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Q91883

- GRP78_XENLA

UniProt

Q91883 - GRP78_XENLA

Protein

78 kDa glucose-regulated protein

Gene

hspa5

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Probably plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei98 – 981ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi38 – 414ATPBy similarity
    Nucleotide bindingi228 – 2303ATPBy similarity
    Nucleotide bindingi294 – 3018ATPBy similarity
    Nucleotide bindingi365 – 3684ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW

    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
    Immunoglobulin heavy chain-binding protein
    Short name:
    BiP
    Gene namesi
    Name:hspa5
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 65863978 kDa glucose-regulated proteinPRO_0000013571Add
    BLAST

    Proteomic databases

    PRIDEiQ91883.

    Structurei

    3D structure databases

    ProteinModelPortaliQ91883.
    SMRiQ91883. Positions 30-571.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi655 – 6584Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the heat shock protein 70 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG051845.
    KOiK09490.

    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.

    Q91883-1 [UniParc]FASTAAdd to Basket

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    MVTMKLFALV LLVSASVFAS DDDDKKDDIG TVVGIDLGTT YSCVGVFKNG    50
    RVEIIANDQG NRITPSYVAF TPEGERLIGD AAKNQLTSNP ENTVFDAKRL 100
    IGRTWNDPSV QQDIKYLPFK VIEKKTKPYI EVDIGDQMKT FAPEEISAMV 150
    LVKMKETAEA YLGRKVTHAV VTVPAYFNDA QRQATKDAGT IAGLNVMRII 200
    NEPTAAAIAY GLDKKEGEKN ILVFDLGGGT FDVSLLTIDN GVFEVVATNG 250
    DTHLGGEDFD QRVMEHFIKL YKKKTGKDVR ADKRAVQKLR REVEKAKRAL 300
    SAQHQSRIEI ESFFEGEDFS ETLTRAKFEE LNMDLFRSTM KPVQKVLDDS 350
    DLKKSDIDEI VLVGGSTRIP KIQQLVKELF NGKEPSRGIN PDEAVAYGAA 400
    VQAGVLSGDQ DTGDLVLLDV CPLTLGIETV GGVMTKLIPR NTVVPTKKSQ 450
    IFSTASDNQP TVTIKVYEGE RPLTKDNHLL GTFDLTGIPP APRGVPQIEV 500
    TFEIDVNGIL RVTAEDKGTG NKNKITITND QNRLTPEEIE RMVTDAEKFA 550
    EEDKKLKERI DTRNELESYA YSLKNQIGDK EKLGGKLSSE DKETIEKAVE 600
    EKIEWLESHQ DADIEDFKAK KKELEEIVQP IVGKLYGGAG APPPEGAEGA 650
    EETEKDEL 658
    Length:658
    Mass (Da):72,635
    Last modified:November 1, 1996 - v1
    Checksum:i43E1468F532E80CF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U62807 mRNA. Translation: AAB08760.1.
    RefSeqiNP_001081462.1. NM_001087993.1.
    UniGeneiXl.3204.

    Genome annotation databases

    GeneIDi397850.
    KEGGixla:397850.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U62807 mRNA. Translation: AAB08760.1 .
    RefSeqi NP_001081462.1. NM_001087993.1.
    UniGenei Xl.3204.

    3D structure databases

    ProteinModelPortali Q91883.
    SMRi Q91883. Positions 30-571.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q91883.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 397850.
    KEGGi xla:397850.

    Phylogenomic databases

    HOVERGENi HBG051845.
    KOi K09490.

    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. "Degradation and endoplasmic reticulum retention of unassembled alpha- and beta-subunits of Na,K-ATPase correlate with interaction of BiP."
      Beggah A., Mathews P., Beguin P., Geering K.
      J. Biol. Chem. 271:20895-20902(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiGRP78_XENLA
    AccessioniPrimary (citable) accession number: Q91883
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 83 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3