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P19120

- HSP7C_BOVIN

UniProt

P19120 - HSP7C_BOVIN

Protein

Heat shock cognate 71 kDa protein

Gene

HSPA8

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (29 May 2007)
      Previous versions | rss
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    Functioni

    Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex By similarity. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase CHIP By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei71 – 711ATP

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi12 – 154ATP
    Nucleotide bindingi202 – 2043ATP
    Nucleotide bindingi268 – 2758ATP
    Nucleotide bindingi339 – 3424ATP

    GO - Molecular functioni

    1. ATPase activity, coupled Source: Ensembl
    2. ATP binding Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. chaperone mediated protein folding requiring cofactor Source: Ensembl
    2. mRNA processing Source: UniProtKB-KW
    3. negative regulation of transcription, DNA-templated Source: UniProtKB
    4. regulation of cell cycle Source: Ensembl
    5. response to stress Source: UniProtKB-KW
    6. RNA splicing Source: UniProtKB-KW
    7. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chaperone, Repressor

    Keywords - Biological processi

    mRNA processing, mRNA splicing, Stress response, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_205580. HSF1-dependent transactivation.
    REACT_211255. GABA synthesis, release, reuptake and degradation.
    REACT_213591. Attenuation phase.
    REACT_214880. CHL1 interactions.
    REACT_218726. Regulation of HSF1-mediated heat shock response.
    REACT_227515. AUF1 (hnRNP D0) destabilizes mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Heat shock cognate 71 kDa protein
    Alternative name(s):
    Heat shock 70 kDa protein 8
    Gene namesi
    Name:HSPA8
    Synonyms:HSC70
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 15

    Subcellular locationi

    Cytoplasm By similarity. Melanosome By similarity. Nucleusnucleolus By similarity. Cell membrane By similarity
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock By similarity.By similarity

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. extracellular vesicular exosome Source: Ensembl
    3. melanosome Source: UniProtKB-SubCell
    4. nucleolus Source: UniProtKB
    5. nucleus Source: UniProtKB
    6. plasma membrane Source: UniProtKB-SubCell
    7. Prp19 complex Source: UniProtKB
    8. ribonucleoprotein complex Source: UniProtKB
    9. spliceosomal complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus, Spliceosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 650649Heat shock cognate 71 kDa proteinPRO_0000078268Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei108 – 1081N6-acetyllysineBy similarity
    Modified residuei153 – 1531PhosphoserineBy similarity
    Modified residuei246 – 2461N6-acetyllysineBy similarity
    Modified residuei319 – 3191N6-acetyllysine; alternateBy similarity
    Modified residuei319 – 3191N6-succinyllysine; alternateBy similarity
    Modified residuei328 – 3281N6-acetyllysineBy similarity
    Modified residuei362 – 3621PhosphoserineBy similarity
    Modified residuei512 – 5121N6-acetyllysine; alternateBy similarity
    Modified residuei512 – 5121N6-succinyllysine; alternateBy similarity
    Modified residuei524 – 5241N6-acetyllysineBy similarity
    Modified residuei561 – 5611N6,N6,N6-trimethyllysine; by METTL21ABy similarity
    Modified residuei589 – 5891N6-acetyllysineBy similarity
    Modified residuei597 – 5971N6-acetyllysineBy similarity
    Modified residuei601 – 6011N6-acetyllysineBy similarity

    Post-translational modificationi

    Acetylated.By similarity
    ISGylated.By similarity
    Trimethylation at Lys-561 reduces fibrillar SNCA binding.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP19120.
    PRIDEiP19120.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Inductioni

    Constitutively synthesized.

    Interactioni

    Subunit structurei

    Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with PACRG. Interacts with HSPH1/HSP105. Interacts with IRAK1BP1 and BAG1. Interacts with DNAJC7 and DNAJB14 (via J domain). Interacts (via C-terminus) with the E3 ligase CHIP forming a 210 kDa complex of one CHIP and two HSPA8 molecules. Interacts with CITED1 (via N-terminus); the interaction suppresses the association of CITED1 to p300/CBP and SMAD-mediated transcription transactivation. Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts with TRIM5 By similarity. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity By similarity. Following LPS binding, may form a complex with CXCR4, GDF5 and HSP90AA1 By similarity. Interacts with PARK2 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CFTRP135692EBI-907802,EBI-349854From a different organism.
    CftrP263615EBI-907802,EBI-6115317From a different organism.

