021395.4.
XP_006510022.1. XM_006509959.1.
XP_006510023.1. XM_006509960.1.
XP_006510024.1. XM_006509961.1.
UniGeneMm.116721.

3D structure databases

ProteinModelPortalQ9JKR6.
SMRQ9JKR6. Positions 35-613.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198427. 8 interactions.
IntActQ9JKR6. 6 interactions.
MINTMINT-4130117.
STRING10090.ENSMUSP00000068594.

PTM databases

PhosphoSiteQ9JKR6.

2D gel databases

REPRODUCTION-2DPAGEIPI00123342.
Q3TZD0.
Q64139.
Q9JKR6.

Proteomic databases

MaxQBQ9JKR6.
PaxDbQ9JKR6.
PRIDEQ9JKR6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000066601; ENSMUSP00000068594; ENSMUSG00000032115.
ENSMUST00000160902; ENSMUSP00000125594; ENSMUSG00000032115.
ENSMUST00000161318; ENSMUSP00000123700; ENSMUSG00000032115.
GeneID12282.
KEGGmmu:12282.
UCSCuc009pdf.2. mouse.

Organism-specific databases

CTD10525.
MGIMGI:108030. Hyou1.

Phylogenomic databases

eggNOGCOG0443.
GeneTreeENSGT00390000016919.
HOGENOMHOG000007865.
HOVERGENHBG106402.
InParanoidQ9JKR6.
KOK09486.
OMADTKENGT.
OrthoDBEOG72RMXD.
PhylomeDBQ9JKR6.
TreeFamTF105048.

Gene expression databases

ArrayExpressQ9JKR6.
BgeeQ9JKR6.
CleanExMM_HYOU1.
GenevestigatorQ9JKR6.

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. 2 hits.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
SUPFAMSSF100934. SSF100934. 1 hit.
PROSITEPS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio280746.
PROQ9JKR6.
SOURCESearch...

Entry information

Entry nameHYOU1_MOUSE
AccessionPrimary (citable) accession number: Q9JKR6
Secondary accession number(s): Q3TAL1 expand/collapse secondary AC list , Q3TZD0, Q3U1U2, Q64139, Q80X75
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot