UniProt ID | SSB2_YEAST | |
---|---|---|
UniProt AC | P40150 | |
Protein Name | Ribosome-associated molecular chaperone SSB2 {ECO:0000303|PubMed:11739779} | |
Gene Name | SSB2 {ECO:0000303|PubMed:3302682} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 613 | |
Subcellular Localization | Cytoplasm . About 50% of the protein is associated with translating ribosomes, but sufficient Ssb exists in the cell for each ribosome to be associated with at least one Ssb molecule. | |
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 SSE1 and FES1 act as nucleotide exchange factors that cause substrate release.. | |
Protein Sequence | MAEGVFQGAIGIDLGTTYSCVATYESSVEIIANEQGNRVTPSFVAFTPQERLIGDAAKNQAALNPRNTVFDAKRLIGRRFDDESVQKDMKTWPFKVIDVDGNPVIEVQYLEETKTFSPQEISAMVLTKMKEIAEAKIGKKVEKAVITVPAYFNDAQRQATKDAGAISGLNVLRIINEPTAAAIAYGLGAGKSEKERHVLIFDLGGGTFDVSLLHIAGGVYTVKSTSGNTHLGGQDFDTNLLEHFKAEFKKKTGLDISDDARALRRLRTAAERAKRTLSSVTQTTVEVDSLFDGEDFESSLTRARFEDLNAALFKSTLEPVEQVLKDAKISKSQIDEVVLVGGSTRIPKVQKLLSDFFDGKQLEKSINPDEAVAYGAAVQGAILTGQSTSDETKDLLLLDVAPLSLGVGMQGDIFGIVVPRNTTVPTIKRRTFTTVSDNQTTVQFPVYQGERVNCKENTLLGEFDLKNIPMMPAGEPVLEAIFEVDANGILKVTAVEKSTGKSSNITISNAVGRLSSEEIEKMVNQAEEFKAADEAFAKKHEARQRLESYVASIEQTVTDPVLSSKLKRGSKSKIEAALSDALAALQIEDPSADELRKAEVGLKRVVTKAMSSR | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MAEGVFQGA ------CCCCCCCCE | 9298649 | ||
26 | Phosphorylation | SCVATYESSVEIIAN EEEEEECCCEEEEEE | 28889911 | ||
27 | Phosphorylation | CVATYESSVEIIANE EEEEECCCEEEEEEC | 28889911 | ||
40 | Phosphorylation | NEQGNRVTPSFVAFT ECCCCEECCEEEEEC | 21126336 | ||
47 | Phosphorylation | TPSFVAFTPQERLIG CCEEEEECCHHHHHC | 27738172 | ||
58 | Ubiquitination | RLIGDAAKNQAALNP HHHCHHHHCCHHHCC | 23749301 | ||
84 | Phosphorylation | GRRFDDESVQKDMKT CCCCCCHHHHHHHCC | 17287358 | ||
87 | Ubiquitination | FDDESVQKDMKTWPF CCCHHHHHHHCCCCC | 23749301 | ||
90 | Ubiquitination | ESVQKDMKTWPFKVI HHHHHHHCCCCCEEE | 24961812 | ||
95 | Ubiquitination | DMKTWPFKVIDVDGN HHCCCCCEEEECCCC | 17644757 | ||
114 | Ubiquitination | VQYLEETKTFSPQEI EEEEEECCCCCHHHH | 17644757 | ||
115 | Phosphorylation | QYLEETKTFSPQEIS EEEEECCCCCHHHHH | 24909858 | ||
117 | Phosphorylation | LEETKTFSPQEISAM EEECCCCCHHHHHHH | 21440633 | ||
122 | Phosphorylation | TFSPQEISAMVLTKM CCCHHHHHHHHHHHH | 28132839 | ||
128 | Ubiquitination | ISAMVLTKMKEIAEA HHHHHHHHHHHHHHH | 24961812 | ||
130 | Ubiquitination | AMVLTKMKEIAEAKI HHHHHHHHHHHHHHC | 23749301 | ||
136 | Ubiquitination | MKEIAEAKIGKKVEK HHHHHHHHCCCCCCE | 17644757 | ||
143 | Ubiquitination | KIGKKVEKAVITVPA HCCCCCCEEEEEEEC | 17644757 | ||
160 | Phosphorylation | NDAQRQATKDAGAIS CHHHHHHHCCCCCCC | 21440633 | ||
161 | Ubiquitination | DAQRQATKDAGAISG HHHHHHHCCCCCCCC | 23749301 | ||
167 | Phosphorylation | TKDAGAISGLNVLRI HCCCCCCCCCCHHHH | 21440633 | ||
179 | Phosphorylation | LRIINEPTAAAIAYG HHHCCCHHHHHHHHH | 22369663 | ||
185 | Phosphorylation | PTAAAIAYGLGAGKS HHHHHHHHHCCCCCC | 22369663 | ||
191 | Ubiquitination | AYGLGAGKSEKERHV HHHCCCCCCCCCCEE | 24961812 | ||
