UTP14_YEAST - dbPTM
UTP14_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UTP14_YEAST
UniProt AC Q04500
Protein Name U3 small nucleolar RNA-associated protein 14
Gene Name UTP14
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 899
Subcellular Localization Nucleus, nucleolus .
Protein Description Involved in nucleolar processing of pre-18S ribosomal RNA..
Protein Sequence MAKKKSKSRSKSSRRVLDALQLAEREINGEFDNSSDNDKRHDARRNGTVVNLLKRSKGDTNSDEDDIDSESFEDEELNSDEALGSDDDYDILNSKFSQTIRDKKENANYQEEEDEGGYTSIDEEDLMPLSQVWDMDEKTAQSNGNDDEDASPQLKLQDTDISSESSSSEESESESEDDEEEEDPFDEISEDEEDIELNTITSKLIDETKSKAPKRLDTYGSGEANEYVLPSANAASGASGKLSLTDMMNVIDDRQVIENANLLKGKSSTYEVPLPQRIQQRHDRKAAYEISRQEVSKWNDIVQQNRRADHLIFPLNKPTEHNHASAFTRTQDVPQTELQEKVDQVLQESNLANPEKDSKFEELSTAKMTPEEMRKRTTEMRLMRELMFREERKARRLKKIKSKTYRKIKKKELMKNRELAAVSSDEDNEDHDIARAKERMTLKHKTNSKWAKDMIKHGMTNDAETREEMEEMLRQGERLKAKMLDRNSDDEEDGRVQTLSDVENEEKENIDSEALKSKLGKTGVMNMAFMKNGEAREREANKETLRQLRAVENGDDIKLFESDEEETNGENIQINKGRRIYTPGSLESNKDMNELNDHTRKENKVDESRSLENRLRAKNSGQSKNARTNAEGAIIVEEESDGEPLQDGQNNQQDEEAKDVNPWLANESDEEHTVKKQSSKVNVIDKDSSKNVKAMNKMEKAELKQKKKKKGKSNDDEDLLLTADDSTRLKIVDPYGGSDDEQGDNVFMFKQQDVIAEAFAGDDVVAEFQEEKKRVIDDEDDKEVDTTLPGWGEWAGAGSKPKNKKRKFIKKVKGVVNKDKRRDKNLQNVIINEKVNKKNLKYQSSAVPFPFENREQYERSLRMPIGQEWTSRASHQELIKPRIMTKPGQVIDPLKAPFK
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
34PhosphorylationINGEFDNSSDNDKRH
HCCCCCCCCCCCHHH		40.7022369663
35PhosphorylationNGEFDNSSDNDKRHD
CCCCCCCCCCCHHHH		46.8422369663
48PhosphorylationHDARRNGTVVNLLKR
HHHHHCCHHHHHHHH		25.4821126336
54AcetylationGTVVNLLKRSKGDTN
CHHHHHHHHCCCCCC		58.7625381059
56PhosphorylationVVNLLKRSKGDTNSD
HHHHHHHCCCCCCCC		39.1324961812
60PhosphorylationLKRSKGDTNSDEDDI
HHHCCCCCCCCHHHC		45.3424961812
62PhosphorylationRSKGDTNSDEDDIDS
HCCCCCCCCHHHCCC		44.4624961812
69PhosphorylationSDEDDIDSESFEDEE
CCHHHCCCCCCCCCC		35.1624961812
71PhosphorylationEDDIDSESFEDEELN
HHHCCCCCCCCCCCC		37.5824961812
79PhosphorylationFEDEELNSDEALGSD
CCCCCCCCCCCCCCC		49.8324961812
85PhosphorylationNSDEALGSDDDYDIL
CCCCCCCCCCHHHHH		38.4224961812
89PhosphorylationALGSDDDYDILNSKF
CCCCCCHHHHHCHHH		16.3324961812
94PhosphorylationDDYDILNSKFSQTIR
CHHHHHCHHHHHHHH		31.4724961812
109PhosphorylationDKKENANYQEEEDEG
HHHHHCCCCCCCCCC		18.1919795423
118PhosphorylationEEEDEGGYTSIDEED
CCCCCCCCCCCCHHH		14.2620377248
119PhosphorylationEEDEGGYTSIDEEDL
CCCCCCCCCCCHHHC		23.6020377248
120PhosphorylationEDEGGYTSIDEEDLM
CCCCCCCCCCHHHCC		21.4021440633
130PhosphorylationEEDLMPLSQVWDMDE
HHHCCCHHHEECCCH		19.4719795423
139PhosphorylationVWDMDEKTAQSNGND
EECCCHHHHHHCCCC		28.0722369663
142PhosphorylationMDEKTAQSNGNDDED
CCHHHHHHCCCCCCC		44.2122369663
151PhosphorylationGNDDEDASPQLKLQD
CCCCCCCCCCHHEEC		26.0422369663
218PhosphorylationKAPKRLDTYGSGEAN
CCCCCCCCCCCCCCC		34.0827214570
219PhosphorylationAPKRLDTYGSGEANE
CCCCCCCCCCCCCCC		14.6823749301
221PhosphorylationKRLDTYGSGEANEYV
CCCCCCCCCCCCCEE		24.0527017623
