HS71A_MOUSE
ID HS71A_MOUSE Reviewed; 641 AA.
AC Q61696; Q61697; Q7TQD8; Q9QWJ5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Heat shock 70 kDa protein 1A;
DE AltName: Full=Heat shock 70 kDa protein 3;
DE Short=HSP70.3;
DE AltName: Full=Hsp68;
GN Name=Hspa1a; Synonyms=Hsp70-3, Hsp70A1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Liver;
RX PubMed=8076831; DOI=10.1016/0378-1119(94)90305-0;
RA Perry M.D., Aujame L., Shtang S., Moran L.A.;
RT "Structure and expression of an inducible HSP70-encoding gene from Mus
RT musculus.";
RL Gene 146:273-278(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129;
RX PubMed=14656967; DOI=10.1101/gr.1736803;
RA Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA Hood L.;
RT "Analysis of the gene-dense major histocompatibility complex class III
RT region and its comparison to mouse.";
RL Genome Res. 13:2621-2636(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 26-49 AND 103-112, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 221-641.
RX PubMed=2868009; DOI=10.1016/s0021-9258(17)35903-3;
RA Lowe D.G., Moran L.A.;
RT "Molecular cloning and analysis of DNA complementary to three mouse Mr =
RT 68,000 heat shock protein mRNAs.";
RL J. Biol. Chem. 261:2102-2112(1986).
RN [6]
RP INTERACTION WITH PGLYRP1, AND SUBCELLULAR LOCATION.
RX PubMed=14585845; DOI=10.1074/jbc.m307513200;
RA Sashchenko L.P., Dukhanina E.A., Yashin D.V., Shatalov Y.V., Romanova E.A.,
RA Korobko E.V., Demin A.V., Lukyanova T.I., Kabanova O.D., Khaidukov S.V.,
RA Kiselev S.L., Gabibov A.G., Gnuchev N.V., Georgiev G.P.;
RT "Peptidoglycan recognition protein tag7 forms a cytotoxic complex with heat
RT shock protein 70 in solution and in lymphocytes.";
RL J. Biol. Chem. 279:2117-2124(2004).
RN [7]
RP INTERACTION WITH DNAAF2.
RX PubMed=19052621; DOI=10.1038/nature07471;
RA Omran H., Kobayashi D., Olbrich H., Tsukahara T., Loges N.T., Hagiwara H.,
RA Zhang Q., Leblond G., O'Toole E., Hara C., Mizuno H., Kawano H.,
RA Fliegauf M., Yagi T., Koshida S., Miyawaki A., Zentgraf H., Seithe H.,
RA Reinhardt R., Watanabe Y., Kamiya R., Mitchell D.R., Takeda H.;
RT "Ktu/PF13 is required for cytoplasmic pre-assembly of axonemal dyneins.";
RL Nature 456:611-616(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH FOXP3.
RX PubMed=23973223; DOI=10.1016/j.immuni.2013.08.006;
RA Chen Z., Barbi J., Bu S., Yang H.Y., Li Z., Gao Y., Jinasena D., Fu J.,
RA Lin F., Chen C., Zhang J., Yu N., Li X., Shan Z., Nie J., Gao Z., Tian H.,
RA Li Y., Yao Z., Zheng Y., Park B.V., Pan Z., Zhang J., Dang E., Li Z.,
RA Wang H., Luo W., Li L., Semenza G.L., Zheng S.G., Loser K., Tsun A.,
RA Greene M.I., Pardoll D.M., Pan F., Li B.;
RT "The ubiquitin ligase Stub1 negatively modulates regulatory T cell
RT suppressive activity by promoting degradation of the transcription factor
RT Foxp3.";
RL Immunity 39:272-285(2013).
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, but they also have an individual specificity such that
CC one co-chaperone may promote folding of a substrate while another may
CC promote degradation. The affinity for polypeptides is regulated by its
CC nucleotide bound state. In the ATP-bound form, it has a low affinity
CC for substrate proteins. However, upon hydrolysis of the ATP to ADP, it
CC undergoes a conformational change that increases its affinity for
CC substrate proteins. It goes through repeated cycles of ATP hydrolysis
CC and nucleotide exchange, which permits cycles of substrate binding and
CC release. The co-chaperones are of three types: J-domain co-chaperones
CC such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide
CC exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70
CC from the ADP-bound to the ATP-bound state thereby promoting substrate
CC release), and the TPR domain chaperones such as HOPX and STUB1.
CC Maintains protein homeostasis during cellular stress through two
CC opposing mechanisms: protein refolding and degradation. Its
CC acetylation/deacetylation state determines whether it functions in
CC protein refolding or protein degradation by controlling the competitive
CC binding of co-chaperones HOPX and STUB1. During the early stress
CC response, the acetylated form binds to HOPX which assists in chaperone-
CC mediated protein refolding, thereafter, it is deacetylated and binds to
CC ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein
CC degradation. Regulates centrosome integrity during mitosis, and is
CC required for the maintenance of a functional mitotic centrosome that
CC supports the assembly of a bipolar mitotic spindle. Enhances STUB1-
CC mediated SMAD3 ubiquitination and degradation and facilitates STUB1-
CC mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated
CC ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg)
CC during inflammation. Negatively regulates heat shock-induced HSF1
CC transcriptional activity during the attenuation and recovery phase
CC period of the heat shock response. {ECO:0000250|UniProtKB:P0DMV8}.
