HSP72_HUMAN
ID HSP72_HUMAN Reviewed; 639 AA.
AC P54652; Q15508; Q53XM3; Q9UE78;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Heat shock-related 70 kDa protein 2;
DE Short=Heat shock 70 kDa protein 2;
GN Name=HSPA2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7829106; DOI=10.1006/geno.1994.1462;
RA Bonnycastle L.L.C., Yu C.-E., Hunt C.R., Trask B.J., Clancy K.P.,
RA Weber J.L., Patterson D., Schellenberg G.D.;
RT "Cloning, sequencing, and mapping of the human chromosome 14 heat shock
RT protein gene (HSPA2).";
RL Genomics 23:85-93(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Goralski T.J., Krensky A.M.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-191 AND GLU-496.
RG NIEHS SNPs program;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Eye;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-126.
RX PubMed=7849706; DOI=10.1093/hmg/3.10.1819;
RA Roux A.-F., Nguyen V.T.T., Squire J.A., Cox D.W.;
RT "A heat shock gene at 14q22: mapping and expression.";
RL Hum. Mol. Genet. 3:1819-1822(1994).
RN [7]
RP INTERACTION WITH FKBP6.
RX PubMed=18529014; DOI=10.1021/bi8001506;
RA Jarczowski F., Fischer G., Edlich F.;
RT "FKBP36 forms complexes with clathrin and Hsp72 in spermatocytes.";
RL Biochemistry 47:6946-6952(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP METHYLATION AT LYS-564, AND MUTAGENESIS OF LYS-564.
RX PubMed=23921388; DOI=10.1074/jbc.m113.483248;
RA Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S.,
RA Melki R., Falnes P.O.;
RT "Identification and characterization of a novel human methyltransferase
RT modulating Hsp70 function through lysine methylation.";
RL J. Biol. Chem. 288:27752-27763(2013).
RN [10]
RP REVIEW.
RX PubMed=26865365; DOI=10.1007/s12192-016-0676-6;
RA Radons J.;
RT "The human HSP70 family of chaperones: where do we stand?";
RL Cell Stress Chaperones 21:379-404(2016).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 6-386 IN COMPLEX WITH ADP AND
RP PHOSPHATE.
RX PubMed=20072699; DOI=10.1371/journal.pone.0008625;
RA Wisniewska M., Karlberg T., Lehtio L., Johansson I., Kotenyova T.,
RA Moche M., Schuler H.;
RT "Crystal structures of the ATPase domains of four human Hsp70 isoforms:
RT HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78.";
RL PLoS ONE 5:E8625-E8625(2010).
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 affinity
CC for polypeptides is regulated by its nucleotide bound state. In the
CC ATP-bound form, it has a low affinity for substrate proteins. However,
CC upon hydrolysis of the ATP to ADP, it undergoes a conformational change
CC that increases its affinity for substrate proteins. It goes through
CC repeated cycles of ATP hydrolysis and nucleotide exchange, which
CC permits cycles of substrate binding and release (PubMed:26865365).
CC Plays a role in spermatogenesis. In association with SHCBP1L may
CC participate in the maintenance of spindle integrity during meiosis in
CC male germ cells (By similarity). {ECO:0000250|UniProtKB:P17156,
CC ECO:0000303|PubMed:26865365}.
CC -!- SUBUNIT: Interacts with FKBP6 (PubMed:18529014). Interacts with ZNF541.
CC Component of the CatSper complex. Interacts with RABL2/RABL2A; binds
CC preferentially to GTP-bound RABL2. Interacts with SHCBP1L; this
CC interaction may promote the recruitment of HSPA2 to the spindle (By
CC similarity). Interacts with FKBP6 (PubMed:18529014).
CC {ECO:0000250|UniProtKB:P17156, ECO:0000269|PubMed:18529014}.
