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Database: UniProt
Entry: P19120
LinkDB: P19120
Original site: P19120 
ID   HSP7C_BOVIN             Reviewed;         650 AA.
AC   P19120; A5D968; Q3MHM4;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   22-APR-2020, entry version 189.
DE   RecName: Full=Heat shock cognate 71 kDa protein;
DE   AltName: Full=Heat shock 70 kDa protein 8;
GN   Name=HSPA8; Synonyms=HSC70;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain cortex;
RX   PubMed=2216746; DOI=10.1093/nar/18.18.5569;
RA   Deluca-Flaherty C., McKay D.B.;
RT   "Nucleotide sequence of the cDNA of a bovine 70 kilodalton heat shock
RT   cognate protein.";
RL   Nucleic Acids Res. 18:5569-5569(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-385 IN COMPLEX WITH ADP.
RX   PubMed=2143562; DOI=10.1038/346623a0;
RA   Flaherty K.M., de Luca-Flaherty C., McKay D.B.;
RT   "Three-dimensional structure of the ATPase fragment of a 70K heat-shock
RT   cognate protein.";
RL   Nature 346:623-628(1990).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-385 IN COMPLEXES WITH ADP AND
RP   ATP.
RX   PubMed=8175707;
RA   Flaherty K.M., Wilbanks S.M., Deluca-Flaherty C., McKay D.B.;
RT   "Structural basis of the 70-kilodalton heat shock cognate protein ATP
RT   hydrolytic activity. II. Structure of the active site with ADP or ATP bound
RT   to wild type and mutant ATPase fragment.";
RL   J. Biol. Chem. 269:12899-12907(1994).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-385 IN COMPLEX WITH ADP.
RX   PubMed=9585559; DOI=10.1021/bi973046m;
RA   Wilbanks S.M., McKay D.B.;
RT   "Structural replacement of active site monovalent cations by the epsilon-
RT   amino group of lysine in the ATPase fragment of bovine Hsc70.";
RL   Biochemistry 37:7456-7462(1998).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-381 IN COMPLEX WITH ADP.
RX   PubMed=9799500; DOI=10.1021/bi981510x;
RA   Sousa M.C., McKay D.B.;
RT   "The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate
RT   protein is essential for transducing the ATP-induced conformational
RT   change.";
RL   Biochemistry 37:15392-15399(1998).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-381 OF MUTANTS.
RX   PubMed=10451379; DOI=10.1021/bi990816g;
RA   Johnson E.R., McKay D.B.;
RT   "Mapping the role of active site residues for transducing an ATP-induced
RT   conformational change in the bovine 70-kDa heat shock cognate protein.";
RL   Biochemistry 38:10823-10830(1999).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (3.12 ANGSTROMS) OF 2-554 IN COMPLEX WITH ADP.
RX   PubMed=18550409; DOI=10.1016/j.molcel.2008.05.006;
RA   Schuermann J.P., Jiang J., Cuellar J., Llorca O., Wang L., Gimenez L.E.,
RA   Jin S., Taylor A.B., Demeler B., Morano K.A., Hart P.J., Valpuesta J.M.,
RA   Lafer E.M., Sousa R.;
RT   "Structure of the Hsp110:Hsc70 nucleotide exchange machine.";
RL   Mol. Cell 31:232-243(2008).
