HSP7G_ARATH - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HSP7G_ARATH
• UniProt AC: Q9LTX9
• Protein Name: Heat shock 70 kDa protein 7, chloroplastic
• Gene Name: HSP70-7
• Organism: Arabidopsis thaliana (Mouse-ear cress).
• Sequence Length: 718
• Subcellular Localization: Plastid, chloroplast stroma .
• Protein Description: Acts redundantly with HSP70-6 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: MASSAAQIHILGGIGFPTSSSSSSTKNLDNKTNSIPRSVFFGNRTSPFTTPTSAFLRMGRRNNNASRYTVGPVRVVNEKVVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKSKDRLVGQIAKRQAVVNPENTFFSVKRFIGRRMNEVAEESKQVSYRVIKDENGNVKLDCPAIGKQFAAEEISAQVLRKLVDDASRFLNDKVTKAVITVPAYFNDSQRTATKDAGRIAGLEVLRIINEPTAASLAYGFERKSNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRVVDWLASTFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTNMSLPFITATADGPKHIETTLTRGKFEELCSDLLDRVRTPVENSLRDAKLSFKDIDEVILVGGSTRIPAVQDLVRKLTGKEPNVSVNPDEVVALGAAVQAGVLSGDVSDIVLLDVTPLSLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSIGSFRLDGIPPAPRGVPQIEVKFDIDANGILSVSASDKGTGKKQDITITGASTLPKDEVDTMVQEAERFAKEDKEKRDAIDTKNQADSVVYQTEKQLKELGEKIPGPVKEKVEAKLQELKEKIASGSTQEIKDTMAALNQEVMQIGQSLYNQPQPGGADSPPGGEASSSSDTSSSAKGGDNGGDVIDADFTDSN

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
18	Phosphorylation	LGGIGFPTSSSSSST ECCCCCCCCCCCCCC	38.69	19880383
19	Phosphorylation	GGIGFPTSSSSSSTK CCCCCCCCCCCCCCC	28.58	19880383
20	Phosphorylation	GIGFPTSSSSSSTKN CCCCCCCCCCCCCCC	36.40	19880383
21	Phosphorylation	IGFPTSSSSSSTKNL CCCCCCCCCCCCCCC	33.72	19880383
23	Phosphorylation	FPTSSSSSSTKNLDN CCCCCCCCCCCCCCC	43.93	19880383
38	Phosphorylation	KTNSIPRSVFFGNRT CCCCCCCCHHCCCCC	20.23	29797451
111	Phosphorylation	TNAEGQRTTPSVVAY ECCCCCCCCCCEEEE	34.86	28295753
112	Phosphorylation	NAEGQRTTPSVVAYT CCCCCCCCCCEEEEE	18.76	28295753
114	Phosphorylation	EGQRTTPSVVAYTKS CCCCCCCCEEEEECC	27.42	28295753
119	Phosphorylation	TPSVVAYTKSKDRLV CCCEEEEECCCCHHH	21.07	28295753
348	Phosphorylation	KIELSSLTQTNMSLP CCCHHHHCCCCCCCC	34.98	22092075
389	Phosphorylation	DLLDRVRTPVENSLR HHHHHCCCHHHHHHH	28.91	25561503
401	Phosphorylation	SLRDAKLSFKDIDEV HHHHCCCCCCCCCEE	29.55	23111157
488	Phosphorylation	KIIPRNTTLPTSKSE EEECCCCCCCCCHHH	34.00	29797451
524	Phosphorylation	EFVRDNKSIGSFRLD EEECCCCCCCCEEEC	38.14	29797451
527	Phosphorylation	RDNKSIGSFRLDGIP CCCCCCCCEEECCCC	12.91	23776212
612	Phosphorylation	DTKNQADSVVYQTEK CCCHHHHHHHHHHHH	19.25	30291188
615	Phosphorylation	NQADSVVYQTEKQLK HHHHHHHHHHHHHHH	13.94	25561503
617	Phosphorylation	ADSVVYQTEKQLKEL HHHHHHHHHHHHHHH	27.71	22074104
715	Phosphorylation	DVIDADFTDSN---- CCCCCCCCCCC----	38.78	23776212
717	Phosphorylation	IDADFTDSN------ CCCCCCCCC------	41.19	23776212

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

Oops, there are no upstream regulatory protein records of HSP7G_ARATH !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HSP7G_ARATH !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of HSP7G_ARATH !!

Protein-Protein Interaction

Oops, there are no PPI records of HSP7G_ARATH !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.