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P20029

- GRP78_MOUSE

UniProt

P20029 - GRP78_MOUSE

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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

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. 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
  16. substantia nigra development Source: Ensembl
Complete GO annotation...

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. extracellular vesicular exosome Source: Ensembl
  10. integral component of endoplasmic reticulum membrane Source: Ensembl
  11. membrane Source: MGI
  12. midbody Source: Ensembl
  13. plasma membrane Source: MGI
Complete GO annotation...

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

BgeeiP20029.
CleanExiMM_HSPA5.
ExpressionAtlasiP20029. baseline and differential.
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

        10         20         30         40         50
MMKFTVVAAA LLLLGAVRAE EEDKKEDVGT VVGIDLGTTY SCVGVFKNGR
60 70 80 90 100
VEIIANDQGN RITPSYVAFT PEGERLIGDA AKNQLTSNPE NTVFDAKRLI
110 120 130 140 150
GRTWNDPSVQ QDIKFLPFKV VEKKTKPYIQ VDIGGGQTKT FAPEEISAMV
160 170 180 190 200
LTKMKETAEA YLGKKVTHAV VTVPAYFNDA QRQATKDAGT IAGLNVMRII
210 220 230 240 250
NEPTAAAIAY GLDKREGEKN ILVFDLGGGT FDVSLLTIDN GVFEVVATNG
260 270 280 290 300
DTHLGGEDFD QRVMEHFIKL YKKKTGKDVR KDNRAVQKLR REVEKAKRAL
310 320 330 340 350
SSQHQARIEI ESFFEGEDFS ETLTRAKFEE LNMDLFRSTM KPVQKVLEDS
360 370 380 390 400
DLKKSDIDEI VLVGGSTRIP KIQQLVKEFF NGKEPSRGIN PDEAVAYGAA
410 420 430 440 450
VQAGVLSGDQ DTGDLVLLDV CPLTLGIETV GGVMTKLIPR NTVVPTKKSQ
460 470 480 490 500
IFSTASDNQP TVTIKVYEGE RPLTKDNHLL GTFDLTGIPP APRGVPQIEV
510 520 530 540 550
TFEIDVNGIL RVTAEDKGTG NKNKITITND QNRLTPEEIE RMVNDAEKFA
560 570 580 590 600
EEDKKLKERI DTRNELESYA YSLKNQIGDK EKLGGKLSSE DKETMEKAVE
610 620 630 640 650
EKIEWLESHQ DADIEDFKAK KKELEEIVQP IISKLYGSGG PPPTGEEDTS

EKDEL
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

Bgeei P20029.
CleanExi MM_HSPA5.
ExpressionAtlasi P20029. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 154 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

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