WTM1_YEAST - dbPTM
WTM1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID WTM1_YEAST
UniProt AC Q12363
Protein Name Transcriptional modulator WTM1
Gene Name WTM1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 437
Subcellular Localization Cytoplasm . Nucleus . Shuttles between the nucleus and the cytoplasm.
Protein Description Transcriptional modulator with roles in meiotic regulation and silencing. Acts either as an adapter to facilitate nuclear import by KAP122 of the RNR2-RNR4 herodimer, also called beta-beta' subunit, which corresponds to the small subunit of the ribonucleotide reductase (RNR); or as an anchor to retain RNR2-RNR4 in the nucleus..
Protein Sequence MPKKVWKSSTPSTYEHISSLRPKFVSRVDNVLHQRKSLTFSNVVVPDKKNNTLTSSVIYSQGSDIYEIDFAVPLQEAASEPVKDYGDAFEGIENTSLSPKFVYQGETVSKMAYLDKTGETTLLSMSKNGSLAWFKEGIKVPIHIVQELMGPATSYASIHSLTRPGDLPEKDFSLAISDFGISNDTETIVKSQSNGDEEDSILKIIDNAGKPGEILRTVHVPGTTVTHTVRFFDNHIFASCSDDNILRFWDTRTSDKPIWVLGEPKNGKLTSFDCSQVSNNLFVTGFSTGIIKLWDARAAEAATTDLTYRQNGEDPIQNEIANFYHAGGDSVVDVQFSATSSSEFFTVGGTGNIYHWNTDYSLSKYNPDDTIAPPQDATEESQTKSLRFLHKGGSRRSPKQIGRRNTAAWHPVIENLVGTVDDDSLVSIYKPYTEESE
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
8PhosphorylationMPKKVWKSSTPSTYE
CCCCCCCCCCCHHHH		24.5922369663
9PhosphorylationPKKVWKSSTPSTYEH
CCCCCCCCCCHHHHH		40.3822369663
10PhosphorylationKKVWKSSTPSTYEHI
CCCCCCCCCHHHHHH		28.4922369663
12PhosphorylationVWKSSTPSTYEHISS
CCCCCCCHHHHHHHH		43.6522369663
13PhosphorylationWKSSTPSTYEHISSL
CCCCCCHHHHHHHHC		33.8522369663
14PhosphorylationKSSTPSTYEHISSLR
CCCCCHHHHHHHHCC		15.1722369663
18PhosphorylationPSTYEHISSLRPKFV
CHHHHHHHHCCHHHH		25.8122369663
19PhosphorylationSTYEHISSLRPKFVS
HHHHHHHHCCHHHHH		28.0022369663
23AcetylationHISSLRPKFVSRVDN
HHHHCCHHHHHHHHH		52.5524489116
37PhosphorylationNVLHQRKSLTFSNVV
HHHHCCCCCEEECEE		34.5322369663
39PhosphorylationLHQRKSLTFSNVVVP
HHCCCCCEEECEECC		31.9122369663
41PhosphorylationQRKSLTFSNVVVPDK
CCCCCEEECEECCCC		24.3922369663
48AcetylationSNVVVPDKKNNTLTS
ECEECCCCCCCEEEE		51.8624489116
48SuccinylationSNVVVPDKKNNTLTS
ECEECCCCCCCEEEE		51.8623954790
79PhosphorylationVPLQEAASEPVKDYG
EEHHHHCCCCCCCHH		49.8628889911
85PhosphorylationASEPVKDYGDAFEGI
CCCCCCCHHHCCCCC		15.9319823750
95PhosphorylationAFEGIENTSLSPKFV
CCCCCCCCCCCCCEE		20.4622369663
96PhosphorylationFEGIENTSLSPKFVY
CCCCCCCCCCCCEEE		38.1322369663
98PhosphorylationGIENTSLSPKFVYQG
CCCCCCCCCCEEECC		26.3022369663
107PhosphorylationKFVYQGETVSKMAYL
CEEECCCEEEEEEEE		36.5828889911
116AcetylationSKMAYLDKTGETTLL
EEEEEECCCCCEEEE		56.7024489116
120PhosphorylationYLDKTGETTLLSMSK
EECCCCCEEEEEECC		24.8827017623
124PhosphorylationTGETTLLSMSKNGSL
CCCEEEEEECCCCCE		24.9127017623
126PhosphorylationETTLLSMSKNGSLAW
CEEEEEECCCCCEEE		21.4227017623
127AcetylationTTLLSMSKNGSLAWF
EEEEEECCCCCEEEH		57.6024489116
130PhosphorylationLSMSKNGSLAWFKEG
EEECCCCCEEEHHCC		25.0622369663
153PhosphorylationQELMGPATSYASIHS
HHHHCCCCCHHHHHC		25.9622369663
154PhosphorylationELMGPATSYASIHSL
HHHCCCCCHHHHHCC		22.3222369663
155PhosphorylationLMGPATSYASIHSLT
HHCCCCCHHHHHCCC		10.4621440633
157PhosphorylationGPATSYASIHSLTRP
CCCCCHHHHHCCCCC		16.7619795423
160PhosphorylationTSYASIHSLTRPGDL
CCHHHHHCCCCCCCC		29.7522369663
162PhosphorylationYASIHSLTRPGDLPE
HHHHHCCCCCCCCCH		37.5222369663
187PhosphorylationGISNDTETIVKSQSN
CCCCCCCEEEECCCC		32.9128889911
193PhosphorylationETIVKSQSNGDEEDS
CEEEECCCCCCCHHC		50.2823749301
200PhosphorylationSNGDEEDSILKIIDN
CCCCCHHCHHHHHHC		32.8528889911
210AcetylationKIIDNAGKPGEILRT
HHHHCCCCCCCEEEE		47.6524489116
