UBS3B_HUMAN - dbPTM
UBS3B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBS3B_HUMAN
UniProt AC Q8TF42
Protein Name Ubiquitin-associated and SH3 domain-containing protein B
Gene Name UBASH3B
Organism Homo sapiens (Human).
Sequence Length 649
Subcellular Localization Cytoplasm. Nucleus .
Protein 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..
Protein Sequence MAQYGHPSPLGMAAREELYSKVTPRRNRQQRPGTIKHGSALDVLLSMGFPRARAQKALASTGGRSVQAACDWLFSHVGDPFLDDPLPREYVLYLRPTGPLAQKLSDFWQQSKQICGKNKAHNIFPHITLCQFFMCEDSKVDALGEALQTTVSRWKCKFSAPLPLELYTSSNFIGLFVKEDSAEVLKKFAADFAAEAASKTEVHVEPHKKQLHVTLAYHFQASHLPTLEKLAQNIDVKLGCDWVATIFSRDIRFANHETLQVIYPYTPQNDDELELVPGDFIFMSPMEQTSTSEGWIYGTSLTTGCSGLLPENYITKADECSTWIFHGSYSILNTSSSNSLTFGDGVLERRPYEDQGLGETTPLTIICQPMQPLRVNSQPGPQKRCLFVCRHGERMDVVFGKYWLSQCFDAKGRYIRTNLNMPHSLPQRSGGFRDYEKDAPITVFGCMQARLVGEALLESNTIIDHVYCSPSLRCVQTAHNILKGLQQENHLKIRVEPGLFEWTKWVAGSTLPAWIPPSELAAANLSVDTTYRPHIPISKLVVSESYDTYISRSFQVTKEIISECKSKGNNILIVAHASSLEACTCQLQGLSPQNSKDFVQMVRKIPYLGFCSCEELGETGIWQLTDPPILPLTHGPTGGFNWRETLLQE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
4Phosphorylation----MAQYGHPSPLG
----CCCCCCCCHHH
14.0927642862
8PhosphorylationMAQYGHPSPLGMAAR
CCCCCCCCHHHHHHH
27.3822199227
8O-linked_GlycosylationMAQYGHPSPLGMAAR
CCCCCCCCHHHHHHH
27.3829237092
19PhosphorylationMAAREELYSKVTPRR
HHHHHHHHHHCCCCC
15.1019605366
20PhosphorylationAAREELYSKVTPRRN
HHHHHHHHHCCCCCC
33.0228152594
21AcetylationAREELYSKVTPRRNR
HHHHHHHHCCCCCCC
36.2525953088
21UbiquitinationAREELYSKVTPRRNR
HHHHHHHHCCCCCCC
36.2521906983
23PhosphorylationEELYSKVTPRRNRQQ
HHHHHHCCCCCCCCC
18.1427134283
34PhosphorylationNRQQRPGTIKHGSAL
CCCCCCCCCCCCCHH
29.5428060719
46PhosphorylationSALDVLLSMGFPRAR
CHHHHHHHCCCCHHH
16.8219413330
56UbiquitinationFPRARAQKALASTGG
CCHHHHHHHHHHCCC
44.3727667366
77UbiquitinationCDWLFSHVGDPFLDD
HHHHHHCCCCCCCCC
10.1021963094
82UbiquitinationSHVGDPFLDDPLPRE
HCCCCCCCCCCCCCE
9.9322817900
93UbiquitinationLPREYVLYLRPTGPL
CCCEEEEEEECCCHH
7.2221963094
98UbiquitinationVLYLRPTGPLAQKLS
EEEEECCCHHHHHHH
20.2222817900
112UbiquitinationSDFWQQSKQICGKNK
HHHHHHHHHHHCCCC
39.0721963094
117UbiquitinationQSKQICGKNKAHNIF
HHHHHHCCCCCCCCC
51.3622817900
140UbiquitinationFMCEDSKVDALGEAL
EECCCHHHHHHHHHH
6.3621963094
145UbiquitinationSKVDALGEALQTTVS
HHHHHHHHHHHHHHH
47.2422817900
152UbiquitinationEALQTTVSRWKCKFS
HHHHHHHHHCCCEEC
30.2629901268
157UbiquitinationTVSRWKCKFSAPLPL
HHHHCCCEECCCCCE
38.33-
187UbiquitinationDSAEVLKKFAADFAA
CHHHHHHHHHHHHHH
35.7529901268
208UbiquitinationEVHVEPHKKQLHVTL
EEEEECCCCCEEEEE
53.5929967540
226PhosphorylationFQASHLPTLEKLAQN
HHHHCCCHHHHHHHC
