UTP22_YEAST - dbPTM
UTP22_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UTP22_YEAST
UniProt AC P53254
Protein Name U3 small nucleolar RNA-associated protein 22
Gene Name UTP22
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1237
Subcellular Localization Nucleus, nucleolus .
Protein Description Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly..
Protein Sequence MATSVKRKASETSDQNIVKVQKKHSTQDSTTDNGSKENDHSSQAINERTVPEQENDESDTSPESNEVATNTAATRHNGKVTATESYDIHIARETAELFKSNIFKLQIDELLEQVKLKQKHVLKVEKFLHKLYDILQEIPDWEEKSLAEVDSFFKNKIVSVPFVDPKPIPQNTNYKFNYKKPDISLIGSFALKAGIYQPNGSSIDTLLTMPKELFEKKDFLNFRCLHKRSVYLAYLTHHLLILLKKDKLDSFLQLEYSYFDNDPLLPILRISCSKPTGDSLSDYNFYKTRFSINLLIGFPYKVFEPKKLLPNRNCIRIAQESKEQSLPATPLYNFSVLSSSTHENYLKYLYKTKKQTESFVEATVLGRLWLQQRGFSSNMSHSGSLGGFGTFEFTILMAALLNGGGINSNKILLHGFSSYQLFKGVIKYLATMDLCHDGHLQFHSNPENSSSSPASKYIDEGFQTPTLFDKSTKVNILTKMTVSSYQILKEYAGETLRMLNNVVQDQFSNIFLTNISRFDNLKYDLCYDVQLPLGKYNNLETSLAATFGSMERVKFITLENFLAHKITNVARYALGDRIKYIQIEMVGQKSDFPITKRKVYSNTGGNHFNFDFVRVKLIVNPSECDKLVTKGPAHSETMSTEAAVFKNFWGIKSSLRRFKDGSITHCCVWSTSSSEPIISSIVNFALQKHVSKKAQISNETIKKFHNFLPLPNLPSSAKTSVLNLSSFFNLKKSFDDLYKIIFQMKLPLSVKSILPVGSAFRYTSLCQPVPFAYSDPDFFQDVILEFETSPKWPDEITSLEKAKTAFLLKIQEELSANSSTYRSFFSRDESIPYNLEIVTLNILTPEGYGFKFRVLTERDEILYLRAIANARNELKPELEATFLKFTAKYLASVRHTRTLENISHSYQFYSPVVRLFKRWLDTHLLLGHITDELAELIAIKPFVDPAPYFIPGSLENGFLKVLKFISQWNWKDDPLILDLVKPEDDIRDTFETSIGAGSELDSKTMKKLSERLTLAQYKGIQMNFTNLRNSDPNGTHLQFFVASKNDPSGILYSSGIPLPIATRLTALAKVAVNLLQTHGLNQQTINLLFTPGLKDYDFVVDLRTPIGLKSSCGILSATEFKNITNDQAPSNFPENLNDLSEKMDPTYQLVKYLNLKYKNSLILSSRKYIGVNGGEKGDKNVITGLIKPLFKGAHKFRVNLDCNVKPVDDENVILNKEAIFHEIAAFGNDMVINFETD
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
10PhosphorylationTSVKRKASETSDQNI
CCCCCCCCCCCCCCC
44.4325521595
12PhosphorylationVKRKASETSDQNIVK
CCCCCCCCCCCCCEE
34.8022369663
13PhosphorylationKRKASETSDQNIVKV
CCCCCCCCCCCCEEE
32.9022369663
25PhosphorylationVKVQKKHSTQDSTTD
EEEEECCCCCCCCCC
36.3228889911
31PhosphorylationHSTQDSTTDNGSKEN
CCCCCCCCCCCCCCC
31.2721082442
35PhosphorylationDSTTDNGSKENDHSS
CCCCCCCCCCCCCCC
42.9528889911
41PhosphorylationGSKENDHSSQAINER
CCCCCCCCCHHHHHC
27.3227214570
42PhosphorylationSKENDHSSQAINERT
CCCCCCCCHHHHHCC
21.8823749301
49PhosphorylationSQAINERTVPEQEND
CHHHHHCCCCCCCCC
33.9421551504
58PhosphorylationPEQENDESDTSPESN
CCCCCCCCCCCCCCC
49.4022369663
60PhosphorylationQENDESDTSPESNEV
CCCCCCCCCCCCCCH
56.3022369663
61PhosphorylationENDESDTSPESNEVA
CCCCCCCCCCCCCHH
31.4922369663
64PhosphorylationESDTSPESNEVATNT
CCCCCCCCCCHHHCC
41.4922890988
69PhosphorylationPESNEVATNTAATRH
CCCCCHHHCCCCCEE
37.9722890988
71PhosphorylationSNEVATNTAATRHNG
CCCHHHCCCCCEECC
17.2022890988
