MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
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To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Heat shock-related 70 kDa protein 2; Short=Heat shock 70 kDa protein 2; |
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| MyHits synonyms | HSP72_HUMAN , P54652 , Q15508 , Q53XM3 , Q9UE78 , 3851755494E7B729 |
 Legends: 1, Phosphoserine. {ECO:0000250|UniProtKB:P14659}; 2, Phosphothreonine. {ECO:0000250|UniProtKB:P14659}; 3, N6,N6,N6-trimethyllysine; by METTL21A; in vitro. {ECO:0000269|PubMed:23921388}; 4, VARIANT C -> S (in dbSNP:rs45456191). {ECO:0000269|Ref.4}; 5, VARIANT K -> E (in dbSNP:rs45447398). {ECO:0000269|Ref.4}; 6, MUTAGEN K->A: Abolishes methylation by METTL21A. {ECO:0000269|PubMed:23921388}; 7, CONFLICT T -> P (in Ref. 5; AAH36107). {ECO:0000305}; 8, CONFLICT Missing (in Ref. 6; AAC50076). {ECO:0000305}; 9, CONFLICT E -> G (in Ref. 5; AAH36107). {ECO:0000305}; 10, CONFLICT L -> S (in Ref. 2; AAD11466). {ECO:0000305}; 11, NP_BIND ATP; 12, ipat:HSP70_2 [T]; 13, ipat:HSP70_3 [T]; 14, ipat:HSP70_1 [T]; 15, STRAND {ECO:0000244|PDB:3I33}; 16, HELIX {ECO:0000244|PDB:3I33}; 17, TURN {ECO:0000244|PDB:3I33}; 18, HELIX {ECO:0000244|PDB:4FSV}.
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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 30-NOV-2016, entry version 163.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT shock 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
RT 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
RT project: 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.,
RA Buerckstuemmer T., 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
RT methyltransferase modulating Hsp70 function through lysine
RT methylation.";
RL J. Biol. Chem. 288:27752-27763(2013).
RN [10]
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
RT isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and
RT HSPA5/BiP/GRP78.";
RL PLoS ONE 5:E8625-E8625(2010).
CC -!- FUNCTION: In cooperation with other chaperones, Hsp70s stabilize
CC preexistent proteins against aggregation and mediate the folding
CC of newly translated polypeptides in the cytosol as well as within
CC organelles. These chaperones participate in all these processes
CC through their ability to recognize nonnative conformations of
CC other proteins. They bind extended peptide segments with a net
CC hydrophobic character exposed by polypeptides during translation
CC and membrane translocation, or following stress-induced damage.
CC Plays a role in spermatogenesis. In association with SHCBP1L may
CC participate in the maintenance of spindle integrity during meiosis
CC in male germ cells. {ECO:0000250|UniProtKB:P17156, ECO:0000305}.
CC -!- SUBUNIT: Interacts with FKBP6 (PubMed:18529014). Interacts with
CC ZNF541. Component of the CatSper complex. Interacts with
CC RABL2/RABL2A; binds preferentially to GTP-bound RABL2. Interacts
CC with SHCBP1L; this interaction may promote the recruitment of
CC HSPA2 to the spindle (By similarity). Interacts with FKBP6
CC (PubMed:18529014). {ECO:0000250|UniProtKB:P17156,
CC ECO:0000269|PubMed:18529014}.
CC -!- INTERACTION:
CC Q96BE0:-; NbExp=2; IntAct=EBI-356991, EBI-9356686;
CC O95429:BAG4; NbExp=4; IntAct=EBI-356991, EBI-2949658;
CC Q9NZL4:HSPBP1; NbExp=6; IntAct=EBI-356991, EBI-356763;
CC O00635:TRIM38; NbExp=3; IntAct=EBI-356991, EBI-2130415;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle
CC {ECO:0000250|UniProtKB:P17156}. Note=Colocalizes with SHCBP1L at
CC spindle during the meiosis process.
CC {ECO:0000250|UniProtKB:P17156}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/hspa2/";
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 UniGene; Hs.432648; -.
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 ProteinModelPortal; P54652; -.
DR SMR; P54652; -.
DR BioGrid; 109538; 76.
DR IntAct; P54652; 36.
DR MINT; MINT-1146083; -.
DR STRING; 9606.ENSP00000247207; -.
DR ChEMBL; CHEMBL2062348; -.