54.6424173317
237UbiquitinationLAQNIDVKLGCDWVA
HHHCCCCCCCCCHHH
35.10-
348UbiquitinationTFGDGVLERRPYEDQ
EECCCEEECCCCCCC
44.2127667366
352PhosphorylationGVLERRPYEDQGLGE
CEEECCCCCCCCCCC
30.26-
360PhosphorylationEDQGLGETTPLTIIC
CCCCCCCCCCEEEEE
31.7328464451
364UbiquitinationLGETTPLTIICQPMQ
CCCCCCEEEEEEECC
14.9727667366
366UbiquitinationETTPLTIICQPMQPL
CCCCEEEEEEECCCC
1.1822817900
376UbiquitinationPMQPLRVNSQPGPQK
ECCCCCCCCCCCCCC
28.6123000965
377PhosphorylationMQPLRVNSQPGPQKR
CCCCCCCCCCCCCCE
34.5921712546
382UbiquitinationVNSQPGPQKRCLFVC
CCCCCCCCCEEEEEE
52.3022817900
383UbiquitinationNSQPGPQKRCLFVCR
CCCCCCCCEEEEEEE
48.4927667366
392UbiquitinationCLFVCRHGERMDVVF
EEEEEECCCCEEEEE
12.5923000965
401UbiquitinationRMDVVFGKYWLSQCF
CEEEEEEHHHHHHHH
23.0722817900
402PhosphorylationMDVVFGKYWLSQCFD
EEEEEEHHHHHHHHC
16.3822817900
411UbiquitinationLSQCFDAKGRYIRTN
HHHHHCCCCCEEEEC
45.8523000965
429UbiquitinationPHSLPQRSGGFRDYE
CCCCCCCCCCCCCCC
37.7122817900
439UbiquitinationFRDYEKDAPITVFGC
CCCCCCCCCEEEEEE
14.4123000965
457UbiquitinationRLVGEALLESNTIID
HHHHHHHHHCCCEEE
9.7627667366
473UbiquitinationVYCSPSLRCVQTAHN
EEECCHHHHHHHHHH
23.9327667366
483UbiquitinationQTAHNILKGLQQENH
HHHHHHHHHHHHCCC
54.5029967540
492UbiquitinationLQQENHLKIRVEPGL
HHHCCCEEEEECCCC
22.4027667366
520UbiquitinationAWIPPSELAAANLSV
CCCCHHHHHHCCCCC
4.6327667366
558UbiquitinationSRSFQVTKEIISECK
HHHHHHHHHHHHHHH
48.3229967540
561UbiquitinationFQVTKEIISECKSKG
HHHHHHHHHHHHHCC
2.7321963094
577UbiquitinationNILIVAHASSLEACT
EEEEEEECCHHHHHH
7.3521963094
596UbiquitinationGLSPQNSKDFVQMVR
CCCCCCHHHHHHHHH
63.8421963094
624UbiquitinationGETGIWQLTDPPILP
CCCCCEEECCCCCCC
3.3521963094

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of UBS3B_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBS3B_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of UBS3B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBL_HUMANCBLphysical
15159412
SHIP1_HUMANINPP5Dphysical
22267732
NCK1_HUMANNCK1physical
22267732
GRB2_HUMANGRB2physical
22267732
EGFR_HUMANEGFRphysical
17880946
CBL_HUMANCBLphysical
17880946
CBL_HUMANCBLphysical
16429130
K1C10_HUMANKRT10physical
19380743
K2C1_HUMANKRT1physical
19380743
K22E_HUMANKRT2physical
19380743
CSK_HUMANCSKphysical
19380743
K1C9_HUMANKRT9physical
19380743
SPTB2_HUMANSPTBN1physical
19380743
K2C5_HUMANKRT5physical
19380743
K1C14_HUMANKRT14physical
19380743
K2C6B_HUMANKRT6Bphysical
19380743
HSP7C_HUMANHSPA8physical
19380743
K2C6A_HUMANKRT6Aphysical
19380743
ACTB_HUMANACTBphysical
19380743
ARAP1_HUMANARAP1physical
19380743
TBB5_HUMANTUBBphysical
19380743