243PhosphorylationSGASGKLSLTDMMNV
CCCCCCCCHHHHHHH		32.4824909858
267PhosphorylationANLLKGKSSTYEVPL
CCCCCCCCCCCCCCC		36.2630377154
297AcetylationISRQEVSKWNDIVQQ
HHHHHHHHHHHHHHH		56.0124489116
356AcetylationSNLANPEKDSKFEEL
CCCCCHHHCCCHHHH		69.4324489116
364PhosphorylationDSKFEELSTAKMTPE
CCCHHHHHHCCCCHH		29.6028889911
423PhosphorylationNRELAAVSSDEDNED
CCCCCCCCCCCCCCC		27.6122369663
424PhosphorylationRELAAVSSDEDNEDH
CCCCCCCCCCCCCCC		38.1222369663
446PhosphorylationRMTLKHKTNSKWAKD
HHHHCCCCCCHHHHH		44.4328889911
449AcetylationLKHKTNSKWAKDMIK
HCCCCCCHHHHHHHH		53.9225381059
460PhosphorylationDMIKHGMTNDAETRE
HHHHHCCCCCHHHHH		34.2428889911
488PhosphorylationAKMLDRNSDDEEDGR
HHHCCCCCCCCCCCC		47.5422369663
498PhosphorylationEEDGRVQTLSDVENE
CCCCCEECHHHHCCH		25.9322369663
500PhosphorylationDGRVQTLSDVENEEK
CCCEECHHHHCCHHH		42.8922369663
517PhosphorylationIDSEALKSKLGKTGV
CCHHHHHHHHCHHCC		33.6819795423
522PhosphorylationLKSKLGKTGVMNMAF
HHHHHCHHCCCCHHH		32.9619795423
542AcetylationAREREANKETLRQLR
HHHHHHHHHHHHHHH		60.1525381059
562PhosphorylationDDIKLFESDEEETNG
CCCEEECCCCCHHCC		42.8822369663
567PhosphorylationFESDEEETNGENIQI
ECCCCCHHCCCCCEE		52.3725521595
585PhosphorylationRRIYTPGSLESNKDM
CCCCCCCCCCCCCCH		30.1130377154
588PhosphorylationYTPGSLESNKDMNEL
CCCCCCCCCCCHHHH		55.2430377154
590AcetylationPGSLESNKDMNELND
CCCCCCCCCHHHHHH		68.5824489116
599PhosphorylationMNELNDHTRKENKVD
HHHHHHHHHHHHCCC		46.4230377154
628PhosphorylationGQSKNARTNAEGAII
CCCCCCCCCCCCCEE		36.0522369663
640PhosphorylationAIIVEEESDGEPLQD
CEEEEECCCCCCCCC		54.9522369663
668PhosphorylationNPWLANESDEEHTVK
CHHHCCCCCCCCCCC		50.5622369663
673PhosphorylationNESDEEHTVKKQSSK
CCCCCCCCCCCCCCC		36.9822369663
678PhosphorylationEHTVKKQSSKVNVID
CCCCCCCCCCCEEEC		40.7930377154
679PhosphorylationHTVKKQSSKVNVIDK
CCCCCCCCCCEEECC		37.8229136822
680AcetylationTVKKQSSKVNVIDKD
CCCCCCCCCEEECCC		42.9725381059
686AcetylationSKVNVIDKDSSKNVK
CCCEEECCCCCHHHH		48.6724489116
688PhosphorylationVNVIDKDSSKNVKAM
CEEECCCCCHHHHHH		49.2928889911
689PhosphorylationNVIDKDSSKNVKAMN
EEECCCCCHHHHHHH		38.0828889911
700AcetylationKAMNKMEKAELKQKK
HHHHHHHHHHHHHHH		43.6025381059
722PhosphorylationDDEDLLLTADDSTRL
CCCCCEEECCCCCCE		28.1923749301
726PhosphorylationLLLTADDSTRLKIVD
CEEECCCCCCEEEEC		18.9024961812
727PhosphorylationLLTADDSTRLKIVDP
EEECCCCCCEEEECC		47.1924961812
735PhosphorylationRLKIVDPYGGSDDEQ
CEEEECCCCCCCCCC		29.6522890988
738PhosphorylationIVDPYGGSDDEQGDN
EECCCCCCCCCCCCC		37.2122369663
841AcetylationKVNKKNLKYQSSAVP
HHCCCCCCCCCCCCC		51.1124489116
845PhosphorylationKNLKYQSSAVPFPFE
CCCCCCCCCCCCCCC		20.1225704821
895AcetylationGQVIDPLKAPFK---
CCCCCCCCCCCC---		60.4424489116
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 UTP14_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UTP14_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 UTP14_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MPP10_YEASTMPP10physical
