UniProt ID | SRC1_YEAST | |
---|---|---|
UniProt AC | Q03707 | |
Protein Name | Inner nuclear membrane protein SRC1 | |
Gene Name | SRC1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 834 | |
Subcellular Localization |
Nucleus inner membrane Multi-pass membrane protein . Targeting to the inner nuclear membrane requires the SRP1 and KAP95 karyopherins and the Ran cycle. |
|
Protein Description | Plays a role in sister chromatid separation.. | |
Protein Sequence | MNSDLEYLEDGFDPNSMKVATLRRILVENNVDFPSNARKNALVGLFDEKVKPQIPQLRKMYLNVRPSDEGIVKMDRPSSSPSIASPRRSRRARREKSASPMAKQFKKNRILDDVSNDDDDDDDDDDDNDKKDDPLIVPSGTDTDEVDDEEDDVITSSSNKSDTNDFQQNSDTRKKRKDPDSDDWSESNSKENKIDNKHLNLLSSDSEIEQDYQKAKKRKTSDLNQEHGNGSAILGKLSVKTPIKNTNRKPVSMDNFNDSLTSSGTENDPFVPNIRHNPKELGTANGTGHSTPLSKLKVSASFADKLPQKEVPSTILVPEVEQQEPSQSERTPSLFSSEGSGSESEAPLLPEITTPGPHQPMGNTSNNVVEMIDTDSSNLVSDEDEVLVPTRIETPQLPTEKDVEKCEARVQELQEEVNEQLEHENGSEFDVKQGSGKVGNRHKFKRALKFLSKSLLALFLFCIFIVIPLLFGLWYREQRLLIGYCGHEVPSHRVSGNSFEFIQKLDNLLQDYRPKCIPCPPNGICYPYLKLKCKPDYKLAPSRLDFLEIIPAQGKCVKDDKKQQLVSEVVEKSLEFLRAKNAQISCGDGKDDIESGMTEDALYQIFNEARAPWIRDDEFEDLWIQVIKDLTEEPEILWRQLSPTDNNIGGNSNNIIKTNDVPRQKRHLPEKFISKTRNFRSTSKKYIGMKCRFEREIYQTYKKFQRPIWLMFLLIVISKVIEIKLKNYYRKKARIEELVTQTMEKLKFQKIKSMSDPKENAYLSIVQLRDIFLSDIVDLKYKNQLWSEVVKYLEHNNSNIKSNLTEIRGEIMKCWEWIGPMELNEPKDSAENKI | |
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 |
---|---|---|---|---|---|
3 | Phosphorylation | -----MNSDLEYLED -----CCCHHHHHHC | 42.12 | 28152593 | |
7 | Phosphorylation | -MNSDLEYLEDGFDP -CCCHHHHHHCCCCC | 23.76 | 19823750 | |
16 | Phosphorylation | EDGFDPNSMKVATLR HCCCCCCCCHHHHHH | 25.93 | 19823750 | |
67 | Phosphorylation | MYLNVRPSDEGIVKM HHHCCCCCCCCCCCC | 37.42 | 21440633 | |
73 | Acetylation | PSDEGIVKMDRPSSS CCCCCCCCCCCCCCC | 32.91 | 25381059 | |
78 | Phosphorylation | IVKMDRPSSSPSIAS CCCCCCCCCCCCCCC | 44.32 | 22369663 | |
79 | Phosphorylation | VKMDRPSSSPSIASP CCCCCCCCCCCCCCH | 49.29 | 22369663 | |
80 | Phosphorylation | KMDRPSSSPSIASPR CCCCCCCCCCCCCHH | 27.31 | 22369663 | |
82 | Phosphorylation | DRPSSSPSIASPRRS CCCCCCCCCCCHHHH | 32.50 | 22369663 | |
85 | Phosphorylation | SSSPSIASPRRSRRA CCCCCCCCHHHHHHH | 19.78 | 22369663 | |
97 | Phosphorylation | RRARREKSASPMAKQ HHHHHHHCCCHHHHH | 29.26 | 19684113 | |
99 | Phosphorylation | ARREKSASPMAKQFK HHHHHCCCHHHHHHH | 23.46 | 25752575 | |
115 | Phosphorylation | NRILDDVSNDDDDDD CCCCCCCCCCCCCCC | 41.35 | 19795423 | |
141 | Phosphorylation | PLIVPSGTDTDEVDD CEEECCCCCCCCCCC | 39.81 | 28889911 | |
161 | Phosphorylation | ITSSSNKSDTNDFQQ EECCCCCCCCCCCCC | 54.65 | 22369663 | |
163 | Phosphorylation | SSSNKSDTNDFQQNS CCCCCCCCCCCCCCC | 43.72 | 22369663 | |
181 | Phosphorylation | KKRKDPDSDDWSESN HHHCCCCCCCCHHHH | 42.74 | 25521595 | |
185 | Phosphorylation | DPDSDDWSESNSKEN CCCCCCCHHHHHHHH | 37.83 | 25521595 | |
187 | Phosphorylation | DSDDWSESNSKENKI CCCCCHHHHHHHHCC | 40.67 | 29136822 | |
189 | Phosphorylation | DDWSESNSKENKIDN CCCHHHHHHHHCCCH | 51.10 | 29136822 | |
203 | Phosphorylation | NKHLNLLSSDSEIEQ HHHHHHHCCCHHHHH | 34.95 | 22369663 | |
204 | Phosphorylation | KHLNLLSSDSEIEQD HHHHHHCCCHHHHHH | 45.16 | 22369663 | |
206 | Phosphorylation | LNLLSSDSEIEQDYQ HHHHCCCHHHHHHHH | 42.28 | 22369663 | |