74PhosphorylationVATNTAATRHNGKVT
HHHCCCCCEECCEEE
29.9622890988
154AcetylationAEVDSFFKNKIVSVP
HHHHHHHHCCEEECE
56.1524489116
159PhosphorylationFFKNKIVSVPFVDPK
HHHCCEEECEECCCC
27.7821551504
166AcetylationSVPFVDPKPIPQNTN
ECEECCCCCCCCCCC
51.6324489116
287AcetylationLSDYNFYKTRFSINL
HHHCCCCCCEEEEEE
29.1424489116
321PhosphorylationCIRIAQESKEQSLPA
CHHHCHHHHHCCCCC
29.4328747907
325PhosphorylationAQESKEQSLPATPLY
CHHHHHCCCCCCCCC
37.0928747907
332PhosphorylationSLPATPLYNFSVLSS
CCCCCCCCCEECCCC
18.5028747907
340PhosphorylationNFSVLSSSTHENYLK
CEECCCCCCCHHHHH
30.3328747907
341PhosphorylationFSVLSSSTHENYLKY
EECCCCCCCHHHHHH
34.8528747907
376PhosphorylationWLQQRGFSSNMSHSG
HHHHCCCCCCCCCCC
24.5130377154
377PhosphorylationLQQRGFSSNMSHSGS
HHHCCCCCCCCCCCC
34.0030377154
408PhosphorylationLNGGGINSNKILLHG
HCCCCCCCCCEEECC
37.2630377154
470AcetylationQTPTLFDKSTKVNIL
CCCCCCCCCCCCEEE
53.3324489116
536PhosphorylationVQLPLGKYNNLETSL
EECCCCCCCCHHHHH
13.9027017623
541PhosphorylationGKYNNLETSLAATFG
CCCCCHHHHHHHHHC
32.0127017623
554AcetylationFGSMERVKFITLENF
HCCHHHEEEEEHHHH
36.9524489116
565AcetylationLENFLAHKITNVARY
HHHHHHHHHHHHHHH
45.6924489116
626AcetylationVNPSECDKLVTKGPA
ECHHHHHHHEECCCC
57.4224489116
662PhosphorylationLRRFKDGSITHCCVW
HHHCCCCCEEEEEEE
34.1519779198
664PhosphorylationRFKDGSITHCCVWST
HCCCCCEEEEEEEEC
15.5719779198
670PhosphorylationITHCCVWSTSSSEPI
EEEEEEEECCCCCCH
9.6719779198
998PhosphorylationETSIGAGSELDSKTM
HHCCCCCCCCCHHHH
34.1627017623
1002PhosphorylationGAGSELDSKTMKKLS
CCCCCCCHHHHHHHH
42.5227017623
1004PhosphorylationGSELDSKTMKKLSER
CCCCCHHHHHHHHHH
37.8727017623
1116PhosphorylationKSSCGILSATEFKNI
CCCCCCCCHHHCCCC
31.0927214570
1158MethylationKYLNLKYKNSLILSS
HHHCCEECCEEEEEC
38.1720137074
1160PhosphorylationLNLKYKNSLILSSRK
HCCEECCEEEEECCC
16.7928889911
1164PhosphorylationYKNSLILSSRKYIGV
ECCEEEEECCCEEEC
22.5428889911
1205UbiquitinationVNLDCNVKPVDDENV
EECCCCCCCCCCCCE
25.9023749301

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 UTP22_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UTP22_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 UTP22_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RRP7_YEASTRRP7physical
14759368
CSK21_YEASTCKA1physical
14759368
CSK22_YEASTCKA2physical
14759368
CSK2B_YEASTCKB1physical
14759368
CSK2C_YEASTCKB2physical
14759368
UTP22_YEASTUTP22physical
14759368
CSK2C_YEASTCKB2physical
11805826
ENP1_YEASTENP1physical
11805826
UTP7_YEASTUTP7physical
11805826
PWP2_YEASTPWP2physical
11805826
GBLP_YEASTASC1physical
11805826
BFR2_YEASTBFR2physical
11805826
BRX1_YEASTBRX1physical
11805826
CSK21_YEASTCKA1physical
11805826
CSK22_YEASTCKA2physical
11805826
CSK2B_YEASTCKB1physical
11805826
