DUR1_YEAST - dbPTM
DUR1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DUR1_YEAST
UniProt AC P32528
Protein Name Urea amidolyase
Gene Name DUR1,2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1835
Subcellular Localization
Protein Description Hydrolysis of urea to ammonia and CO(2)..
Protein Sequence MTVSSDTTAEISLGWSIQDWIDFHKSSSSQASLRLLESLLDSQNVAPVDNAWISLISKENLLHQFQILKSRENKETLPLYGVPIAVKDNIDVRGLPTTAACPSFAYEPSKDSKVVELLRNAGAIIVGKTNLDQFATGLVGTRSPYGKTPCAFSKEHVSGGSSAGSASVVARGIVPIALGTDTAGSGRVPAALNNLIGLKPTKGVFSCQGVVPACKSLDCVSIFALNLSDAERCFRIMCQPDPDNDEYSRPYVSNPLKKFSSNVTIAIPKNIPWYGETKNPVLFSNAVENLSRTGANVIEIDFEPLLELARCLYEGTWVAERYQAIQSFLDSKPPKESLDPTVISIIEGAKKYSAVDCFSFEYKRQGILQKVRRLLESVDVLCVPTCPLNPTMQQVADEPVLVNSRQGTWTNFVNLADLAALAVPAGFRDDGLPNGITLIGKKFTDYALLELANRYFQNIFPNGSRTYGTFTSSSVKPANDQLVGPDYDPSTSIKLAVVGAHLKGLPLHWQLEKVNATYLCTTKTSKAYQLFALPKNGPVLKPGLRRVQDSNGSQIELEVYSVPKELFGAFISMVPEPLGIGSVELESGEWIKSFICEESGYKAKGTVDITKYGGFRAYFEMLKKKESQKKKLFDTVLIANRGEIAVRIIKTLKKLGIRSVAVYSDPDKYSQHVTDADVSVPLHGTTAAQTYLDMNKIIDAAKQTNAQAIIPGYGFLSENADFSDACTSAGITFVGPSGDIIRGLGLKHSARQIAQKAGVPLVPGSLLITSVEEAKKVAAELEYPVMVKSTAGGGGIGLQKVDSEEDIEHIFETVKHQGETFFGDAGVFLERFIENARHVEVQLMGDGFGKAIALGERDCSLQRRNQKVIEETPAPNLPEKTRLALRKAAESLGSLLNYKCAGTVEFIYDEKKDEFYFLEVNTRLQVEHPITEMVTGLDLVEWMIRIAANDAPDFDSTKVEVNGVSMEARLYAENPLKNFRPSPGLLVDVKFPDWARVDTWVKKGTNISPEYDPTLAKIIVHGKDRDDAISKLNQALEETKVYGCITNIDYLKSIITSDFFAKAKVSTNILNSYQYEPTAIEITLPGAHTSIQDYPGRVGYWRIGVPPSGPMDAYSFRLANRIVGNDYRTPAIEVTLTGPSIVFHCETVIAITGGTALCTLDGQEIPQHKPVEVKRGSTLSIGKLTSGCRAYLGIRGGIDVPKYLGSYSTFTLGNVGGYNGRVLKLGDVLFLPSNEENKSVECLPQNIPQSLIPQISETKEWRIGVTCGPHGSPDFFKPESIEEFFSEKWKVHYNSNRFGVRLIGPKPKWARSNGGEGGMHPSNTHDYVYSLGAINFTGDEPVIITCDGPSLGGFVCQAVVPEAELWKVGQVKPGDSIQFVPLSYESSRSLKESQDVAIKSLDGTKLRRLDSVSILPSFETPILAQMEKVNELSPKVVYRQAGDRYVLVEYGDNEMNFNISYRIECLISLVKKNKTIGIVEMSQGVRSVLIEFDGYKVTQKELLKVLVAYETEIQFDENWKITSNIIRLPMAFEDSKTLACVQRYQETIRSSAPWLPNNVDFIANVNGISRNEVYDMLYSARFMVLGLGDVFLGSPCAVPLDPRHRFLGSKYNPSRTYTERGAVGIGGMYMCIYAANSPGGYQLVGRTIPIWDKLCLAASSEVPWLMNPFDQVEFYPVSEEDLDKMTEDCDNGVYKVNIEKSVFDHQEYLRWINANKDSITAFQEGQLGERAEEFAKLIQNANSELKESVTVKPDEEEDFPEGAEIVYSEYSGRFWKSIASVGDVIEAGQGLLIIEAMKAEMIISAPKSGKIIKICHGNGDMVDSGDIVAVIETLA
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
