NOL10_YEAST - dbPTM
NOL10_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NOL10_YEAST
UniProt AC P48234
Protein Name Ribosome biogenesis protein ENP2
Gene Name ENP2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 707
Subcellular Localization Nucleus, nucleolus .
Protein Description May be involved in rRNA-processing and ribosome biosynthesis..
Protein Sequence MVLKSTSANDVSVYQVSGTNVSRSLPDWIAKKRKRQLKNDLEYQNRVELIQDFEFSEASNKIKVSRDGQYCMATGTYKPQIHVYDFANLSLKFDRHTDAENVDFTILSDDWTKSVHLQNDRSIQFQNKGGLHYTTRIPKFGRSLVYNKVNCDLYVGASGNELYRLNLEKGRFLNPFKLDTEGVNHVSINEVNGLLAAGTETNVVEFWDPRSRSRVSKLYLENNIDNRPFQVTTTSFRNDGLTFACGTSNGYSYIYDLRTSEPSIIKDQGYGFDIKKIIWLDNVGTENKIVTCDKRIAKIWDRLDGKAYASMEPSVDINDIEHVPGTGMFFTANESIPMHTYYIPSLGPSPRWCSFLDSITEELEEKPSDTVYSNYRFITRDDVKKLNLTHLVGSRVLRAYMHGFFINTELYDKVSLIANPDAYKDEREREIRRRIEKERESRIRSSGAVQKPKIKVNKTLVDKLSQKRGDKVAGKVLTDDRFKEMFEDEEFQVDEDDYDFKQLNPVKSIKETEEGAAKRIRALTAAEESDEERIAMKDGRGHYDYEDEESDEEESDDETNQKSNKEELSEKDLRKMEKQKALIERRKKEKEQSERFMNEMKAGTSTSTQRDESAHVTFGEQVGELLEVENGKKSNESILRRNQRGEAELTFIPQRKSKKDGNYKSRRHDNSSDEEGIDENGNKKDNGRSKPRFENRRRASKNAFRGM
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
5Phosphorylation---MVLKSTSANDVS
---CCCCCCCCCCEE		24.3530377154
12PhosphorylationSTSANDVSVYQVSGT
CCCCCCEEEEEEECC		20.2619779198
14PhosphorylationSANDVSVYQVSGTNV
CCCCEEEEEEECCCC		8.8319779198
17PhosphorylationDVSVYQVSGTNVSRS
CEEEEEEECCCCCCC		25.1126447709
19PhosphorylationSVYQVSGTNVSRSLP
EEEEEECCCCCCCHH		25.5826447709
22PhosphorylationQVSGTNVSRSLPDWI
EEECCCCCCCHHHHH		20.4426447709
31AcetylationSLPDWIAKKRKRQLK
CHHHHHHHHHHHHHH		43.9324489116
38AcetylationKKRKRQLKNDLEYQN
HHHHHHHHHHHHHHH		39.8322865919
90PhosphorylationVYDFANLSLKFDRHT
EEECCCEEEEECCCC		29.3515665377
389PhosphorylationDVKKLNLTHLVGSRV
HHHHCCCHHHHHHHH		16.4627017623
394PhosphorylationNLTHLVGSRVLRAYM
CCHHHHHHHHHHHHH		16.2527017623
400PhosphorylationGSRVLRAYMHGFFIN
HHHHHHHHHCCEEEC		5.3428889911
411PhosphorylationFFINTELYDKVSLIA
EEECCHHHHHEEEEC		13.9028889911
424AcetylationIANPDAYKDEREREI
ECCCCCCHHHHHHHH		55.6324489116
445PhosphorylationERESRIRSSGAVQKP
HHHHHHHCCCCCCCC		30.6530377154
458AcetylationKPKIKVNKTLVDKLS
CCCCCCCHHHHHHHH		46.3425381059
463AcetylationVNKTLVDKLSQKRGD
CCHHHHHHHHHHCCC		42.4324489116
465PhosphorylationKTLVDKLSQKRGDKV
HHHHHHHHHHCCCCC		39.1223749301
475AcetylationRGDKVAGKVLTDDRF
CCCCCCCEECCCHHH		25.0825381059
507AcetylationFKQLNPVKSIKETEE
CHHCCCCCCHHHCHH		47.9625381059
508PhosphorylationKQLNPVKSIKETEEG
HHCCCCCCHHHCHHH		38.8428889911
510AcetylationLNPVKSIKETEEGAA
CCCCCCHHHCHHHHH		66.7225381059
518AcetylationETEEGAAKRIRALTA
HCHHHHHHHHHHHHH		48.0725381059
524PhosphorylationAKRIRALTAAEESDE
HHHHHHHHHHHCCHH		23.8822890988
529PhosphorylationALTAAEESDEERIAM
HHHHHHCCHHHHHCC		41.6522369663
537AcetylationDEERIAMKDGRGHYD
HHHHHCCCCCCCCCC		48.2725381059
543PhosphorylationMKDGRGHYDYEDEES
