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HSP74_PONAB
ID   HSP74_PONAB             Reviewed;         840 AA.
AC   Q5RDM4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Heat shock 70 kDa protein 4;
GN   Name=HSPA4;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Interacts with TJP1/ZO-1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; CR857880; CAH90133.1; -; mRNA.
DR   RefSeq; NP_001125029.1; NM_001131557.1.
DR   AlphaFoldDB; Q5RDM4; -.
DR   SMR; Q5RDM4; -.
DR   STRING; 9601.ENSPPYP00000017643; -.
DR   Ensembl; ENSPPYT00000018354; ENSPPYP00000017643; ENSPPYG00000015777.
DR   GeneID; 100171909; -.
DR   KEGG; pon:100171909; -.
DR   CTD; 3308; -.
DR   eggNOG; KOG0103; Eukaryota.
DR   GeneTree; ENSGT00940000156067; -.
DR   InParanoid; Q5RDM4; -.
DR   OrthoDB; 406172at2759; -.
DR   Proteomes; UP000001595; Chromosome 5.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:GOC.
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:0051131; P:chaperone-mediated protein complex assembly; IEA:Ensembl.
DR   GO; GO:0045040; P:protein insertion into mitochondrial outer membrane; IEA:Ensembl.
DR   CDD; cd11737; HSPA4_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; IPR042052; HSPA4_NBD.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 2.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; ATP-binding; Cytoplasm; Methylation; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Stress response.
FT   CHAIN           1..840
FT                   /note="Heat shock 70 kDa protein 4"
FT                   /id="PRO_0000255933"
FT   REGION          500..575
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          783..840
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..534
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..567
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         53
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61316"
FT   MOD_RES         76
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
FT   MOD_RES         89
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
FT   MOD_RES         336
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
FT   MOD_RES         393
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
FT   MOD_RES         415
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61316"
FT   MOD_RES         430
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
FT   MOD_RES         538
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
FT   MOD_RES         546
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
FT   MOD_RES         647
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
FT   MOD_RES         660
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61316"
FT   MOD_RES         679
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
FT   MOD_RES         756
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
FT   MOD_RES         773
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P34932"
SQ   SEQUENCE   840 AA;  94299 MW;  6766F4FB7B1E2431 CRC64;
     MSVVGIDLGF QSCYVAVARA GGIETIANEY SDRCTPACIS FGPKNRSIGA AAKSQVISNA
     KNTVQGFKRF HGRAFSDPFV EAEKSNLAYD VVQLPTGLTG IKVTYMEEER NFTTEQVTAM
     LLSKLKETAE SVLKKPVVDC VVSVPCFYTD AERRSVMDAT QIAGLNCLRL MNETTAVALA
     YGIYKQDLPA LEEKPRNVVF VDMGHSAYQV SVCAFNRGKL KVLATAFDTT LGGRKFDEVL
     VNHFCEEFGK KYKLDIKSKI RALLRLSQEC EKLKKLMSAN ASDLPLSIEC FMNDVDVSGT
     MNRGKFLEMC NDLLARVEPP LRSVLEQTKL KKEDIYAVEI VGGATRIPAV KEKISKFFGK
     ELSTTLNADE AVTRGCALQC AILSPAFKVR EFSITDVVPY PISLRWNSPA EEGSSDCEVF
     SKNHAAPFSK VLTFYRKEPF TLEAYYSSPQ DLPYPDPAIA QFSVQKVTPQ SDGSSSKVKV
     KVRVNVHGIF SVSSASLVEV HKSEENEEPM ETDQNAKEEE KMQVDQEEPH VEEQQQQTPA
     ENKAESEEME TSQAGSKDKK MDQPPQAKKA KVKTSTVDLP IENQLLWQID REMLNLYIEN
     EGKMIMQDKL EKERNDAKNA VEEYVYEMRD KLSGEYEKFV SEDDRNSFTL KLEDTENWLY
     EDGEDQPKQV YVDKLAELKN LGQPIKIRFQ ESEERPKLFE ELGKQIQQYM KIISSFKNKE
     DQYDHLDAAD MTKVEKSTNE AMEWMNNKLN LQNKQSLTMD PVVKSKEIEA KIKELTSICS
     PIISKPKPKV EPPKEEQKNA EQNGPVDGQG DNPGPQAAEQ GTDAAVPSDS DKKLPEMDID
 
 
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