UniProt Accession

 BACD2_HUMAN; Q13829; Q5TZQ1 

Genbank Protein ID

 M80783; AK312387; CR456819; BT020121; AY065346; AC002094; CH471159; BC001643; BC001949 

Genbank Nucleotide ID

 AAA58385.1; BAG35304.1; CAG33100.1; AAV38924.1; AAL38649.1; EAW51077.1; AAH01643.1; AAH01949.1 

Protein Name

 BTB/POZ domain-containing adapter for CUL3-mediated RhoA degradation protein 2 

Protein Synonyms/Alias

 hBACURD2; BTB/POZ domain-containing protein TNFAIP1; Protein B12; Tumor necrosis factor, alpha-induced protein 1, endothelial 

Gene Name

 TNFAIP1 

Gene Synonyms/Alias

 BACURD2; EDP1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
14	LCPASGAKPKLSGFK	ubiquitination	[1, 2]
21	KPKLSGFKGGGLGNK	ubiquitination	[2, 3, 4, 5, 6, 7]
67	RMEVLTDKEGWILID	ubiquitination	[2, 4]
78	ILIDRCGKHFGTILN	ubiquitination	[2]
155	RLIESSTKPVVKLLY	ubiquitination	[2]
188	KNIELFDKLSLRFNG	ubiquitination	[2]
235	IVYATEKKQTKVEFP	ubiquitination	[2]
238	ATEKKQTKVEFPEAR	ubiquitination	[2]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [6] 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]
 [7] 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] 

Functional Description

 Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex involved in regulation of cytoskeleton structure. The BCR(BACURD2) E3 ubiquitin ligase complex mediates the ubiquitination of RHOA, leading to its degradation by the proteasome, thereby regulating the actin cytoskeleton and cell migration. Its interaction with RHOB may regulate apoptosis. May enhance the PCNA-dependent DNA polymerase delta activity. 

Sequence Annotation

 DOMAIN 28 96 BTB.
 MOD_RES 278 278 Phosphoserine.
 MOD_RES 280 280 Phosphoserine; by CK2.  

Keyword

 Complete proteome; Cytoplasm; Endosome; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation pathway. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 316 AA 

Protein Sequence

Gene Ontology

 GO:0031463; C:Cul3-RING ubiquitin ligase complex; IDA:UniProtKB.
 GO:0005768; C:endosome; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0017049; F:GTP-Rho binding; IDA:UniProtKB.
 GO:0006915; P:apoptotic process; TAS:UniProtKB.
 GO:0016477; P:cell migration; IMP:UniProtKB.
 GO:0006260; P:DNA replication; ISS:UniProtKB.
 GO:0009790; P:embryo development; ISS:UniProtKB.
 GO:0006955; P:immune response; IEP:UniProtKB.
 GO:0035024; P:negative regulation of Rho protein signal transduction; IMP:UniProtKB.
 GO:0045740; P:positive regulation of DNA replication; IEA:Compara.
 GO:0043161; P:proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
 GO:0051260; P:protein homooligomerization; IEA:InterPro.
 GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
 GO:0043149; P:stress fiber assembly; IMP:UniProtKB. 

Interpro

 IPR000210; BTB/POZ-like.
 IPR011333; BTB/POZ_fold.
 IPR003131; T1-type_BTB. 

Pfam

 PF02214; K_tetra 

SMART

 SM00225; BTB 

PROSITE

 PS50097; BTB 

PRINTS