SHB_HUMAN - dbPTM
SHB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SHB_HUMAN
UniProt AC Q15464
Protein Name SH2 domain-containing adapter protein B
Gene Name SHB
Organism Homo sapiens (Human).
Sequence Length 509
Subcellular Localization Cytoplasm. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Associates with membrane lipid rafts upon TCR stimulation.
Protein Description Adapter protein which regulates several signal transduction cascades by linking activated receptors to downstream signaling components. May play a role in angiogenesis by regulating FGFR1, VEGFR2 and PDGFR signaling. May also play a role in T-cell antigen receptor/TCR signaling, interleukin-2 signaling, apoptosis and neuronal cells differentiation by mediating basic-FGF and NGF-induced signaling cascades. May also regulate IRS1 and IRS2 signaling in insulin-producing cells..
Protein Sequence MAKWLNKYFSLGNSKTKSPPQPPRPDYREQRRRGERPSQPPQAVPQASSAASASCGPATASCFSASSGSLPDDSGSTSDLIRAYRAQKERDFEDPYNGPGSSLRKLRAMCRLDYCGGSGEPGGVQRAFSASSASGAAGCCCASSGAGAAASSSSSSGSPHLYRSSSERRPATPAEVRYISPKHRLIKVESAAGGGAGDPLGGACAGGRTWSPTACGGKKLLNKCAASAAEESGAGKKDKVTIADDYSDPFDAKNDLKSKAGKGESAGYMEPYEAQRIMTEFQRQESVRSQHKGIQLYDTPYEPEGQSVDSDSESTVSPRLRESKLPQDDDRPADEYDQPWEWNRVTIPALAAQFNGNEKRQSSPSPSRDRRRQLRAPGGGFKPIKHGSPEFCGILGERVDPAVPLEKQIWYHGAISRGDAENLLRLCKECSYLVRNSQTSKHDYSLSLRSNQGFMHMKLAKTKEKYVLGQNSPPFDSVPEVIHYYTTRKLPIKGAEHLSLLYPVAVRTL
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
8PhosphorylationMAKWLNKYFSLGNSK
CCHHHHHHHCCCCCC		9.4228152594
10PhosphorylationKWLNKYFSLGNSKTK
HHHHHHHCCCCCCCC		32.0722617229
14PhosphorylationKYFSLGNSKTKSPPQ
HHHCCCCCCCCCCCC		39.6526434552
15UbiquitinationYFSLGNSKTKSPPQP
HHCCCCCCCCCCCCC		65.0633845483
16PhosphorylationFSLGNSKTKSPPQPP
HCCCCCCCCCCCCCC		36.2523186163
18PhosphorylationLGNSKTKSPPQPPRP
CCCCCCCCCCCCCCC		47.2323403867
27PhosphorylationPQPPRPDYREQRRRG
CCCCCCCHHHHHHCC		20.80-
59PhosphorylationSASCGPATASCFSAS
HHCCCCCCHHHHHCC		23.4128348404
61PhosphorylationSCGPATASCFSASSG
CCCCCCHHHHHCCCC		16.0228348404
64PhosphorylationPATASCFSASSGSLP
CCCHHHHHCCCCCCC		31.4128348404
66PhosphorylationTASCFSASSGSLPDD
CHHHHHCCCCCCCCC		33.7528348404
67PhosphorylationASCFSASSGSLPDDS
HHHHHCCCCCCCCCC		31.9228348404
69PhosphorylationCFSASSGSLPDDSGS
HHHCCCCCCCCCCCC		38.3828348404
96PhosphorylationERDFEDPYNGPGSSL
HCCCCCCCCCCCHHH		45.1025159151
101PhosphorylationDPYNGPGSSLRKLRA
CCCCCCCHHHHHHHH		29.3628152594
102PhosphorylationPYNGPGSSLRKLRAM
CCCCCCHHHHHHHHH		37.8025159151
114PhosphorylationRAMCRLDYCGGSGEP
HHHHCCCCCCCCCCC		9.5121945579
118PhosphorylationRLDYCGGSGEPGGVQ
CCCCCCCCCCCCHHH		25.8521945579
129PhosphorylationGGVQRAFSASSASGA
CHHHHCCCCCCCCCC		26.6823927012
131PhosphorylationVQRAFSASSASGAAG
HHHCCCCCCCCCCCC		25.8227251275
132PhosphorylationQRAFSASSASGAAGC
HHCCCCCCCCCCCCC		26.6027251275
