UniProt ID | ULP2_YEAST | |
---|---|---|
UniProt AC | P40537 | |
Protein Name | Ubiquitin-like-specific protease 2 | |
Gene Name | ULP2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1034 | |
Subcellular Localization | ||
Protein Description | Insertion mutation in SMT4 confers temperature and benomyl sensitivity; high copy suppressor of a temperature sensitive mutation in MIF2.. | |
Protein Sequence | MSARKRKFNSLKPLDTLNSSRASSPRSSASLPPKRYNTFRKDPKIVDHLNNASTKDFLPVLSMNSESKRQIELSDNDVDNNDEGEGVNSGCSDQDFEPLQSSPLKRHSSLKSTSNGLLFQMSNNLGNGSPEPAVASTSPNGSIISTKLNLNGQFSCVDSKTLRIYRHKAPCIMTFVSDHNHPKFSLYFQQSVIYNSQVNLLDDVELIILDKKNSFMAIILKDLKKVKMILDVNNSSININTNILIWSTASSASNKKIKSIKRFLLMSYSSSIKVEILDHKEQILERLKHLIHPISSSSPSLNMERAINSTKNAFDSLRLKKTKLSTNDDESPQIHTHFLSNKPHGLQSLTKRTRIASLGKKEHSISVPKSNISPSDFYNTNGTETLQSHAVSQLRRSNRFKDVSDPANSNSNSEFDDATTEFETPELFKPSLCYKFNDGSSYTITNQDFKCLFNKDWVNDSILDFFTKFYIESSIEKSIIKREQVHLMSSFFYTKLISNPADYYSNVKKWVNNTDLFSKKYVVIPINISYHWFSCIITNLDAILDFHQNKDKNDAINSDEISINNPLVNILTFDSLRQTHSREIDPIKEFLISYALDKYSIQLDKTQIKMKTCPVPQQPNMSDCGVHVILNIRKFFENPVETIDVWKNSKIKSKHFTAKMINKYFDKNERNSARKNLRHTLKLLQLNYISYLKKENLYEEVMQMEEKKSTNINNNENYDDDDEEIQIIENIDQSSKDNNAQLTSEPPCSRSSSISTTEREPTELHNSVVRQPTGEIITDNEDPVRAASPETASVSPPIRHNILKSSSPFISESANETEQEEFTSPYFGRPSLKTRAKQFEGVSSPIKNDQALSSTHDIMMPSPKPKRIYPSKKIPQLSSHVQSLSTDSMERQSSPNNTNIVISDTEQDSRLGVNSESKNTSGIVNRDDSDVNLIGSSLPNVAEKNHDNTQESNGNNDSLGKILQNVDKELNEKLVDIDDVAFSSPTRGIPRTSATSKGSNAQLLSNYGDENNQSQDSVWDEGRDNPILLEDEDP | |
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 |
---|---|---|---|---|---|
16 | Phosphorylation | NSLKPLDTLNSSRAS CCCCCCCCCCCCCCC | 35.21 | 23749301 | |
20 | Phosphorylation | PLDTLNSSRASSPRS CCCCCCCCCCCCCCC | 30.69 | 21440633 | |
74 | Phosphorylation | SKRQIELSDNDVDNN CCCEEECCCCCCCCC | 22.90 | 21440633 | |
89 | Phosphorylation | DEGEGVNSGCSDQDF CCCCCCCCCCCCCCC | 38.48 | 21440633 | |
92 | Phosphorylation | EGVNSGCSDQDFEPL CCCCCCCCCCCCCCC | 41.66 | 21440633 | |
101 | Phosphorylation | QDFEPLQSSPLKRHS CCCCCCCCCCCCCCC | 41.42 | 21440633 | |
298 | Phosphorylation | IHPISSSSPSLNMER HCCCCCCCCCCCHHH | 22.06 | 21082442 | |
682 | Acetylation | KNLRHTLKLLQLNYI HHHHHHHHHHHHHHH | 48.59 | 17397211 | |
751 | Phosphorylation | SEPPCSRSSSISTTE CCCCCCCCCCCCCCC | 16.49 | 28889911 | |
753 | Phosphorylation | PPCSRSSSISTTERE CCCCCCCCCCCCCCC | 23.08 | 23749301 | |
773 | Phosphorylation | NSVVRQPTGEIITDN CCCCCCCCCCCCCCC | 38.82 | 27017623 | |
778 | Phosphorylation | QPTGEIITDNEDPVR CCCCCCCCCCCCCCC | 38.13 | 27214570 | |
788 | Phosphorylation | EDPVRAASPETASVS CCCCCCCCCCCCCCC | 23.45 | 19547744 | |
791 | Phosphorylation | VRAASPETASVSPPI CCCCCCCCCCCCCCC | 27.84 | 23749301 | |
793 | Phosphorylation | AASPETASVSPPIRH CCCCCCCCCCCCCHH | 30.46 | 23749301 | |