CC   -!- FUNCTION: Molecular chaperone implicated in a wide variety of cellular
CC       processes, including protection of the proteome from stress, folding
CC       and transport of newly synthesized polypeptides, activation of
CC       proteolysis of misfolded proteins and the formation and dissociation of
CC       protein complexes. Plays a pivotal role in the protein quality control
CC       system, ensuring the correct folding of proteins, the re-folding of
CC       misfolded proteins and controlling the targeting of proteins for
CC       subsequent degradation. This is achieved through cycles of ATP binding,
CC       ATP hydrolysis and ADP release, mediated by co-chaperones. The co-
CC       chaperones have been shown to not only regulate different steps of the
CC       ATPase cycle of HSP70, but they also have an individual specificity
CC       such that one co-chaperone may promote folding of a substrate while
CC       another may promote degradation. The affinity of HSP70 for polypeptides
CC       is regulated by its nucleotide bound state. In the ATP-bound form, it
CC       has a low affinity for substrate proteins. However, upon hydrolysis of
CC       the ATP to ADP, it undergoes a conformational change that increases its
CC       affinity for substrate proteins. HSP70 goes through repeated cycles of
CC       ATP hydrolysis and nucleotide exchange, which permits cycles of
CC       substrate binding and release. The HSP70-associated co-chaperones are
CC       of three types: J-domain co-chaperones HSP40s (stimulate ATPase
CC       hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as
CC       BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-
CC       bound state thereby promoting substrate release), and the TPR domain
CC       chaperones such as HOPX and STUB1. Acts as a repressor of
CC       transcriptional activation. Inhibits the transcriptional coactivator
CC       activity of CITED1 on Smad-mediated transcription. Component of the
CC       PRP19-CDC5L complex that forms an integral part of the spliceosome and
CC       is required for activating pre-mRNA splicing. May have a scaffolding
CC       role in the spliceosome assembly as it contacts all other components of
CC       the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates
CC       LPS-induced inflammatory response, including TNF secretion.
CC       Participates in the ER-associated degradation (ERAD) quality control
CC       pathway in conjunction with J domain-containing co-chaperones and the
CC       E3 ligase STUB1. {ECO:0000250|UniProtKB:P11142}.
CC   -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC       containing untranslated mRNAs (By similarity). Interacts with PACRG (By
CC       similarity). Interacts with HSPH1/HSP105 (By similarity). Interacts
CC       with IRAK1BP1 and BAG1 (By similarity). Interacts with DNAJC7 (By
CC       similarity). Interacts with DNAJB12 (via J domain) (By similarity).
CC       Interacts with DNAJB14 (via J domain) (By similarity). Interacts (via
CC       C-terminus) with the E3 ligase STUB1 forming a 210 kDa complex of one
CC       STUB1 and two HSPA8 molecules (By similarity). Interacts with CITED1
CC       (via N-terminus); the interaction suppresses the association of CITED1
CC       to p300/CBP and Smad-mediated transcription transactivation (By
CC       similarity). Component of the PRP19-CDC5L splicing complex composed of
CC       a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and
CC       BCAS2, and at least three less stably associated proteins CTNNBL1,
CC       CWC15 and HSPA8 (By similarity). Interacts with TRIM5 (By similarity).
CC       Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8,
CC       CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may
CC       have a histone H3-specific methyltransferase activity (By similarity).
CC       Interacts with METTL21A (By similarity). Following LPS binding, may
CC       form a complex with CXCR4, GDF5 and HSP90AA1 (By similarity). Interacts
CC       with PRKN (By similarity). Interacts with FOXP3 (By similarity).
CC       Interacts with DNAJC9 (via J domain) (By similarity). Interacts with
CC       MLLT11 (By similarity). Interacts with RNF207 (By similarity).
CC       Interacts with DNAJC21 (By similarity). Interacts with DNAJB2 (By
CC       similarity). Interacts with TTC1 (via TPR repeats) (By similarity).
CC       Interacts with SGTA (via TPR repeats) (By similarity). Interacts with
CC       HSF1 (via transactivation domain) (By similarity). Interacts with HOPX,
CC       STUB1, HSP40, HSP901, BAG2 and BAG3 (By similarity). Interacts with
CC       HSPC138 (By similarity). Interacts with ZMYND10 (By similarity).
CC       Interacts with VGF-derived peptide TLQP-21 (By similarity). Interacts
CC       with BCL2L1, GIMAP5 and MCL1; the interaction with BCL2L1 or MCL1 is
CC       impaired in the absence of GIMAP5 (By similarity). Interacts with
CC       NLPR12 (By similarity). Interacts with TTC4 (By similarity).
