SSB1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SSB1_SCHPO
• UniProt AC: Q10284
• Protein Name: Ribosome-associated molecular chaperone sks2 {ECO:0000305}
• Gene Name: sks2 {ECO:0000303|PubMed:9161410}
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 613
• Subcellular Localization: Cytoplasm . Associated with translating ribosomes.
• Protein Description: Ribosome-bound, Hsp70-type chaperone that assists in the cotranslational folding of newly synthesized proteins in the cytosol. Stimulates folding by interacting with nascent chains, binding to short, largely hydrophobic sequences exposed by unfolded proteins, thereby stabilizing longer, more slowly translated, and aggregation-prone nascent polypeptides and domains that cannot fold stably until fully synthesized. The Hsp70-protein substrate interaction depends on ATP-binding and on allosteric regulation between the NBD and the SBD. The ATP-bound state is characterized by a fast exchange rate of substrate (low affinity state), while in the ADP-bound state exchange is much slower (high affinity state). During the Hsp70 cycle, the chaperone switches between the ATP-bound state (open conformation) and the ADP-bound state (closed conformation) by major conformational rearrangements involving mainly the lid domain. Ssb cooperates with a specific Hsp40/Hsp70 co-chaperone termed the ribosome-associated complex (RAC), which stimulates the ATPase activity of the ribosome-associated pool of Ssbs and switches it to the high affinity substrate binding state. Hsp110 chaperone pss1 and fes1 act as nucleotide exchange factors that cause substrate release..
• Protein Sequence: MSEVYEGAIGIDLGTTYSCVAVWETANVEIIPNDQGARTTPSFVAFTETERLVGDAAKNQAAMNPRNTVFDAKRLIGRRYEDPETQKDIKHWPFKVIDNNGIPTIEVNYLGEKKQFTAQEISAMVLTKMKEISEAKLNKRVEKAVITVPAYFSDSQRAATKDAGAIAGLNVLRIINEPTAAAIAYGLDAKSDKPKNVLIFDLGGGTFDVSLLKIQGGVFEVLATAGDTHLGGEDFDNALVEHFIQEFKRKQKIDISDDPRALRRLRSACERAKRALSSVTQTTVEVDSLSNGIDFSSSITRARFEDINATTFKATIDPVAKVLKDSKVPKADVHDIVLVGGSTRIPKVQRLVSDFFDGRALNKSINPDEAVAYGAAVQAAVLTNKADSDKTQDLLLLDVVPLSLGVAMEGNVFGVVCPRNTPIPTIKKRTFTTVADNQTTVTFPVYQGERVNCAENEPLGEFQLTGIPPMPRGQAELEATFELDANGILKVTAVEKTTGRSAHIEITNSVGHLSSTKIQEMIENADKFKQQDKDFAKKLEAKSQLESYISNIETTISEPNVMMKLKRGDKSKIEAQLAECMSQLELEDTNTDALRKAELRLKRTVQKAFASLR

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
39	Phosphorylation	PNDQGARTTPSFVAF CCCCCCCCCCCEEEE		25720772
40	Phosphorylation	NDQGARTTPSFVAFT CCCCCCCCCCEEEEE		28889911
151	Phosphorylation	AVITVPAYFSDSQRA EEEEEEECCCHHHHH		28889911
153	Phosphorylation	ITVPAYFSDSQRAAT EEEEECCCHHHHHCC		28889911
155	Phosphorylation	VPAYFSDSQRAATKD EEECCCHHHHHCCCC		28889911
256	Phosphorylation	RKQKIDISDDPRALR HHCCCCCCCCHHHHH		28889911
353	Phosphorylation	PKVQRLVSDFFDGRA HHHHHHHHHHCCCCC		28889911
364	Phosphorylation	DGRALNKSINPDEAV CCCCCCCCCCHHHHH		25720772
421	Phosphorylation	GVVCPRNTPIPTIKK EEECCCCCCCCCCEE		28889911
439	Phosphorylation	TTVADNQTTVTFPVY EEECCCCEEEEEEEE		25720772
501	Phosphorylation	VEKTTGRSAHIEITN EEECCCCCEEEEEEC		28889911
509	Phosphorylation	AHIEITNSVGHLSST EEEEEECCCCCCCHH		28889911
514	Phosphorylation	TNSVGHLSSTKIQEM ECCCCCCCHHHHHHH		28889911
515	Phosphorylation	NSVGHLSSTKIQEMI CCCCCCCHHHHHHHH		28889911
516	Phosphorylation	SVGHLSSTKIQEMIE CCCCCCHHHHHHHHH		28889911
543	Phosphorylation	AKKLEAKSQLESYIS HHHHHHHHHHHHHHH		25720772
547	Phosphorylation	EAKSQLESYISNIET HHHHHHHHHHHHHEE		25720772
548	Phosphorylation	AKSQLESYISNIETT HHHHHHHHHHHHEEC		25720772
550	Phosphorylation	SQLESYISNIETTIS HHHHHHHHHHEECCC		25720772
582	Phosphorylation	AQLAECMSQLELEDT HHHHHHHHHHCCCCC		24763107
604	Phosphorylation	AELRLKRTVQKAFAS HHHHHHHHHHHHHHH		25720772
611	Phosphorylation	TVQKAFASLR----- HHHHHHHHCC-----		25720772

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

Oops, there are no upstream regulatory protein records of SSB1_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SSB1_SCHPO !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SSB1_SCHPO !!

Protein-Protein Interaction

Oops, there are no PPI records of SSB1_SCHPO !!

Drug and Disease Associations

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