795 | Phosphorylation | SPETASVSPPIRHNI CCCCCCCCCCCHHHH | 23.59 | 25704821 | |
805 | Phosphorylation | IRHNILKSSSPFISE CHHHHHHCCCCCCCC | 32.38 | 27017623 | |
824 | Phosphorylation | TEQEEFTSPYFGRPS HHCHHHCCCCCCCCH | 23.95 | 27017623 | |
843 | Phosphorylation | AKQFEGVSSPIKNDQ HHHCCCCCCCCCCCC | 41.05 | 21440633 | |
844 | Phosphorylation | KQFEGVSSPIKNDQA HHCCCCCCCCCCCCH | 28.39 | 21440633 | |
862 | Phosphorylation | THDIMMPSPKPKRIY CCCCCCCCCCCCCCC | 27.88 | 21440633 | |
893 | Phosphorylation | TDSMERQSSPNNTNI HHHHHCCCCCCCCCE | 54.72 | 22369663 | |
894 | Phosphorylation | DSMERQSSPNNTNIV HHHHCCCCCCCCCEE | 24.25 | 22369663 | |
898 | Phosphorylation | RQSSPNNTNIVISDT CCCCCCCCCEEEECC | 32.72 | 22369663 | |
903 | Phosphorylation | NNTNIVISDTEQDSR CCCCEEEECCCCCCC | 27.82 | 22369663 | |
905 | Phosphorylation | TNIVISDTEQDSRLG CCEEEECCCCCCCCC | 28.84 | 22369663 | |
915 | Phosphorylation | DSRLGVNSESKNTSG CCCCCCCCCCCCCCC | 40.62 | 28889911 | |
917 | Phosphorylation | RLGVNSESKNTSGIV CCCCCCCCCCCCCCC | 30.90 | 28889911 | |
920 | Phosphorylation | VNSESKNTSGIVNRD CCCCCCCCCCCCCCC | 31.87 | 22369663 | |
921 | Phosphorylation | NSESKNTSGIVNRDD CCCCCCCCCCCCCCC | 35.60 | 20377248 | |
929 | Phosphorylation | GIVNRDDSDVNLIGS CCCCCCCCCCCCCCC | 47.98 | 22369663 | |
936 | Phosphorylation | SDVNLIGSSLPNVAE CCCCCCCCCCCCHHH | 23.00 | 22369663 | |
937 | Phosphorylation | DVNLIGSSLPNVAEK CCCCCCCCCCCHHHH | 42.50 | 22369663 | |
958 | Phosphorylation | ESNGNNDSLGKILQN CCCCCCCHHHHHHHH | 40.94 | 23749301 | |
983 | Phosphorylation | DIDDVAFSSPTRGIP CHHHCCCCCCCCCCC | 26.18 | 22369663 | |
984 | Phosphorylation | IDDVAFSSPTRGIPR HHHCCCCCCCCCCCC | 24.68 | 22369663 | |
986 | Phosphorylation | DVAFSSPTRGIPRTS HCCCCCCCCCCCCCC | 43.40 | 20377248 | |
992 | Phosphorylation | PTRGIPRTSATSKGS CCCCCCCCCCCCCCC | 19.84 | 24961812 | |
993 | Phosphorylation | TRGIPRTSATSKGSN CCCCCCCCCCCCCCC | 30.72 | 24961812 | |
995 | Phosphorylation | GIPRTSATSKGSNAQ CCCCCCCCCCCCCHH | 30.64 | 24961812 | |
996 | Phosphorylation | IPRTSATSKGSNAQL CCCCCCCCCCCCHHH | 34.43 | 24961812 | |
1005 | Phosphorylation | GSNAQLLSNYGDENN CCCHHHHHHCCCCCC | 36.28 | 21440633 | |
1007 | Phosphorylation | NAQLLSNYGDENNQS CHHHHHHCCCCCCCC | 23.68 | 21440633 | |
1014 | Phosphorylation | YGDENNQSQDSVWDE CCCCCCCCCCCCCCC | 37.77 | 21551504 | |
1017 | Phosphorylation | ENNQSQDSVWDEGRD CCCCCCCCCCCCCCC | 19.92 | 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 ULP2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ULP2_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 ULP2_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
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 THR-778; SER-788 ANDSER-903, AND MASS 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 THR-920, AND MASSSPECTROMETRY. |