HSP7C_BOVIN
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 03-AUG-2022, entry version 200.
DE RecName: Full=Heat shock cognate 71 kDa protein;
DE EC=3.6.4.10 {ECO:0000250|UniProtKB:P11142};
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; DOI=10.1016/s0021-9258(18)99961-8;
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. Plays a critical role in
CC mitochondrial import, delivers preproteins to the mitochondrial import
CC receptor TOMM70. Acts as a repressor of transcriptional activation.
CC Inhibits the transcriptional coactivator activity of CITED1 on Smad-
CC mediated transcription. Component of the PRP19-CDC5L complex that forms
CC an integral part of the spliceosome and is required for activating pre-
CC mRNA splicing. May have a scaffolding role in the spliceosome assembly
CC as it contacts all other components of the core complex. Binds
CC bacterial lipopolysaccharide (LPS) and mediates LPS-induced
CC inflammatory response, including TNF secretion by monocytes.
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. Interacts with VGF-derived peptide TLQP-21.
CC {ECO:0000250|UniProtKB:P11142}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.10;
CC Evidence={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). Interacts
CC with TOMM70; the interaction is required for preprotein mitochondrial
CC import (By similarity). May interact with DNJC9; the interaction seems
CC to be histone-dependent (By similarity). {ECO:0000250|UniProtKB:P11142,
CC ECO:0000250|UniProtKB:P63017, 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}.
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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; 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; 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 AlphaFoldDB; P19120; -.
DR BMRB; P19120; -.
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 VEuPathDB; HostDB:ENSBTAG00000013162; -.
DR VGNC; VGNC:54632; HSPA8.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00950000183206; -.
DR HOGENOM; CLU_005965_3_0_1; -.
DR InParanoid; P19120; -.
DR OrthoDB; 288077at2759; -.
DR TreeFam; TF105042; -.
DR EvolutionaryTrace; P19120; -.
DR PRO; PR:P19120; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000013162; Expressed in prefrontal cortex and 100 other tissues.
DR ExpressionAtlas; P19120; baseline.
DR GO; GO:0005776; C:autophagosome; 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:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
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: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: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: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; IPR043129; ATPase_NBD.
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 SUPFAM; SSF53067; SSF53067; 2.
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; Hydrolase; Isopeptide bond; Membrane; Methylation;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Spliceosome;
KW Stress response; Transcription; 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 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 REGION 614..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 12..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 202..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 268..275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 339..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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:0007829|PDB:1BA1"
FT STRAND 13..22
FT /evidence="ECO:0007829|PDB:1BA1"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:1BA1"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:1BA1"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1BA1"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1BA1"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:1BA1"
FT TURN 57..61
FT /evidence="ECO:0007829|PDB:1BA1"
FT HELIX 63..65
FT /evidence="ECO:0007829|PDB:1BA1"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4FL9"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:1BA1"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:1BA1"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:1BA1"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:1BA1"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:1BA1"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:1BA1"
FT HELIX 116..135
FT /evidence="ECO:0007829|PDB:1BA1"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:1BA1"
FT HELIX 152..164
FT /evidence="ECO:0007829|PDB:1BA1"
FT STRAND 168..174
FT /evidence="ECO:0007829|PDB:1BA1"
FT HELIX 175..182
FT /evidence="ECO:0007829|PDB:1BA1"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:1BA1"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:2QWL"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:1BA1"
FT STRAND 205..213
FT /evidence="ECO:0007829|PDB:1BA1"
FT STRAND 216..225
FT /evidence="ECO:0007829|PDB:1BA1"
FT HELIX 230..249
FT /evidence="ECO:0007829|PDB:1BA1"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:4FL9"
FT HELIX 257..273
FT /evidence="ECO:0007829|PDB:1BA1"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:1BA1"
FT STRAND 277..288
FT /evidence="ECO:0007829|PDB:1BA1"
FT STRAND 291..298
FT /evidence="ECO:0007829|PDB:1BA1"
FT HELIX 299..312
FT /evidence="ECO:0007829|PDB:1BA1"
FT HELIX 314..323
FT /evidence="ECO:0007829|PDB:1BA1"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:1BA1"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:1BA1"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:1BA1"
FT HELIX 344..353
FT /evidence="ECO:0007829|PDB:1BA1"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:1BA1"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:1BA1"
FT HELIX 368..380
FT /evidence="ECO:0007829|PDB:1BA1"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:2QWO"
FT STRAND 392..396
FT /evidence="ECO:0007829|PDB:3C7N"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:4FL9"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:4FL9"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:4FL9"
FT STRAND 419..432
FT /evidence="ECO:0007829|PDB:4FL9"
FT STRAND 438..446
FT /evidence="ECO:0007829|PDB:4FL9"
FT HELIX 450..452
FT /evidence="ECO:0007829|PDB:4FL9"
FT STRAND 453..461
FT /evidence="ECO:0007829|PDB:4FL9"
FT STRAND 474..480
FT /evidence="ECO:0007829|PDB:4FL9"
FT STRAND 486..492
FT /evidence="ECO:0007829|PDB:4FL9"
FT TURN 493..495
FT /evidence="ECO:0007829|PDB:4FL9"
FT STRAND 498..503
FT /evidence="ECO:0007829|PDB:4FL9"
FT HELIX 512..524
FT /evidence="ECO:0007829|PDB:4FL9"
FT HELIX 526..534
FT /evidence="ECO:0007829|PDB:4FL9"
FT STRAND 539..542
FT /evidence="ECO:0007829|PDB:4FL9"
FT HELIX 547..549
FT /evidence="ECO:0007829|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
