HSP7C_ARATH - dbPTM
HSP7C_ARATH - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
64SulfoxidationAAKNQVAMNPINTVF
HHHCCCCCCCCHHHH
6.8725693801
84PhosphorylationIGRRFTDSSVQSDIK
HCCCCCCCCCCCCCE
29.3819880383
191AcetylationAIAYGLDKKATSVGE
HHHHCCCCCCCCCCC
49.7224727099
194PhosphorylationYGLDKKATSVGEKNV
HCCCCCCCCCCCCCE
32.5923776212
195PhosphorylationGLDKKATSVGEKNVL
CCCCCCCCCCCCCEE
32.7423776212
228PhosphorylationGIFEVKATAGDTHLG
CEEEEEECCCCCCCC
26.0022092075
232PhosphorylationVKATAGDTHLGGEDF
EEECCCCCCCCCCCC
20.3430407730
428PhosphorylationQRNTTIPTKKEQVFS
ECCCCCCCCHHHEEE
51.3919880383
457UbiquitinationEGERARTKDNNLLGK
ECCCCCCCCCCCCCE
53.56-
531PhosphorylationMVQEAEKYKSEDEEH
HHHHHHHHCCCCHHH
15.9725561503
533PhosphorylationQEAEKYKSEDEEHKK
HHHHHHCCCCHHHHH
47.3825561503
555SulfoxidationLENYAYNMRNTIRDE
HHHHHHHHHHCCCHH
1.9723289948
607PhosphorylationDKMKELESICNPIIA
HHHHHHHHHHHHHHH
45.1019880383
616SulfoxidationCNPIIAKMYQGGEAG
HHHHHHHHHCCCCCC
1.9223289948
630SulfoxidationGGPAAGGMDEDVPPS
CCCCCCCCCCCCCCC
5.0923289948

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSP7C_ARATH !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUMO3_ARATHSUMO3physical
20855607
SUMO1_ARATHSUMO1physical
20855607
WPP1_ARATHWPP1physical
19617588
WIT1_ARATHWIT1physical
19617588

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HSP7C_ARATH

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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
ReferencePubMed
"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.

TOP