| Tag | Content |
|---|
| CPLM ID | CPLM-014372 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Heat shock 70 kDa protein 1A |
Protein Synonyms/Alias | Heat shock 70 kDa protein 3; HSP70.3; Hsp68 |
Gene Name | Hspa1a |
Gene Synonyms/Alias | Hsp70-3; Hsp70A1 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 628 | GFGAQAPKGASGSGP | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage (By similarity). |
Sequence Annotation | MOD_RES 2 2 N-acetylalanine (By similarity).
MOD_RES 108 108 N6-acetyllysine (By similarity).
MOD_RES 246 246 N6-acetyllysine (By similarity).
MOD_RES 348 348 N6-acetyllysine (By similarity).
MOD_RES 561 561 N6,N6,N6-trimethyllysine; by METTL21A; in
MOD_RES 631 631 Phosphoserine (By similarity).
MOD_RES 633 633 Phosphoserine (By similarity).
MOD_RES 636 636 Phosphothreonine (By similarity). |
Keyword | Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Methylation; Nucleotide-binding; Phosphoprotein; Reference proteome; Stress response. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 641 AA |
Protein Sequence | MAKNTAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA 60
LNPQNTVFDA KRLIGRKFGD AVVQSDMKHW PFQVVNDGDK PKVQVNYKGE SRSFFPEEIS 120
SMVLTKMKEI AEAYLGHPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA 180
IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVSH 240
FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA 300
RFEELCSDLF RGTLEPVEKA LRDAKMDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN 360
KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI 420
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT RDNNLLGRFE LSGIPPAPRG VPQIEVTFDI 480
DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAERYKAEDE VQRDRVAAKN 540
ALESYAFNMK SAVEDEGLKG KLSEADKKKV LDKCQEVISW LDSNTLADKE EFVHKREELE 600
RVCSPIISGL YQGAGAPGAG GFGAQAPKGA SGSGPTIEEV D 641 |
Gene Ontology | GO:0016607; C:nuclear speck; ISS:UniProtKB. GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB. GO:0005524; F:ATP binding; IEA:UniProtKB-KW. GO:0006402; P:mRNA catabolic process; ISS:UniProtKB. GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB. GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB. GO:0006986; P:response to unfolded protein; ISS:UniProtKB. |
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Pfam | |
SMART | |
PROSITE | |
PRINTS | |