HSP7F_ARATH - dbPTM
HSP7F_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HSP7F_ARATH
UniProt AC Q9STW6
Protein Name Heat shock 70 kDa protein 6, chloroplastic
Gene Name HSP70-6
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 718
Subcellular Localization Plastid, chloroplast stroma .
Protein Description Acts redundantly with HSP70-7 in the thermotolerance of germinating seeds. Plays an important role in the protein precursor import into chloroplasts.; 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 MASSAAQIHVLGGIGFASSSSSKRNLNGKGGTFMPRSAFFGTRTGPFSTPTSAFLRMGTRNGGGASRYAVGPVRVVNEKVVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKSGDRLVGQIAKRQAVVNPENTFFSVKRFIGRKMNEVDEESKQVSYRVVRDENNNVKLECPAINKQFAAEEISAQVLRKLVDDASRFLNDKVTKAVITVPAYFNDSQRTATKDAGRIAGLEVLRIINEPTAASLAYGFDRKANETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRVVDWLAAEFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTNMSLPFITATADGPKHIETTLTRAKFEELCSDLLDRVRTPVENSLRDAKLSFKDIDEVILVGGSTRIPAVQELVRKVTGKEPNVTVNPDEVVALGAAVQAGVLAGDVSDIVLLDVTPLSIGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSLGSFRLDGIPPAPRGVPQIEVKFDIDANGILSVSAVDKGTGKKQDITITGASTLPKDEVDQMVQEAERFAKDDKEKRDAIDTKNQADSVVYQTEKQLKELGEKIPGEVKEKVEAKLQELKDKIGSGSTQEIKDAMAALNQEVMQIGQSLYNQPGAGGPGAGPSPGGEGASSGDSSSSKGGDGDDVIDADFTDSQ
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
59PhosphorylationSAFLRMGTRNGGGAS
HHHCCCCCCCCCCCC
16.1829797451
111PhosphorylationTNAEGQRTTPSVVAY
ECCCCCCCCCCEEEE
34.8628295753
112PhosphorylationNAEGQRTTPSVVAYT
CCCCCCCCCCEEEEE
18.7628295753
114PhosphorylationEGQRTTPSVVAYTKS
CCCCCCCCEEEEECC
27.4228295753
119PhosphorylationTPSVVAYTKSGDRLV
CCCEEEEECCCCHHH
14.7028295753
153SulfoxidationKRFIGRKMNEVDEES
HHHHCCCHHCCCHHH
5.0825693801
348PhosphorylationKIELSSLTQTNMSLP
CCCHHHHCCCCCCCC
34.9822092075
389PhosphorylationDLLDRVRTPVENSLR
HHHHHCCCHHHHHHH
28.9125561503
401PhosphorylationSLRDAKLSFKDIDEV
HHHHCCCCCCCCCEE
29.5523111157
488PhosphorylationKIIPRNTTLPTSKSE
EEECCCCCCCCCHHH
34.0029797451
524PhosphorylationEFVRDNKSLGSFRLD
HEECCCCCCCCEEEC
44.1923776212
527PhosphorylationRDNKSLGSFRLDGIP
CCCCCCCCEEECCCC
16.7023776212
612PhosphorylationDTKNQADSVVYQTEK
CCCHHHHHHHHHHHH
19.2530291188
615PhosphorylationNQADSVVYQTEKQLK
HHHHHHHHHHHHHHH
13.9425561503
617PhosphorylationADSVVYQTEKQLKEL
HHHHHHHHHHHHHHH
27.7122074104
715PhosphorylationDVIDADFTDSQ----
CCCCCCCCCCC----
34.9830291188
717PhosphorylationIDADFTDSQ------
CCCCCCCCC------
34.4323776212

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 HSP7F_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HSP7F_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 HSP7F_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUMO3_ARATHSUMO3physical
20855607

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HSP7F_ARATH

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Related Literatures of Post-Translational Modification

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