UBA1_RAT - dbPTM
UBA1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBA1_RAT
UniProt AC Q5U300
Protein Name Ubiquitin-like modifier-activating enzyme 1 {ECO:0000250|UniProtKB:Q02053}
Gene Name Uba1 {ECO:0000312|EMBL:AAH85791.1, ECO:0000312|RGD:1359327}
Organism Rattus norvegicus (Rat).
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. 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 MSSSPLSKKRRVSGPDPKPGSNCSSAQSVLSEVSSVPTNGMAKNGSEADIDESLYSRQLYVLGHEAMKMLQTSSVLVSGLRGLGVEIAKNIILGGVKAVTLHDQGTTQWADLSSQFYLREEDIGKNRAEVSQPRLAELNSYVPVTAYTGPLVEDFLSGFQVVVLTNSPLEEQLRVGEFCHSRGIKLVVADTRGLFGQLFCDFGEEMVLTDSNGEQPLSAMVSMVTKDNPGVVTCLDEARHGFETGDFVSFSEVQGMVQLNGCQPIEIKVLGPYTFSICDTSNFSDYIRGGIVSQVKVPKKISFKSLPASLAEPDFVMTDFAKYSRPAQLHIGFQALHQFCAQHNRPPRPRNEEDATELVTLAQAVNARSPPAVQQDNVDEDLIRKLAYVAAGDLAPINAFIGGLAAQEVMKACSGKFMPIMQWLYFDALECLPEDKEALTEDKCLPRQNRYDGQVAVFGSDLQEKLGKQKYFLVGAGAIGCELLKNFAMIGLGCGEGGEVVVTDMDTIEKSNLNRQFLFRPWDVTKLKSDTAAAAVRQMNPYIQVTSHQNRVGPDTERIYDDDFFQNLDGVANALDNVDARMYMDRRCVYYRKPLLESGTLGTKGNVQVVIPFLTESYSSSQDPPEKSIPICTLKNFPNAIEHTLQWARDEFEGLFKQPAENVNQYLTDSKFVERTLRLAGTQPLEVLEAVQRSLVLQRPQTWGDCVTWACHHWHTQYCNNIRQLLHNFPPDQLTSSGAPFWSGPKRCPHPLTFDVNNTLHLDYVMAAANLFAQTYGLTGSQDRAAVASLLQSVQVPEFTPKSGVKIHVSDQELQSANASVDDSRLEELKATLPSPDKLPGFKMYPIDFEKDDDSNFHMDFIVAASNLRAENYDISPADRHKSKLIAGKIIPAIATTTAAVVGLVCLELYKVVQGHQQLDSYKNGFLNLALPFFGFSEPLAAPRHQYYNQEWTLWDRFEVQGLQPNGEEMTLKQFLDYFKTEHKLEITMLSQGVSMLYSFFMPAAKLKERLDQPMTEIVSRVSKRKLGRHVRALVLELCCNDESGEDVEVPYVRYTIR
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
2Phosphorylation------MSSSPLSKK
------CCCCCCCCC
51.3230181290
2Acetylation------MSSSPLSKK
------CCCCCCCCC
51.32-
3Phosphorylation-----MSSSPLSKKR
-----CCCCCCCCCC
48.0822673903
4Phosphorylation----MSSSPLSKKRR
----CCCCCCCCCCC
38.8722673903
7Phosphorylation-MSSSPLSKKRRVSG
-CCCCCCCCCCCCCC
39.2430181290
13PhosphorylationLSKKRRVSGPDPKPG
CCCCCCCCCCCCCCC
42.6829779826
21PhosphorylationGPDPKPGSNCSSAQS
CCCCCCCCCCHHHHH
43.1027097102
24PhosphorylationPKPGSNCSSAQSVLS
CCCCCCCHHHHHHHH
32.7227097102
25PhosphorylationKPGSNCSSAQSVLSE
CCCCCCHHHHHHHHH
32.3127097102
28PhosphorylationSNCSSAQSVLSEVSS
CCCHHHHHHHHHHCC
25.4127097102
31PhosphorylationSSAQSVLSEVSSVPT
HHHHHHHHHHCCCCC
33.5223984901
34PhosphorylationQSVLSEVSSVPTNGM
HHHHHHHCCCCCCCC