CC       {ECO:0000250|UniProtKB:P11142, ECO:0000250|UniProtKB:P63017,
CC       ECO:0000250|UniProtKB:P63018}.
CC   -!- INTERACTION:
CC       P19120; P13569: CFTR; Xeno; NbExp=2; IntAct=EBI-907802, EBI-349854;
CC       P19120; P26361: Cftr; Xeno; NbExp=5; IntAct=EBI-907802, EBI-6115317;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Melanosome
CC       {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Cell membrane
CC       {ECO:0000250}. Note=Localized in cytoplasmic mRNP granules containing
CC       untranslated mRNAs. Translocates rapidly from the cytoplasm to the
CC       nuclei, and especially to the nucleoli, upon heat shock (By
CC       similarity). {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- INDUCTION: Constitutively synthesized.
CC   -!- DOMAIN: The N-terminal nucleotide binding domain (NBD) (also known as
CC       the ATPase domain) is responsible for binding and hydrolyzing ATP. The
CC       C-terminal substrate-binding domain (SBD) (also known as peptide-
CC       binding domain) binds to the client/substrate proteins. The two domains
CC       are allosterically coupled so that, when ATP is bound to the NBD, the
CC       SBD binds relatively weakly to clients. When ADP is bound in the NBD, a
CC       conformational change enhances the affinity of the SBD for client
CC       proteins. {ECO:0000250|UniProtKB:P11142}.
CC   -!- PTM: Acetylated. {ECO:0000250|UniProtKB:P11142}.
CC   -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P11142}.
CC   -!- PTM: Trimethylation at Lys-561 reduces fibrillar SNCA binding.
CC       {ECO:0000250|UniProtKB:P11142}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
DR   EMBL; X53827; CAA37823.1; -; mRNA.
DR   EMBL; X53335; CAA37422.1; -; mRNA.
DR   EMBL; BT030487; ABQ12927.1; -; mRNA.
DR   EMBL; BC105182; AAI05183.1; -; mRNA.
DR   PIR; S11456; S11456.
DR   RefSeq; NP_776770.2; NM_174345.4.
DR   PDB; 1ATR; X-ray; 2.34 A; A=1-386.
DR   PDB; 1ATS; X-ray; 2.43 A; A=1-386.
DR   PDB; 1BA0; X-ray; 1.90 A; A=1-386.
DR   PDB; 1BA1; X-ray; 1.70 A; A=1-386.
DR   PDB; 1BUP; X-ray; 1.70 A; A=1-386.
DR   PDB; 1HPM; X-ray; 1.70 A; A=1-386.
DR   PDB; 1HX1; X-ray; 1.90 A; A=4-381.
DR   PDB; 1KAX; X-ray; 1.70 A; A=1-381.
DR   PDB; 1KAY; X-ray; 1.70 A; A=1-381.
DR   PDB; 1KAZ; X-ray; 1.70 A; A=1-381.
DR   PDB; 1NGA; X-ray; 2.18 A; A=1-386.
DR   PDB; 1NGB; X-ray; 2.18 A; A=1-386.
DR   PDB; 1NGC; X-ray; 2.20 A; A=1-386.
DR   PDB; 1NGD; X-ray; 2.18 A; A=1-386.
DR   PDB; 1NGE; X-ray; 2.05 A; A=1-386.
DR   PDB; 1NGF; X-ray; 2.17 A; A=1-386.
DR   PDB; 1NGG; X-ray; 2.19 A; A=1-386.
DR   PDB; 1NGH; X-ray; 2.23 A; A=1-386.
DR   PDB; 1NGI; X-ray; 2.15 A; A=1-386.
DR   PDB; 1NGJ; X-ray; 2.10 A; A=1-386.
DR   PDB; 1Q2G; Model; -; B=4-381.
DR   PDB; 1QQM; X-ray; 1.90 A; A=4-381.
DR   PDB; 1QQN; X-ray; 1.90 A; A=4-381.
DR   PDB; 1QQO; X-ray; 1.90 A; A=4-381.
DR   PDB; 1YUW; X-ray; 2.60 A; A=1-554.