    Protein-protein interaction databases

    BioGridi159144. 2 interactions.
    DIPiDIP-35481N.
    IntActiP19120. 6 interactions.
    MINTiMINT-157582.
    STRINGi9913.ENSBTAP00000017497.

    Structurei

    Secondary structure

    1
    650
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 104
    Beta strandi13 – 2210
    Beta strandi25 – 284
    Beta strandi36 – 394
    Beta strandi42 – 443
    Beta strandi49 – 513
    Helixi53 – 564
    Turni57 – 615
    Helixi63 – 653
    Beta strandi66 – 683
    Helixi70 – 723
    Turni73 – 753
    Helixi81 – 877
    Beta strandi91 – 977
    Beta strandi100 – 1078
    Beta strandi110 – 1145
    Helixi116 – 13520
    Beta strandi141 – 1466
    Helixi152 – 16413
    Beta strandi168 – 1747
    Helixi175 – 1828
    Turni183 – 1864
    Beta strandi187 – 1915
    Beta strandi193 – 2008
    Beta strandi205 – 2139
    Beta strandi216 – 22510
    Helixi230 – 24920
    Helixi253 – 2553
    Helixi257 – 27317
    Turni274 – 2763
    Beta strandi277 – 28812
    Beta strandi291 – 2988
    Helixi299 – 31214
    Helixi314 – 32310
    Helixi328 – 3303
    Beta strandi333 – 3386
    Helixi339 – 3424
    Helixi344 – 35310
    Turni354 – 3563
    Helixi365 – 3673
    Helixi368 – 38013
    Beta strandi386 – 3883
    Beta strandi392 – 3965
    Beta strandi401 – 4055
    Turni406 – 4083
    Beta strandi409 – 4146
    Beta strandi419 – 43214
    Beta strandi438 – 4469
    Helixi450 – 4523
    Beta strandi453 – 4619
    Beta strandi474 – 4807
    Beta strandi486 – 4927
    Turni493 – 4953
    Beta strandi498 – 5036
    Helixi512 – 52413
    Helixi526 – 5349
    Beta strandi539 – 5424
    Helixi547 – 5493

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ATRX-ray2.34A1-386[»]
    1ATSX-ray2.43A1-386[»]
    1BA0X-ray1.90A1-386[»]
    1BA1X-ray1.70A1-386[»]
    1BUPX-ray1.70A1-386[»]
    1HPMX-ray1.70A1-386[»]
    1HX1X-ray1.90A4-381[»]
    1KAXX-ray1.70A1-381[»]
    1KAYX-ray1.70A1-381[»]
    1KAZX-ray1.70A1-381[»]
    1NGAX-ray2.18A1-386[»]
    1NGBX-ray2.18A1-386[»]
    1NGCX-ray2.20A1-386[»]
    1NGDX-ray2.18A1-386[»]
    1NGEX-ray2.05A1-386[»]
    1NGFX-ray2.17A1-386[»]
    1NGGX-ray2.19A1-386[»]
    1NGHX-ray2.23A1-386[»]
    1NGIX-ray2.15A1-386[»]
    1NGJX-ray2.10A1-386[»]
    1Q2Gmodel-B4-381[»]
    1QQMX-ray1.90A4-381[»]
    1QQNX-ray1.90A4-381[»]
    1QQOX-ray1.90A4-381[»]
    1YUWX-ray2.60A1-554[»]
    2BUPX-ray1.70A1-381[»]
    2QW9X-ray1.85A/B1-394[»]
    2QWLX-ray1.75A/B1-394[»]
    2QWMX-ray1.86A/B1-394[»]
    2QWNX-ray2.40A1-394[»]
    2QWOX-ray1.70A1-394[»]
    2QWPX-ray1.75A1-394[»]
    2QWQX-ray2.21A1-394[»]
    2QWRX-ray2.21A1-394[»]
    3C7NX-ray3.12B1-554[»]
    3HSCX-ray1.93A1-386[»]
    4FL9X-ray1.90A1-554[»]
    ProteinModelPortaliP19120.
    SMRiP19120. Positions 1-621.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19120.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni186 – 377192Interaction with BAG1By similarityAdd
    BLAST

    Domaini

    The N-terminal 1-386 residues constitute the ATPase domain, while residues 387-646 form the peptide-binding domain.By similarity

    Sequence similaritiesi

    Belongs to the heat shock protein 70 family.Curated

    Phylogenomic databases

    eggNOGiCOG0443.
    GeneTreeiENSGT00750000117237.
    HOGENOMiHOG000228135.
    HOVERGENiHBG051845.
    InParanoidiP19120.
    KOiK03283.
    OMAiGENKIFT.
    OrthoDBiEOG7PCJGF.
    TreeFamiTF105042.