DR iPTMnet; P54652; -.
DR PhosphoSitePlus; P54652; -.
DR SwissPalm; P54652; -.
DR BioMuta; HSPA2; -.
DR DMDM; 1708307; -.
DR REPRODUCTION-2DPAGE; IPI00007702; -.
DR EPD; P54652; -.
DR MaxQB; P54652; -.
DR PaxDb; P54652; -.
DR PeptideAtlas; P54652; -.
DR PRIDE; P54652; -.
DR DNASU; 3306; -.
DR Ensembl; ENST00000247207; ENSP00000247207; ENSG00000126803.
DR Ensembl; ENST00000394709; ENSP00000378199; ENSG00000126803.
DR GeneID; 3306; -.
DR KEGG; hsa:3306; -.
DR UCSC; uc001xhj.4; human.
DR CTD; 3306; -.
DR DisGeNET; 3306; -.
DR GeneCards; HSPA2; -.
DR HGNC; HGNC:5235; HSPA2.
DR HPA; HPA000798; -.
DR HPA; HPA052504; -.
DR MIM; 140560; gene.
DR neXtProt; NX_P54652; -.
DR OpenTargets; ENSG00000126803; -.
DR PharmGKB; PA29501; -.
DR eggNOG; KOG0101; Eukaryota.
DR eggNOG; COG0443; LUCA.
DR GeneTree; ENSGT00820000127001; -.
DR HOGENOM; HOG000228135; -.
DR HOVERGEN; HBG051845; -.
DR InParanoid; P54652; -.
DR KO; K03283; -.
DR OMA; KENDDRG; -.
DR OrthoDB; EOG091G03SF; -.
DR PhylomeDB; P54652; -.
DR TreeFam; TF105042; -.
DR BioCyc; ZFISH:ENSG00000126803-MONOMER; -.
DR Reactome; R-HSA-1221632; Meiotic synapsis.
DR Reactome; R-HSA-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-HSA-3371568; Attenuation phase.
DR SIGNOR; P54652; -.
DR ChiTaRS; HSPA2; human.
DR EvolutionaryTrace; P54652; -.
DR GeneWiki; HSPA2; -.
DR GenomeRNAi; 3306; -.
DR PRO; PR:P54652; -.
DR Proteomes; UP000005640; Chromosome 14.
DR Bgee; ENSG00000126803; -.
DR CleanEx; HS_HSPA2; -.
DR ExpressionAtlas; P54652; baseline and differential.
DR Genevisible; P54652; HS.
DR GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
DR GO; GO:0036128; C:CatSper complex; ISS:UniProtKB.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA: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; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000795; C:synaptonemal complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR GO; GO:0051861; F:glycolipid binding; IEA:Ensembl.
DR GO; GO:0051082; F:unfolded protein binding; IDA:UniProtKB.
DR GO; GO:0007140; P:male meiosis; TAS:ProtInc.
DR GO; GO:0007141; P:male meiosis I; IEA:Ensembl.
DR GO; GO:0090084; P:negative regulation of inclusion body assembly; IDA:UniProtKB.
DR GO; GO:1901896; P:positive regulation of calcium-transporting ATPase activity; IEA:Ensembl.
DR GO; GO:0031662; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G2/M transition of mitotic cell cycle; 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 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.
DR InterPro; IPR029047; HSP70_peptide-bd.
DR InterPro; IPR013126; Hsp_70_fam.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
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; ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW Cytoskeleton; Differentiation; Methylation; Nucleotide-binding;
KW Phosphoprotein; Polymorphism; Reference proteome; Spermatogenesis;
KW Stress response.
FT CHAIN 1 639 Heat shock-related 70 kDa protein 2.
FT /FTId=PRO_0000078258.
FT NP_BIND 13 16 ATP.
FT NP_BIND 205 207 ATP.
FT NP_BIND 271 278 ATP.
FT NP_BIND 342 345 ATP.
FT BINDING 72 72 ATP.
FT MOD_RES 403 403 Phosphoserine.
FT {ECO:0000250|UniProtKB:P14659}.
FT MOD_RES 408 408 Phosphothreonine.
FT {ECO:0000250|UniProtKB:P14659}.
FT MOD_RES 414 414 Phosphothreonine.
FT {ECO:0000250|UniProtKB:P14659}.
