CPLM-008387

Genbank Nucleotide ID

B-cell receptor-associated protein 31

Protein Synonyms/Alias

BCR-associated protein 31; Bap31; 6C6-AG tumor-associated antigen; Protein CDM; p28

Homo sapiens (Human)

Position	Peptide	Type	References
34	ISPKRWQKIFKSRLV	ubiquitination	[1]
37	KRWQKIFKSRLVELL	ubiquitination	[1]
72	DAVREIRKYDDVTEK	ubiquitination	[1]
79	KYDDVTEKVNLQNNP	ubiquitination	[1, 2]
95	AMEHFHMKLFRAQRN	ubiquitination	[1, 2, 3, 4]
137	LASNEAFKKQAESAS	ubiquitination	[1, 3]
138	ASNEAFKKQAESASE	ubiquitination	[1, 4]
148	ESASEAAKKYMEEND	ubiquitination	[1, 4]
149	SASEAAKKYMEENDQ	ubiquitination	[1]
158	MEENDQLKKGAAVDG	ubiquitination	[1, 4]
159	EENDQLKKGAAVDGG	ubiquitination	[1]
167	GAAVDGGKLDVGNAE	ubiquitination	[1, 4]
176	DVGNAEVKLEEENRS	ubiquitination	[1, 4]
185	EEENRSLKADLQKLK	ubiquitination	[1, 4, 5, 6]
190	SLKADLQKLKDELAS	acetylation	[6]
190	SLKADLQKLKDELAS	ubiquitination	[5]
192	KADLQKLKDELASTK	ubiquitination	[1, 5, 6]
199	KDELASTKQKLEKAE	ubiquitination	[1, 6]
201	ELASTKQKLEKAENQ	ubiquitination	[6]
204	STKQKLEKAENQVLA	acetylation	[7]
204	STKQKLEKAENQVLA	ubiquitination	[1, 2, 4, 6]
214	NQVLAMRKQSEGLTK	ubiquitination	[1]
221	KQSEGLTKEYDRLLE	ubiquitination	[1, 4, 5, 6, 8]
243	AVDGPMDKKEE****	acetylation	[9]
243	AVDGPMDKKEE****	ubiquitination	[1, 4, 5, 6, 10, 11]
244	VDGPMDKKEE*****	ubiquitination	[1, 4, 6, 10]

[1] 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]
[2] 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]
[3] 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]
[4] 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]
[5] 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]
[6] 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]
[7] Regulation of cellular metabolism by protein lysine acetylation.
Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
[8] 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]
[9] 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]
[10] 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]
[11] 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

May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi. May be involved in CASP8-mediated apoptosis.

MOTIF 243 246 Di-lysine motif.

Alternative splicing; Apoptosis; Complete proteome; Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport; Membrane; Protein transport; Reference proteome; Transmembrane; Transmembrane helix; Transport.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005829; C:cytosol; TAS:Reactome.
GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
GO:0000139; C:Golgi membrane; IEA:Compara.
GO:0071556; C:integral to lumenal side of endoplasmic reticulum membrane; TAS:Reactome.
GO:0005887; C:integral to plasma membrane; IDA:UniProtKB.
GO:0005811; C:lipid particle; IDA:UniProtKB.
GO:0005102; F:receptor binding; NAS:UniProtKB.
GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; TAS:Reactome.
GO:0035584; P:calcium-mediated signaling using intracellular calcium source; IMP:UniProtKB.
GO:0006921; P:cellular component disassembly involved in execution phase of apoptosis; TAS:Reactome.
GO:0007204; P:elevation of cytosolic calcium ion concentration; IMP:UniProtKB.
GO:0051561; P:elevation of mitochondrial calcium ion concentration; IMP:UniProtKB.
GO:0006955; P:immune response; NAS:UniProtKB.
GO:0006886; P:intracellular protein transport; IEA:InterPro.
GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:UniProtKB.
GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO:0032471; P:reduction of endoplasmic reticulum calcium ion concentration; IMP:UniProtKB.
GO:0007283; P:spermatogenesis; IEA:Compara.
GO:0016192; P:vesicle-mediated transport; IEA:UniProtKB-KW.