HSP7Q_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HSP7Q_YEAST
• UniProt AC: Q05931
• Protein Name: Heat shock protein SSQ1, mitochondrial
• Gene Name: SSQ1
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 657
• Subcellular Localization: Mitochondrion matrix .
• Protein Description: Has a role in mitochondrial iron homeostasis. Appears to be involved in the processing of the intermediate form of the frataxin homolog YFH1. Required for the assembly of iron-sulfur (Fe/S) clusters in mitochondria..
• Protein Sequence: MLKSGRLNFLKLNINSRLLYSTNPQLTKKVIGIDLGTTNSAVAYIRDSNDKKSATIIENDEGQRTTPSIVAFDVKSSPQNKDQMKTLVGMAAKRQNAINSENTFFATKRLIGRAFNDKEVQRDMAVMPYKIVKCESNGQAYLSTSNGLIQSPSQIASILLKYLKQTSEEYLGEKVNLAVITVPAYFNDSQRQATKDAGKLAGLNVLRVINEPTAAALSFGIDDKRNNGLIAVYDLGGGTFDISILDIEDGVFEVRATNGDTHLGGEDFDNVIVNYIIDTFIHENPEITREEITKNRETMQRLKDVSERAKIDLSHVKKTFIELPFVYKSKHLRVPMTEEELDNMTLSLINRTIPPVKQALKDADIEPEDIDEVILVGGMTRMPKIRSVVKDLFGKSPNSSVNPDETVALGAAIQGGILSGEIKNVLLLDVTPLTLGIETFGGAFSPLIPRNTTVPVKKTEIFSTGVDGQAGVDIKVFQGERGLVRNNKLIGDLKLTGITPLPKGIPQIYVTFDIDADGIINVSAAEKSSGKQQSITVIPNSGLSEEEIAKLIEEANANRAQDNLIRQRLELISKADIMISDTENLFKRYEKLISSEKEYSNIVEDIKALRQAIKNFKANENDMSIDVNGIKKATDALQGRALKLFQSATKNQQNQGK

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
4	Phosphorylation	----MLKSGRLNFLK ----CCCCCCCCEEE	25.78	17287358
37	Phosphorylation	VIGIDLGTTNSAVAY EEEEECCCCCCEEEE	30.05	28889911
38	Phosphorylation	IGIDLGTTNSAVAYI EEEECCCCCCEEEEE	25.94	28889911
40	Phosphorylation	IDLGTTNSAVAYIRD EECCCCCCEEEEEEC	23.25	28889911
44	Phosphorylation	TTNSAVAYIRDSNDK CCCCEEEEEECCCCC	7.01	26447709
189	Phosphorylation	VPAYFNDSQRQATKD ECCCCCHHHHHHHHH	28.50	19779198
199	Acetylation	QATKDAGKLAGLNVL HHHHHHHHHCCCCEE	36.56	24489116
224	Acetylation	LSFGIDDKRNNGLIA HHCCCCCCCCCEEEE	53.96	24489116
390	Acetylation	PKIRSVVKDLFGKSP HHHHHHHHHHHCCCC	46.70	24489116
453	Phosphorylation	PLIPRNTTVPVKKTE CCCCCCCCCCCEEEE	26.76	29734811
607	Acetylation	SNIVEDIKALRQAIK HCHHHHHHHHHHHHH	54.40	22865919
624	Phosphorylation	KANENDMSIDVNGIK HCCCCCCEECHHHHH	20.64	27017623

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

Oops, there are no upstream regulatory protein records of HSP7Q_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HSP7Q_YEAST !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of HSP7Q_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GRPE_YEAST	MGE1	physical	11601843
JAC1_YEAST	JAC1	genetic	11278728
HSP77_YEAST	SSC1	genetic	10779357
NFU1_YEAST	NFU1	genetic	10468587
JAC1_YEAST	JAC1	genetic	16551614
SRO9_YEAST	SRO9	physical	19536198
GYS1_YEAST	GSY1	physical	19536198
AFT1_YEAST	AFT1	genetic	18843040
SRS2_YEAST	SRS2	genetic	21459050
GLRX5_YEAST	GRX5	physical	23615440

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND MASSSPECTROMETRY.
PubMed: 17287358