FT MOD_RES 564 564 N6,N6,N6-trimethyllysine; by METTL21A; in
FT vitro. {ECO:0000269|PubMed:23921388}.
FT VARIANT 191 191 C -> S (in dbSNP:rs45456191).
FT {ECO:0000269|Ref.4}.
FT /FTId=VAR_032706.
FT VARIANT 496 496 K -> E (in dbSNP:rs45447398).
FT {ECO:0000269|Ref.4}.
FT /FTId=VAR_032707.
FT MUTAGEN 564 564 K->A: Abolishes methylation by METTL21A.
FT {ECO:0000269|PubMed:23921388}.
FT CONFLICT 14 14 T -> P (in Ref. 5; AAH36107).
FT {ECO:0000305}.
FT CONFLICT 54 54 Missing (in Ref. 6; AAC50076).
FT {ECO:0000305}.
FT CONFLICT 80 80 E -> G (in Ref. 5; AAH36107).
FT {ECO:0000305}.
FT CONFLICT 266 266 L -> S (in Ref. 2; AAD11466).
FT {ECO:0000305}.
FT STRAND 8 12 {ECO:0000244|PDB:3I33}.
FT STRAND 14 23 {ECO:0000244|PDB:3I33}.
FT STRAND 26 29 {ECO:0000244|PDB:3I33}.
FT STRAND 37 40 {ECO:0000244|PDB:3I33}.
FT STRAND 43 45 {ECO:0000244|PDB:3I33}.
FT STRAND 50 52 {ECO:0000244|PDB:3I33}.
FT HELIX 54 58 {ECO:0000244|PDB:3I33}.
FT TURN 59 62 {ECO:0000244|PDB:3I33}.
FT HELIX 64 66 {ECO:0000244|PDB:4FSV}.
FT HELIX 71 73 {ECO:0000244|PDB:3I33}.
FT TURN 74 76 {ECO:0000244|PDB:3I33}.
FT HELIX 82 88 {ECO:0000244|PDB:3I33}.
FT STRAND 92 98 {ECO:0000244|PDB:3I33}.
FT STRAND 101 108 {ECO:0000244|PDB:3I33}.
FT STRAND 111 115 {ECO:0000244|PDB:3I33}.
FT HELIX 117 136 {ECO:0000244|PDB:3I33}.
FT STRAND 142 147 {ECO:0000244|PDB:3I33}.
FT HELIX 153 166 {ECO:0000244|PDB:3I33}.
FT STRAND 169 175 {ECO:0000244|PDB:3I33}.
FT HELIX 176 183 {ECO:0000244|PDB:3I33}.
FT TURN 184 187 {ECO:0000244|PDB:3I33}.
FT STRAND 191 194 {ECO:0000244|PDB:3I33}.
FT STRAND 197 203 {ECO:0000244|PDB:3I33}.
FT STRAND 208 216 {ECO:0000244|PDB:3I33}.
FT STRAND 219 228 {ECO:0000244|PDB:3I33}.
FT HELIX 233 252 {ECO:0000244|PDB:3I33}.
FT HELIX 260 276 {ECO:0000244|PDB:3I33}.
FT TURN 277 279 {ECO:0000244|PDB:3I33}.
FT STRAND 280 291 {ECO:0000244|PDB:3I33}.
FT STRAND 294 301 {ECO:0000244|PDB:3I33}.
FT HELIX 302 308 {ECO:0000244|PDB:3I33}.
FT HELIX 310 315 {ECO:0000244|PDB:3I33}.
FT HELIX 317 327 {ECO:0000244|PDB:3I33}.
FT HELIX 331 333 {ECO:0000244|PDB:3I33}.
FT STRAND 336 341 {ECO:0000244|PDB:3I33}.
FT HELIX 342 345 {ECO:0000244|PDB:3I33}.
FT HELIX 347 356 {ECO:0000244|PDB:3I33}.
FT TURN 357 359 {ECO:0000244|PDB:3I33}.
FT TURN 368 370 {ECO:0000244|PDB:3I33}.
FT HELIX 371 383 {ECO:0000244|PDB:3I33}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 200 213 ipat:HSP70_2 [T]
FT MYHIT 7 615 ipfam:HSP70 [T]
FT MYHIT 337 351 ipat:HSP70_3 [T]
FT MYHIT 10 17 ipat:HSP70_1 [T]
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
//
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