UBA1_MOUSE - dbPTM
UBA1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBA1_MOUSE
UniProt AC Q02053
Protein Name Ubiquitin-like modifier-activating enzyme 1
Gene Name Uba1
Organism Mus musculus (Mouse).
Sequence Length 1058
Subcellular Localization Cytoplasm . Mitochondrion . Nucleus .
Protein Description Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system. [PubMed: 1511901 Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Essential for the formation of radiation-induced foci, timely DNA repair and for response to replication stress. Promotes the recruitment of TP53BP1 and BRCA1 at DNA damage sites.]
Protein Sequence MSSSPLSKKRRVSGPDPKPGSNCSPAQSALSEVSSVPTNGMAKNGSEADIDESLYSRQLYVLGHEAMKMLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTGPLVEDFLSSFQVVVLTNSPLEAQLRVGEFCHSRGIKLVVADTRGLFGQLFCDFGEEMVLTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARHGFETGDFVSFSEVQGMIQLNGCQPMEIKVLGPYTFSICDTSNFSDYIRGGIVSQVKVPKKISFKSLPASLVEPDFVMTDFAKYSRPAQLHIGFQALHQFCALHNQPPRPRNEEDATELVGLAQAVNARSPPSVKQNSLDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEALTEEKCLPRQNRYDGQVAVFGSDFQEKLSKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEVVVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPYIQVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNIDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLTDSKFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWGDCVTWACHHWHTQYCNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNTLHLDYVMAAANLFAQTYGLTGSQDRAAVASLLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSRLEELKATLPSPDKLPGFKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDISPADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHQQLDSYKNGFLNLALPFFGFSEPLAAPRHQYYNQEWTLWDRFEVQGLQPNGEEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRYTIR
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
2Acetylation------MSSSPLSKK
------CCCCCCCCC		51.32-
2Phosphorylation------MSSSPLSKK
------CCCCCCCCC		51.3223527152
3Phosphorylation-----MSSSPLSKKR
-----CCCCCCCCCC		48.0825266776
4Phosphorylation----MSSSPLSKKRR
----CCCCCCCCCCC		38.8723527152
7Phosphorylation-MSSSPLSKKRRVSG
-CCCCCCCCCCCCCC		39.2425367039
13PhosphorylationLSKKRRVSGPDPKPG
CCCCCCCCCCCCCCC		42.6825521595
21PhosphorylationGPDPKPGSNCSPAQS
CCCCCCCCCCCHHHH		43.1025521595
24PhosphorylationPKPGSNCSPAQSALS
CCCCCCCCHHHHHHH		27.7625521595
28PhosphorylationSNCSPAQSALSEVSS
CCCCHHHHHHHHHCC		33.0325521595
31PhosphorylationSPAQSALSEVSSVPT
CHHHHHHHHHCCCCC		35.3522942356
34PhosphorylationQSALSEVSSVPTNGM
HHHHHHHCCCCCCCC		22.9025619855
35PhosphorylationSALSEVSSVPTNGMA
HHHHHHCCCCCCCCC		36.9725619855
38PhosphorylationSEVSSVPTNGMAKNG