210SuccinylationKIIDNAGKPGEILRT
HHHHCCCCCCCEEEE		47.6523954790
241PhosphorylationNHIFASCSDDNILRF
CEEEEECCCCCEEEE		45.5721440633
256AcetylationWDTRTSDKPIWVLGE
EECCCCCCCEEEEEC		37.8624489116
308PhosphorylationAATTDLTYRQNGEDP
HHHCCCCCHHCCCCC		19.9425752575
370PhosphorylationSKYNPDDTIAPPQDA
CCCCCCCCCCCCCCC		26.8128889911
384AcetylationATEESQTKSLRFLHK
CCHHHHCCCHHHHHC		39.6024489116
384UbiquitinationATEESQTKSLRFLHK
CCHHHHCCCHHHHHC		39.6023749301
399AcetylationGGSRRSPKQIGRRNT
CCCCCCHHHHCCCCC		56.6525381059
406PhosphorylationKQIGRRNTAAWHPVI
HHHCCCCCHHHHHHH		18.8822369663
419PhosphorylationVIENLVGTVDDDSLV
HHHHHCCCCCCCCCE		17.1822369663
424PhosphorylationVGTVDDDSLVSIYKP
CCCCCCCCCEEEECC		37.3522369663
427PhosphorylationVDDDSLVSIYKPYTE
CCCCCCEEEECCCCC		26.0322369663
429PhosphorylationDDSLVSIYKPYTEES
CCCCEEEECCCCCCC		9.8222369663
432PhosphorylationLVSIYKPYTEESE--
CEEEECCCCCCCC--		23.7222369663
433PhosphorylationVSIYKPYTEESE---
EEEECCCCCCCC---		41.6321440633
436PhosphorylationYKPYTEESE------
ECCCCCCCC------		42.2322369663
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 WTM1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of WTM1_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 WTM1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WTM2_YEASTWTM2physical
11805837
TCPZ_YEASTCCT6physical
11805837
TCPB_YEASTCCT2physical
11805837
TCPA_YEASTTCP1physical
11805837
TCPG_YEASTCCT3physical
11805837
WTM1_YEASTWTM1physical
9234739
WTM2_YEASTWTM2physical
9234739
NAP1_YEASTNAP1physical
16554755
AROF_YEASTARO3physical
16429126
RIR2_YEASTRNR2physical
16429126
RIR4_YEASTRNR4physical
16429126
ATR_YEASTMEC1genetic
16452505
SML1_YEASTSML1genetic
16452505
RIR2_YEASTRNR2physical
16452505
RIR4_YEASTRNR4physical
16452505
RIR2_YEASTRNR2physical
16432237
RIR4_YEASTRNR4physical
16432237
KA122_YEASTKAP122physical
16432237
WTM2_YEASTWTM2physical
18719252
DIF1_YEASTDIF1genetic
18851834
TBCC_YEASTCIN2genetic
20959818
IES4_YEASTIES4genetic
20959818
NU133_YEASTNUP133genetic
21127252
CTH1_YEASTCTH1physical
22152479
CTH2_YEASTTIS11physical
22152479
H3_YEASTHHT1genetic
27708008
MTU1_YEASTSLM3genetic
27708008
AIM18_YEASTAIM18genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
FRMSR_YEASTYKL069Wgenetic
27708008
ENV10_YEASTENV10genetic
27708008
H4_YEASTHHF1genetic
27708008
MET8_YEASTMET8genetic
27708008
SNF5_YEASTSNF5genetic
27708008
ELO2_YEASTELO2genetic
27708008
BCS1_YEASTBCS1genetic
27708008
EFM5_YEASTAML1genetic
27708008
IRE1_YEASTIRE1genetic
27708008
NAM8_YEASTNAM8genetic
27708008
COX23_YEASTCOX23genetic
27708008
GPP1_YEASTGPP1genetic
27708008
FLX1_YEASTFLX1genetic
27708008
BNA3_YEASTBNA3genetic
27708008
YJ24_YEASTKCH1genetic
27708008
PUF3_YEASTPUF3genetic
27708008
NEJ1_YEASTNEJ1genetic
27708008
PUN1_YEASTPUN1genetic
27708008
YPT7_YEASTYPT7genetic
27708008
YHM2_YEASTYHM2genetic
27708008
AEP2_YEASTAEP2genetic
27708008
ELP6_YEASTELP6genetic
27708008
SWS2_YEASTSWS2genetic
27708008
LSM7_YEASTLSM7genetic
27708008
COQ2_YEASTCOQ2genetic
27708008
MNT4_YEASTMNT4genetic
27708008
COQ10_YEASTCOQ10genetic
27708008
DPP3_YEASTYOL057Wgenetic
27708008
HMI1_YEASTHMI1genetic
27708008
BUB3_YEASTBUB3genetic
27708008
CUR1_YEASTCUR1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of WTM1_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 THR-10; THR-39; SER-79;THR-107; THR-187; SER-193; SER-200 AND THR-370, 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-10, AND MASSSPECTROMETRY.

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