SH2B2_HUMAN - dbPTM
SH2B2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SH2B2_HUMAN
UniProt AC O14492
Protein Name SH2B adapter protein 2
Gene Name SH2B2
Organism Homo sapiens (Human).
Sequence Length 632
Subcellular Localization Cytoplasm . Cell membrane . Cytoplasmic before PDGF stimulation. After PDGF stimulation, localized at the cell membrane and peripheral region.
Protein Description Adapter protein for several members of the tyrosine kinase receptor family. Involved in multiple signaling pathways. May be involved in coupling from immunoreceptor to Ras signaling. Acts as a negative regulator of cytokine signaling in collaboration with CBL. Binds to EPOR and suppresses EPO-induced STAT5 activation, possibly through a masking effect on STAT5 docking sites in EPOR. Suppresses PDGF-induced mitogenesis. May induce cytoskeletal reorganization via interaction with VAV3..
Protein Sequence MNGAGPGPAAAAPVPVPVPVPDWRQFCELHAQAAAVDFAHKFCRFLRDNPAYDTPDAGASFSRHFAANFLDVFGEEVRRVLVAGPTTRGAAVSAEAMEPELADTSALKAAPYGHSRSSEDVSTHAATKARVRKGFSLRNMSLCVVDGVRDMWHRRASPEPDAAAAPRTAEPRDKWTRRLRLSRTLAAKVELVDIQREGALRFMVADDAAAGSGGSAQWQKCRLLLRRAVAEERFRLEFFVPPKASRPKVSIPLSAIIEVRTTMPLEMPEKDNTFVLKVENGAEYILETIDSLQKHSWVADIQGCVDPGDSEEDTELSCTRGGCLASRVASCSCELLTDAVDLPRPPETTAVGAVVTAPHSRGRDAVRESLIHVPLETFLQTLESPGGSGSDSNNTGEQGAETDPEAEPELELSDYPWFHGTLSRVKAAQLVLAGGPRNHGLFVIRQSETRPGEYVLTFNFQGKAKHLRLSLNGHGQCHVQHLWFQSVLDMLRHFHTHPIPLESGGSADITLRSYVRAQDPPPEPGPTPPAAPASPACWSDSPGQHYFSSLAAAACPPASPSDAAGASSSSASSSSAASGPAPPRPVEGQLSARSRSNSAERLLEAVAATAAEEPPEAAPGRARAVENQYSFY
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
52PhosphorylationFLRDNPAYDTPDAGA
HHCCCCCCCCCCCCC		22.93-
60PhosphorylationDTPDAGASFSRHFAA
CCCCCCCHHHHHHHH		23.8824719451
108UbiquitinationLADTSALKAAPYGHS
HCCCHHHHCCCCCCC		42.07-
112PhosphorylationSALKAAPYGHSRSSE
HHHHCCCCCCCCCCC		23.8123312004
115PhosphorylationKAAPYGHSRSSEDVS
HCCCCCCCCCCCCHH		29.5125849741
117PhosphorylationAPYGHSRSSEDVSTH
CCCCCCCCCCCHHHH		40.8821082442
118PhosphorylationPYGHSRSSEDVSTHA
CCCCCCCCCCHHHHH		36.3826657352
122PhosphorylationSRSSEDVSTHAATKA
CCCCCCHHHHHHHHH		27.1428060719
123PhosphorylationRSSEDVSTHAATKAR
CCCCCHHHHHHHHHH		18.5127251275
127PhosphorylationDVSTHAATKARVRKG
CHHHHHHHHHHHHCC		26.4828060719
136PhosphorylationARVRKGFSLRNMSLC
HHHHCCCCCCCEEEE		34.7823312004
141PhosphorylationGFSLRNMSLCVVDGV
CCCCCCEEEEEEECH		23.3624245541
157PhosphorylationDMWHRRASPEPDAAA
HHHHHCCCCCCCCCC		28.1629255136
160PhosphorylationHRRASPEPDAAAAPR
HHCCCCCCCCCCCCC		39.6724719451
179PhosphorylationRDKWTRRLRLSRTLA
CCHHHHHHHHHHHHH		6.1024719451
184PhosphorylationRRLRLSRTLAAKVEL
HHHHHHHHHHHCEEE		19.8524719451
200PhosphorylationDIQREGALRFMVADD
EECCCCCEEEEEECH		6.7924719451
310PhosphorylationGCVDPGDSEEDTELS
CCCCCCCCHHHHHCE		49.1230576142
314PhosphorylationPGDSEEDTELSCTRG
CCCCHHHHHCEECCC		41.9529978859