22.9023984901
35PhosphorylationSVLSEVSSVPTNGMA
HHHHHHCCCCCCCCC
36.9727097102
38PhosphorylationSEVSSVPTNGMAKNG
HHHCCCCCCCCCCCC
42.1027097102
46PhosphorylationNGMAKNGSEADIDES
CCCCCCCCCCCCCHH
38.7223712012
55PhosphorylationADIDESLYSRQLYVL
CCCCHHHHHHHHHHH
15.8722276854
56PhosphorylationDIDESLYSRQLYVLG
CCCHHHHHHHHHHHH
20.8828689409
388PhosphorylationDLIRKLAYVAAGDLA
HHHHHHHHHHHCCCH
10.89-
465UbiquitinationFGSDLQEKLGKQKYF
ECHHHHHHHCCCCEE
49.97-
465AcetylationFGSDLQEKLGKQKYF
ECHHHHHHHCCCCEE
49.9722902405
526AcetylationFRPWDVTKLKSDTAA
CCCCCHHHCCHHHHH
54.4922902405
528SuccinylationPWDVTKLKSDTAAAA
CCCHHHCCHHHHHHH
48.09-
528SuccinylationPWDVTKLKSDTAAAA
CCCHHHCCHHHHHHH
48.09-
598PhosphorylationYRKPLLESGTLGTKG
EECCCHHCCCCCCCC
36.7323984901
600PhosphorylationKPLLESGTLGTKGNV
CCCHHCCCCCCCCCE
31.1523984901
603PhosphorylationLESGTLGTKGNVQVV
HHCCCCCCCCCEEEE
38.6023984901
671UbiquitinationNQYLTDSKFVERTLR
HHHHCCHHHHHHHHH
57.13-
671AcetylationNQYLTDSKFVERTLR
HHHHCCHHHHHHHHH
57.1322902405
800PhosphorylationSVQVPEFTPKSGVKI
HCCCCCCCCCCCCEE
28.3022108457
810PhosphorylationSGVKIHVSDQELQSA
CCCEEEECHHHHHHC
21.2929779826
816PhosphorylationVSDQELQSANASVDD
ECHHHHHHCCCCCCH
35.7927097102
820PhosphorylationELQSANASVDDSRLE
HHHHCCCCCCHHHHH
26.3627097102
824PhosphorylationANASVDDSRLEELKA
CCCCCCHHHHHHHHH
34.0123984901
832PhosphorylationRLEELKATLPSPDKL
HHHHHHHHCCCCCCC
37.3028432305
835PhosphorylationELKATLPSPDKLPGF
HHHHHCCCCCCCCCC
49.1730240740
838UbiquitinationATLPSPDKLPGFKMY
HHCCCCCCCCCCEEE
61.02-
838AcetylationATLPSPDKLPGFKMY
HHCCCCCCCCCCEEE
61.0222902405
873PhosphorylationSNLRAENYDISPADR
CCCCCCCCCCCHHHH
13.22-
876PhosphorylationRAENYDISPADRHKS
CCCCCCCCHHHHHHH
15.9028551015
980AcetylationKQFLDYFKTEHKLEI
HHHHHHHHHCCHHHH
46.93-
1020PhosphorylationQPMTEIVSRVSKRKL
CHHHHHHHHHHHHHH
32.4023984901
1023PhosphorylationTEIVSRVSKRKLGRH
HHHHHHHHHHHHHHH
26.1523984901

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_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBA1_RAT !!

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of UBA1_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBA1_RAT

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Related Literatures of Post-Translational Modification

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