192 | Phosphorylation | YGLGAGKSEKERHVL HHCCCCCCCCCCEEE | 22369663 | ||
194 | Ubiquitination | LGAGKSEKERHVLIF CCCCCCCCCCEEEEE | 24961812 | ||
211 | Phosphorylation | GGGTFDVSLLHIAGG CCCEEEEEEEEEECC | 17287358 | ||
223 | Ubiquitination | AGGVYTVKSTSGNTH ECCEEEEECCCCCCE | 17644757 | ||
224 | Phosphorylation | GGVYTVKSTSGNTHL CCEEEEECCCCCCEE | 21440633 | ||
225 | Phosphorylation | GVYTVKSTSGNTHLG CEEEEECCCCCCEEC | 21440633 | ||
226 | Phosphorylation | VYTVKSTSGNTHLGG EEEEECCCCCCEECC | 21440633 | ||
229 | Phosphorylation | VKSTSGNTHLGGQDF EECCCCCCEECCCCC | 28889911 | ||
238 | Phosphorylation | LGGQDFDTNLLEHFK ECCCCCCCCHHHHHH | 28889911 | ||
245 | Ubiquitination | TNLLEHFKAEFKKKT CCHHHHHHHHHHHHH | 17644757 | ||
249 | Ubiquitination | EHFKAEFKKKTGLDI HHHHHHHHHHHCCCC | 22817900 | ||
250 | Ubiquitination | HFKAEFKKKTGLDIS HHHHHHHHHHCCCCC | 22817900 | ||
251 | Ubiquitination | FKAEFKKKTGLDISD HHHHHHHHHCCCCCH | 23749301 | ||
252 | Phosphorylation | KAEFKKKTGLDISDD HHHHHHHHCCCCCHH | 23749301 | ||
257 | Phosphorylation | KKTGLDISDDARALR HHHCCCCCHHHHHHH | 28152593 | ||
274 | Ubiquitination | RTAAERAKRTLSSVT HHHHHHHHHHHHHCC | 17644757 | ||
289 | Phosphorylation | QTTVEVDSLFDGEDF EEEEEEECCCCCCCH | 17287358 | ||
298 | Phosphorylation | FDGEDFESSLTRARF CCCCCHHHHHHHHHH | 17287358 | ||
301 | Phosphorylation | EDFESSLTRARFEDL CCHHHHHHHHHHHHH | 17287358 | ||
314 | Ubiquitination | DLNAALFKSTLEPVE HHHHHHHHHCCHHHH | 24961812 | ||
315 | Phosphorylation | LNAALFKSTLEPVEQ HHHHHHHHCCHHHHH | 25521595 | ||
316 | Phosphorylation | NAALFKSTLEPVEQV HHHHHHHCCHHHHHH | 21440633 | ||
325 | Ubiquitination | EPVEQVLKDAKISKS HHHHHHHHHCCCCHH | 23749301 | ||
328 | Ubiquitination | EQVLKDAKISKSQID HHHHHHCCCCHHHCC | 22817900 | ||
330 | Phosphorylation | VLKDAKISKSQIDEV HHHHCCCCHHHCCEE | 29688323 | ||
331 | Ubiquitination | LKDAKISKSQIDEVV HHHCCCCHHHCCEEE | 23749301 | ||
332 | Phosphorylation | KDAKISKSQIDEVVL HHCCCCHHHCCEEEE | 21440633 | ||
344 | Phosphorylation | VVLVGGSTRIPKVQK EEEECCCCCCHHHHH | 29688323 | ||
351 | Ubiquitination | TRIPKVQKLLSDFFD CCCHHHHHHHHHHCC | 23749301 | ||
354 | Phosphorylation | PKVQKLLSDFFDGKQ HHHHHHHHHHCCHHH | 28152593 | ||
360 | Ubiquitination | LSDFFDGKQLEKSIN HHHHCCHHHHHHCCC | 24961812 | ||
364 | Ubiquitination | FDGKQLEKSINPDEA CCHHHHHHCCCHHHH | 17644757 | ||
422 | Phosphorylation | GIVVPRNTTVPTIKR EEEECCCCCCCEEEE | 27017623 | ||
423 | Phosphorylation | IVVPRNTTVPTIKRR EEECCCCCCCEEEEC | 22369663 | ||
426 | Phosphorylation | PRNTTVPTIKRRTFT CCCCCCCEEEECEEE | 23749301 | ||
428 | Acetylation | NTTVPTIKRRTFTTV CCCCCEEEECEEEEE | 23572591 | ||
428 | Ubiquitination | NTTVPTIKRRTFTTV CCCCCEEEECEEEEE | 23749301 | ||
431 | Phosphorylation | VPTIKRRTFTTVSDN CCEEEECEEEEECCC | 29136822 | ||
433 | Phosphorylation | TIKRRTFTTVSDNQT EEEECEEEEECCCCE | 19779198 | ||
434 | Phosphorylation | IKRRTFTTVSDNQTT EEECEEEEECCCCEE | 19779198 | ||
436 | Phosphorylation | RRTFTTVSDNQTTVQ ECEEEEECCCCEEEE | 19779198 | ||
440 | Phosphorylation | TTVSDNQTTVQFPVY EEECCCCEEEEEEEE | 29136822 | ||