12068309
NLE1_YEASTRSA4physical
16554755
NOP14_YEASTNOP14physical
16554755
GCN1_YEASTGCN1physical
16554755
CSR1_YEASTCSR1physical
16554755
IMA1_YEASTSRP1physical
16554755
ISA2_YEASTISA2physical
16554755
BUD23_YEASTBUD23physical
23604635
RS3_YEASTRPS3physical
23604635
MPP10_YEASTMPP10physical
23604635
IMP4_YEASTIMP4physical
23604635
PHB2_YEASTPHB2genetic
27708008
CDC27_YEASTCDC27genetic
27708008
KRR1_YEASTKRR1genetic
27708008
APC11_YEASTAPC11genetic
27708008
FBRL_YEASTNOP1genetic
27708008
NOP14_YEASTNOP14genetic
27708008
NHP2_YEASTNHP2genetic
27708008
PDC2_YEASTPDC2genetic
27708008
CDC1_YEASTCDC1genetic
27708008
FCF1_YEASTFCF1genetic
27708008
UTP5_YEASTUTP5genetic
27708008
UTP6_YEASTUTP6genetic
27708008
RMRP_YEASTSNM1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
DAM1_YEASTDAM1genetic
27708008
BCD1_YEASTBCD1genetic
27708008
RRP3_YEASTRRP3genetic
27708008
UTP9_YEASTUTP9genetic
27708008
NU192_YEASTNUP192genetic
27708008
NUP85_YEASTNUP85genetic
27708008
CDC11_YEASTCDC11genetic
27708008
DCA13_YEASTSOF1genetic
27708008
NEP1_YEASTEMG1genetic
27708008
UTP13_YEASTUTP13genetic
27708008
UTP15_YEASTUTP15genetic
27708008
ROT1_YEASTROT1genetic
27708008
RRP5_YEASTRRP5genetic
27708008
HAS1_YEASTHAS1genetic
27708008
ATC3_YEASTDRS2genetic
27708008
CSG2_YEASTCSG2genetic
27708008
PEX34_YEASTPEX34genetic
27708008
YD114_YEASTYDL114Wgenetic
27708008
NOP6_YEASTNOP6genetic
27708008
TRS85_YEASTTRS85genetic
27708008
SAC3_YEASTSAC3genetic
27708008
MRM2_YEASTMRM2genetic
27708008
CHO2_YEASTCHO2genetic
27708008
YHK5_YEASTYHR045Wgenetic
27708008
LRP1_YEASTLRP1genetic
27708008
CTM1_YEASTCTM1genetic
27708008
TDA11_YEASTTDA11genetic
27708008
STB5_YEASTSTB5genetic
27708008
VPS53_YEASTVPS53genetic
27708008
AVT1_YEASTAVT1genetic
27708008
PTE1_YEASTTES1genetic
27708008
MRT4_YEASTMRT4genetic
27708008
RL1D1_YEASTUTP30genetic
27708008
HBS1_YEASTHBS1genetic
27708008
BAS1_YEASTBAS1genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
DOM34_YEASTDOM34genetic
27708008
YNO0_YEASTYNL140Cgenetic
27708008
RRP6_YEASTRRP6genetic
27708008
BUD21_YEASTBUD21genetic
27708008
SUR1_YEASTSUR1genetic
27708008
YP068_YEASTYPL068Cgenetic
27708008
MDL2_YEASTMDL2genetic
27708008
DHR1_YEASTECM16physical
26729466
IMP4_YEASTIMP4physical
26729466
MPP10_YEASTMPP10physical
26729466
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UTP14_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-34; SER-35; SER-151;SER-423; SER-424; SER-488; SER-500; SER-562; SER-668 AND SER-738, ANDMASS 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-34; SER-35; SER-423;SER-424; SER-500 AND SER-562, 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-423; SER-424; SER-668AND SER-738, 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-34; SER-35; SER-151;SER-423; SER-424; SER-562 AND SER-738, AND MASS SPECTROMETRY.

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