UniProt Accession

 UB2L3_HUMAN; P68036; B2R4A7; B4DDG1; B4DSZ4; E7EWS7; P51966; P70653; Q9HAV1 

Genbank Protein ID

 S81003; X92962; AJ000519; AF300336; CR456606; AK293179; AK299985; AK311761; AP000553; AP000557; AP000558; CH471095; BC053368 

Genbank Nucleotide ID

 AAB36017.1; CAA63538.1; CAA04156.1; AAG17922.1; CAG30492.1; BAG56722.1; BAG61806.1; BAG34704.1; EAW59459.1; AAH53368.1 

Protein Name

 Ubiquitin-conjugating enzyme E2 L3 

Protein Synonyms/Alias

 L-UBC; UbcH7; Ubiquitin carrier protein L3; Ubiquitin-conjugating enzyme E2-F1; Ubiquitin-protein ligase L3 

Gene Name

 UBE2L3 

Gene Synonyms/Alias

 UBCE7; UBCH7 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
9	AASRRLMKELEEIRK	acetylation	[1, 2, 3, 4, 5]
9	AASRRLMKELEEIRK	ubiquitination	[6, 7]
20	EIRKCGMKNFRNIQV	acetylation	[5]
20	EIRKCGMKNFRNIQV	ubiquitination	[5, 6, 7, 8, 9]
48	PDNPPYDKGAFRIEI	ubiquitination	[7, 10, 11]
64	FPAEYPFKPPKITFK	acetylation	[4]
64	FPAEYPFKPPKITFK	ubiquitination	[5, 6, 7, 8, 9, 10, 11, 12]
67	EYPFKPPKITFKTKI	ubiquitination	[7, 9, 13, 14]
71	KPPKITFKTKIYHPN	ubiquitination	[7, 9, 13, 14]
73	PKITFKTKIYHPNID	ubiquitination	[5, 6, 7, 8, 9, 10, 11, 14, 15]
82	YHPNIDEKGQVCLPV	acetylation	[4, 5]
82	YHPNIDEKGQVCLPV	ubiquitination	[5, 6, 7, 8, 9, 10, 11, 12, 15]
96	VISAENWKPATKTDQ	ubiquitination	[5, 6, 7, 9, 12]
100	ENWKPATKTDQVIQS	ubiquitination	[6]
131	DLAEEYSKDRKKFCK	acetylation	[1, 2, 3, 5]
131	DLAEEYSKDRKKFCK	ubiquitination	[5, 7, 8, 10, 11, 12, 14, 15]
138	KDRKKFCKNAEEFTK	acetylation	[1, 2]
138	KDRKKFCKNAEEFTK	ubiquitination	[7, 12]
145	KNAEEFTKKYGEKRP	acetylation	[3, 5]
145	KNAEEFTKKYGEKRP	ubiquitination	[7, 8, 11]
150	FTKKYGEKRPVD***	ubiquitination	[7]

Reference

 [1] 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]
 [2] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation.
 Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C.
 Sci Signal. 2011 Jul 26;4(183):ra48. [PMID: 21791702]
 [3] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [11] 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]
 [12] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [13] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [14] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [15] 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] 

Functional Description

 Ubiquitin-conjugating enzyme E2 that specifically acts with HECT-type and RBR family E3 ubiquitin-protein ligases. Does not function with most RING-containing E3 ubiquitin-protein ligases because it lacks intrinsic E3-independent reactivity with lysine: in contrast, it has activity with the RBR family E3 enzymes, such as PARK2 and ARIH1, that function like function like RING-HECT hybrids. Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Involved in the selective degradation of short-lived and abnormal proteins. Down- regulated during the S-phase it is involved in progression through the cell cycle. Regulates nuclear hormone receptors transcriptional activity. May play a role in myelopoiesis. 

Sequence Annotation

 ACT_SITE 86 86 Glycyl thioester intermediate (By
 MOD_RES 9 9 N6-acetyllysine.
 MOD_RES 131 131 N6-acetyllysine.
 MOD_RES 138 138 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; Nucleotide-binding; Nucleus; Reference proteome; Transcription; Transcription regulation; Ubl conjugation; Ubl conjugation pathway. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 154 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0000151; C:ubiquitin ligase complex; TAS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0019899; F:enzyme binding; TAS:UniProtKB.
 GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008283; P:cell proliferation; IMP:UniProtKB.
 GO:0071385; P:cellular response to glucocorticoid stimulus; IDA:UniProtKB.
 GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:UniProtKB. 

Interpro

 IPR000608; UBQ-conjugat_E2.
 IPR023313; UBQ-conjugating_AS.
 IPR016135; UBQ-conjugating_enzyme/RWD. 

Pfam

 PF00179; UQ_con 

SMART

  

PROSITE

 PS00183; UBIQUITIN_CONJUGAT_1
 PS50127; UBIQUITIN_CONJUGAT_2 

PRINTS