212 | Phosphorylation | DSEIEQDYQKAKKRK CHHHHHHHHHHHHHC | 16.17 | 22890988 | |
220 | Phosphorylation | QKAKKRKTSDLNQEH HHHHHHCCCCCCHHH | 31.35 | 20377248 | |
221 | Phosphorylation | KAKKRKTSDLNQEHG HHHHHCCCCCCHHHC | 43.04 | 17287358 | |
231 | Phosphorylation | NQEHGNGSAILGKLS CHHHCCCCCHHHEEE | 19.01 | 28152593 | |
236 | Acetylation | NGSAILGKLSVKTPI CCCCHHHEEEECCCC | 33.86 | 24489116 | |
240 | Acetylation | ILGKLSVKTPIKNTN HHHEEEECCCCCCCC | 45.25 | 25381059 | |
241 | Phosphorylation | LGKLSVKTPIKNTNR HHEEEECCCCCCCCC | 28.26 | 21551504 | |
252 | Phosphorylation | NTNRKPVSMDNFNDS CCCCCCCCHHCCCHH | 29.01 | 19779198 | |
259 | Phosphorylation | SMDNFNDSLTSSGTE CHHCCCHHCCCCCCC | 34.35 | 19779198 | |
261 | Phosphorylation | DNFNDSLTSSGTEND HCCCHHCCCCCCCCC | 25.46 | 19779198 | |
262 | Phosphorylation | NFNDSLTSSGTENDP CCCHHCCCCCCCCCC | 31.87 | 23749301 | |
263 | Phosphorylation | FNDSLTSSGTENDPF CCHHCCCCCCCCCCC | 44.49 | 23749301 | |
265 | Phosphorylation | DSLTSSGTENDPFVP HHCCCCCCCCCCCCC | 33.30 | 23749301 | |
283 | Phosphorylation | HNPKELGTANGTGHS CCHHHHCCCCCCCCC | 29.58 | 22369663 | |
287 | Phosphorylation | ELGTANGTGHSTPLS HHCCCCCCCCCCCHH | 31.37 | 22369663 | |
290 | Phosphorylation | TANGTGHSTPLSKLK CCCCCCCCCCHHHCE | 32.82 | 22369663 | |
291 | Phosphorylation | ANGTGHSTPLSKLKV CCCCCCCCCHHHCEE | 23.68 | 22369663 | |
294 | Phosphorylation | TGHSTPLSKLKVSAS CCCCCCHHHCEEEHH | 36.83 | 22369663 | |
295 | Acetylation | GHSTPLSKLKVSASF CCCCCHHHCEEEHHH | 61.07 | 24489116 | |
299 | Phosphorylation | PLSKLKVSASFADKL CHHHCEEEHHHHHCC | 19.33 | 22369663 | |
301 | Phosphorylation | SKLKVSASFADKLPQ HHCEEEHHHHHCCCC | 17.29 | 22369663 | |
305 | Acetylation | VSASFADKLPQKEVP EEHHHHHCCCCCCCC | 59.65 | 24489116 | |
326 | Phosphorylation | EVEQQEPSQSERTPS CHHHCCCCCCCCCCH | 45.65 | 28889911 | |
328 | Phosphorylation | EQQEPSQSERTPSLF HHCCCCCCCCCCHHH | 33.12 | 28132839 | |
394 | Phosphorylation | LVPTRIETPQLPTEK EECCCCCCCCCCCHH | 17.60 | 22369663 | |
399 | Phosphorylation | IETPQLPTEKDVEKC CCCCCCCCHHHHHHH | 65.35 | 22890988 | |
405 | Ubiquitination | PTEKDVEKCEARVQE CCHHHHHHHHHHHHH | 36.90 | 23749301 | |
427 | Phosphorylation | QLEHENGSEFDVKQG HHHHCCCCCCEECCC | 46.82 | 23749301 | |
432 | Ubiquitination | NGSEFDVKQGSGKVG CCCCCEECCCCCCCC | 51.27 | 23749301 | |
491 | Phosphorylation | YCGHEVPSHRVSGNS ECCCCCCCCCCCCCH | 29.15 | 25005228 | |
682 | Phosphorylation | KTRNFRSTSKKYIGM HCCCCCCCCHHHCCC | 40.07 | 28889911 | |
683 | Phosphorylation | TRNFRSTSKKYIGMK CCCCCCCCHHHCCCE | 28.53 | 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 SRC1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SRC1_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 SRC1_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-80; SER-82;SER-203; SER-204; THR-241; SER-263; SER-301; THR-394 AND SER-427, ANDMASS SPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-80; SER-85;SER-203; SER-204; SER-206; SER-299 AND SER-301, AND MASS SPECTROMETRY. | |
"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-221, AND MASSSPECTROMETRY. | |
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; SER-85; SER-204 ANDSER-206, AND MASS SPECTROMETRY. |