    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.
    PROSITEiPS00297. 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.

    P19120-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL    50
    IGDAAKNQVA MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR 100
    PKVQVEYKGE TKSFYPEEVS SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF 150
    NDSQRQATKD AGTIAGLNVL RIINEPTAAA IAYGLDKKVG AERNVLIFDL 200
    GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH FIAEFKRKHK 250
    KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA 300
    RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL 350
    QDFFNGKELN KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS 400
    LGIETAGGVM TVLIKRNTTI PTKQTQTFTT YSDNQPGVLI QVYEGERAMT 450
    KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI DANGILNVSA VDKSTGKENK 500
    ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN SLESYAFNMK 550
    ATVEDEKLQG KINDEDKQKI LDKCNEIINW LDKNQTAEKE EFEHQQKELE 600
    KVCNPIITKL YQSAGGMPGG MPGGMPGGFP GGGAPPSGGA SSGPTIEEVD 650
    Length:650
    Mass (Da):71,241
    Last modified:May 29, 2007 - v2
    Checksum:iFBE109C14A28B925
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti180 – 1801A → T in AAI05183. 1 PublicationCurated
    Sequence conflicti543 – 5431E → K in CAA37422. (PubMed:2216746)Curated
    Sequence conflicti543 – 5431E → K in CAA37823. (PubMed:2216746)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53827 mRNA. Translation: CAA37823.1.
    X53335 mRNA. Translation: CAA37422.1.
    BT030487 mRNA. Translation: ABQ12927.1.
    BC105182 mRNA. Translation: AAI05183.1.
    PIRiS11456.
    RefSeqiNP_776770.2. NM_174345.4.
    UniGeneiBt.12309.

    Genome annotation databases

    EnsembliENSBTAT00000017497; ENSBTAP00000017497; ENSBTAG00000013162.
    GeneIDi281831.
    KEGGibta:281831.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53827 mRNA. Translation: CAA37823.1 .
    X53335 mRNA. Translation: CAA37422.1 .
    BT030487 mRNA. Translation: ABQ12927.1 .
    BC105182 mRNA. Translation: AAI05183.1 .
    PIRi S11456.
    RefSeqi NP_776770.2. NM_174345.4.
    UniGenei Bt.12309.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ATR X-ray 2.34 A 1-386 [» ]
    1ATS X-ray 2.43 A 1-386 [» ]
    1BA0 X-ray 1.90 A 1-386 [» ]
    1BA1 X-ray 1.70 A 1-386 [» ]
    1BUP X-ray 1.70 A 1-386 [» ]
    1HPM X-ray 1.70 A 1-386 [» ]
    1HX1 X-ray 1.90 A 4-381 [» ]
    1KAX X-ray 1.70 A 1-381 [» ]
    1KAY X-ray 1.70 A 1-381 [» ]
    1KAZ X-ray 1.70 A 1-381 [» ]
    1NGA X-ray 2.18 A 1-386 [» ]
    1NGB X-ray 2.18 A 1-386 [» ]
    1NGC X-ray 2.20 A 1-386 [» ]
    1NGD X-ray 2.18 A 1-386 [» ]
    1NGE X-ray 2.05 A 1-386 [» ]
    1NGF X-ray 2.17 A 1-386 [» ]
    1NGG X-ray 2.19 A 1-386 [» ]
    1NGH X-ray 2.23 A 1-386 [» ]
    1NGI X-ray 2.15 A 1-386 [» ]
    1NGJ X-ray 2.10 A 1-386 [» ]
    1Q2G model - B 4-381 [» ]
    1QQM X-ray 1.90 A 4-381 [» ]
    1QQN X-ray 1.90 A 4-381 [» ]
    1QQO X-ray 1.90 A 4-381 [» ]
    1YUW X-ray 2.60 A 1-554 [» ]
    2BUP X-ray 1.70 A 1-381 [» ]
    2QW9 X-ray 1.85 A/B 1-394 [» ]
    2QWL X-ray 1.75 A/B 1-394 [» ]
    2QWM X-ray 1.86 A/B 1-394 [» ]
    2QWN X-ray 2.40 A 1-394 [» ]
    2QWO X-ray 1.70 A 1-394 [» ]
    2QWP X-ray 1.75 A 1-394 [» ]
    2QWQ X-ray 2.21 A 1-394 [» ]
    2QWR X-ray 2.21 A 1-394 [» ]
    3C7N X-ray 3.12 B 1-554 [» ]
    3HSC X-ray 1.93 A 1-386 [» ]
    4FL9 X-ray 1.90 A 1-554 [» ]
    ProteinModelPortali P19120.
    SMRi P19120. Positions 1-621.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 159144. 2 interactions.
    DIPi DIP-35481N.
    IntActi P19120. 6 interactions.
    MINTi MINT-157582.
    STRINGi 9913.ENSBTAP00000017497.

