CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010913
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin-like modifier-activating enzyme 1 
Protein Synonyms/Alias
 Ubiquitin-activating enzyme E1; Ubiquitin-activating enzyme E1 X; Ubiquitin-like modifier-activating enzyme 1 X 
Gene Name
 Uba1 
Gene Synonyms/Alias
 Sbx; Ube1; Ube1ax; Ube1x 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
296GGIVSQVKVPKKISFubiquitination[1]
299VSQVKVPKKISFKSLubiquitination[1]
304VPKKISFKSLPASLVubiquitination[1]
322FVMTDFAKYSRPAQLubiquitination[1]
374ARSPPSVKQNSLDEDubiquitination[1]
443KEALTEEKCLPRQNRubiquitination[1]
465FGSDFQEKLSKQKYFubiquitination[1]
526FRPWDVTKLKSDTAAubiquitination[1]
528PWDVTKLKSDTAAAAacetylation[2, 3]
528PWDVTKLKSDTAAAAsuccinylation[3]
528PWDVTKLKSDTAAAAubiquitination[1]
593RRCVYYRKPLLESGTubiquitination[1]
604ESGTLGTKGNVQVVIubiquitination[1]
627SSQDPPEKSIPICTLubiquitination[1, 4]
635SIPICTLKNFPNAIEubiquitination[1, 4]
657DEFEGLFKQPAENVNubiquitination[1]
671NQYLTDSKFVERTLRacetylation[2, 3, 5]
671NQYLTDSKFVERTLRubiquitination[1]
746APFWSGPKRCPHPLTubiquitination[1, 4]
802QVPEFTPKSGVKIHVacetylation[3]
802QVPEFTPKSGVKIHVubiquitination[1]
806FTPKSGVKIHVSDQEubiquitination[1]
838ATLPSPDKLPGFKMYacetylation[5]
838ATLPSPDKLPGFKMYubiquitination[1]
843PDKLPGFKMYPIDFEubiquitination[1]
882ISPADRHKSKLIAGKubiquitination[1]
889KSKLIAGKIIPAIATubiquitination[4]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs.
 Mathew R, Seiler MP, Scanlon ST, Mao AP, Constantinides MG, Bertozzi-Villa C, Singer JD, Bendelac A.
 Nature. 2012 Nov 22;491(7425):618-21. [PMID: 23086144]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
Functional Description
 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 an ubiquitin- E1 thioester and free AMP. 
Sequence Annotation
 REPEAT 63 199 1-1.
 REPEAT 459 611 1-2.
 NP_BIND 478 507 ATP (By similarity).
 REGION 63 611 2 approximate repeats.
 ACT_SITE 632 632 Glycyl thioester intermediate (By
 MOD_RES 13 13 Phosphoserine (By similarity).
 MOD_RES 21 21 Phosphoserine.
 MOD_RES 24 24 Phosphoserine.
 MOD_RES 31 31 Phosphoserine.
 MOD_RES 46 46 Phosphoserine.
 MOD_RES 55 55 Phosphotyrosine.
 MOD_RES 671 671 N6-acetyllysine (By similarity).
 MOD_RES 800 800 Phosphothreonine (By similarity).
 MOD_RES 810 810 Phosphoserine (By similarity).
 MOD_RES 816 816 Phosphoserine.
 MOD_RES 820 820 Phosphoserine.
 MOD_RES 835 835 Phosphoserine.
 MOD_RES 980 980 N6-acetyllysine (By similarity).  
Keyword
 3D-structure; Acetylation; ATP-binding; Complete proteome; Direct protein sequencing; Ligase; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1058 AA 
Protein Sequence
MSSSPLSKKR RVSGPDPKPG SNCSPAQSAL SEVSSVPTNG MAKNGSEADI DESLYSRQLY 60
VLGHEAMKML QTSSVLVSGL RGLGVEIAKN IILGGVKAVT LHDQGTTQWA DLSSQFYLRE 120
EDIGKNRAEV SQPRLAELNS YVPVTAYTGP LVEDFLSSFQ VVVLTNSPLE AQLRVGEFCH 180
SRGIKLVVAD TRGLFGQLFC DFGEEMVLTD SNGEQPLSAM VSMVTKDNPG VVTCLDEARH 240
GFETGDFVSF SEVQGMIQLN GCQPMEIKVL GPYTFSICDT SNFSDYIRGG IVSQVKVPKK 300
ISFKSLPASL VEPDFVMTDF AKYSRPAQLH IGFQALHQFC ALHNQPPRPR NEEDATELVG 360
LAQAVNARSP PSVKQNSLDE DLIRKLAYVA AGDLAPINAF IGGLAAQEVM KACSGKFMPI 420
MQWLYFDALE CLPEDKEALT EEKCLPRQNR YDGQVAVFGS DFQEKLSKQK YFLVGAGAIG 480
CELLKNFAMI GLGCGEGGEV VVTDMDTIEK SNLNRQFLFR PWDVTKLKSD TAAAAVRQMN 540
PYIQVTSHQN RVGPDTERIY DDDFFQNLDG VANALDNIDA RMYMDRRCVY YRKPLLESGT 600
LGTKGNVQVV IPFLTESYSS SQDPPEKSIP ICTLKNFPNA IEHTLQWARD EFEGLFKQPA 660
ENVNQYLTDS KFVERTLRLA GTQPLEVLEA VQRSLVLQRP QTWGDCVTWA CHHWHTQYCN 720
NIRQLLHNFP PDQLTSSGAP FWSGPKRCPH PLTFDVNNTL HLDYVMAAAN LFAQTYGLTG 780
SQDRAAVASL LQSVQVPEFT PKSGVKIHVS DQELQSANAS VDDSRLEELK ATLPSPDKLP 840
GFKMYPIDFE KDDDSNFHMD FIVAASNLRA ENYDISPADR HKSKLIAGKI IPAIATTTAA 900
VVGLVCLELY KVVQGHQQLD SYKNGFLNLA LPFFGFSEPL AAPRHQYYNQ EWTLWDRFEV 960
QGLQPNGEEM TLKQFLDYFK TEHKLEITML SQGVSMLYSF FMPAAKLKER LDQPMTEIVS 1020
RVSKRKLGRH VRALVLELCC NDESGEDVEV PYVRYTIR 1058 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0008641; F:small protein activating enzyme activity; IEA:InterPro.
 GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. 
Interpro
 IPR009036; Molybdenum_cofac_synth_MoeB.
 IPR016040; NAD(P)-bd_dom.
 IPR000594; ThiF_NAD_FAD-bd.
 IPR018965; Ub-activating_enz_e1_C.
 IPR023280; Ub-like_act_enz_cat_cys_dom.
 IPR000127; UBact_repeat.
 IPR019572; Ubiquitin-activating_enzyme.
 IPR018075; UBQ-activ_enz_E1.
 IPR018074; UBQ-activ_enz_E1_AS.
 IPR000011; UBQ/SUMO-activ_enz_E1-like. 
Pfam
 PF00899; ThiF
 PF09358; UBA_e1_C
 PF10585; UBA_e1_thiolCys
 PF02134; UBACT 
SMART
 SM00985; UBA_e1_C 
PROSITE
 PS00536; UBIQUITIN_ACTIVAT_1
 PS00865; UBIQUITIN_ACTIVAT_2 
PRINTS
 PR01849; UBIQUITINACT.