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P20029

- GRP78_MOUSE

UniProt

P20029 - GRP78_MOUSE

Protein

78 kDa glucose-regulated protein

Gene

Hspa5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei97 – 971ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi37 – 404ATPBy similarity
    Nucleotide bindingi228 – 2303ATPBy similarity
    Nucleotide bindingi294 – 3018ATPBy similarity
    Nucleotide bindingi365 – 3684ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. misfolded protein binding Source: BHF-UCL
    3. protein binding Source: IntAct
    4. ribosome binding Source: MGI

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: BHF-UCL
    2. cellular response to antibiotic Source: Ensembl
    3. cellular response to glucose starvation Source: Ensembl
    4. cellular response to interleukin-4 Source: MGI
    5. cerebellar Purkinje cell layer development Source: BHF-UCL
    6. cerebellum structural organization Source: BHF-UCL
    7. ER overload response Source: MGI
    8. maintenance of protein localization in endoplasmic reticulum Source: UniProtKB
    9. negative regulation of apoptotic process Source: Ensembl
    10. negative regulation of transforming growth factor beta receptor signaling pathway Source: MGI
    11. positive regulation of cell migration Source: UniProtKB
    12. positive regulation of embryonic development Source: BHF-UCL
    13. positive regulation of protein ubiquitination Source: BHF-UCL
    14. proteolysis involved in cellular protein catabolic process Source: BHF-UCL
    15. response to endoplasmic reticulum stress Source: MGI

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_32838. ATF6-alpha activates chaperone genes.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    78 kDa glucose-regulated protein
    Short name:
    GRP-78
    Alternative name(s):
    Heat shock 70 kDa protein 5
    Immunoglobulin heavy chain-binding protein
    Short name:
    BiP
    Gene namesi
    Name:Hspa5
    Synonyms:Grp78
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:95835. Hspa5.

    Subcellular locationi

    Endoplasmic reticulum lumen 1 PublicationPROSITE-ProRule annotation. Melanosome By similarity. Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cell surface Source: MGI
    2. COP9 signalosome Source: Ensembl
    3. endoplasmic reticulum Source: MGI
    4. endoplasmic reticulum chaperone complex Source: Ensembl
    5. endoplasmic reticulum-Golgi intermediate compartment Source: MGI
    6. endoplasmic reticulum lumen Source: BHF-UCL
    7. endoplasmic reticulum membrane Source: MGI
    8. extracellular region Source: Reactome
    9. integral component of endoplasmic reticulum membrane Source: Ensembl
    10. melanosome Source: UniProtKB-SubCell
    11. membrane Source: MGI
    12. midbody Source: Ensembl
    13. plasma membrane Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 19192 PublicationsAdd
    BLAST
    Chaini20 – 65563678 kDa glucose-regulated proteinPRO_0000013568Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei126 – 1261N6-acetyllysine1 Publication
    Modified residuei161 – 1611Nitrated tyrosine1 Publication
    Modified residuei214 – 2141N6-acetyllysine1 Publication
    Modified residuei327 – 3271N6-acetyllysine1 Publication
    Modified residuei354 – 3541N6-acetyllysine1 Publication
    Modified residuei448 – 4481N6-succinyllysine1 Publication
    Modified residuei519 – 5191PhosphothreonineBy similarity
    Modified residuei586 – 5861N6,N6,N6-trimethyllysine; by METTL21A; in vitro1 Publication
    Modified residuei650 – 6501Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Methylation, Nitration, Phosphoprotein

    Proteomic databases

    MaxQBiP20029.
    PaxDbiP20029.
    PRIDEiP20029.

    2D gel databases

    COMPLUYEAST-2DPAGEP20029.
    REPRODUCTION-2DPAGEIPI00319992.
    P20029.
    SWISS-2DPAGEP20029.
    UCD-2DPAGEP20029.

    PTM databases

    PhosphoSiteiP20029.

    Expressioni

    Gene expression databases

    ArrayExpressiP20029.
    BgeeiP20029.
    CleanExiMM_HSPA5.
    GenevestigatoriP20029.