CC -!- SUBUNIT: Component of the CatSper complex (By similarity). Identified
CC in a IGF2BP1-dependent mRNP granule complex containing untranslated
CC mRNAs (By similarity). Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C
CC and TSC2 (By similarity). Interacts with TERT; the interaction occurs
CC in the absence of the RNA component, TERC, and dissociates once the
CC TERT complex has formed (By similarity). Interacts with METTL21A (By
CC similarity). Interacts with DNAAF2 (PubMed:19052621). Interacts with
CC TRIM5 (via B30.2/SPRY domain) (By similarity). Interacts with PRKN (By
CC similarity). Interacts with FOXP3 (PubMed:23973223). Interacts with
CC NOD2; the interaction enhances NOD2 stability (By similarity).
CC Interacts with DNAJC9 (via J domain) (By similarity). Interacts with
CC ATF5; the interaction protects ATF5 from degradation via proteasome-
CC dependent and caspase-dependent processes (By similarity). Interacts
CC with RNF207 (via the C-terminus); this interaction additively increases
CC KCNH2 expression (By similarity). Interacts with HSF1 (via
CC transactivation domain); this interaction results in the inhibition of
CC heat shock- and HSF1-induced transcriptional activity during the
CC attenuation and recovery phase period of the heat shock response.
CC Interacts with NAA10, HSP40, HSP90 and HDAC4. The acetylated form and
CC the non-acetylated form interact with HOPX and STUB1 respectively.
CC Interacts with NEDD1 and SMAD3. Interacts (via NBD) with BAG1, BAG2,
CC BAG3 and HSPH1/HSP105. Interacts with DNAJC8 (By similarity). Interacts
CC with NLRP12. Interacts with PGLYRP (PubMed:14585845).
CC {ECO:0000250|UniProtKB:P0DMV8, ECO:0000269|PubMed:14585845,
CC ECO:0000269|PubMed:19052621, ECO:0000269|PubMed:23973223}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0DMV8}. Nucleus
CC {ECO:0000250|UniProtKB:P0DMV8}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:P0DMV8}. Secreted
CC {ECO:0000269|PubMed:14585845}. Note=Localized in cytoplasmic mRNP
CC granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P0DMV8}.
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:P0DMV8}.
CC -!- PTM: In response to cellular stress, acetylated at Lys-77 by NA110 and
CC then gradually deacetylated by HDAC4 at later stages. Acetylation
CC enhances its chaperone activity and also determines whether it will
CC function as a chaperone for protein refolding or degradation by
CC controlling its binding to co-chaperones HOPX and STUB1. The acetylated
CC form and the non-acetylated form bind to HOPX and STUB1 respectively.
CC Acetylation also protects cells against various types of cellular
CC stress. {ECO:0000250|UniProtKB:P0DMV8}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; M76613; AAA57233.1; -; Genomic_DNA.
DR EMBL; AF109906; AAC84169.1; -; Genomic_DNA.
DR EMBL; BC054782; AAH54782.1; -; mRNA.
DR EMBL; M12571; AAA57234.1; -; mRNA.
DR EMBL; M12572; AAA57235.1; -; mRNA.
DR CCDS; CCDS50080.1; -.
DR PIR; A26283; A26283.
DR RefSeq; NP_034609.2; NM_010479.2.
DR AlphaFoldDB; Q61696; -.
DR SMR; Q61696; -.
DR BioGRID; 228756; 29.
DR CORUM; Q61696; -.
DR IntAct; Q61696; 6.
DR MINT; Q61696; -.
DR STRING; 10090.ENSMUSP00000084586; -.
DR CarbonylDB; Q61696; -.
DR iPTMnet; Q61696; -.
DR PhosphoSitePlus; Q61696; -.
DR REPRODUCTION-2DPAGE; Q61696; -.
DR EPD; Q61696; -.
DR jPOST; Q61696; -.
DR MaxQB; Q61696; -.
DR PaxDb; Q61696; -.
DR PRIDE; Q61696; -.
DR ProteomicsDB; 273139; -.
DR DNASU; 193740; -.
DR Ensembl; ENSMUST00000087328; ENSMUSP00000084586; ENSMUSG00000091971.
DR GeneID; 193740; -.
DR KEGG; mmu:193740; -.
DR UCSC; uc008cep.1; mouse.
DR CTD; 3303; -.
DR MGI; MGI:96244; Hspa1a.
DR VEuPathDB; HostDB:ENSMUSG00000091971; -.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00940000161215; -.
DR HOGENOM; CLU_005965_3_0_1; -.
DR InParanoid; Q61696; -.
DR OMA; VNEAESY; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; Q61696; -.
DR TreeFam; TF105042; -.
DR Reactome; R-MMU-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-MMU-3371568; Attenuation phase.