DR   PDB; 2BUP; X-ray; 1.70 A; A=1-381.
DR   PDB; 2QW9; X-ray; 1.85 A; A/B=1-394.
DR   PDB; 2QWL; X-ray; 1.75 A; A/B=1-394.
DR   PDB; 2QWM; X-ray; 1.86 A; A/B=1-394.
DR   PDB; 2QWN; X-ray; 2.40 A; A=1-394.
DR   PDB; 2QWO; X-ray; 1.70 A; A=1-394.
DR   PDB; 2QWP; X-ray; 1.75 A; A=1-394.
DR   PDB; 2QWQ; X-ray; 2.21 A; A=1-394.
DR   PDB; 2QWR; X-ray; 2.21 A; A=1-394.
DR   PDB; 3C7N; X-ray; 3.12 A; B=1-554.
DR   PDB; 3HSC; X-ray; 1.93 A; A=1-386.
DR   PDB; 4FL9; X-ray; 1.90 A; A=1-554.
DR   PDB; 6H54; X-ray; 2.02 A; A=1-554.
DR   PDBsum; 1ATR; -.
DR   PDBsum; 1ATS; -.
DR   PDBsum; 1BA0; -.
DR   PDBsum; 1BA1; -.
DR   PDBsum; 1BUP; -.
DR   PDBsum; 1HPM; -.
DR   PDBsum; 1HX1; -.
DR   PDBsum; 1KAX; -.
DR   PDBsum; 1KAY; -.
DR   PDBsum; 1KAZ; -.
DR   PDBsum; 1NGA; -.
DR   PDBsum; 1NGB; -.
DR   PDBsum; 1NGC; -.
DR   PDBsum; 1NGD; -.
DR   PDBsum; 1NGE; -.
DR   PDBsum; 1NGF; -.
DR   PDBsum; 1NGG; -.
DR   PDBsum; 1NGH; -.
DR   PDBsum; 1NGI; -.
DR   PDBsum; 1NGJ; -.
DR   PDBsum; 1Q2G; -.
DR   PDBsum; 1QQM; -.
DR   PDBsum; 1QQN; -.
DR   PDBsum; 1QQO; -.
DR   PDBsum; 1YUW; -.
DR   PDBsum; 2BUP; -.
DR   PDBsum; 2QW9; -.
DR   PDBsum; 2QWL; -.
DR   PDBsum; 2QWM; -.
DR   PDBsum; 2QWN; -.
DR   PDBsum; 2QWO; -.
DR   PDBsum; 2QWP; -.
DR   PDBsum; 2QWQ; -.
DR   PDBsum; 2QWR; -.
DR   PDBsum; 3C7N; -.
DR   PDBsum; 3HSC; -.
DR   PDBsum; 4FL9; -.
DR   PDBsum; 6H54; -.
DR   SMR; P19120; -.
DR   BioGrid; 159144; 2.
DR   DIP; DIP-35481N; -.
DR   IntAct; P19120; 8.
DR   MINT; P19120; -.
DR   STRING; 9913.ENSBTAP00000017497; -.
DR   BindingDB; P19120; -.
DR   ChEMBL; CHEMBL1275213; -.
DR   PaxDb; P19120; -.
DR   PeptideAtlas; P19120; -.
DR   PRIDE; P19120; -.
DR   Ensembl; ENSBTAT00000017497; ENSBTAP00000017497; ENSBTAG00000013162.
DR   GeneID; 281831; -.
DR   KEGG; bta:281831; -.
DR   CTD; 3312; -.
DR   VGNC; VGNC:54632; HSPA8.
DR   eggNOG; KOG0101; Eukaryota.
DR   eggNOG; COG0443; LUCA.
DR   GeneTree; ENSGT00950000183206; -.
DR   HOGENOM; CLU_005965_3_0_1; -.
DR   InParanoid; P19120; -.
DR   KO; K03283; -.
DR   OMA; CFNIKST; -.
DR   OrthoDB; 288077at2759; -.