CC -!- INTERACTION:
CC P54652; Q6DHV7-2: ADAL; NbExp=3; IntAct=EBI-356991, EBI-18899653;
CC P54652; Q96MA6: AK8; NbExp=3; IntAct=EBI-356991, EBI-8466265;
CC P54652; Q66PJ3-4: ARL6IP4; NbExp=3; IntAct=EBI-356991, EBI-5280499;
CC P54652; Q96DX5: ASB9; NbExp=3; IntAct=EBI-356991, EBI-745641;
CC P54652; Q9UBL3: ASH2L; NbExp=3; IntAct=EBI-356991, EBI-540797;
CC P54652; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-356991, EBI-9089489;
CC P54652; O95429: BAG4; NbExp=5; IntAct=EBI-356991, EBI-2949658;
CC P54652; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-356991, EBI-742750;
CC P54652; Q9NNX6-10: CD209; NbExp=3; IntAct=EBI-356991, EBI-12300031;
CC P54652; Q9Y4F5-3: CEP170B; NbExp=3; IntAct=EBI-356991, EBI-12950757;
CC P54652; Q8WUX9: CHMP7; NbExp=3; IntAct=EBI-356991, EBI-749253;
CC P54652; Q96EY1-3: DNAJA3; NbExp=3; IntAct=EBI-356991, EBI-11526226;
CC P54652; A0A024RCP2: DOM3Z; NbExp=3; IntAct=EBI-356991, EBI-25847826;
CC P54652; Q92782-2: DPF1; NbExp=3; IntAct=EBI-356991, EBI-23669343;
CC P54652; Q53R41: FASTKD1; NbExp=3; IntAct=EBI-356991, EBI-3957005;
CC P54652; Q9NSA1: FGF21; NbExp=4; IntAct=EBI-356991, EBI-3909329;
CC P54652; P15407: FOSL1; NbExp=3; IntAct=EBI-356991, EBI-744510;
CC P54652; Q06547-2: GABPB1; NbExp=3; IntAct=EBI-356991, EBI-618189;
CC P54652; Q06547-3: GABPB1; NbExp=3; IntAct=EBI-356991, EBI-9088619;
CC P54652; Q9NZL4: HSPBP1; NbExp=7; IntAct=EBI-356991, EBI-356763;
CC P54652; P42858: HTT; NbExp=3; IntAct=EBI-356991, EBI-466029;
CC P54652; Q0VD86: INCA1; NbExp=3; IntAct=EBI-356991, EBI-6509505;
CC P54652; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-356991, EBI-743960;
CC P54652; Q6P597: KLC3; NbExp=3; IntAct=EBI-356991, EBI-1643885;
CC P54652; A0A0C4DGV4: LAMTOR5; NbExp=3; IntAct=EBI-356991, EBI-10173304;
CC P54652; Q92615: LARP4B; NbExp=3; IntAct=EBI-356991, EBI-1052558;
CC P54652; Q99683: MAP3K5; NbExp=3; IntAct=EBI-356991, EBI-476263;
CC P54652; P30301: MIP; NbExp=3; IntAct=EBI-356991, EBI-8449636;
CC P54652; Q13562: NEUROD1; NbExp=3; IntAct=EBI-356991, EBI-3908303;
CC P54652; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-356991, EBI-25830200;
CC P54652; Q8N2H9-4: PELI3; NbExp=3; IntAct=EBI-356991, EBI-25852006;
CC P54652; O15534: PER1; NbExp=3; IntAct=EBI-356991, EBI-2557276;
CC P54652; Q58EX7-2: PLEKHG4; NbExp=3; IntAct=EBI-356991, EBI-21503705;
CC P54652; Q5SXH7-1: PLEKHS1; NbExp=3; IntAct=EBI-356991, EBI-26412802;
CC P54652; Q14181: POLA2; NbExp=3; IntAct=EBI-356991, EBI-712752;
CC P54652; Q9H1D9: POLR3F; NbExp=3; IntAct=EBI-356991, EBI-710067;
CC P54652; P79522: PRR3; NbExp=3; IntAct=EBI-356991, EBI-2803328;
CC P54652; Q92530: PSMF1; NbExp=3; IntAct=EBI-356991, EBI-945916;
CC P54652; Q9HD47-3: RANGRF; NbExp=3; IntAct=EBI-356991, EBI-9089733;
CC P54652; Q9NUC0: SERTAD4; NbExp=3; IntAct=EBI-356991, EBI-1773811;
CC P54652; Q9UHI5: SLC7A8; NbExp=3; IntAct=EBI-356991, EBI-13292283;
CC P54652; O14544: SOCS6; NbExp=3; IntAct=EBI-356991, EBI-3929549;
CC P54652; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-356991, EBI-10696971;