HHHCCCCCCCCCCCC		42.1025619855
41OxidationSSVPTNGMAKNGSEA
CCCCCCCCCCCCCCC		5.3517242355
46PhosphorylationNGMAKNGSEADIDES
CCCCCCCCCCCCCHH		38.7225521595
53PhosphorylationSEADIDESLYSRQLY
CCCCCCHHHHHHHHH		28.9425619855
55PhosphorylationADIDESLYSRQLYVL
CCCCHHHHHHHHHHH		15.8725619855
56PhosphorylationDIDESLYSRQLYVLG
CCCHHHHHHHHHHHH		20.8825619855
60PhosphorylationSLYSRQLYVLGHEAM
HHHHHHHHHHHHHHH		5.8125367039
131PhosphorylationGKNRAEVSQPRLAEL
CCCCHHCCCCCHHHH		26.4422802335
179S-palmitoylationQLRVGEFCHSRGIKL
HHHHHHHHHHCCCEE		2.1826165157
185UbiquitinationFCHSRGIKLVVADTR
HHHHCCCEEEEECCC		37.74-
234S-nitrosocysteineDNPGVVTCLDEARHG
CCCCCEEEEHHHCCC		2.81-
234S-nitrosylationDNPGVVTCLDEARHG
CCCCCEEEEHHHCCC		2.8124926564
278S-palmitoylationGPYTFSICDTSNFSD
CCEEEEEECCCCHHH		4.5328680068
281PhosphorylationTFSICDTSNFSDYIR
EEEEECCCCHHHHCC		23.72-
296UbiquitinationGGIVSQVKVPKKISF
CCCCCCCCCCCCCCC		45.22-
299UbiquitinationVSQVKVPKKISFKSL
CCCCCCCCCCCCCCC		66.77-
302PhosphorylationVKVPKKISFKSLPAS
CCCCCCCCCCCCCHH		35.1930387612
304UbiquitinationVPKKISFKSLPASLV
CCCCCCCCCCCHHHC		44.27-
322UbiquitinationFVMTDFAKYSRPAQL
EEEECHHHCCCCCEE		43.69-
340GlutathionylationFQALHQFCALHNQPP
HHHHHHHHHHCCCCC		2.9524333276
356PhosphorylationPRNEEDATELVGLAQ
CCCHHHHHHHHHHHH		42.0228464351
369PhosphorylationAQAVNARSPPSVKQN
HHHHHCCCCCCCCCC		38.4626824392
374UbiquitinationARSPPSVKQNSLDED
CCCCCCCCCCCCCHH		48.37-
377PhosphorylationPPSVKQNSLDEDLIR
CCCCCCCCCCHHHHH		34.4025521595
385UbiquitinationLDEDLIRKLAYVAAG
CCHHHHHHHHHHHHC		30.40-
388PhosphorylationDLIRKLAYVAAGDLA
HHHHHHHHHHHCCCH		10.89-
443UbiquitinationKEALTEEKCLPRQNR
HHHHCCCCCCCCCCC		34.53-
465AcetylationFGSDFQEKLSKQKYF
ECHHHHHHHHCCCEE		47.4823954790
465UbiquitinationFGSDFQEKLSKQKYF
ECHHHHHHHHCCCEE		47.48-
481S-palmitoylationVGAGAIGCELLKNFA
ECCCHHHHHHHHHCE		2.4526165157
526UbiquitinationFRPWDVTKLKSDTAA
CCCCCHHHCCHHHHH		54.49-
528AcetylationPWDVTKLKSDTAAAA
CCCHHHCCHHHHHHH		48.0923806337
528SuccinylationPWDVTKLKSDTAAAA
CCCHHHCCHHHHHHH		48.0923806337
528SuccinylationPWDVTKLKSDTAAAA
CCCHHHCCHHHHHHH		48.09-
528UbiquitinationPWDVTKLKSDTAAAA
CCCHHHCCHHHHHHH		48.09-
531PhosphorylationVTKLKSDTAAAAVRQ
HHHCCHHHHHHHHHH		25.86-
542PhosphorylationAVRQMNPYIQVTSHQ
HHHHHCCEEEEEECC		10.0525367039
593UbiquitinationRRCVYYRKPLLESGT
CCCCEEECCCHHCCC		24.72-
600PhosphorylationKPLLESGTLGTKGNV
CCCHHCCCCCCCCCE		31.1525338131
604UbiquitinationESGTLGTKGNVQVVI
HCCCCCCCCCEEEEE		46.84-
627UbiquitinationSSQDPPEKSIPICTL
CCCCCCCCCCCEEEE		60.50-
628PhosphorylationSQDPPEKSIPICTLK
CCCCCCCCCCEEEEC		31.7522324799
635UbiquitinationSIPICTLKNFPNAIE
CCCEEEECCCCCHHH		38.09-
657UbiquitinationDEFEGLFKQPAENVN
HHHHHHHCCCCHHHH		61.49-
