UTR1_YEAST - dbPTM
UTR1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UTR1_YEAST
UniProt AC P21373
Protein Name NAD(+) kinase
Gene Name UTR1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 530
Subcellular Localization
Protein Description Specifically phosphorylates NAD in the presence of ATP, dATP, or CTP as phosphoryl donors..
Protein Sequence MKENDMNNGVDKWVNEEDGRNDHHNNNNNLMKKAMMNNEQIDRTQDIDNAKEMLRKISSESSSRRSSLLNKDSSLVNGNANSGGGTSINGTRGSSKSSNTHFQYASTAYGVRMLSKDISNTKVELDVENLMIVTKLNDVSLYFLTRELVEWVLVHFPRVTVYVDSELKNSKKFAAGELCEDSKCRESRIKYWTKDFIREHDVFFDLVVTLGGDGTVLFVSSIFQRHVPPVMSFSLGSLGFLTNFKFEHFREDLPRIMNHKIKTNLRLRLECTIYRRHRPEVDPNTGKKICVVEKLSTHHILNEVTIDRGPSPFLSMLELYGDGSLMTVAQADGLIAATPTGSTAYSLSAGGSLVCPTVNAIALTPICPHALSFRPIILPESINLKVKVSMKSRAPAWAAFDGKDRIELQKGDFITICASPYAFPTVEASPDEFINSISRQLNWNVREQQKSFTHILSQKNQEKYAHEANKVRNQAEPLEVIRDKYSLEADATKENNNGSDDESDDESVNCEACKLKPSSVPKPSQARFSV
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
58PhosphorylationKEMLRKISSESSSRR
HHHHHHHHCCCHHHH
30.9620377248
59PhosphorylationEMLRKISSESSSRRS
HHHHHHHCCCHHHHH
44.9920377248
61PhosphorylationLRKISSESSSRRSSL
HHHHHCCCHHHHHHH
35.2520377248
62PhosphorylationRKISSESSSRRSSLL
HHHHCCCHHHHHHHC
24.6620377248
63PhosphorylationKISSESSSRRSSLLN
HHHCCCHHHHHHHCC
40.7820377248
66PhosphorylationSESSSRRSSLLNKDS
CCCHHHHHHHCCCCC
24.9920377248
67PhosphorylationESSSRRSSLLNKDSS
CCHHHHHHHCCCCCC
34.7619823750
73PhosphorylationSSLLNKDSSLVNGNA
HHHCCCCCCCCCCCC
27.4720377248
74PhosphorylationSLLNKDSSLVNGNAN
HHCCCCCCCCCCCCC
46.6122369663
82PhosphorylationLVNGNANSGGGTSIN
CCCCCCCCCCCCCCC
36.0822369663
86PhosphorylationNANSGGGTSINGTRG
CCCCCCCCCCCCCCC
29.7022369663
87PhosphorylationANSGGGTSINGTRGS
CCCCCCCCCCCCCCC
19.8222369663
91PhosphorylationGGTSINGTRGSSKSS
CCCCCCCCCCCCCCC
27.6322369663
94PhosphorylationSINGTRGSSKSSNTH
CCCCCCCCCCCCCCC
31.1622369663
95PhosphorylationINGTRGSSKSSNTHF
CCCCCCCCCCCCCCC
39.1022369663
96UbiquitinationNGTRGSSKSSNTHFQ
CCCCCCCCCCCCCCC
60.6517644757
97PhosphorylationGTRGSSKSSNTHFQY
CCCCCCCCCCCCCCH
30.6722369663
98PhosphorylationTRGSSKSSNTHFQYA
CCCCCCCCCCCCCHH
49.8622369663
100PhosphorylationGSSKSSNTHFQYAST
CCCCCCCCCCCHHHH
26.4722369663
104PhosphorylationSSNTHFQYASTAYGV
CCCCCCCHHHHHHHH
11.1122369663
106PhosphorylationNTHFQYASTAYGVRM
CCCCCHHHHHHHHHH
14.5022369663
107PhosphorylationTHFQYASTAYGVRML
CCCCHHHHHHHHHHE
18.7422369663
109PhosphorylationFQYASTAYGVRMLSK
CCHHHHHHHHHHEEC
19.0822369663
165PhosphorylationRVTVYVDSELKNSKK
CEEEEECHHHCCCCC
34.4827017623
451PhosphorylationNVREQQKSFTHILSQ
CHHHHHHHHHHHHHH
30.9222369663
453PhosphorylationREQQKSFTHILSQKN
HHHHHHHHHHHHHHH
18.3322369663
470UbiquitinationKYAHEANKVRNQAEP
HHHHHHHHHHCCCCC
50.0123749301
499PhosphorylationTKENNNGSDDESDDE
CCCCCCCCCCCCCCC
43.9721440633
503PhosphorylationNNGSDDESDDESVNC
CCCCCCCCCCCCCCC
58.3121440633
507PhosphorylationDDESDDESVNCEACK
CCCCCCCCCCCHHCC
26.1421551504
518PhosphorylationEACKLKPSSVPKPSQ
HHCCCCCCCCCCCCC
42.2420377248
519PhosphorylationACKLKPSSVPKPSQA
HCCCCCCCCCCCCCC
51.4720377248
524PhosphorylationPSSVPKPSQARFSV-
CCCCCCCCCCCCCC-
42.4721440633
529PhosphorylationKPSQARFSV------
CCCCCCCCC------
22.7421440633