317PhosphorylationSEEDTELSCTRGGCL
CHHHHHCEECCCCHH		13.7529978859
319PhosphorylationEDTELSCTRGGCLAS
HHHHCEECCCCHHHH		29.0429978859
330PhosphorylationCLASRVASCSCELLT
HHHHHHHHCCCEECC		12.0524719451
332PhosphorylationASRVASCSCELLTDA
HHHHHHCCCEECCCC		14.2328348404
348PhosphorylationDLPRPPETTAVGAVV
CCCCCCCCCEEEEEE		26.3128270605
349PhosphorylationLPRPPETTAVGAVVT
CCCCCCCCEEEEEEE		20.0628270605
353PhosphorylationPETTAVGAVVTAPHS
CCCCEEEEEEECCCC		5.9924719451
356PhosphorylationTAVGAVVTAPHSRGR
CEEEEEEECCCCCCC		28.0728270605
360PhosphorylationAVVTAPHSRGRDAVR
EEEECCCCCCCHHHH		35.0628270605
373PhosphorylationVRESLIHVPLETFLQ
HHHHHCCCCHHHHHH		4.6024719451
375PhosphorylationESLIHVPLETFLQTL
HHHCCCCHHHHHHHH		10.6132142685
572PhosphorylationGASSSSASSSSAASG
CCCCCCCCCCCCCCC		32.4725332170
591PhosphorylationRPVEGQLSARSRSNS
CCCCCCCCCCCCCCH		17.4725332170
594PhosphorylationEGQLSARSRSNSAER
CCCCCCCCCCCHHHH		39.5125921289
598PhosphorylationSARSRSNSAERLLEA
CCCCCCCHHHHHHHH		32.5225921289
629PhosphorylationARAVENQYSFY----
CCHHHCCCCCC----		16.6028152594
630PhosphorylationRAVENQYSFY-----
CHHHCCCCCC-----		14.3328152594
632PhosphorylationVENQYSFY-------
HHCCCCCC-------		16.2325839225
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 SH2B2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SH2B2_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 SH2B2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBL_HUMANCBLphysical
10374881
NTRK1_HUMANNTRK1physical
9856458
GRB2_HUMANGRB2physical
9856458
CBL_HUMANCBLphysical
18273061
CBL_HUMANCBLphysical
15737992
SHIP2_HUMANINPPL1physical
17620296
INSR_HUMANINSRphysical
17620296
CBL_HUMANCBLphysical
17620296
SRBS1_HUMANSORBS1physical
17548467
PGFRB_HUMANPDGFRBphysical
9989826
CBL_HUMANCBLphysical
9989826
GRB2_HUMANGRB2physical
9233773
SHC1_HUMANSHC1physical
9233773
ERBB2_HUMANERBB2physical
16273093
SH2B2_HUMANSH2B2physical
15767667
SH2B1_HUMANSH2B1physical
15767667
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 SH2B2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"APS, an adaptor protein containing pleckstrin homology (PH) and Srchomology-2 (SH2) domains inhibits the JAK-STAT pathway incollaboration with c-Cbl.";
Wakioka T., Sasaki A., Mitsui K., Yokouchi M., Inoue A., Komiya S.,Yoshimura A.;
Leukemia 13:760-767(1999).
Cited for: FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH CBL AND EPOR.
"Cloning and characterization of APS, an adaptor molecule containingPH and SH2 domains that is tyrosine phosphorylated upon B-cellreceptor stimulation.";
Yokouchi M., Suzuki R., Masuhara M., Komiya S., Inoue A.,Yoshimura A.;
Oncogene 15:7-15(1997).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INTERACTION WITH GRB2;KIT AND SHC1, AND PHOSPHORYLATION AT TYR-629.

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