CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012250
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Ubiquitin conjugation factor E4 A 
Protein Synonyms/Alias
  
Gene Name
 UBE4A 
Gene Synonyms/Alias
 KIAA0126 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
33KQFAAIQKEQLKQQSubiquitination[1, 2]
104DNSDPSLKSGNGIPSubiquitination[1, 2, 3, 4, 5, 6]
185YSCFQRAKEEITKVPubiquitination[1]
190RAKEEITKVPENLLPubiquitination[1, 2]
317FVEYIQPKDPTNGQMubiquitination[1, 3]
386EKIYQMLKNLLQLSPacetylation[7, 8]
451KLCQPFCKPRSSRLLubiquitination[1]
468NPTYCALKELNDEERubiquitination[1, 2, 4]
478NDEERKIKNVHMRGLubiquitination[1]
487VHMRGLDKETCLIPAubiquitination[1, 2]
531RLHDQMVKINQNLHRubiquitination[1, 2, 3, 4]
766DTYRESIKDLADYASubiquitination[9]
774DLADYASKNLEAMNPubiquitination[3, 9]
810IQYLSKIKIQQIEKDubiquitination[3]
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] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] 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]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] 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]
 [9] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473] 
Functional Description
 Binds to the ubiquitin moieties of preformed conjugates and catalyzes ubiquitin chain assembly in conjunction with E1, E2, and E3 (By similarity). 
Sequence Annotation
 DOMAIN 991 1054 U-box.
 MOD_RES 386 386 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Reference proteome; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1066 AA 
Protein Sequence
MTDQENNNNI SSNPFAALFG SLADAKQFAA IQKEQLKQQS DELPASPDDS DNSVSESLDE 60
FDYSVAEISR SFRSQQEICE QLNINHMIQR IFLITLDNSD PSLKSGNGIP SRCVYLEEMA 120
VELEDQDWLD MSNVEQALFA RLLLQDPGNH LINMTSSTTL NLSADRDAGE RHIFCYLYSC 180
FQRAKEEITK VPENLLPFAV QCRNLTVSNT RTVLLTPEIY VDQNIHEQLV DLMLEAIQGA 240
HFEDVTEFLE EVIEALILDE EVRTFPEVMI PVFDILLGRI KDLELCQILL YAYLDILLYF 300
TRQKDMAKVF VEYIQPKDPT NGQMYQKTLL GVILSISCLL KTPGVVENHG YFLNPSRSSP 360
QEIKVQEANI HQFMAQFHEK IYQMLKNLLQ LSPETKHCIL SWLGNCLHAN AGRTKIWANQ 420
MPEIFFQMYA SDAFFLNLGA ALLKLCQPFC KPRSSRLLTF NPTYCALKEL NDEERKIKNV 480
HMRGLDKETC LIPAVQEPKF PQNYNLVTEN LALTEYTLYL GFHRLHDQMV KINQNLHRLQ 540
VAWRDAQQSS SPAADNLREQ FERLMTIYLS TKTAMTEPQM LQNCLNLQVS MAVLLVQLAI 600
GNEGSQPIEL TFPLPDGYSS LAYVPEFFAD NLGDFLIFLR RFADDILETS ADSLEHVLHF 660
ITIFTGSIER MKNPHLRAKL AEVLEAVMPH LDQTPNPLVS SVFHRKRVFC NFQYAPQLAE 720
ALIKVFVDIE FTGDPHQFEQ KFNYRRPMYP ILRYMWGTDT YRESIKDLAD YASKNLEAMN 780
PPLFLRFLNL LMNDAIFLLD EAIQYLSKIK IQQIEKDRGE WDSLTPEARR EKEAGLQMFG 840
QLARFHNIMS NETIGTLAFL TSEIKSLFVH PFLAERIISM LNYFLQHLVG PKMGALKVKD 900
FSEFDFKPQQ LVSDICTIYL NLGDEENFCA TVPKDGRSYS PTLFAQTVRV LKKINKPGNM 960
IMAFSNLAER IKSLADLQQQ EEETYADACD EFLDPIMSTL MCDPVVLPSS RVTVDRSTIA 1020
RHLLSDQTDP FNRSPLTMDQ IRPNTELKEK IQRWLAERKQ QKEQLE 1066 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0000151; C:ubiquitin ligase complex; TAS:ProtInc.
 GO:0034450; F:ubiquitin-ubiquitin ligase activity; IEA:Compara.
 GO:0000209; P:protein polyubiquitination; IEA:Compara.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc. 
Interpro
 IPR019474; Ub_conjug_fac_E4_core.
 IPR003613; Ubox_domain.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF04564; U-box
 PF10408; Ufd2P_core 
SMART
 SM00504; Ubox 
PROSITE
  
PRINTS