441 | Phosphorylation | TVSDNQTTVQFPVYQ EECCCCEEEEEEEEC | 23749301 | ||
455 | Ubiquitination | QGERVNCKENTLLGE CCCCCCCCCCEEECE | 24961812 | ||
458 | Phosphorylation | RVNCKENTLLGEFDL CCCCCCCEEECEECC | 30377154 | ||
466 | Ubiquitination | LLGEFDLKNIPMMPA EECEECCCCCCCCCC | 17644757 | ||
497 | Ubiquitination | LKVTAVEKSTGKSSN EEEEEEEECCCCCCC | 23749301 | ||
498 | Phosphorylation | KVTAVEKSTGKSSNI EEEEEEECCCCCCCE | 24961812 | ||
499 | Phosphorylation | VTAVEKSTGKSSNIT EEEEEECCCCCCCEE | 28889911 | ||
501 | Ubiquitination | AVEKSTGKSSNITIS EEEECCCCCCCEEEE | 23749301 | ||
502 | Phosphorylation | VEKSTGKSSNITISN EEECCCCCCCEEEEC | 22369663 | ||
503 | Phosphorylation | EKSTGKSSNITISNA EECCCCCCCEEEECH | 22369663 | ||
506 | Phosphorylation | TGKSSNITISNAVGR CCCCCCEEEECHHHC | 22369663 | ||
508 | Phosphorylation | KSSNITISNAVGRLS CCCCEEEECHHHCCC | 22369663 | ||
515 | Phosphorylation | SNAVGRLSSEEIEKM ECHHHCCCHHHHHHH | 25521595 | ||
516 | Phosphorylation | NAVGRLSSEEIEKMV CHHHCCCHHHHHHHH | 22369663 | ||
521 | Ubiquitination | LSSEEIEKMVNQAEE CCHHHHHHHHHHHHH | 23749301 | ||
530 | Ubiquitination | VNQAEEFKAADEAFA HHHHHHHHHHHHHHH | 23749301 | ||
538 | Ubiquitination | AADEAFAKKHEARQR HHHHHHHHHHHHHHH | 23749301 | ||
539 | Ubiquitination | ADEAFAKKHEARQRL HHHHHHHHHHHHHHH | 17644757 | ||
548 | Phosphorylation | EARQRLESYVASIEQ HHHHHHHHHHHHHHH | 22369663 | ||
549 | Phosphorylation | ARQRLESYVASIEQT HHHHHHHHHHHHHHH | 22369663 | ||
552 | Phosphorylation | RLESYVASIEQTVTD HHHHHHHHHHHHCCC | 22369663 | ||
556 | Phosphorylation | YVASIEQTVTDPVLS HHHHHHHHCCCHHHH | 22369663 | ||
558 | Phosphorylation | ASIEQTVTDPVLSSK HHHHHHCCCHHHHHH | 22369663 | ||
563 | Phosphorylation | TVTDPVLSSKLKRGS HCCCHHHHHHCCCCC | 22369663 | ||
564 | Phosphorylation | VTDPVLSSKLKRGSK CCCHHHHHHCCCCCH | 21440633 | ||
565 | Ubiquitination | TDPVLSSKLKRGSKS CCHHHHHHCCCCCHH | 23749301 | ||
567 | Ubiquitination | PVLSSKLKRGSKSKI HHHHHHCCCCCHHHH | 17644757 | ||
571 | Ubiquitination | SKLKRGSKSKIEAAL HHCCCCCHHHHHHHH | 17644757 | ||
572 | Phosphorylation | KLKRGSKSKIEAALS HCCCCCHHHHHHHHH | 22369663 | ||
573 | Ubiquitination | LKRGSKSKIEAALSD CCCCCHHHHHHHHHH | 24961812 | ||
579 | Phosphorylation | SKIEAALSDALAALQ HHHHHHHHHHHHHHC | 22369663 | ||
591 | Phosphorylation | ALQIEDPSADELRKA HHCCCCCCHHHHHHH | 22369663 | ||
597 | Ubiquitination | PSADELRKAEVGLKR CCHHHHHHHHHHHHH | 23749301 | ||
603 | Ubiquitination | RKAEVGLKRVVTKAM HHHHHHHHHHHHHHH | 22817900 | ||
607 | Phosphorylation | VGLKRVVTKAMSSR- HHHHHHHHHHHHCC- | 21440633 | ||
608 | Ubiquitination | GLKRVVTKAMSSR-- HHHHHHHHHHHCC-- | 23749301 | ||
611 | Phosphorylation | RVVTKAMSSR----- HHHHHHHHCC----- | 21082442 | ||
612 | Phosphorylation | VVTKAMSSR------ HHHHHHHCC------ | 28889911 |
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 SSB2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SSB2_YEAST !! |
* 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 SSB2_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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