CC P54652; Q496A3: SPATS1; NbExp=3; IntAct=EBI-356991, EBI-3923692;
CC P54652; P05455: SSB; NbExp=3; IntAct=EBI-356991, EBI-358037;
CC P54652; O60506-4: SYNCRIP; NbExp=3; IntAct=EBI-356991, EBI-11123832;
CC P54652; Q7Z7C8-2: TAF8; NbExp=3; IntAct=EBI-356991, EBI-9089028;
CC P54652; Q8N0U2: TMEM61; NbExp=3; IntAct=EBI-356991, EBI-25830583;
CC P54652; O00635: TRIM38; NbExp=4; IntAct=EBI-356991, EBI-2130415;
CC P54652; O60636: TSPAN2; NbExp=3; IntAct=EBI-356991, EBI-3914288;
CC P54652; P49459: UBE2A; NbExp=3; IntAct=EBI-356991, EBI-2339348;
CC P54652; Q9NX94: WBP1L; NbExp=3; IntAct=EBI-356991, EBI-10316321;
CC P54652; Q9BRR0: ZKSCAN3; NbExp=3; IntAct=EBI-356991, EBI-1965777;
CC P54652; Q15973: ZNF124; NbExp=3; IntAct=EBI-356991, EBI-2555767;
CC P54652; Q8WUU4: ZNF296; NbExp=3; IntAct=EBI-356991, EBI-8834821;
CC P54652; Q9BYN7-2: ZNF341; NbExp=3; IntAct=EBI-356991, EBI-16435478;
CC P54652; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-356991, EBI-18036029;
CC P54652; Q96BE0; NbExp=2; IntAct=EBI-356991, EBI-9356686;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P17156}. Note=Colocalizes with SHCBP1L at
CC spindle during the meiosis process. {ECO:0000250|UniProtKB:P17156}.
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:0000305|PubMed:26865365}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/hspa2/";
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DR EMBL; L26336; AAA52698.1; -; Genomic_DNA.
DR EMBL; U56725; AAD11466.1; -; mRNA.
DR EMBL; BT009815; AAP88817.1; -; mRNA.
DR EMBL; DQ489378; ABE96830.1; -; Genomic_DNA.
DR EMBL; BC001752; AAH01752.1; -; mRNA.
DR EMBL; BC036107; AAH36107.1; -; mRNA.
DR EMBL; AH006615; AAC50076.1; -; Genomic_DNA.
DR CCDS; CCDS9766.1; -.
DR PIR; A55719; A55719.
DR PIR; I37564; I37564.
DR RefSeq; NP_068814.2; NM_021979.3.
DR PDB; 3I33; X-ray; 1.30 A; A=6-386.
DR PDB; 4FSV; X-ray; 1.80 A; A=2-387.
DR PDB; 5FPD; X-ray; 1.97 A; A/B=4-386.
DR PDB; 5FPE; X-ray; 1.96 A; A/B=4-386.
DR PDB; 5FPM; X-ray; 1.96 A; A/B=4-386.
DR PDB; 5FPN; X-ray; 1.96 A; A/B=4-639.
DR PDBsum; 3I33; -.
DR PDBsum; 4FSV; -.
DR PDBsum; 5FPD; -.
DR PDBsum; 5FPE; -.
DR PDBsum; 5FPM; -.
DR PDBsum; 5FPN; -.
DR AlphaFoldDB; P54652; -.
DR SMR; P54652; -.
DR BioGRID; 109538; 542.
DR CORUM; P54652; -.
DR ELM; P54652; -.
DR IntAct; P54652; 120.
DR MINT; P54652; -.
DR STRING; 9606.ENSP00000378199; -.
DR BindingDB; P54652; -.
DR ChEMBL; CHEMBL2062348; -.
DR DrugBank; DB04216; Quercetin.
DR GlyConnect; 1303; 1 N-Linked glycan (1 site).
DR GlyGen; P54652; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; P54652; -.
DR MetOSite; P54652; -.
DR PhosphoSitePlus; P54652; -.
DR SwissPalm; P54652; -.
DR BioMuta; HSPA2; -.
DR DMDM; 1708307; -.
DR REPRODUCTION-2DPAGE; IPI00007702; -.
DR EPD; P54652; -.
DR jPOST; P54652; -.
DR MassIVE; P54652; -.
DR MaxQB; P54652; -.
DR PaxDb; P54652; -.
DR PeptideAtlas; P54652; -.
DR PRIDE; P54652; -.
DR ProteomicsDB; 56690; -.
DR Antibodypedia; 6; 280 antibodies from 35 providers.