668PhosphorylationENVNQYLTDSKFVER
HHHHHHHCCHHHHHH		33.0428464351
670PhosphorylationVNQYLTDSKFVERTL
HHHHHCCHHHHHHHH		23.8218779572
671AcetylationNQYLTDSKFVERTLR
HHHHCCHHHHHHHHH		57.1323806337
671MalonylationNQYLTDSKFVERTLR
HHHHCCHHHHHHHHH		57.1326320211
671UbiquitinationNQYLTDSKFVERTLR
HHHHCCHHHHHHHHH		57.13-
746UbiquitinationAPFWSGPKRCPHPLT
CCCCCCCCCCCCCCE		70.88-
793PhosphorylationAVASLLQSVQVPEFT
HHHHHHHHCCCCCCC		17.9423737553
800PhosphorylationSVQVPEFTPKSGVKI
HCCCCCCCCCCCCEE		28.3025266776
802AcetylationQVPEFTPKSGVKIHV
CCCCCCCCCCCEEEE		57.7023806337
802UbiquitinationQVPEFTPKSGVKIHV
CCCCCCCCCCCEEEE		57.70-
803PhosphorylationVPEFTPKSGVKIHVS
CCCCCCCCCCEEEEC		50.4526745281
806MalonylationFTPKSGVKIHVSDQE
CCCCCCCEEEECHHH		30.5326320211
806UbiquitinationFTPKSGVKIHVSDQE
CCCCCCCEEEECHHH		30.53-
810PhosphorylationSGVKIHVSDQELQSA
CCCEEEECHHHHHHC		21.2925521595
816PhosphorylationVSDQELQSANASVDD
ECHHHHHHCCCCCCH		35.7927087446
820PhosphorylationELQSANASVDDSRLE
HHHHCCCCCCHHHHH		26.3627087446
824PhosphorylationANASVDDSRLEELKA
CCCCCCHHHHHHHHH		34.0125619855
832PhosphorylationRLEELKATLPSPDKL
HHHHHHHHCCCCCCC		37.3027180971
835PhosphorylationELKATLPSPDKLPGF
HHHHHCCCCCCCCCC		49.1725521595
838AcetylationATLPSPDKLPGFKMY
HHCCCCCCCCCCEEE		61.0223236377
838UbiquitinationATLPSPDKLPGFKMY
HHCCCCCCCCCCEEE		61.02-
843UbiquitinationPDKLPGFKMYPIDFE
CCCCCCCEEEECCCC		43.36-
851UbiquitinationMYPIDFEKDDDSNFH
EEECCCCCCCCCCCC		67.46-
873PhosphorylationSNLRAENYDISPADR
CCCCCCCCCCCHHHH		13.2229899451
876PhosphorylationRAENYDISPADRHKS
CCCCCCCCHHHHHHH		15.9025521595
882UbiquitinationISPADRHKSKLIAGK
CCHHHHHHHHHHHCC		50.62-
883PhosphorylationSPADRHKSKLIAGKI
CHHHHHHHHHHHCCH		26.94-
889UbiquitinationKSKLIAGKIIPAIAT
HHHHHHCCHHHHHHH		28.57-
923UbiquitinationHQQLDSYKNGFLNLA
HHHHHHHHCCCCCEE		55.32-
971PhosphorylationQPNGEEMTLKQFLDY
CCCCCEECHHHHHHH		33.8023140645
980AcetylationKQFLDYFKTEHKLEI
HHHHHHHHHCCHHHH		46.93-
1044PhosphorylationELCCNDESGEDVEVP
HHHCCCCCCCCCCCC		50.80-
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 UBA1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBA1_MOUSE !!
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 UBA1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYCP1_HUMANSYCP1physical
20360068
UBA1_HUMANUBA1physical
20360068
PIP_HUMANPIPphysical
20360068
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBA1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-24; SER-31;SER-816; SER-820 AND SER-835, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND MASSSPECTROMETRY.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-55, AND MASSSPECTROMETRY.

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