CPLM-018094

Genbank Nucleotide ID

Ubiquitin-associated and SH3 domain-containing protein B

Protein Synonyms/Alias

Cbl-interacting protein p70; Suppressor of T-cell receptor signaling 1; STS-1; T-cell ubiquitin ligand 2; TULA-2; Tyrosine-protein phosphatase STS1/TULA2

Homo sapiens (Human)

Position	Peptide	Type	References
21	AREELYSKVTPRRNR	ubiquitination	[1, 2, 3, 4]
112	SDFWQQSKQICGKNK	ubiquitination	[2, 3, 4, 5]
187	DSAEVLKKFAADFAA	ubiquitination	[3]
401	RMDVVFGKYWLSQCF	ubiquitination	[1]
411	LSQCFDAKGRYIRTN	ubiquitination	[1, 2, 3, 4, 5, 6]
492	LQQENHLKIRVEPGL	ubiquitination	[3]
596	GLSPQNSKDFVQMVR	ubiquitination	[5]

[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] 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]
[3] 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]
[4] 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]
[5] 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]
[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]

Functional Description

Interferes with CBL-mediated down-regulation and degradation of receptor-type tyrosine kinases. Promotes accumulation of activated target receptors, such as T-cell receptors and EGFR, on the cell surface. Exhibits tyrosine phosphatase activity toward several substrates including EGFR, FAK, SYK, and ZAP70. Down-regulates proteins that are dually modified by both protein tyrosine phosphorylation and ubiquitination.

DOMAIN 27 76 UBA.
DOMAIN 254 319 SH3.
REGION 380 649 Protein tyrosine phosphatase (By
ACT_SITE 390 390 By similarity.
ACT_SITE 391 391 Tele-phosphohistidine intermediate (By
ACT_SITE 576 576 By similarity.
MOD_RES 20 20 Phosphoserine.
MOD_RES 23 23 Phosphothreonine.

3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Hydrolase; Nucleus; Phosphoprotein; Polymorphism; Protein phosphatase; Reference proteome; SH3 domain.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.

IPR013078; His_Pase_superF_clade-1.
IPR001452; SH3_domain.
IPR009060; UBA-like.
IPR000449; UBA/transl_elong_EF1B_N.
IPR015940; UBA/transl_elong_EF1B_N_euk.

PF00300; His_Phos_1
PF00018; SH3_1
PF00627; UBA

SM00326; SH3
SM00165; UBA

PS50002; SH3
PS50030; UBA