CCCCCCCCCCCCCCC		24.0422890988
545PhosphorylationDGRGHYDYEDEESDE
CCCCCCCCCCCCCCC		20.3622890988
550PhosphorylationYDYEDEESDEEESDD
CCCCCCCCCCCCCCC		48.5525521595
555PhosphorylationEESDEEESDDETNQK
CCCCCCCCCCHHHHH		54.3525521595
559PhosphorylationEEESDDETNQKSNKE
CCCCCCHHHHHHCHH		50.3622890988
565AcetylationETNQKSNKEELSEKD
HHHHHHCHHHHCHHH		60.7125381059
605PhosphorylationNEMKAGTSTSTQRDE
HHHHCCCCCCCCCHH		21.3130377154
634PhosphorylationEVENGKKSNESILRR
EEECCCCCCHHHHHH		49.6828889911
637PhosphorylationNGKKSNESILRRNQR
CCCCCCHHHHHHCCC		31.0430377154
665PhosphorylationKKDGNYKSRRHDNSS
CCCCCCCCCCCCCCC		24.9627717283
671PhosphorylationKSRRHDNSSDEEGID
CCCCCCCCCCCCCCC		45.2728889911
672PhosphorylationSRRHDNSSDEEGIDE
CCCCCCCCCCCCCCC		56.1228889911
701AcetylationENRRRASKNAFRGM-
HHHHHHHHHHHCCC-		51.8425381059
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 NOL10_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NOL10_YEAST !!
Disease-associated PTM Sites based on SAP

* 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 NOL10_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARE1_YEASTARE1physical
22875988
SHE9_YEASTSHE9physical
22875988
NST1_YEASTNST1physical
22875988
BFR2_YEASTBFR2physical
24357410
MCM1_YEASTMCM1genetic
27708008
PYC2_YEASTPYC2genetic
27708008
AIM11_YEASTAIM11genetic
27708008
PMT3_YEASTPMT3genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
STU1_YEASTSTU1genetic
27708008
MCM7_YEASTMCM7genetic
27708008
APC11_YEASTAPC11genetic
27708008
CDC26_YEASTCDC26genetic
27708008
KTHY_YEASTCDC8genetic
27708008
SEC22_YEASTSEC22genetic
27708008
SYA_YEASTALA1genetic
27708008
BUR1_YEASTSGV1genetic
27708008
YAJ9_YEASTYAR029Wgenetic
27708008
ICS2_YEASTICS2genetic
27708008
VPS41_YEASTVPS41genetic
27708008
INO2_YEASTINO2genetic
27708008
ACL4_YEASTYDR161Wgenetic
27708008
APT2_YEASTAPT2genetic
27708008
VAM7_YEASTVAM7genetic
27708008
INM1_YEASTINM1genetic
27708008
VPS53_YEASTVPS53genetic
27708008
FABG_YEASTOAR1genetic
27708008
MCR1_YEASTMCR1genetic
27708008
SRL3_YEASTSRL3genetic
27708008
POM33_YEASTPOM33genetic
27708008
APTH1_YEASTYLR118Cgenetic
27708008
EIF3J_YEASTHCR1genetic
27708008
YL287_YEASTYLR287Cgenetic
27708008
RL6B_YEASTRPL6Bgenetic
27708008
RAD14_YEASTRAD14genetic
27708008
PET8_YEASTPET8genetic
27708008
PMS1_YEASTPMS1genetic
27708008
LDS2_YEASTLDS2genetic
27708008
YP109_YEASTYPL109Cgenetic
27708008
NHP6A_YEASTNHP6Agenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NOL10_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-529; SER-550 ANDSER-555, 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-529; SER-550 ANDSER-555, 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-529, 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-529; SER-550 ANDSER-555, AND MASS SPECTROMETRY.

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