K1C16_HUMANKRT16physical
19380743
BCR_HUMANBCRphysical
19380743
ABL1_HUMANABL1physical
19380743
HS90B_HUMANHSP90AB1physical
19380743
CRK_HUMANCRKphysical
19380743
IQGA1_HUMANIQGAP1physical
19380743
K1C17_HUMANKRT17physical
19380743
SHIP2_HUMANINPPL1physical
19380743
TBA1B_HUMANTUBA1Bphysical
19380743
MYH10_HUMANMYH10physical
19380743
HS90A_HUMANHSP90AA1physical
19380743
MYO1D_HUMANMYO1Dphysical
19380743
SPTA1_HUMANSPTA1physical
19380743
SPTN1_HUMANSPTAN1physical
19380743
K2C79_HUMANKRT79physical
19380743
TCPG_HUMANCCT3physical
19380743
ACTN4_HUMANACTN4physical
19380743
TCPQ_HUMANCCT8physical
19380743
K2C8_HUMANKRT8physical
19380743
HS71L_HUMANHSPA1Lphysical
19380743
UBC_HUMANUBCphysical
19380743
K2C73_HUMANKRT73physical
19380743
ACACA_HUMANACACAphysical
19380743
GRP78_HUMANHSPA5physical
19380743
DSC1_HUMANDSC1physical
19380743
TCPH_HUMANCCT7physical
19380743
COR1C_HUMANCORO1Cphysical
19380743
DDX6_HUMANDDX6physical
19380743
TCPA_HUMANTCP1physical
19380743
UBS3A_HUMANUBASH3Aphysical
19380743
DCD_HUMANDCDphysical
19380743
TCPZ_HUMANCCT6Aphysical
19380743
CBL_HUMANCBLphysical
19380743
MCCB_HUMANMCCC2physical
19380743
DNJA1_HUMANDNAJA1physical
19380743
MYH9_HUMANMYH9physical
19380743
TCPW_HUMANCCT6Bphysical
19380743
KSYK_HUMANSYKphysical
20585042
ACTB_HUMANACTBphysical
24189400
ACTG_HUMANACTG1physical
24189400
EGFR_HUMANEGFRphysical
24189400
ERRFI_HUMANERRFI1physical
24189400
GFAP_HUMANGFAPphysical
24189400
GRB2_HUMANGRB2physical
24189400
HNRH1_HUMANHNRNPH1physical
24189400
HNRH2_HUMANHNRNPH2physical
24189400
HNRPF_HUMANHNRNPFphysical
24189400
HNRPU_HUMANHNRNPUphysical
24189400
ROA2_HUMANHNRNPA2B1physical
24189400
RS27A_HUMANRPS27Aphysical
24189400
S10A8_HUMANS100A8physical
24189400
UBS3B_HUMANUBASH3Bphysical
24189400
UBS3B_HUMANUBASH3Bphysical
25416956
S2548_HUMANSLC25A48physical
25416956
TAU_HUMANMAPTphysical
16364302
PKP4_HUMANPKP4physical
21516116
AURKB_HUMANAURKBphysical
26766443
CUL3_HUMANCUL3physical
26766443
KI20A_HUMANKIF20Aphysical
26766443
EWS_HUMANEWSR1physical
24189400
H11_HUMANHIST1H1Aphysical
24189400
H12_HUMANHIST1H1Cphysical
24189400
H13_HUMANHIST1H1Dphysical
24189400
H14_HUMANHIST1H1Ephysical
24189400
H1T_HUMANHIST1H1Tphysical
24189400
HSP7C_HUMANHSPA8physical
24189400
LG3BP_HUMANLGALS3BPphysical
24189400
MYH9_HUMANMYH9physical
24189400

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBS3B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20 AND THR-23, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-19, AND MASSSPECTROMETRY.

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