HSP7P_ARATH - dbPTM
HSP7P_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSP7P_ARATH
UniProt AC F4HQD4
Protein Name Heat shock 70 kDa protein 15
Gene Name HSP70-15
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 831
Subcellular Localization Cytoplasm . Nucleus . Predominantly detected in the cytoplasm.
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 MSVVGFDFGNENCLVAVARQRGIDVVLNDESNRETPAIVCFGDKQRFIGTAGAASTMMNPKNSISQIKRLIGRQFSDPELQRDIKSLPFSVTEGPDGYPLIHANYLGEIRAFTPTQVMGMMLSNLKGIAEKNLNTAVVDCCIGIPVYFTDLQRRAVLDAATIAGLHPLHLIHETTATALAYGIYKTDLPENDQLNVAFIDIGHASMQVCIAGFKKGQLKILSHAFDRSLGGRDFDEVLFNHFAAKFKDEYKIDVSQNAKASLRLRATCEKLKKVLSANPMAPLNIECLMAEKDVRGVIKREEFEEISIPILERVKRPLEKALSDAGLTVEDVHMVEVVGSGSRVPAMIKILTEFFGKEPRRTMNASECVSRGCALQCAILSPTFKVREFQVHESFPFSISLAWKGAATDAQNGGTENQQSTIVFPKGNPIPSVKALTFYRSGTFSIDVQYSDVNDLQAPPKISTYTIGPFQSSKGERAKLKVKVRLNLHGIVSVESATLLEEEEVEVSVTKDQSEETAKMDTDKASAEAAPASGDSDVNMQDAKDTSDATGTDNGVPESAEKPVQMETDSKAEAPKKKVKKTNVPLSELVYGALKTVEVEKAVEKEFEMALQDRVMEETKDRKNAVESYVYDMRNKLSDKYQEYITDSEREAFLANLQEVEDWLYEDGEDETKGVYVAKLEELKKVGDPVEVRYKESLERGSVIDQLGYCINSYREAAVSNDPKFDHIELAEKQKVLNECVEAEAWLREKQQQQDTLPKYATPALLSADVKSKAEALDKFCRPIMTKPKPAAKAEAPQAKGGEQADEGKSEPEQPASAEAMETENPAEGST
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
123PhosphorylationQVMGMMLSNLKGIAE
HHHHHHHHCCHHHHH
23.4019880383
437PhosphorylationIPSVKALTFYRSGTF
CCCEEEEEEEECCEE
24.3929654922
526PhosphorylationKMDTDKASAEAAPAS
CCCCCHHHHHCCCCC
32.1723776212
533PhosphorylationSAEAAPASGDSDVNM
HHHCCCCCCCCCCCH
41.9123776212
536PhosphorylationAAPASGDSDVNMQDA
CCCCCCCCCCCHHHH
47.1630291188
648PhosphorylationYQEYITDSEREAFLA
HHHHCCHHHHHHHHH
29.8819880383
810PhosphorylationEQADEGKSEPEQPAS
CCCCCCCCCCCCCCC
70.0523776212
817PhosphorylationSEPEQPASAEAMETE
CCCCCCCCHHHHHCC
33.0723776212
823PhosphorylationASAEAMETENPAEGS
CCHHHHHCCCCCCCC
28.1623776212
830PhosphorylationTENPAEGST------
CCCCCCCCC------
23.5823776212
831PhosphorylationENPAEGST-------
CCCCCCCC-------
54.1923776212

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 HSP7P_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSP7P_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 HSP7P_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of HSP7P_ARATH !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HSP7P_ARATH

loading...

Related Literatures of Post-Translational Modification

TOP