    Interactioni

    Subunit structurei

    Interacts with TMEM132A and TRIM21. May form a complex with ERLEC1, OS9, SEL1L and SYVN1 By similarity. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. 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. Interacts with DNAJC1 (via J domain). Interacts with METTL23. Interacts with CEMIP; the interaction induces calcium leakage from the endoplamic reticulum and cell migration By similarity. Interacts with DNAJC10 and MX1.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ERN1O754602EBI-772325,EBI-371750From a different organism.

    Protein-protein interaction databases

    BioGridi200078. 42 interactions.
    DIPiDIP-32341N.
    IntActiP20029. 25 interactions.
    MINTiMINT-1177274.

    Structurei

    3D structure databases

    ProteinModelPortaliP20029.
    SMRiP20029. Positions 27-638.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi652 – 6554Prevents secretion from ER

    Sequence similaritiesi

    Belongs to the heat shock protein 70 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0443.
    GeneTreeiENSGT00750000117237.
    HOGENOMiHOG000228135.
    HOVERGENiHBG051845.
    InParanoidiP20029.
    KOiK09490.
    OMAiDKRAVQK.
    OrthoDBiEOG780RKX.
    PhylomeDBiP20029.
    TreeFamiTF105044.

    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.
    SUPFAMiSSF100920. SSF100920. 1 hit.
    SSF100934. SSF100934. 1 hit.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    PS00297. HSP70_1. 1 hit.
    PS00329. 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.

    P20029-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMKFTVVAAA LLLLGAVRAE EEDKKEDVGT VVGIDLGTTY SCVGVFKNGR    50
    VEIIANDQGN RITPSYVAFT PEGERLIGDA AKNQLTSNPE NTVFDAKRLI 100
    GRTWNDPSVQ QDIKFLPFKV VEKKTKPYIQ VDIGGGQTKT FAPEEISAMV 150
    LTKMKETAEA YLGKKVTHAV VTVPAYFNDA QRQATKDAGT IAGLNVMRII 200
    NEPTAAAIAY GLDKREGEKN ILVFDLGGGT FDVSLLTIDN GVFEVVATNG 250
    DTHLGGEDFD QRVMEHFIKL YKKKTGKDVR KDNRAVQKLR REVEKAKRAL 300
    SSQHQARIEI ESFFEGEDFS ETLTRAKFEE LNMDLFRSTM KPVQKVLEDS 350
    DLKKSDIDEI VLVGGSTRIP KIQQLVKEFF NGKEPSRGIN PDEAVAYGAA 400
    VQAGVLSGDQ DTGDLVLLDV CPLTLGIETV GGVMTKLIPR NTVVPTKKSQ 450
    IFSTASDNQP TVTIKVYEGE RPLTKDNHLL GTFDLTGIPP APRGVPQIEV 500
    TFEIDVNGIL RVTAEDKGTG NKNKITITND QNRLTPEEIE RMVNDAEKFA 550
    EEDKKLKERI DTRNELESYA YSLKNQIGDK EKLGGKLSSE DKETMEKAVE 600
    EKIEWLESHQ DADIEDFKAK KKELEEIVQP IISKLYGSGG PPPTGEEDTS 650
    EKDEL 655
    Length:655
    Mass (Da):72,422
    Last modified:November 1, 1997 - v3
    Checksum:iAFB795D15E20FAC2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti43 – 431V → F in BAA11462. (PubMed:8645260)Curated
    Sequence conflicti245 – 2451V → W in BAA11462. (PubMed:8645260)Curated
    Sequence conflicti329 – 3291E → G in BAA11462. (PubMed:8645260)Curated
    Sequence conflicti361 – 3611V → A in BAA11462. (PubMed:8645260)Curated
    Sequence conflicti474 – 4741T → R in CAA05361. (PubMed:2895472)Curated
    Sequence conflicti591 – 5911D → G in AAA37742. (PubMed:2583523)Curated
    Sequence conflicti596 – 5961E → K AA sequence (PubMed:2559088)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ002387 mRNA. Translation: CAA05361.1.
    M19351 mRNA. Translation: AAA37315.1.
    D78645 mRNA. Translation: BAA11462.1.
    AK076079 mRNA. Translation: BAC36166.1.
    AK146647 mRNA. Translation: BAE27328.1.
    AK148539 mRNA. Translation: BAE28609.1.
    AK151647 mRNA. Translation: BAE30576.1.
    AK152020 mRNA. Translation: BAE30882.1.
    AK166739 mRNA. Translation: BAE38982.1.
    AK169034 mRNA. Translation: BAE40825.1.
    BC050927 mRNA. Translation: AAH50927.1.
    U16277 Genomic DNA. Translation: AAA76734.1.
    M30779 mRNA. Translation: AAA37742.1.
    CCDSiCCDS15950.1.
    PIRiA37048.
    RefSeqiNP_001156906.1. NM_001163434.1.
    NP_071705.3. NM_022310.3.
    UniGeneiMm.330160.
    Mm.470180.