69AcetylationLHQFQILKSRENKET
HHHHHHHHCCCCCCC		49.4422865919
136PhosphorylationTNLDQFATGLVGTRS
CCHHHHCCCCCCCCC		32.1322369663
141PhosphorylationFATGLVGTRSPYGKT
HCCCCCCCCCCCCCC		22.0922369663
143PhosphorylationTGLVGTRSPYGKTPC
CCCCCCCCCCCCCCC		23.4722369663
145PhosphorylationLVGTRSPYGKTPCAF
CCCCCCCCCCCCCCC		32.2822369663
154AcetylationKTPCAFSKEHVSGGS
CCCCCCCCCCCCCCC		45.4422865919
260PhosphorylationSNPLKKFSSNVTIAI
CCCCHHCCCCCEEEE		29.8619823750
261PhosphorylationNPLKKFSSNVTIAIP
CCCHHCCCCCEEEEC		38.1519823750
264PhosphorylationKKFSSNVTIAIPKNI
HHCCCCCEEEECCCC		14.6719823750
526AcetylationLCTTKTSKAYQLFAL
EEECCCCCCHHEEEC		57.2422865919
611UbiquitinationKGTVDITKYGGFRAY
EEEEEECEECHHHHH		42.0824961812
803PhosphorylationIGLQKVDSEEDIEHI
CCCEECCCHHHHHHH		45.9622369663
880UbiquitinationPAPNLPEKTRLALRK
CCCCCCHHHHHHHHH		36.6823749301
1400PhosphorylationSQDVAIKSLDGTKLR
CCCEEEECCCCCEEE		26.1117563356
1411PhosphorylationTKLRRLDSVSILPSF
CEEEECCCEEECCCC		23.5022369663
1413PhosphorylationLRRLDSVSILPSFET
EEECCCEEECCCCCC		23.5121440633
1417PhosphorylationDSVSILPSFETPILA
CCEEECCCCCCCHHH		32.0622369663
1433PhosphorylationMEKVNELSPKVVYRQ
HHHHHCCCCCEEEEE		19.2529734811
1700AcetylationVYKVNIEKSVFDHQE
EEEEEECCCCCCHHH		48.3922865919
1798BiotinylationLLIIEAMKAEMIISA
EEEEEEEEEEEEEEC		48.52-
1798N6-biotinyllysineLLIIEAMKAEMIISA
EEEEEEEEEEEEEEC		48.52-
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 DUR1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DUR1_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 DUR1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RV161_YEASTRVS161genetic
20093466
RTG2_YEASTRTG2genetic
20093466
FIS1_YEASTFIS1genetic
20093466
PFKA2_YEASTPFK2genetic
20093466
MKS1_YEASTMKS1genetic
20093466
COQ2_YEASTCOQ2genetic
21623372
DUR1_YEASTDUR1,2physical
22940862
MRM2_YEASTMRM2genetic
27708008
RV161_YEASTRVS161genetic
27708008
BRE1_YEASTBRE1genetic
27708008
EF2_YEASTEFT2genetic
27708008
RTG2_YEASTRTG2genetic
27708008
FIS1_YEASTFIS1genetic
27708008
PFKA2_YEASTPFK2genetic
27708008
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DUR1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-1400, AND MASSSPECTROMETRY.

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