DR DNASU; 3306; -.
DR Ensembl; ENST00000247207.7; ENSP00000247207.6; ENSG00000126803.10.
DR Ensembl; ENST00000394709.2; ENSP00000378199.1; ENSG00000126803.10.
DR GeneID; 3306; -.
DR KEGG; hsa:3306; -.
DR MANE-Select; ENST00000247207.7; ENSP00000247207.6; NM_021979.4; NP_068814.2.
DR UCSC; uc001xhj.4; human.
DR CTD; 3306; -.
DR DisGeNET; 3306; -.
DR GeneCards; HSPA2; -.
DR HGNC; HGNC:5235; HSPA2.
DR HPA; ENSG00000126803; Tissue enhanced (brain, skeletal muscle).
DR MIM; 140560; gene.
DR neXtProt; NX_P54652; -.
DR OpenTargets; ENSG00000126803; -.
DR PharmGKB; PA29501; -.
DR VEuPathDB; HostDB:ENSG00000126803; -.
DR eggNOG; KOG0101; Eukaryota.
DR GeneTree; ENSGT00940000154813; -.
DR HOGENOM; CLU_005965_3_0_1; -.
DR InParanoid; P54652; -.
DR OMA; GCKVQNA; -.
DR OrthoDB; 288077at2759; -.
DR PhylomeDB; P54652; -.
DR TreeFam; TF105042; -.
DR PathwayCommons; P54652; -.
DR Reactome; R-HSA-1221632; Meiotic synapsis.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-HSA-3371568; Attenuation phase.
DR SignaLink; P54652; -.
DR SIGNOR; P54652; -.
DR BioGRID-ORCS; 3306; 18 hits in 1080 CRISPR screens.
DR ChiTaRS; HSPA2; human.
DR EvolutionaryTrace; P54652; -.
DR GeneWiki; HSPA2; -.
DR GenomeRNAi; 3306; -.
DR Pharos; P54652; Tchem.
DR PRO; PR:P54652; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P54652; protein.
DR Bgee; ENSG00000126803; Expressed in inferior vagus X ganglion and 205 other tissues.
DR ExpressionAtlas; P54652; baseline and differential.
DR Genevisible; P54652; HS.
DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
DR GO; GO:0036128; C:CatSper complex; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0072687; C:meiotic spindle; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0000795; C:synaptonemal complex; IEA:Ensembl.
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:0051087; F:chaperone binding; IEA:Ensembl.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0051861; F:glycolipid binding; IEA:Ensembl.
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:0048156; F:tau protein binding; IEA:Ensembl.
DR GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
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:0007141; P:male meiosis I; IEA:Ensembl.
DR GO; GO:0007140; P:male meiotic nuclear division; TAS:ProtInc.
DR GO; GO:0090084; P:negative regulation of inclusion body assembly; IDA:UniProtKB.
DR GO; GO:1901896; P:positive regulation of ATPase-coupled calcium transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:0042026; P:protein refolding; IDA:UniProtKB.
DR GO; GO:0009409; P:response to cold; ISS:AgBase.
DR GO; GO:0009408; P:response to heat; ISS:AgBase.
DR GO; GO:0006986; P:response to unfolded protein; TAS:ProtInc.
DR GO; GO:0007286; P:spermatid development; TAS:ProtInc.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR GO; GO:0070194; P:synaptonemal complex disassembly; IEA:Ensembl.
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; ATP-binding; Chaperone; Cytoplasm; Cytoskeleton;
KW Differentiation; Methylation; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Spermatogenesis; Stress response.
FT CHAIN 1..639
FT /note="Heat shock-related 70 kDa protein 2"
FT /id="PRO_0000078258"
FT REGION 2..389
FT /note="Nucleotide-binding domain (NBD)"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT REGION 397..512
FT /note="Substrate-binding domain (SBD)"
FT /evidence="ECO:0000250|UniProtKB:P11142"
FT REGION 613..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 13..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 205..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 271..278
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 342..345
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14659"
FT MOD_RES 408
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14659"
FT MOD_RES 414
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14659"
FT MOD_RES 564
FT /note="N6,N6,N6-trimethyllysine; by METTL21A; in vitro"
FT /evidence="ECO:0000269|PubMed:23921388"
FT VARIANT 191
FT /note="C -> S (in dbSNP:rs45456191)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_032706"
FT VARIANT 496
FT /note="K -> E (in dbSNP:rs45447398)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_032707"
FT MUTAGEN 564
FT /note="K->A: Abolishes methylation by METTL21A."
