UniProt ID | HSP7C_ARATH | |
---|---|---|
UniProt AC | O65719 | |
Protein Name | Heat shock 70 kDa protein 3 | |
Gene Name | HSP70-3 | |
Organism | Arabidopsis thaliana (Mouse-ear cress). | |
Sequence Length | 649 | |
Subcellular Localization | Cytoplasm . Nucleus matrix . | |
Protein 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).. | |
Protein Sequence | MAGKGEGPAIGIDLGTTYSCVGVWQHDRVEIIANDQGNRTTPSYVAFTDSERLIGDAAKNQVAMNPINTVFDAKRLIGRRFTDSSVQSDIKLWPFTLKSGPAEKPMIVVNYKGEDKEFSAEEISSMILIKMREIAEAYLGTTIKNAVVTVPAYFNDSQRQATKDAGVIAGLNVMRIINEPTAAAIAYGLDKKATSVGEKNVLIFDLGGGTFDVSLLTIEEGIFEVKATAGDTHLGGEDFDNRMVNHFVQEFKRKNKKDISGNPRALRRLRTACERAKRTLSSTAQTTIEIDSLFDGIDFYAPITRARFEELNIDLFRKCMEPVEKCLRDAKMDKNSIDDVVLVGGSTRIPKVQQLLVDFFNGKELCKSINPDEAVAYGAAVQAAILSGEGNEKVQDLLLLDVTPLSLGLETAGGVMTVLIQRNTTIPTKKEQVFSTYSDNQPGVLIQVYEGERARTKDNNLLGKFELSGIPPAPRGVPQITVCFDIDANGILNVSAEDKTTGQKNKITITNDKGRLSKDEIEKMVQEAEKYKSEDEEHKKKVDAKNALENYAYNMRNTIRDEKIGEKLAGDDKKKIEDSIEAAIEWLEANQLAECDEFEDKMKELESICNPIIAKMYQGGEAGGPAAGGMDEDVPPSAGGAGPKIEEVD | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
64 | Sulfoxidation | AAKNQVAMNPINTVF HHHCCCCCCCCHHHH | 6.87 | 25693801 | |
84 | Phosphorylation | IGRRFTDSSVQSDIK HCCCCCCCCCCCCCE | 29.38 | 19880383 | |
191 | Acetylation | AIAYGLDKKATSVGE HHHHCCCCCCCCCCC | 49.72 | 24727099 | |
194 | Phosphorylation | YGLDKKATSVGEKNV HCCCCCCCCCCCCCE | 32.59 | 23776212 | |
195 | Phosphorylation | GLDKKATSVGEKNVL CCCCCCCCCCCCCEE | 32.74 | 23776212 | |
228 | Phosphorylation | GIFEVKATAGDTHLG CEEEEEECCCCCCCC | 26.00 | 22092075 | |
232 | Phosphorylation | VKATAGDTHLGGEDF EEECCCCCCCCCCCC | 20.34 | 30407730 | |
428 | Phosphorylation | QRNTTIPTKKEQVFS ECCCCCCCCHHHEEE | 51.39 | 19880383 | |
457 | Ubiquitination | EGERARTKDNNLLGK ECCCCCCCCCCCCCE | 53.56 | - | |
531 | Phosphorylation | MVQEAEKYKSEDEEH HHHHHHHHCCCCHHH | 15.97 | 25561503 | |
533 | Phosphorylation | QEAEKYKSEDEEHKK HHHHHHCCCCHHHHH | 47.38 | 25561503 | |
555 | Sulfoxidation | LENYAYNMRNTIRDE HHHHHHHHHHCCCHH | 1.97 | 23289948 | |
607 | Phosphorylation | DKMKELESICNPIIA HHHHHHHHHHHHHHH | 45.10 | 19880383 | |
616 | Sulfoxidation | CNPIIAKMYQGGEAG HHHHHHHHHCCCCCC | 1.92 | 23289948 | |
630 | Sulfoxidation | GGPAAGGMDEDVPPS CCCCCCCCCCCCCCC | 5.09 | 23289948 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of HSP7C_ARATH !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HSP7C_ARATH !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of HSP7C_ARATH !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SUMO3_ARATH | SUMO3 | physical | 20855607 | |
SUMO1_ARATH | SUMO1 | physical | 20855607 | |
WPP1_ARATH | WPP1 | physical | 19617588 | |
WIT1_ARATH | WIT1 | physical | 19617588 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Phosphoproteomic analysis of nuclei-enriched fractions fromArabidopsis thaliana."; Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A.,Andreasson E., Rathjen J.P., Peck S.C.; J. Proteomics 72:439-451(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, AND MASSSPECTROMETRY. | |
Ubiquitylation | |
Reference | PubMed |
"Tandem affinity purification and mass spectrometric analysis ofubiquitylated proteins in Arabidopsis."; Saracco S.A., Hansson M., Scalf M., Walker J.M., Smith L.M.,Vierstra R.D.; Plant J. 59:344-358(2009). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-457, AND IDENTIFICATIONBY MASS SPECTROMETRY. |