    Genome annotation databases

    EnsembliENSMUST00000028222; ENSMUSP00000028222; ENSMUSG00000026864.
    ENSMUST00000100171; ENSMUSP00000097747; ENSMUSG00000026864.
    GeneIDi14828.
    KEGGimmu:14828.
    UCSCiuc008jis.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ002387 mRNA. Translation: CAA05361.1 .
    M19351 mRNA. Translation: AAA37315.1 .
    D78645 mRNA. Translation: BAA11462.1 .
    AK076079 mRNA. Translation: BAC36166.1 .
    AK146647 mRNA. Translation: BAE27328.1 .
    AK148539 mRNA. Translation: BAE28609.1 .
    AK151647 mRNA. Translation: BAE30576.1 .
    AK152020 mRNA. Translation: BAE30882.1 .
    AK166739 mRNA. Translation: BAE38982.1 .
    AK169034 mRNA. Translation: BAE40825.1 .
    BC050927 mRNA. Translation: AAH50927.1 .
    U16277 Genomic DNA. Translation: AAA76734.1 .
    M30779 mRNA. Translation: AAA37742.1 .
    CCDSi CCDS15950.1.
    PIRi A37048.
    RefSeqi NP_001156906.1. NM_001163434.1.
    NP_071705.3. NM_022310.3.
    UniGenei Mm.330160.
    Mm.470180.

    3D structure databases

    ProteinModelPortali P20029.
    SMRi P20029. Positions 27-638.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 200078. 42 interactions.
    DIPi DIP-32341N.
    IntActi P20029. 25 interactions.
    MINTi MINT-1177274.

    PTM databases

    PhosphoSitei P20029.

    2D gel databases

    COMPLUYEAST-2DPAGE P20029.
    REPRODUCTION-2DPAGE IPI00319992.
    P20029.
    SWISS-2DPAGE P20029.
    UCD-2DPAGE P20029.

    Proteomic databases

    MaxQBi P20029.
    PaxDbi P20029.
    PRIDEi P20029.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028222 ; ENSMUSP00000028222 ; ENSMUSG00000026864 .
    ENSMUST00000100171 ; ENSMUSP00000097747 ; ENSMUSG00000026864 .
    GeneIDi 14828.
    KEGGi mmu:14828.
    UCSCi uc008jis.2. mouse.

    Organism-specific databases

    CTDi 3309.
    MGIi MGI:95835. Hspa5.

    Phylogenomic databases

    eggNOGi COG0443.
    GeneTreei ENSGT00750000117237.
    HOGENOMi HOG000228135.
    HOVERGENi HBG051845.
    InParanoidi P20029.
    KOi K09490.
    OMAi DKRAVQK.
    OrthoDBi EOG780RKX.
    PhylomeDBi P20029.
    TreeFami TF105044.

    Enzyme and pathway databases

    Reactomei REACT_32838. ATF6-alpha activates chaperone genes.

    Miscellaneous databases

    ChiTaRSi HSPA5. mouse.
    NextBioi 287039.
    PROi P20029.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20029.
    Bgeei P20029.
    CleanExi MM_HSPA5.
    Genevestigatori P20029.