DIM1_YEASTDIM1physical
11805826
UTP12_YEASTDIP2physical
11805826
RRP44_YEASTDIS3physical
11805826
DHR1_YEASTECM16physical
11805826
NEP1_YEASTEMG1physical
11805826
IMP3_YEASTIMP3physical
11805826
NAT10_YEASTKRE33physical
11805826
MPP10_YEASTMPP10physical
11805826
UTP17_YEASTNAN1physical
11805826
FBRL_YEASTNOP1physical
11805826
NOP14_YEASTNOP14physical
11805826
ROK1_YEASTROK1physical
11805826
RRP7_YEASTRRP7physical
11805826
UTP20_YEASTUTP20physical
11805826
UTP4_YEASTUTP4physical
11805826
UTP6_YEASTUTP6physical
11805826
UTP8_YEASTUTP8physical
11805826
NOL10_YEASTENP2physical
11805826
UTP10_YEASTUTP10physical
11805826
RL1D1_YEASTUTP30physical
11805826
CMS1_YEASTCMS1physical
11805826
UTP21_YEASTUTP21physical
11805826
PNO1_YEASTPNO1physical
11805826
NOC2_YEASTNOC2physical
11805826
NOC4_YEASTNOC4physical
11805826
ENP1_YEASTENP1physical
12150911
NOC4_YEASTNOC4physical
12150911
NOP14_YEASTNOP14physical
12150911
PWP2_YEASTPWP2physical
12150911
UTP6_YEASTUTP6physical
12150911
BFR2_YEASTBFR2physical
12150911
UTP12_YEASTDIP2physical
12150911
DHR1_YEASTECM16physical
12150911
NEP1_YEASTEMG1physical
12150911
IMP3_YEASTIMP3physical
12150911
NAT10_YEASTKRE33physical
12150911
MPP10_YEASTMPP10physical
12150911
UTP17_YEASTNAN1physical
12150911
FBRL_YEASTNOP1physical
12150911
ROK1_YEASTROK1physical
12150911
RL20A_YEASTRPL20Bphysical
12150911
RL20B_YEASTRPL20Bphysical
12150911
RL30_YEASTRPL30physical
12150911
RS11A_YEASTRPS11Aphysical
12150911
RS11B_YEASTRPS11Aphysical
12150911
RS13_YEASTRPS13physical
12150911
RS17A_YEASTRPS17Aphysical
12150911
RS17B_YEASTRPS17Bphysical
12150911
RS3A2_YEASTRPS1Bphysical
12150911
RS24A_YEASTRPS24Bphysical
12150911
RS24B_YEASTRPS24Bphysical
12150911
RS4A_YEASTRPS4Aphysical
12150911
RS4B_YEASTRPS4Aphysical
12150911
RS5_YEASTRPS5physical
12150911
RS7A_YEASTRPS7Aphysical
12150911
UTP20_YEASTUTP20physical
12150911
UTP4_YEASTUTP4physical
12150911
UTP8_YEASTUTP8physical
12150911
NOL10_YEASTENP2physical
12150911
UTP10_YEASTUTP10physical
12150911
RL1D1_YEASTUTP30physical
12150911
UTP21_YEASTUTP21physical
12150911
DIM1_YEASTDIM1physical
12150911
MPP10_YEASTMPP10physical
15590835
TSR1_YEASTTSR1physical
16554755
HMO1_YEASTHMO1physical
16554755
CSK2B_YEASTCKB1physical
16554755
CSK21_YEASTCKA1physical
16554755
EBP2_YEASTEBP2physical
16554755
STM1_YEASTSTM1physical
16554755
IFH1_YEASTIFH1physical
16554755
RRP5_YEASTRRP5physical
16554755
NOP2_YEASTNOP2physical
16554755
TDA7_YEASTTDA7physical
16554755
NOC2_YEASTNOC2physical
16554755
RRS1_YEASTRRS1physical
16554755
NOP53_YEASTNOP53physical
16554755
BFR2_YEASTBFR2physical
16429126
CSK21_YEASTCKA1physical
16429126
CSK22_YEASTCKA2physical
16429126
