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HS105_RAT
ID   HS105_RAT               Reviewed;         858 AA.
AC   Q66HA8;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Heat shock protein 105 kDa;
DE   AltName: Full=Heat shock 110 kDa protein;
GN   Name=Hsph1; Synonyms=Hsp105, Hsp110;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung;
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   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-558 AND SER-810, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Acts as a nucleotide-exchange factor (NEF) for chaperone
CC       proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B
CC       thereby triggering substrate release. Prevents the aggregation of
CC       denatured proteins in cells under severe stress, on which the ATP
CC       levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone
CC       activities. {ECO:0000250|UniProtKB:Q61699,
CC       ECO:0000250|UniProtKB:Q92598}.
CC   -!- SUBUNIT: Interacts with HSPA8/HSC70. Interacts with HSPA1A (via NBD)
CC       and HSPA1B (via NBD). {ECO:0000250|UniProtKB:Q61699,
CC       ECO:0000250|UniProtKB:Q92598}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q92598}.
CC   -!- PTM: Phosphorylation on Ser-509 may be important for regulation of the
CC       HSPA8/HSC70 chaperone activity. {ECO:0000250|UniProtKB:Q61699}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; BC081945; AAH81945.1; -; mRNA.
DR   RefSeq; NP_001011901.1; NM_001011901.1.
DR   AlphaFoldDB; Q66HA8; -.
DR   SMR; Q66HA8; -.
DR   BioGRID; 252555; 3.
DR   STRING; 10116.ENSRNOP00000001201; -.
DR   iPTMnet; Q66HA8; -.
DR   PhosphoSitePlus; Q66HA8; -.
DR   SwissPalm; Q66HA8; -.
DR   jPOST; Q66HA8; -.
DR   PaxDb; Q66HA8; -.
DR   PRIDE; Q66HA8; -.
DR   Ensembl; ENSRNOT00000001201; ENSRNOP00000001201; ENSRNOG00000000902.
DR   GeneID; 288444; -.
DR   KEGG; rno:288444; -.
DR   UCSC; RGD:1311609; rat.
DR   CTD; 10808; -.
DR   RGD; 1311609; Hsph1.
DR   eggNOG; KOG0103; Eukaryota.
DR   GeneTree; ENSGT00940000159635; -.
DR   HOGENOM; CLU_005965_5_1_1; -.
DR   InParanoid; Q66HA8; -.
DR   OMA; NMLSHAY; -.
DR   OrthoDB; 406172at2759; -.
DR   PhylomeDB; Q66HA8; -.
DR   Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR   ChiTaRS; Hspa4; rat.
DR   PRO; PR:Q66HA8; -.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Bgee; ENSRNOG00000000902; Expressed in frontal cortex and 20 other tissues.
DR   Genevisible; Q66HA8; RN.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR   GO; GO:0043014; F:alpha-tubulin binding; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; ISO:RGD.
DR   GO; GO:2001234; P:negative regulation of apoptotic signaling pathway; ISO:RGD.
DR   GO; GO:1903748; P:negative regulation of establishment of protein localization to mitochondrion; ISO:RGD.
DR   GO; GO:1903751; P:negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide; ISO:RGD.
DR   GO; GO:1903753; P:negative regulation of p38MAPK cascade; ISO:RGD.
DR   GO; GO:0006457; P:protein folding; IBA:GO_Central.
DR   CDD; cd11739; HSPH1_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 2.
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   InterPro; IPR042053; HSPH1_NBD.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 2.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q92598"
FT   CHAIN           2..858
FT                   /note="Heat shock protein 105 kDa"
FT                   /id="PRO_0000235976"
FT   REGION          500..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          801..858
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        524..562
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        565..585
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        808..833
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92598"
FT   MOD_RES         471
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61699"
FT   MOD_RES         509
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61699"
FT   MOD_RES         510
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61699"
FT   MOD_RES         558
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         562
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92598"
FT   MOD_RES         810
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         816
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92598"
SQ   SEQUENCE   858 AA;  96419 MW;  0AF62115FF795C66 CRC64;
     MSVVGLDVGS QSCYIAVARA GGIETIANEF SDRCTPSVIS FGPKNRTIGV AAKNQQITHA
     NNTVSSFKRF HGRAFNDPFI QKEKENLSYD LVPMKNGGVG IKVMYMDEDH LFSVEQITAM
     LLTKLKETAE NNLKKPVTDC VISVPSFFTD AERRSVLDAA QIVGLNCLRL MNDMTAVALN
     YGIYKQDLPN ADEKPRVVVF VDMGHSSFQV SACAFNKGKL KVLGTAFDPF LGGKNFDEKL
     VEHFCAEFKT KYKLDAKSKI RALLRLHQEC EKLKKLMSSN STDLPLNIEC FMNDKDVSAK
     MNRSQFEELC AELLQKIEVP LHLLMEQTHL KTEEVSAIEI VGGATRIPAV KERIARFFGK
     DVSTTLNADE AVARGCALQC AILSPAFKVR EFSVTDAVPF PISLVWNHDS EETEGVHEVF
     SRNHAAPFSK VLTFLRRGPF ELEAFYSDPQ AVPYPEAKIG RFVVQNVSAQ KDGEKSKVKV
     KVRVNTHGIF TISTASMVEK VPTEEEDGSS VEADMECPNQ KPAESSDVDK NIQQDNSEAG
     TQPQVQTDGQ QTSQSPPSPE LTSEENKIPD ADKANEKKVD QPPEAKKPKI KVVNVELPVE
     ANLVWQLGRD LLNMYIETEG KMIMQDKLEK ERNDAKNAVE ECVYEFRDKL CGPYEKFICE
     QEHEKFLRLL TETEDWLYEE GEDQAKQAYI DKLEELMKMG TPVKVRFQEA EERPRVLEEL
     GQRLQHYAKI AADFRGKDEK YNHIDESEMK KVEKSVNEVM EWMNNVMNAQ AKRSLHQDPV
     VRTHEISAKV KELNNVCEPV VTQPKPKIES PKLERTPNGP NMDKKEDLEG KSNLGADAPH
     QNGECHPNEK GSVSMDLD
 
 
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