    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 SSF100920. SSF100920. 1 hit.
    SSF100934. SSF100934. 1 hit.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    PS00297. HSP70_1. 1 hit.
    PS00329. HSP70_2. 1 hit.
    PS01036. HSP70_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning of the immunoglobulin heavy chain binding protein."
      Haas I.G., Meo T.
      Proc. Natl. Acad. Sci. U.S.A. 85:2250-2254(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Identification of immunoglobulin heavy chain binding protein as glucose-regulated protein 78 on the basis of amino acid sequence, immunological cross-reactivity, and functional activity."
      Kozutsumi Y., Normington K., Press E., Slaughter C., Sambrook J., Gething M.J.
      J. Cell Sci. Suppl. 11:115-137(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-46.
    3. "Molecular characterization of seizure-related genes isolated by differential screening."
      Kajiwara K., Nagawawa H., Shimizu-Nishikawa K., Ookura T., Kimura M., Sugaya E.
      Biochem. Biophys. Res. Commun. 219:795-799(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6.
      Tissue: Brain.
    4. "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.
      Tissue: Kidney.
    5. "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/6.
      Tissue: Brain.
    6. "Structure and regulation of the mouse GRP78 (BiP) promoter by glucose and calcium ionophore."
      Tillman J.B., Mote P.L., Walford R.L., Spindler S.R.
      Gene 158:225-229(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
      Strain: C3B10RF1.
      Tissue: Liver.
    7. "Separation and sequencing of familiar and novel murine proteins using preparative two-dimensional gel electrophoresis."
      Merrick B.A., Patterson R.M., Wichter L.L., He C., Selkirk J.K.
      Electrophoresis 15:735-745(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-36.
      Tissue: Fibroblast.
    8. Lubec G., Kang S.U., Klug S., Friebe K., Yang J.W., Zigmond M.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 51-75; 140-153; 156-164; 166-182; 187-215; 308-337; 354-368; 449-493; 525-541 AND 623-634, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain and Hippocampus.
    9. "Differential screening of a cDNA library with cDNA probes amplified in a heterologous host: isolation of murine GRP78 (BiP) and other serum-regulated low-abundance mRNAs."
      Parfett C.L.J., Hofbauer R., Brudzynski K., Edwards D.R., Denhardt D.T.
      Gene 82:291-303(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 488-655.
    10. "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.
    11. Cited for: INTERACTION WITH DNAJC1.
    12. "ERdj5, an endoplasmic reticulum (ER)-resident protein containing DnaJ and thioredoxin domains, is expressed in secretory cells or following ER stress."
      Cunnea P.M., Miranda-Vizuete A., Bertoli G., Simmen T., Damdimopoulos A.E., Hermann S., Leinonen S., Huikko M.P., Gustafsson J.-A., Sitia R., Spyrou G.
      J. Biol. Chem. 278:1059-1066(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNAJC10.
    13. Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    14. "Age-specific CUGBP1-eIF2 complex increases translation of CCAAT/enhancer-binding protein beta in old liver."
      Timchenko L.T., Salisbury E., Wang G.-L., Nguyen H., Albrecht J.H., Hershey J.W., Timchenko N.A.
      J. Biol. Chem. 281:32806-32819(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN AN EIF2 COMPLEX WITH EIF2S1; EIF2S2; CELF1; CALR; CALR3 AND HSP90B1.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-650, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    16. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Interferon-inducible antiviral protein MxA enhances cell death triggered by endoplasmic reticulum stress."
      Numajiri Haruki A., Naito T., Nishie T., Saito S., Nagata K.
      J. Interferon Cytokine Res. 31:847-856(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MX1.
    18. "Identification and characterization of a novel human methyltransferase modulating Hsp70 function through lysine methylation."
      Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S., Melki R., Falnes P.O.
      J. Biol. Chem. 288:27752-27763(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT LYS-586.
    19. "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-126; LYS-214; LYS-327 AND LYS-354, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiGRP78_MOUSE
    AccessioniPrimary (citable) accession number: P20029
    Secondary accession number(s): O35642, Q3UFF2, Q61630
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 153 of the entry and version 3 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