Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q3S4T7

- GRP78_SPETR

UniProt

Q3S4T7 - GRP78_SPETR

Protein

78 kDa glucose-regulated protein

Gene

HSPA5

Organism
Spermophilus tridecemlineatus (Thirteen-lined ground squirrel) (Ictidomys tridecemlineatus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 67 (01 Oct 2014)
      Sequence version 1 (11 Oct 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 sitei96 – 961ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi36 – 394ATPBy similarity
    Nucleotide bindingi227 – 2293ATPBy similarity
    Nucleotide bindingi293 – 3008ATPBy similarity
    Nucleotide bindingi364 – 3674ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. maintenance of protein localization in endoplasmic reticulum Source: UniProtKB
    2. positive regulation of cell migration Source: UniProtKB

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    78 kDa glucose-regulated protein
    Short name:
    GRP-78
    Alternative name(s):
    Heat shock 70 kDa protein 5
    Gene namesi
    Name:HSPA5
    Synonyms:GRP78
    OrganismiSpermophilus tridecemlineatus (Thirteen-lined ground squirrel) (Ictidomys tridecemlineatus)
    Taxonomic identifieri43179 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiSciuridaeXerinaeMarmotiniIctidomys
    ProteomesiUP000005215: Unplaced

    Subcellular locationi

    Endoplasmic reticulum lumen PROSITE-ProRule annotation. Melanosome By similarity. Cytoplasm By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell
    2. melanosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818By similarityAdd
    BLAST
    Chaini19 – 65463678 kDa glucose-regulated proteinPRO_0000250503Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei125 – 1251N6-acetyllysineBy similarity
    Modified residuei160 – 1601Nitrated tyrosineBy similarity
    Modified residuei213 – 2131N6-acetyllysineBy similarity
    Modified residuei326 – 3261N6-acetyllysineBy similarity
    Modified residuei353 – 3531N6-acetyllysineBy similarity
    Modified residuei447 – 4471N6-succinyllysineBy similarity
    Modified residuei518 – 5181PhosphothreonineBy similarity
    Modified residuei585 – 5851N6,N6,N6-trimethyllysine; by METTL21A; in vitroBy similarity
    Modified residuei649 – 6491PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Methylation, Nitration, Phosphoprotein

    Proteomic databases

    PRIDEiQ3S4T7.

    Interactioni

    Subunit structurei

    Interacts with DNAJC1 (via J domain) 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 CABP1, DNAJB11, HSP90B1, HSPA5, HYOU, PDIA2, PDIA4, PPIB, SDF2L1, UGT1A1 and very small amounts of ERP29, but not, or at very low levels, CALR nor CANX. Interacts with TMEM132A and TRIM21. May form a complex with ERLEC1, OS9, SEL1L and SYVN1 By similarity. Interacts with MX1. Interacts with METTL23 and DNAJC10. Interacts with CEMIP; the interaction induces calcium leakage from the endoplamic reticulum and cell migration By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ3S4T7.
    SMRiQ3S4T7. Positions 28-570.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi651 – 6544Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the heat shock protein 70 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000228135.
    HOVERGENiHBG051845.

    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.

    Q3S4T7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLSLVAAVL LLLCAARAEE EDKKEDVGTV VGIDLGTTYS CVGVFKNGRV    50
    EIIANDQGNR ITPSYVAFTP EGERLIGDAA KNQLTSNPEN TVFDAKRLIG 100
    RTWNDPSVQQ DIKFLPFKVV EKKTKPYIQV DIGGGQTKTF APEEISAMVL 150
    TKMKETAEAY LGKKVTHAVV TVPAYFNDAQ RQATKDAGTI AGLNVMRIIN 200
    EPTAAAIAYG LDKREGEKNI LVFDLGGGTF DVSLLTIDNG VFEVVATNGD 250
    THLGGEDFDQ RVMEHFIKLY KKKTGKDVRK DNRAVQKLRR EVEKAKRALS 300
    SQHQARIEIE SFYEGEDFSE TLTRAKFEEL NMDLFRSTMK PVQKVLEDSD 350
    LKKSDIDEIV LVGGSTRIPK IQQLVKEFFN GKEPSRGINP DEAVAYGAAV 400
    QAGVLSGDQD TGDLVLLDVC PLTLGIETVG GVMTKLIPRN TVVPTKKSQI 450
    SSTASDNQPT VTIKVYEGER PLTKDNHLLG TFDLTGIPPA PRGVPQIEVT 500
    FEIDVNGILR VTAEDKGTGN KNKITITNDQ NRLTPEEIER MVNDAEKFAE 550
    EDKRLKERID TRNELESYAY SLKNQIGDKE KLGGKLSSED KETMEKAVEE 600
    KIEWLESHQD ADIEDFKAKK KELEEIVQPI ISKLYGSAGP PPTGEEDTSE 650
    RDEL 654
    Length:654
    Mass (Da):72,329
    Last modified:October 11, 2005 - v1
    Checksum:iCCA5709DA9C16913
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ166628 mRNA. Translation: AAZ94625.1.
    RefSeqiNP_001269183.1. NM_001282254.1.

    Genome annotation databases

    GeneIDi101974907.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ166628 mRNA. Translation: AAZ94625.1 .
    RefSeqi NP_001269183.1. NM_001282254.1.

    3D structure databases

    ProteinModelPortali Q3S4T7.
    SMRi Q3S4T7. Positions 28-570.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q3S4T7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 101974907.

    Organism-specific databases

    CTDi 3309.

    Phylogenomic databases

    HOGENOMi HOG000228135.
    HOVERGENi HBG051845.

    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. "Induction of the endoplasmic reticulum molecular chaperone GRP78 in hibernating ground squirrels, Spermophilus tridecemlineatus."
      Hapsatou M., Storey K.B.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiGRP78_SPETR
    AccessioniPrimary (citable) accession number: Q3S4T7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2006
    Last sequence update: October 11, 2005
    Last modified: October 1, 2014
    This is version 67 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, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3