DR   TreeFam; TF105042; -.
DR   Reactome; R-BTA-3371453; Regulation of HSF1-mediated heat shock response.
DR   Reactome; R-BTA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
DR   Reactome; R-BTA-3371568; Attenuation phase.
DR   Reactome; R-BTA-3371571; HSF1-dependent transactivation.
DR   Reactome; R-BTA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR   Reactome; R-BTA-6798695; Neutrophil degranulation.
DR   Reactome; R-BTA-72163; mRNA Splicing - Major Pathway.
DR   Reactome; R-BTA-8856828; Clathrin-mediated endocytosis.
DR   Reactome; R-BTA-8876725; Protein methylation.
DR   EvolutionaryTrace; P19120; -.
DR   PRO; PR:P19120; -.
DR   Proteomes; UP000009136; Chromosome 15.
DR   Bgee; ENSBTAG00000013162; Expressed in brain and 9 other tissues.
DR   ExpressionAtlas; P19120; baseline.
DR   GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR   GO; GO:0005764; C:lysosome; IBA:GO_Central.
DR   GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0099524; C:postsynaptic cytosol; IBA:GO_Central.
DR   GO; GO:0099523; C:presynaptic cytosol; IBA:GO_Central.
DR   GO; GO:0000974; C:Prp19 complex; ISS:UniProtKB.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR   GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATPase activity; IBA:GO_Central.
DR   GO; GO:0042623; F:ATPase activity, coupled; IBA:GO_Central.
DR   GO; GO:1990833; F:clathrin-uncoating ATPase activity; IBA:GO_Central.
DR   GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR   GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR   GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR   GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR   GO; GO:0008088; P:axo-dendritic transport; IBA:GO_Central.
DR   GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR   GO; GO:1904764; P:chaperone-mediated autophagy translocation complex disassembly; IBA:GO_Central.
DR   GO; GO:0061741; P:chaperone-mediated protein transport involved in chaperone-mediated autophagy; IBA:GO_Central.
DR   GO; GO:0061738; P:late endosomal microautophagy; IBA:GO_Central.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR   GO; GO:0061740; P:protein targeting to lysosome involved in chaperone-mediated autophagy; IBA:GO_Central.
DR   GO; GO:0006986; P:response to unfolded protein; IBA:GO_Central.
DR   GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR   GO; GO:1990832; P:slow axonal transport; IBA:GO_Central.
DR   GO; GO:0016191; P:synaptic vesicle uncoating; IDA:SynGO.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Cell membrane; Chaperone;
KW   Cytoplasm; Isopeptide bond; Membrane; Methylation; mRNA processing;
KW   mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Spliceosome; Stress response; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   CHAIN           2..650
FT                   /note="Heat shock cognate 71 kDa protein"
FT                   /id="PRO_0000078268"
FT   NP_BIND         12..15
FT                   /note="ATP"
FT   NP_BIND         202..204
FT                   /note="ATP"
FT   NP_BIND         268..275
FT                   /note="ATP"
FT   NP_BIND         339..342
FT                   /note="ATP"
FT   REGION          2..386
FT                   /note="Nucleotide-binding domain (NBD)"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   REGION          186..377
FT                   /note="Interaction with BAG1"
FT                   /evidence="ECO:0000250"
FT   REGION          394..509
FT                   /note="Substrate-binding domain (SBD)"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   BINDING         71
FT                   /note="ATP"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   MOD_RES         108
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P63017"
FT   MOD_RES         153
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   MOD_RES         246
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   MOD_RES         319
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   MOD_RES         319
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P63017"
FT   MOD_RES         328
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P63017"
FT   MOD_RES         329
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   MOD_RES         362
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   MOD_RES         469
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   MOD_RES         512
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P63017"
FT   MOD_RES         512
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P63017"
FT   MOD_RES         524
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P63017"
FT   MOD_RES         541
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   MOD_RES         561
FT                   /note="N6,N6,N6-trimethyllysine; by METTL21A; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   MOD_RES         561
FT                   /note="N6,N6-dimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   MOD_RES         589
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   MOD_RES         597
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   MOD_RES         601
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   CROSSLNK        512
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   CROSSLNK        512
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P11142"
FT   CONFLICT        180
FT                   /note="A -> T (in Ref. 3; AAI05183)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        543
FT                   /note="E -> K (in Ref. 1; CAA37422/CAA37823)"
