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Q9JKR6

- HYOU1_MOUSE

UniProt

Q9JKR6 - HYOU1_MOUSE

Protein

Hypoxia up-regulated protein 1

Gene

Hyou1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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

    1. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. response to ischemia Source: MGI

    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

    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
    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

    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.
    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

    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

    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:
    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

    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: October 1, 2014
    This is version 112 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