DR Reactome; R-MMU-3371571; HSF1-dependent transactivation.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 193740; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Hspa1a; mouse.
DR PRO; PR:Q61696; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q61696; protein.
DR Bgee; ENSMUSG00000091971; Expressed in substantia propria of cornea and 195 other tissues.
DR ExpressionAtlas; Q61696; baseline and differential.
DR Genevisible; Q61696; MM.
DR GO; GO:0016235; C:aggresome; ISO:MGI.
DR GO; GO:0005814; C:centriole; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0008180; C:COP9 signalosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016234; C:inclusion body; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISS:MGI.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0140545; F:ATP-dependent protein disaggregase activity; ISO:MGI.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0055131; F:C3HC4-type RING finger domain binding; ISO:MGI.
DR GO; GO:0031249; F:denatured protein binding; ISO:MGI.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0001664; F:G protein-coupled receptor binding; ISO:MGI.
DR GO; GO:0031072; F:heat shock protein binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0051787; F:misfolded protein binding; ISO:MGI.
DR GO; GO:0044183; F:protein folding chaperone; IDA:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0051082; F:unfolded protein binding; ISO:MGI.
DR GO; GO:0046034; P:ATP metabolic process; ISO:MGI.
DR GO; GO:0070370; P:cellular heat acclimation; ISO:MGI.
DR GO; GO:0034605; P:cellular response to heat; ISO:MGI.
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:0006281; P:DNA repair; IMP:MGI.
DR GO; GO:0007041; P:lysosomal transport; IMP:UniProtKB.
DR GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0060548; P:negative regulation of cell death; ISO:MGI.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:MGI.
DR GO; GO:0090084; P:negative regulation of inclusion body assembly; ISO:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0097201; P:negative regulation of transcription from RNA polymerase II promoter in response to stress; ISS:UniProtKB.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; ISO:MGI.
DR GO; GO:0090063; P:positive regulation of microtubule nucleation; ISS:UniProtKB.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0070434; P:positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; ISO:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; ISO:MGI.
DR GO; GO:0006457; P:protein folding; IDA:UniProtKB.
DR GO; GO:0042026; P:protein refolding; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISO:MGI.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; ISS:UniProtKB.
DR GO; GO:0031396; P:regulation of protein ubiquitination; ISO:MGI.
DR GO; GO:0009408; P:response to heat; IDA:MGI.
DR GO; GO:0006986; P:response to unfolded protein; ISS:UniProtKB.
DR GO; GO:0000723; P:telomere maintenance; IMP:MGI.
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 Acetylation; ATP-binding; Chaperone; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Methylation; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Secreted; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P0DMV8"
FT CHAIN 2..641
FT /note="Heat shock 70 kDa protein 1A"
FT /id="PRO_0000078250"
FT REGION 2..386
FT /note="Nucleotide-binding domain (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT REGION 394..509
FT /note="Substrate-binding domain (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT REGION 618..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 12..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 202..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 268..275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 339..342
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P0DMV8"
FT MOD_RES 77
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0DMV8"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0DMV8"
FT MOD_RES 246
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0DMV8"
FT MOD_RES 348
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0DMV8"
FT MOD_RES 469
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P0DMV8"
FT MOD_RES 561
FT /note="N6,N6,N6-trimethyllysine; by METTL21A; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0DMV8"
FT MOD_RES 561
FT /note="N6,N6-dimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0DMV8"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DMV8"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DMV8"
FT MOD_RES 636
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P0DMV8"
FT CONFLICT 221..225
FT /note="ATAGD -> TDGRT (in Ref. 5; AAA57234)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="G -> E (in Ref. 5; AAA57234)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="F -> V (in Ref. 5; AAA57234)"
FT /evidence="ECO:0000305"
FT CONFLICT 238..244
FT /note="VSHFVEE -> EDLREQ (in Ref. 5; AAA57234)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="T -> R (in Ref. 5; AAA57234)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="H -> Q (in Ref. 5; AAA57234)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="R -> A (in Ref. 1; AAA57233)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="V -> G (in Ref. 5; AAA57235)"
FT /evidence="ECO:0000305"
FT CONFLICT 413..416
FT /note="LIKR -> RHQA (in Ref. 5; AAA57234/AAA57235)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="S -> T (in Ref. 3; AAH54782)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 641 AA; 70079 MW; F49C33E602EAE334 CRC64;
MAKNTAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
LNPQNTVFDA KRLIGRKFGD AVVQSDMKHW PFQVVNDGDK PKVQVNYKGE SRSFFPEEIS
SMVLTKMKEI AEAYLGHPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA
IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVSH
FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA
RFEELCSDLF RGTLEPVEKA LRDAKMDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN
KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT RDNNLLGRFE LSGIPPAPRG VPQIEVTFDI
DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAERYKAEDE VQRDRVAAKN
ALESYAFNMK SAVEDEGLKG KLSEADKKKV LDKCQEVISW LDSNTLADKE EFVHKREELE
RVCSPIISGL YQGAGAPGAG GFGAQAPKGA SGSGPTIEEV D
