| UniProt ID | UBR2_YEAST | |
|---|---|---|
| UniProt AC | Q07963 | |
| Protein Name | E3 ubiquitin-protein ligase UBR2 | |
| Gene Name | UBR2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1872 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | E3 ubiquitin-protein ligase which probably functions outside the N-end rule pathway, since it lacks the residues essential for the degradation of N-end rule substrates. Mediates RPN4 ubiquitination and subsequent degradation.. | |
| Protein Sequence | MEDSDLSITNIRDFLTELPKLAKCEYSETTSYLLWKTLNLRLKHSDNDINWRSLVSILNSEAWENEKYRDILNGRKWRTLEFENDHHSVGNMHIGTACTRLCFPSETIYYCFTCSTNPLYEICELCFDKEKHVNHSYVAKVVMRPEGRICHCGDPFAFNDPSDAFKCKNELNNIPISNDNSNVTDDENVISLLNYVLDFLIDVTVSYKEEAEAHSSERKASSLMHPNQNSITDDIMEKHECEPLVNDENFVFFDNNWSNTRKEAHMEWAIQIEEEECNVHYMDLASTITRILNTPVEYAISITKALEDSHDVVTVLQSENFFEIDQIAKEFQKENIVVHVRKADDIFKRKLTDDLTDWLYSLCFKAATSLQNKYALRISMLDVWYSHFSKMRVSPTNTNPDFSKINLLGGFLISNEDSDESWFKPWSLENIEDERISKILTNYNERLIRAHSPNTVSHFYNFYGSRFQYIIINSINILSKKSKFKMLKIMASLFSLRDESRKFLAAQYIDVYLSVLYDAVASDAKECQVTLMSILGQYTFQDPSIANMTISSGFIERTIRFAFTLMAFNPEDLMSYLPISLYNGFKLPTETIRNRRTIICFKDLCTIMSANTVPEELLSNEAIFNAIIESFSEFSNVLPLKRETKEHVEVENFDFSAFYFFFSSILIMTDGYTRSISLVKDAAFRKQIVLKLLDVAQTREFESLTNSRKAISPDNASTNENDSNKATLSTVRETICNYVAETINFQVGVNTQYFFNPMSYLFKFVIQWSQCGRYEPIPASLTNYINLFEVFQDKQKALYISESALSTLVLIGQINVGFWVRNGTPITHQARMYTKYSMREFTYISDIFNVQFSMAMCNPDELMVTYLSRWGLKHWANGVPMYDYPDTETTVAVVNECILLLIQLLTEVRSLVMKSSKEGFERTFKSEIIHALCFDTCSYAQIVNCIPEHITKHPSFDIYLEKYANYTSPVSLTDNGIFVLKEKYKDEIDPYYIGLSSSRRYDVEKNIRLNMANLKKMKYEDTFVPAKKVKDLLKNTLFSGLYSISSVNTFGLFLKNTLDHIIKYDYDNLLPRVVHLIHLCVVNNLNEFMGILWHEYAIVDTEFCHYHSIGSILYYCLLKDNFSESHGKIREIFRYLMETAPHVNVNSYLREQTTSYTPGILWPTKEDKSHKDKEFERKKHLARLRKKKLMKKLAQQQMKFMENNSVDTSDISTPRTTSPSLSPTRINAENSSNTINSCCDDDCVFCKMPKDDDVFVYFSYQERNICDHGIDFTNPTDVNRINSLFSGKQTKDSAIQENPQDDDGTRLKFTSCEPVLRACGHGSHTKCLSGHMKSIRGIQNQTTKNIPLSYGSGLIYCPVCNSLSNSFLPKTNDIDKRTSSQFFMCIEKRSEAEENLDPMSSICIKAAMILGDLQGKKVTTIEDAYKVVNSVFINTISNTELRLRSHKKEGKIVNMERISSQCILTLHLVCELKSFIYKKFVNSKTFSSEISRKIWNWNEFLIKGNNVNLLLYMSQNFDNIDGGKTPQPPNLCIYEMFKRRFHQLLLLLARDMMRVNFYKDCRNKIKISSNGSEEPSTSFSYLFNTFKKYVDLFKPDDVRFDFTSLEKIKDFICSLLLESLSIFCRRTFLLFNIQYDDDGDGDNNNNRSNNFMDVKQREIELIFRYFKLPNLTHFLKDFFYNELTQNIERYNDGNDNLRIQQVIYDMVQNINTRAYPSPEHIQLIELPLNLSKFSLDNDEISNKCDKYEIAVCLLCGQKCHIQKSIALQGYLQGECTDHMRNGCEITSAYGVFLMTGTNAIYLSYGKRGTFYAAPYLSKYGETNEDYKFGTPVYLNRARYANLANEIVFGNMIPHIVFRLTDGSADLGGWETM | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 30 | Phosphorylation | KCEYSETTSYLLWKT CCCCCHHHHHHHHHH | 16.01 | 19779198 | |
| 32 | Phosphorylation | EYSETTSYLLWKTLN CCCHHHHHHHHHHHC | 12.06 | 19779198 | |
| 221 | Phosphorylation | HSSERKASSLMHPNQ HCCHHHHHHCCCCCC | 27.34 | 28889911 | |
| 222 | Phosphorylation | SSERKASSLMHPNQN CCHHHHHHCCCCCCC | 34.27 | 19779198 | |
| 303 | Phosphorylation | VEYAISITKALEDSH HHHHHHHHHHCCCCC | 11.95 | 28889911 | |
| 394 | Phosphorylation | HFSKMRVSPTNTNPD HHHCCCCCCCCCCCC | 18.68 | 23749301 | |
| 492 | Phosphorylation | KMLKIMASLFSLRDE HHHHHHHHHHCCCHH | 16.74 | 28889911 | |
| 495 | Phosphorylation | KIMASLFSLRDESRK HHHHHHHCCCHHHHH | 27.99 | 28889911 | |
| 508 | Phosphorylation | RKFLAAQYIDVYLSV HHHHHHHHHHHHHHH | 8.38 | 25371407 | |
| 522 | Phosphorylation | VLYDAVASDAKECQV HHHHHHCCCCCCCCH | 31.35 | 25371407 | |
| 677 | Phosphorylation | DGYTRSISLVKDAAF CCCCCCHHHHCCHHH | 28.49 | 21440633 | |