CSK2B_YEASTCKB1physical
16429126
CSK2C_YEASTCKB2physical
16429126
DIM1_YEASTDIM1physical
16429126
UTP12_YEASTDIP2physical
16429126
DHR1_YEASTECM16physical
16429126
NEP1_YEASTEMG1physical
16429126
GBP2_YEASTGBP2physical
16429126
IMP3_YEASTIMP3physical
16429126
MPP10_YEASTMPP10physical
16429126
NOC4_YEASTNOC4physical
16429126
FBRL_YEASTNOP1physical
16429126
NOP14_YEASTNOP14physical
16429126
PNO1_YEASTPNO1physical
16429126
PWP2_YEASTPWP2physical
16429126
ROK1_YEASTROK1physical
16429126
RS11A_YEASTRPS11Aphysical
16429126
RS11B_YEASTRPS11Aphysical
16429126
RS13_YEASTRPS13physical
16429126
RS17A_YEASTRPS17Aphysical
16429126
RS3A2_YEASTRPS1Bphysical
16429126
RS24A_YEASTRPS24Bphysical
16429126
RS24B_YEASTRPS24Bphysical
16429126
RS4A_YEASTRPS4Aphysical
16429126
RS4B_YEASTRPS4Aphysical
16429126
RRP7_YEASTRRP7physical
16429126
UTP10_YEASTUTP10physical
16429126
UTP21_YEASTUTP21physical
16429126
RL1D1_YEASTUTP30physical
16429126
UTP6_YEASTUTP6physical
16429126
UTP7_YEASTUTP7physical
16429126
NOL10_YEASTENP2physical
16429126
CMS1_YEASTCMS1physical
16429126
ENP1_YEASTENP1physical
16429126
NAT10_YEASTKRE33physical
16429126
RS8A_YEASTRPS8Aphysical
16429126
RS8B_YEASTRPS8Aphysical
16429126
RRP5_YEASTRRP5physical
16429126
UTP20_YEASTUTP20physical
16429126
RS22A_YEASTRPS22Aphysical
16429126
RS7A_YEASTRPS7Aphysical
16429126
UTP17_YEASTNAN1physical
16429126
UTP4_YEASTUTP4physical
16429126
UTP8_YEASTUTP8physical
16429126
RS5_YEASTRPS5physical
16429126
RL30_YEASTRPL30physical
16429126
GBLP_YEASTASC1physical
16429126
IFH1_YEASTIFH1physical
17452446
FHL1_YEASTFHL1physical
17452446
UTP8_YEASTUTP8physical
17634288
HSP71_YEASTSSA1physical
19536198
SSB1_YEASTSSB1physical
19536198
LSM6_YEASTLSM6genetic
20093466
NNK1_YEASTNNK1genetic
20093466
VIP1_YEASTVIP1genetic
20093466
PHO23_YEASTPHO23genetic
20093466
PMA2_YEASTPMA2genetic
20093466
IFH1_YEASTIFH1physical
23973296
NNK1_YEASTNNK1genetic
22282571
RRP7_YEASTRRP7physical
24130456
UTP8_YEASTUTP8physical
23194188
SYYC_YEASTTYS1physical
23194188
XPOT_YEASTLOS1physical
23194188
RS8A_YEASTRPS8Aphysical
23604635
RS8B_YEASTRPS8Aphysical
23604635
PXR1_YEASTPXR1physical
24823796
IFH1_YEASTIFH1physical
27818142
RRP7_YEASTRRP7physical
27818142

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UTP22_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-10; SER-42; THR-49;SER-58 AND THR-60, 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-10, AND MASSSPECTROMETRY.
"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-10; THR-12 AND SER-13,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-10, AND MASSSPECTROMETRY.

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