134PhosphorylationAFSASSASGAAGCCC
CCCCCCCCCCCCCCC		30.8027251275
143PhosphorylationAAGCCCASSGAGAAA
CCCCCCCCCCCCCCC		18.5227251275
144PhosphorylationAGCCCASSGAGAAAS
CCCCCCCCCCCCCCC		17.7127251275
151PhosphorylationSGAGAAASSSSSSGS
CCCCCCCCCCCCCCC		26.4828450419
152PhosphorylationGAGAAASSSSSSGSP
CCCCCCCCCCCCCCC		29.5228450419
153PhosphorylationAGAAASSSSSSGSPH
CCCCCCCCCCCCCCC		31.5728450419
154PhosphorylationGAAASSSSSSGSPHL
CCCCCCCCCCCCCCC		30.3928450419
155PhosphorylationAAASSSSSSGSPHLY
CCCCCCCCCCCCCCC		40.4428450419
156PhosphorylationAASSSSSSGSPHLYR
CCCCCCCCCCCCCCC		45.2828450419
158PhosphorylationSSSSSSGSPHLYRSS
CCCCCCCCCCCCCCC		15.8727422710
162PhosphorylationSSGSPHLYRSSSERR
CCCCCCCCCCCCCCC		12.8628450419
164PhosphorylationGSPHLYRSSSERRPA
CCCCCCCCCCCCCCC		25.3426699800
165PhosphorylationSPHLYRSSSERRPAT
CCCCCCCCCCCCCCC		27.5026699800
166PhosphorylationPHLYRSSSERRPATP
CCCCCCCCCCCCCCH		36.0527422710
172PhosphorylationSSERRPATPAEVRYI
CCCCCCCCHHHEEEC		26.2229396449
180PhosphorylationPAEVRYISPKHRLIK
HHHEEECCCCCEEEE		20.9724719451
187SumoylationSPKHRLIKVESAAGG
CCCCEEEEEECCCCC		44.5428112733
190PhosphorylationHRLIKVESAAGGGAG
CEEEEEECCCCCCCC		26.8025159151
201PhosphorylationGGAGDPLGGACAGGR
CCCCCCCCCCCCCCC		27.3417389395
209PhosphorylationGACAGGRTWSPTACG
CCCCCCCCCCCCCCC		33.3023403867
211PhosphorylationCAGGRTWSPTACGGK
CCCCCCCCCCCCCHH		16.2625159151
213PhosphorylationGGRTWSPTACGGKKL
CCCCCCCCCCCHHHH		29.1223403867
218AcetylationSPTACGGKKLLNKCA
CCCCCCHHHHHHHHH		26.0725953088
241PhosphorylationAGKKDKVTIADDYSD
CCCCCCEEECCCCCC		19.0526356563
246PhosphorylationKVTIADDYSDPFDAK
CEEECCCCCCCCCCH		18.6027273156
247PhosphorylationVTIADDYSDPFDAKN
EEECCCCCCCCCCHH		45.8925159151
265PhosphorylationSKAGKGESAGYMEPY
HHCCCCCCCCCCCHH		35.3521945579
268PhosphorylationGKGESAGYMEPYEAQ
CCCCCCCCCCHHHHH		9.6821945579
272PhosphorylationSAGYMEPYEAQRIMT
CCCCCCHHHHHHHHH		15.5821945579
279PhosphorylationYEAQRIMTEFQRQES
HHHHHHHHHHHHHHH		31.1429083192
286PhosphorylationTEFQRQESVRSQHKG
HHHHHHHHHHHHCCC		17.9429083192
289PhosphorylationQRQESVRSQHKGIQL
HHHHHHHHHCCCEEE		34.1933259812
297PhosphorylationQHKGIQLYDTPYEPE
HCCCEEEECCCCCCC		11.0322617229
299PhosphorylationKGIQLYDTPYEPEGQ
CCEEEECCCCCCCCC		17.7628796482
301PhosphorylationIQLYDTPYEPEGQSV
EEEECCCCCCCCCCC		46.3230183078
307PhosphorylationPYEPEGQSVDSDSES
CCCCCCCCCCCCCCC		38.4525159151
310PhosphorylationPEGQSVDSDSESTVS
CCCCCCCCCCCCCCC		40.6625159151
312PhosphorylationGQSVDSDSESTVSPR
CCCCCCCCCCCCCHH		37.0830183078
314PhosphorylationSVDSDSESTVSPRLR
CCCCCCCCCCCHHHH		37.7528102081
315PhosphorylationVDSDSESTVSPRLRE
CCCCCCCCCCHHHHH		22.4330175587
317PhosphorylationSDSESTVSPRLRESK
CCCCCCCCHHHHHCC		12.3725159151
323PhosphorylationVSPRLRESKLPQDDD
CCHHHHHCCCCCCCC		32.8122322096
333PhosphorylationPQDDDRPADEYDQPW
CCCCCCCHHHCCCCC		24.1415951569