| 709 | Ubiquitination | ESLTNSRKAISPDNA HHHHCCCCCCCCCCC | 50.31 | 12872131 | |
| 712 | Phosphorylation | TNSRKAISPDNASTN HCCCCCCCCCCCCCC | 30.94 | 28889911 | |
| 717 | Phosphorylation | AISPDNASTNENDSN CCCCCCCCCCCCCCC | 37.71 | 23749301 | |
| 718 | Phosphorylation | ISPDNASTNENDSNK CCCCCCCCCCCCCCC | 44.11 | 23749301 | |
| 723 | Phosphorylation | ASTNENDSNKATLST CCCCCCCCCCHHHHH | 52.38 | 28889911 | |
| 729 | Phosphorylation | DSNKATLSTVRETIC CCCCHHHHHHHHHHH | 22.09 | 27017623 | |
| 730 | Phosphorylation | SNKATLSTVRETICN CCCHHHHHHHHHHHH | 27.05 | 27017623 | |
| 991 | Phosphorylation | YKDEIDPYYIGLSSS HCCCCCCEEECCCCC | 12.17 | 30377154 | |
| 992 | Phosphorylation | KDEIDPYYIGLSSSR CCCCCCEEECCCCCC | 8.23 | 30377154 | |
| 996 | Phosphorylation | DPYYIGLSSSRRYDV CCEEECCCCCCCCCH | 22.51 | 30377154 | |
| 997 | Phosphorylation | PYYIGLSSSRRYDVE CEEECCCCCCCCCHH | 32.67 | 30377154 | |
| 998 | Phosphorylation | YYIGLSSSRRYDVEK EEECCCCCCCCCHHH | 19.87 | 30377154 | |
| 1208 | Phosphorylation | MENNSVDTSDISTPR HHCCCCCCCCCCCCC | 26.58 | 27738172 | |
| 1209 | Phosphorylation | ENNSVDTSDISTPRT HCCCCCCCCCCCCCC | 28.60 | 27738172 | |
| 1212 | Phosphorylation | SVDTSDISTPRTTSP CCCCCCCCCCCCCCC | 37.03 | 27017623 | |
| 1213 | Phosphorylation | VDTSDISTPRTTSPS CCCCCCCCCCCCCCC | 19.68 | 27017623 | |
| 1216 | Phosphorylation | SDISTPRTTSPSLSP CCCCCCCCCCCCCCC | 32.59 | 23749301 | |
| 1217 | Phosphorylation | DISTPRTTSPSLSPT CCCCCCCCCCCCCCC | 39.66 | 22369663 | |
| 1218 | Phosphorylation | ISTPRTTSPSLSPTR CCCCCCCCCCCCCCE | 16.33 | 22369663 | |
| 1220 | Phosphorylation | TPRTTSPSLSPTRIN CCCCCCCCCCCCEEC | 41.04 | 21440633 | |
| 1222 | Phosphorylation | RTTSPSLSPTRINAE CCCCCCCCCCEECCC | 28.67 | 22369663 | |
| 1224 | Phosphorylation | TSPSLSPTRINAENS CCCCCCCCEECCCCC | 40.58 | 22369663 | |
| 1286 | Phosphorylation | NRINSLFSGKQTKDS HHHHHHHCCCCCCCC | 50.83 | 27017623 | |
| 1291 | Ubiquitination | LFSGKQTKDSAIQEN HHCCCCCCCCHHHCC | 47.38 | 23749301 | |
| 1311 | Phosphorylation | GTRLKFTSCEPVLRA CCEEEEECCHHHHHH | 21.44 | 25371407 | |
| 1334 | Phosphorylation | CLSGHMKSIRGIQNQ HHHHHHHHHHCCCCC | 15.22 | 27017623 | |
| 1380 | Phosphorylation | DIDKRTSSQFFMCIE CCCHHCCHHEEEEEE | 30.32 | 28889911 | |
| 1741 | Phosphorylation | SLDNDEISNKCDKYE CCCCHHHCCCCCHHH | 28.34 | 25704821 |
| 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 UBR2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UBR2_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 UBR2_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| 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-221; SER-1218; SER-1222AND SER-1380, AND MASS SPECTROMETRY. | |
| "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-1222, AND MASSSPECTROMETRY. | |
| "A proteomics approach to understanding protein ubiquitination."; Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.; Nat. Biotechnol. 21:921-926(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-712, UBIQUITINATION ATLYS-709, AND MASS SPECTROMETRY. | |
| Ubiquitylation | |
| Reference | PubMed |
| "A proteomics approach to understanding protein ubiquitination."; Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.; Nat. Biotechnol. 21:921-926(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-712, UBIQUITINATION ATLYS-709, AND MASS SPECTROMETRY. | |