    Chemistry

    BindingDBi P19120.
    ChEMBLi CHEMBL1275213.

    Proteomic databases

    PaxDbi P19120.
    PRIDEi P19120.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000017497 ; ENSBTAP00000017497 ; ENSBTAG00000013162 .
    GeneIDi 281831.
    KEGGi bta:281831.

    Organism-specific databases

    CTDi 3312.

    Phylogenomic databases

    eggNOGi COG0443.
    GeneTreei ENSGT00750000117237.
    HOGENOMi HOG000228135.
    HOVERGENi HBG051845.
    InParanoidi P19120.
    KOi K03283.
    OMAi GENKIFT.
    OrthoDBi EOG7PCJGF.
    TreeFami TF105042.

    Enzyme and pathway databases

    Reactomei REACT_205580. HSF1-dependent transactivation.
    REACT_211255. GABA synthesis, release, reuptake and degradation.
    REACT_213591. Attenuation phase.
    REACT_214880. CHL1 interactions.
    REACT_218726. Regulation of HSF1-mediated heat shock response.
    REACT_227515. AUF1 (hnRNP D0) destabilizes mRNA.

    Miscellaneous databases

    EvolutionaryTracei P19120.
    NextBioi 20805740.
    PROi P19120.

    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 PS00297. HSP70_1. 1 hit.
    PS00329. HSP70_2. 1 hit.
    PS01036. HSP70_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the cDNA of a bovine 70 kilodalton heat shock cognate protein."
      Deluca-Flaherty C., McKay D.B.
      Nucleic Acids Res. 18:5569-5569(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain cortex.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. NIH - Mammalian Gene Collection (MGC) project
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Crossbred X Angus.
      Tissue: Ileum.
    4. "Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein."
      Flaherty K.M., de Luca-Flaherty C., McKay D.B.
      Nature 346:623-628(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-385 IN COMPLEX WITH ADP.
    5. "Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment."
      Flaherty K.M., Wilbanks S.M., Deluca-Flaherty C., McKay D.B.
      J. Biol. Chem. 269:12899-12907(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-385 IN COMPLEXES WITH ADP AND ATP.
    6. "Structural replacement of active site monovalent cations by the epsilon-amino group of lysine in the ATPase fragment of bovine Hsc70."
      Wilbanks S.M., McKay D.B.
      Biochemistry 37:7456-7462(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-385 IN COMPLEX WITH ADP.
    7. "The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change."
      Sousa M.C., McKay D.B.
      Biochemistry 37:15392-15399(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-381 IN COMPLEX WITH ADP.
    8. "Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein."
      Johnson E.R., McKay D.B.
      Biochemistry 38:10823-10830(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-381 OF MUTANTS.
    9. Cited for: X-RAY CRYSTALLOGRAPHY (3.12 ANGSTROMS) OF 2-554 IN COMPLEX WITH ADP.

    Entry informationi

    Entry nameiHSP7C_BOVIN
    AccessioniPrimary (citable) accession number: P19120
    Secondary accession number(s): A5D968, Q3MHM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 138 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3