336PhosphorylationDDRPADEYDQPWEWN
CCCCHHHCCCCCCCC		22.0427273156
355PhosphorylationPALAAQFNGNEKRQS
HHHHHHHCCCCCCCC		40.0617016520
362PhosphorylationNGNEKRQSSPSPSRD
CCCCCCCCCCCCCHH		48.5323403867
363PhosphorylationGNEKRQSSPSPSRDR
CCCCCCCCCCCCHHH		22.5123403867
365PhosphorylationEKRQSSPSPSRDRRR
CCCCCCCCCCHHHHH		37.1423403867
367PhosphorylationRQSSPSPSRDRRRQL
CCCCCCCCHHHHHHH		51.6723403867
388PhosphorylationFKPIKHGSPEFCGIL
CCCCCCCCHHHCCCC		22.4522167270
423PhosphorylationSRGDAENLLRLCKEC
CCCCHHHHHHHHHHC		1.9017389395
437PhosphorylationCSYLVRNSQTSKHDY
CCHHHHCCCCCCCCC		25.03-
444PhosphorylationSQTSKHDYSLSLRSN
CCCCCCCCEEEEECC		15.9529759185
445PhosphorylationQTSKHDYSLSLRSNQ
CCCCCCCEEEEECCC		19.9627050516
447PhosphorylationSKHDYSLSLRSNQGF
CCCCCEEEEECCCCC		18.7817081983
450PhosphorylationDYSLSLRSNQGFMHM
CCEEEEECCCCCCCE		38.5129759185
466PhosphorylationLAKTKEKYVLGQNSP
EEECHHHEECCCCCC		11.2922964224
472PhosphorylationKYVLGQNSPPFDSVP
HEECCCCCCCCCCCC		26.5122964224
477PhosphorylationQNSPPFDSVPEVIHY
CCCCCCCCCCHHHHH		39.6922964224
484PhosphorylationSVPEVIHYYTTRKLP
CCCHHHHHEECCCCC		7.44-
485PhosphorylationVPEVIHYYTTRKLPI
CCHHHHHEECCCCCC		6.3522817900
486PhosphorylationPEVIHYYTTRKLPIK
CHHHHHEECCCCCCC		16.9822964224
487PhosphorylationEVIHYYTTRKLPIKG
HHHHHEECCCCCCCC		15.0822964224
502PhosphorylationAEHLSLLYPVAVRTL
HHHHHHHEEEEEECC		10.8529523821
508PhosphorylationLYPVAVRTL------
HEEEEEECC------		30.1622199227
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 SHB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SHB_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 SHB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VGFR2_HUMANKDRphysical
15026417
IL2RB_HUMANIL2RBphysical
12200137
IL2RG_HUMANIL2RGphysical
12200137
JAK1_HUMANJAK1physical
12200137
JAK3_HUMANJAK3physical
12200137
LAT_HUMANLATphysical
10488157
PLCG1_HUMANPLCG1physical
10488157
LCP2_HUMANLCP2physical
12084069
ZAP70_HUMANZAP70physical
12084069
VAV_HUMANVAV1physical
12084069
LAT_HUMANLATphysical
12084069
GRB2_HUMANGRB2physical
9484780
EPS8_HUMANEPS8physical
7537362
SRC_HUMANSRCphysical
7537362
P85A_HUMANPIK3R1physical
7537362
FGFR1_HUMANFGFR1physical
7537362
ABL1_HUMANABL1physical
17112510
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 SHB_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND MASSSPECTROMETRY.
"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-314; SER-317 ANDSER-388, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388, 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-114; TYR-246 ANDTYR-268, AND MASS SPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-114; TYR-246; TYR-268AND TYR-336, AND MASS SPECTROMETRY.
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-246, AND MASSSPECTROMETRY.

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