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 UTR1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UTR1_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 UTR1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TIR4_YEASTTIR4physical
18467557
YEF1_YEASTYEF1genetic
19158096
POS5_YEASTPOS5genetic
19158096
LTE1_YEASTLTE1genetic
20093466
RL19A_YEASTRPL19Bgenetic
20093466
RL19B_YEASTRPL19Bgenetic
20093466
AIM4_YEASTAIM4genetic
20093466
ODPB_YEASTPDB1genetic
20093466
INO2_YEASTINO2genetic
20093466
ARO1_YEASTARO1genetic
20093466
MNN10_YEASTMNN10genetic
20093466
RV167_YEASTRVS167genetic
20093466
STP1_YEASTSTP1genetic
20093466
ODPA_YEASTPDA1genetic
20093466
CTU1_YEASTNCS6genetic
20093466
MUP1_YEASTMUP1genetic
20093466
PACC_YEASTRIM101genetic
20093466
SDS3_YEASTSDS3genetic
20093466
DHOM_YEASTHOM6genetic
20093466
DCOR_YEASTSPE1genetic
20093466
LHS1_YEASTLHS1genetic
20093466
COX12_YEASTCOX12genetic
20093466
LIPB_YEASTLIP2genetic
20093466
VID22_YEASTVID22genetic
20093466
SOK2_YEASTSOK2genetic
20093466
MOT3_YEASTMOT3genetic
20093466
TOM70_YEASTTOM70genetic
20093466
ODP2_YEASTLAT1genetic
20093466
MED9_YEASTCSE2genetic
20093466
FUMH_YEASTFUM1genetic
20093466
GGPPS_YEASTBTS1genetic
20093466
LGE1_YEASTLGE1genetic
20093466
SPEE_YEASTSPE3genetic
20093466
ACON2_YEASTACO2genetic
21623372
QCR7_YEASTQCR7genetic
21623372
FOLE_YEASTMET7genetic
21623372
QCR8_YEASTQCR8genetic
21623372
GGPPS_YEASTBTS1genetic
21623372
ODPB_YEASTPDB1genetic
21623372
ERG2_YEASTERG2genetic
21623372
COX6_YEASTCOX6genetic
21623372
GSH1_YEASTGSH1genetic
21623372
QCR1_YEASTCOR1genetic
21623372
ODP2_YEASTLAT1genetic
21623372
HFA1_YEASTHFA1genetic
21623372
IDH2_YEASTIDH2genetic
21623372
ODPA_YEASTPDA1genetic
21623372
MET22_YEASTMET22genetic
21623372
COQ7_YEASTCAT5genetic
21623372
COX8_YEASTCOX8genetic
21623372
CYS3_YEASTCYS3genetic
21623372
GCSH_YEASTGCV3genetic
21623372
COQ3_YEASTCOQ3genetic
21623372
COX9_YEASTCOX9genetic
21623372
IDH1_YEASTIDH1genetic
21623372
ODPB_YEASTPDB1genetic
27708008
LIPB_YEASTLIP2genetic
27708008
ODP2_YEASTLAT1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
GPT1_YEASTSCT1genetic
27708008
FMT_YEASTFMT1genetic
27708008
HAP3_YEASTHAP3genetic
27708008
BRE1_YEASTBRE1genetic
27708008
S2538_YEASTYDL119Cgenetic
27708008
ARO1_YEASTARO1genetic
27708008
DHSD_YEASTSDH4genetic
27708008
MNN10_YEASTMNN10genetic
27708008
HRQ1_YEASTHRQ1genetic
27708008
OMS1_YEASTOMS1genetic
27708008
STP1_YEASTSTP1genetic
27708008
MIG1_YEASTMIG1genetic
27708008
MTO1_YEASTMTO1genetic
27708008
SODM_YEASTSOD2genetic
27708008
COX23_YEASTCOX23genetic
27708008
YIA6_YEASTYIA6genetic
27708008
DAL81_YEASTDAL81genetic
27708008
LHS1_YEASTLHS1genetic
27708008
DCOR_YEASTSPE1genetic
27708008
YRA2_YEASTYRA2genetic
27708008
COX8_YEASTCOX8genetic
27708008
RCF1_YEASTRCF1genetic
27708008
SOK2_YEASTSOK2genetic
27708008
MAC1_YEASTMAC1genetic
27708008
MSS1_YEASTMSS1genetic
27708008
MOT3_YEASTMOT3genetic
27708008
COX5A_YEASTCOX5Agenetic
27708008
TOM7_YEASTTOM7genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UTR1_YEAST

loading...

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-74; SER-97; SER-98;THR-100; SER-499; SER-503 AND SER-518, 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-59; SER-67; SER-97 ANDSER-98, 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-63 AND SER-67, AND MASSSPECTROMETRY.

TOP