CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021192
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin-like modifier-activating enzyme 5 
Protein Synonyms/Alias
 Ubiquitin-activating enzyme 5; ThiFP1; UFM1-activating enzyme; Ubiquitin-activating enzyme E1 domain-containing protein 1 
Gene Name
 UBA5 
Gene Synonyms/Alias
 UBE1DC1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
42GGRVRIEKMSSEVVDubiquitination[1]
376TVAYTIPKKQEDSVTubiquitination[2]
377VAYTIPKKQEDSVTEubiquitination[2]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983
Functional Description
 E1-like enzyme which activates UFM1 and SUMO2. 
Sequence Annotation
 ACT_SITE 250 250 Glycyl thioester intermediate.
 METAL 226 226 Zinc.
 METAL 229 229 Zinc.
 METAL 303 303 Zinc.
 METAL 308 308 Zinc.
 BINDING 83 83 ATP; via amide nitrogen.
 BINDING 104 104 ATP.
 BINDING 127 127 ATP.
 BINDING 150 150 ATP.
 BINDING 184 184 ATP.
 MOD_RES 45 45 Phosphoserine.
 MOD_RES 358 358 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 404 AA 
Protein Sequence
MAESVERLQQ RVQELERELA QERSLQVPRS GDGGGGRVRI EKMSSEVVDS NPYSRLMALK 60
RMGIVSDYEK IRTFAVAIVG VGGVGSVTAE MLTRCGIGKL LLFDYDKVEL ANMNRLFFQP 120
HQAGLSKVQA AEHTLRNINP DVLFEVHNYN ITTVENFQHF MDRISNGGLE EGKPVDLVLS 180
CVDNFEARMT INTACNELGQ TWMESGVSEN AVSGHIQLII PGESACFACA PPLVVAANID 240
EKTLKREGVC AASLPTTMGV VAGILVQNVL KFLLNFGTVS FYLGYNAMQD FFPTMSMKPN 300
PQCDDRNCRK QQEEYKKKVA ALPKQEVIQE EEEIIHEDNE WGIELVSEVS EEELKNFSGP 360
VPDLPEGITV AYTIPKKQED SVTELTVEDS GESLEDLMAK MKNM 404 
Gene Ontology
 GO:0016235; C:aggresome; IDA:HPA.
 GO:0005737; C:cytoplasm; IDA:LIFEdb.
 GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0048037; F:cofactor binding; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
 GO:0071566; F:UFM1 activating enzyme activity; IDA:UniProtKB.
 GO:0071569; P:protein ufmylation; IDA:UniProtKB. 
Interpro
 IPR006140; D-isomer_2_OHA_DH_NAD-bd.
 IPR009036; Molybdenum_cofac_synth_MoeB.
 IPR016040; NAD(P)-bd_dom.
 IPR000594; ThiF_NAD_FAD-bd. 
Pfam
 PF00899; ThiF 
SMART
  
PROSITE
  
PRINTS