FT                   /evidence="ECO:0000305"
FT   STRAND          7..10
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   STRAND          13..22
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   STRAND          25..28
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   STRAND          36..39
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   STRAND          42..44
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   STRAND          49..51
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   HELIX           53..56
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   TURN            57..61
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   HELIX           63..65
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   STRAND          66..68
FT                   /evidence="ECO:0000244|PDB:4FL9"
FT   HELIX           70..72
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   TURN            73..75
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   HELIX           81..87
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   STRAND          91..97
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   STRAND          100..107
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   STRAND          110..114
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   HELIX           116..135
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   STRAND          141..146
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   HELIX           152..164
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   STRAND          168..174
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   HELIX           175..182
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   TURN            183..186
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   STRAND          187..191
FT                   /evidence="ECO:0000244|PDB:2QWL"
FT   STRAND          193..200
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   STRAND          205..213
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   STRAND          216..225
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   HELIX           230..249
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   HELIX           253..255
FT                   /evidence="ECO:0000244|PDB:4FL9"
FT   HELIX           257..273
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   TURN            274..276
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   STRAND          277..288
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   STRAND          291..298
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   HELIX           299..312
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   HELIX           314..323
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   HELIX           328..330
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   STRAND          333..338
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   HELIX           339..342
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   HELIX           344..353
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   TURN            354..356
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   HELIX           365..367
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   HELIX           368..380
FT                   /evidence="ECO:0000244|PDB:1BA1"
FT   STRAND          386..388
FT                   /evidence="ECO:0000244|PDB:2QWO"
FT   STRAND          392..396
FT                   /evidence="ECO:0000244|PDB:3C7N"
FT   STRAND          401..405
FT                   /evidence="ECO:0000244|PDB:4FL9"
FT   TURN            406..408
FT                   /evidence="ECO:0000244|PDB:4FL9"
FT   STRAND          409..414
FT                   /evidence="ECO:0000244|PDB:4FL9"
FT   STRAND          419..432
FT                   /evidence="ECO:0000244|PDB:4FL9"
FT   STRAND          438..446
FT                   /evidence="ECO:0000244|PDB:4FL9"
FT   HELIX           450..452
FT                   /evidence="ECO:0000244|PDB:4FL9"
FT   STRAND          453..461
FT                   /evidence="ECO:0000244|PDB:4FL9"
FT   STRAND          474..480
FT                   /evidence="ECO:0000244|PDB:4FL9"
FT   STRAND          486..492
FT                   /evidence="ECO:0000244|PDB:4FL9"
FT   TURN            493..495
FT                   /evidence="ECO:0000244|PDB:4FL9"
FT   STRAND          498..503
FT                   /evidence="ECO:0000244|PDB:4FL9"
FT   HELIX           512..524
FT                   /evidence="ECO:0000244|PDB:4FL9"
FT   HELIX           526..534
FT                   /evidence="ECO:0000244|PDB:4FL9"
FT   STRAND          539..542
FT                   /evidence="ECO:0000244|PDB:4FL9"
FT   HELIX           547..549
FT                   /evidence="ECO:0000244|PDB:4FL9"
SQ   SEQUENCE   650 AA;  71241 MW;  FBE109C14A28B925 CRC64;
     MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
     MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS
     SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA
     IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH
     FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA
     RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN
     KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI
     PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI
     DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN
     SLESYAFNMK ATVEDEKLQG KINDEDKQKI LDKCNEIINW LDKNQTAEKE EFEHQQKELE
     KVCNPIITKL YQSAGGMPGG MPGGMPGGFP GGGAPPSGGA SSGPTIEEVD
//
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