FT /evidence="ECO:0000269|PubMed:23921388"
FT CONFLICT 14
FT /note="T -> P (in Ref. 5; AAH36107)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="Missing (in Ref. 6; AAC50076)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="E -> G (in Ref. 5; AAH36107)"
FT /evidence="ECO:0000305"
FT CONFLICT 266
FT /note="L -> S (in Ref. 2; AAD11466)"
FT /evidence="ECO:0000305"
FT STRAND 8..12
FT /evidence="ECO:0007829|PDB:3I33"
FT STRAND 14..23
FT /evidence="ECO:0007829|PDB:3I33"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:3I33"
FT STRAND 37..40
FT /evidence="ECO:0007829|PDB:3I33"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:3I33"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:3I33"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:3I33"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:3I33"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:4FSV"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:3I33"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:3I33"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:3I33"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:3I33"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:3I33"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:3I33"
FT HELIX 117..136
FT /evidence="ECO:0007829|PDB:3I33"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3I33"
FT HELIX 153..166
FT /evidence="ECO:0007829|PDB:3I33"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:3I33"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:3I33"
FT TURN 184..187
FT /evidence="ECO:0007829|PDB:3I33"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:3I33"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:3I33"
FT STRAND 208..216
FT /evidence="ECO:0007829|PDB:3I33"
FT STRAND 219..228
FT /evidence="ECO:0007829|PDB:3I33"
FT HELIX 233..252
FT /evidence="ECO:0007829|PDB:3I33"
FT HELIX 260..276
FT /evidence="ECO:0007829|PDB:3I33"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:3I33"
FT STRAND 280..291
FT /evidence="ECO:0007829|PDB:3I33"
FT STRAND 294..301
FT /evidence="ECO:0007829|PDB:3I33"
FT HELIX 302..308
FT /evidence="ECO:0007829|PDB:3I33"
FT HELIX 310..315
FT /evidence="ECO:0007829|PDB:3I33"
FT HELIX 317..327
FT /evidence="ECO:0007829|PDB:3I33"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:3I33"
FT STRAND 336..341
FT /evidence="ECO:0007829|PDB:3I33"
FT HELIX 342..345
FT /evidence="ECO:0007829|PDB:3I33"
FT HELIX 347..356
FT /evidence="ECO:0007829|PDB:3I33"
FT TURN 357..359
FT /evidence="ECO:0007829|PDB:3I33"
FT TURN 368..370
FT /evidence="ECO:0007829|PDB:3I33"
FT HELIX 371..383
FT /evidence="ECO:0007829|PDB:3I33"
SQ SEQUENCE 639 AA; 70021 MW; 3851755494E7B729 CRC64;
MSARGPAIGI DLGTTYSCVG VFQHGKVEII ANDQGNRTTP SYVAFTDTER LIGDAAKNQV
AMNPTNTIFD AKRLIGRKFE DATVQSDMKH WPFRVVSEGG KPKVQVEYKG ETKTFFPEEI
SSMVLTKMKE IAEAYLGGKV HSAVITVPAY FNDSQRQATK DAGTITGLNV LRIINEPTAA
AIAYGLDKKG CAGGEKNVLI FDLGGGTFDV SILTIEDGIF EVKSTAGDTH LGGEDFDNRM
VSHLAEEFKR KHKKDIGPNK RAVRRLRTAC ERAKRTLSSS TQASIEIDSL YEGVDFYTSI
TRARFEELNA DLFRGTLEPV EKALRDAKLD KGQIQEIVLV GGSTRIPKIQ KLLQDFFNGK
ELNKSINPDE AVAYGAAVQA AILIGDKSEN VQDLLLLDVT PLSLGIETAG GVMTPLIKRN
TTIPTKQTQT FTTYSDNQSS VLVQVYEGER AMTKDNNLLG KFDLTGIPPA PRGVPQIEVT
FDIDANGILN VTAADKSTGK ENKITITNDK GRLSKDDIDR MVQEAERYKS EDEANRDRVA
AKNALESYTY NIKQTVEDEK LRGKISEQDK NKILDKCQEV INWLDRNQMA EKDEYEHKQK
ELERVCNPII SKLYQGGPGG GSGGGGSGAS GGPTIEEVD
