UniProt ID | NOC2_YEAST | |
---|---|---|
UniProt AC | P39744 | |
Protein Name | Nucleolar complex protein 2 | |
Gene Name | NOC2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 710 | |
Subcellular Localization | Nucleus, nucleolus . | |
Protein Description | Involved in the intranuclear transport of ribosomal precursors.. | |
Protein Sequence | MGKVSKSTKKFQSKHLKHTLDQRRKEKIQKKRIQGRRGNKTDQEKADAAGTREQQQLKKSAKEEVFKDMSVETFFEKGIEIPKENKKLKKKTTKEQSDEDSSSSEEEEDMGQSMAKLAEKDPEFYKYLEENDKDLLDFAGTNPLDGIDSQDEGEDAERNSNIEEKSEQMELEKEKIELSLKLVRKWKKQLHDSPSLKLLRNIISAFKVAVNLNKEENIEDYKYAITDEKAFHELMFMVLKDVPQAIQKMAPYKIVKGARTLPNGGNVSRVSSIVKSHAGSLLILLNDITNTETAALVLHSVNELMPYLLSYRRILKELIKSIVGVWSTTRELETQIASFAFLINTTKEFKKSMLETTLKTTYSTFIKSCRKTNMRSMPLINFQKNSAAELFGIDEVLGYQVGFEYIRQLAIHLRNTMNATTKKSSKINSAEAYKIVYNWQFCHSLDFWSRVLSFACQPEKENGSESPLRQLIYPLVQVTLGVIRLIPTPQFFPLRFYLIKSLIRLSQNSGVFIPIYPLLSEILTSTAFTKAPKKSPNLAAFDFEHNIKCTQAYLNTKIYQEGLSEQFVDLLGDYFALYCKNIAFPELVTPVIISLRRYIKTSTNVKLNKRLSTVVEKLNQNSTFIQEKRSDVEFGPTNKSEVSRFLNDVAWNKTPLGSYVAVQREVKEEKARLMRESMEEQDKERETEEAKLLNSLESDDDNEDVEMSDA | |
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 |
---|---|---|---|---|---|
14 | Acetylation | STKKFQSKHLKHTLD CHHHHHHHHHHHHHH | 42.02 | 25381059 | |
17 | Acetylation | KFQSKHLKHTLDQRR HHHHHHHHHHHHHHH | 33.97 | 25381059 | |
45 | Ubiquitination | GNKTDQEKADAAGTR CCCCHHHHHHHHCHH | 46.03 | 23749301 | |
45 | Acetylation | GNKTDQEKADAAGTR CCCCHHHHHHHHCHH | 46.03 | 25381059 | |
62 | Acetylation | QQLKKSAKEEVFKDM HHHHHHHHHHHHHCC | 62.59 | 25381059 | |
70 | Phosphorylation | EEVFKDMSVETFFEK HHHHHCCCHHHHHHC | 27.25 | 22369663 | |
73 | Phosphorylation | FKDMSVETFFEKGIE HHCCCHHHHHHCCCC | 31.31 | 22890988 | |
103 | Phosphorylation | QSDEDSSSSEEEEDM CCCCCCCCCHHHHHH | 45.80 | 21551504 | |
104 | Phosphorylation | SDEDSSSSEEEEDMG CCCCCCCCHHHHHHH | 51.48 | 21551504 | |
120 | Acetylation | SMAKLAEKDPEFYKY HHHHHHHHCHHHHHH | 73.33 | 24489116 | |
120 | Succinylation | SMAKLAEKDPEFYKY HHHHHHHHCHHHHHH | 73.33 | 23954790 | |
141 | Phosphorylation | DLLDFAGTNPLDGID CHHHHCCCCCCCCCC | 30.18 | 22890988 | |
149 | Phosphorylation | NPLDGIDSQDEGEDA CCCCCCCCCCCCCCH | 37.30 | 22369663 | |
160 | Phosphorylation | GEDAERNSNIEEKSE CCCHHHCCCHHHHHH | 45.46 | 22369663 | |
166 | Phosphorylation | NSNIEEKSEQMELEK CCCHHHHHHHHHHHH | 36.02 | 17330950 | |
181 | Acetylation | EKIELSLKLVRKWKK HHHHHHHHHHHHHHH | 41.37 | 24489116 | |
197 | Acetylation | LHDSPSLKLLRNIIS HCCCCCHHHHHHHHH | 50.22 | 24489116 | |
222 | Acetylation | EENIEDYKYAITDEK CCCHHHHCEEECCHH | 40.29 | 24489116 | |
384 | Methylation | MPLINFQKNSAAELF CCEEECCCCCHHHHH | 49.05 | 20137074 | |
464 | Phosphorylation | QPEKENGSESPLRQL CCCCCCCCCCHHHHH | 46.62 | 27017623 | |
500 | Acetylation | PLRFYLIKSLIRLSQ CHHHHHHHHHHHHHH | 36.29 | 24489116 | |
534 | Acetylation | AFTKAPKKSPNLAAF CCCCCCCCCCCCCCC | 70.82 | 24489116 | |
548 | Acetylation | FDFEHNIKCTQAYLN CCCCCCCCCCHHHHH | 36.22 | 24489116 | |
612 | Phosphorylation | VKLNKRLSTVVEKLN HHHHHHHHHHHHHHH | 24.16 | 21551504 | |
617 | Acetylation | RLSTVVEKLNQNSTF HHHHHHHHHHCCCCC | 40.92 | 24489116 | |
622 | Phosphorylation | VEKLNQNSTFIQEKR HHHHHCCCCCCHHHH | 18.22 | 22369663 | |
623 | Phosphorylation | EKLNQNSTFIQEKRS HHHHCCCCCCHHHHC | 32.10 | 22369663 | |
639 | Acetylation | VEFGPTNKSEVSRFL CCCCCCCHHHHHHHH | 50.93 | 24489116 | |
677 | Phosphorylation | KARLMRESMEEQDKE HHHHHHHHHHHHHHH | 22.56 | 24961812 | |
695 | Phosphorylation | EEAKLLNSLESDDDN HHHHHHHHHCCCCCC | 33.22 | 22890988 | |
698 | Phosphorylation | KLLNSLESDDDNEDV HHHHHHCCCCCCCCC | 52.19 | 22369663 | |
708 | Phosphorylation | DNEDVEMSDA----- CCCCCCCCCC----- | 19.51 | 22369663 |
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 NOC2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NOC2_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 NOC2_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 SER-70; SER-149; SER-698 ANDSER-708, 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 SER-149, 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-70; SER-149; SER-160;SER-166; SER-698 AND SER-708, AND MASS SPECTROMETRY. |