SH22A_HUMAN - dbPTM
SH22A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SH22A_HUMAN
UniProt AC Q9NP31
Protein Name SH2 domain-containing protein 2A
Gene Name SH2D2A
Organism Homo sapiens (Human).
Sequence Length 389
Subcellular Localization Cytoplasm.
Protein Description Could be a T-cell-specific adapter protein involved in the control of T-cell activation. May play a role in the CD4-p56-LCK-dependent signal transduction pathway. Could also play an important role in normal and pathological angiogenesis. Could be an adapter protein that facilitates and regulates interaction of KDR with effector proteins important to endothelial cell survival and proliferation..
Protein Sequence MEFPLAQICPQGSHEAPIPTFSTFQITDMTRRSCQNLGYTAASPQAPEAASNTGNAERAEEVPGEGSLFLQAETRAWFQKTQAHWLLQHGAAPAWFHGFITRREAERLLEPKPQGCYLVRFSESAVTFVLTYRSRTCCRHFLLAQLRDGRHVVLGEDSAHARLQDLLLHYTAHPLSPYGETLTEPLARQTPEPAGLSLRTEESNFGSKSQDPNPQYSPIIKQGQAPVPMQKEGAGEKEPSQLLRPKPPIPAKPQLPPEVYTIPVPRHRPAPRPKPSNPIYNEPDEPIAFYAMGRGSPGEAPSNIYVEVEDEGLPATLGHPVLRKSWSRPVPGGQNTGGSQLHSENSVIGQGPPLPHQPPPAWRHTLPHNLSRQVLQDRGQAWLPLGPPQ
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
2 (in isoform 4)Phosphorylation-56.8426552605
4 (in isoform 4)Phosphorylation-17.3026552605
5 (in isoform 4)Phosphorylation-7.1326552605
9 (in isoform 4)Phosphorylation-1.0526552605
12 (in isoform 4)Phosphorylation-18.9926552605
21 (in isoform 4)Phosphorylation-5.63-
39PhosphorylationRSCQNLGYTAASPQA
HHHHHCCCCCCCCCC		9.0720090780
43PhosphorylationNLGYTAASPQAPEAA
HCCCCCCCCCCCHHH		18.3225159151
67PhosphorylationEEVPGEGSLFLQAET
CCCCCCCEEEEEEEH		16.2027732954
74PhosphorylationSLFLQAETRAWFQKT
EEEEEEEHHHHHHHH		28.8027732954
131PhosphorylationSAVTFVLTYRSRTCC
CCEEEEEEECCCCHH		16.1622210691
132PhosphorylationAVTFVLTYRSRTCCR
CEEEEEEECCCCHHH		11.4822210691
178PhosphorylationTAHPLSPYGETLTEP
CCCCCCCCCCCCCHH		24.9820090780
190PhosphorylationTEPLARQTPEPAGLS
CHHHHHCCCCCCCCC		24.8626356563
197PhosphorylationTPEPAGLSLRTEESN
CCCCCCCCCEECCCC		18.1926356563
198 (in isoform 4)Phosphorylation-10.6427642862
199 (in isoform 4)Phosphorylation-36.3927642862
209PhosphorylationESNFGSKSQDPNPQY
CCCCCCCCCCCCCCC		41.3223186163
216PhosphorylationSQDPNPQYSPIIKQG
CCCCCCCCCCCCCCC		20.0625159151
217PhosphorylationQDPNPQYSPIIKQGQ
CCCCCCCCCCCCCCC		12.3625159151
221UbiquitinationPQYSPIIKQGQAPVP
CCCCCCCCCCCCCCC		49.44-
226 (in isoform 2)Phosphorylation-23.9025147952
242 (in isoform 4)Phosphorylation-5.2727642862
258 (in isoform 4)Phosphorylation-46.3327642862
260PhosphorylationPQLPPEVYTIPVPRH
CCCCCCEEECCCCCC		9.4028796482
261PhosphorylationQLPPEVYTIPVPRHR
CCCCCEEECCCCCCC		24.7928796482
262 (in isoform 4)Phosphorylation-1.4527642862
272 (in isoform 4)Phosphorylation-54.7227642862
276PhosphorylationPAPRPKPSNPIYNEP
CCCCCCCCCCCCCCC		62.4529978859
280PhosphorylationPKPSNPIYNEPDEPI
CCCCCCCCCCCCCCE		18.0920090780
287 (in isoform 4)Phosphorylation-3.7827642862
290 (in isoform 2)Phosphorylation-6.1525147952
290PhosphorylationPDEPIAFYAMGRGSP
CCCCEEEEEECCCCC		6.1520090780
294MethylationIAFYAMGRGSPGEAP
EEEEEECCCCCCCCC		29.36115388825
296PhosphorylationFYAMGRGSPGEAPSN
EEEECCCCCCCCCCC		28.5025159151
300 (in isoform 2)Phosphorylation-20.8025147952
302PhosphorylationGSPGEAPSNIYVEVE
CCCCCCCCCEEEEEC		42.8029978859
305PhosphorylationGEAPSNIYVEVEDEG
CCCCCCEEEEECCCC		8.5320090780
316PhosphorylationEDEGLPATLGHPVLR
CCCCCCCCCCCCCCC		31.1926074081
325PhosphorylationGHPVLRKSWSRPVPG
CCCCCCCCCCCCCCC		24.6926074081
327PhosphorylationPVLRKSWSRPVPGGQ
CCCCCCCCCCCCCCC		33.5226074081
336PhosphorylationPVPGGQNTGGSQLHS
CCCCCCCCCCCCCCC		34.7226074081
337 (in isoform 2)Phosphorylation-41.1127251275
339PhosphorylationGGQNTGGSQLHSENS
CCCCCCCCCCCCCCC		30.8026074081
343PhosphorylationTGGSQLHSENSVIGQ
CCCCCCCCCCCCCCC		47.2526074081
365PhosphorylationPPPAWRHTLPHNLSR
CCCHHHHCCCCCHHH		33.1528555341
371PhosphorylationHTLPHNLSRQVLQDR
HCCCCCHHHHHHHHC		26.4523186163
378MethylationSRQVLQDRGQAWLPL
HHHHHHHCCCCCCCC		26.60115388831
381 (in isoform 2)Phosphorylation-16.7627251275
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
260YPhosphorylationKinaseLCKP06239
PSP
280YPhosphorylationKinaseLCKP06239
PSP
290YPhosphorylationKinaseLCKP06239
PSP
305YPhosphorylationKinaseLCKP06239
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SH22A_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 SH22A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TERA_HUMANVCPphysical
15752563
SMAD2_HUMANSMAD2physical
16806069
SMAD3_HUMANSMAD3physical
16806069
KDM1B_HUMANKDM1Bphysical
26186194
PEAK1_HUMANPEAK1physical
26186194
ASB3_HUMANASB3physical
25814554
FA46A_HUMANFAM46Aphysical
25814554
FA46B_HUMANFAM46Bphysical
25814554
PPR21_HUMANPPP1R21physical
25814554
LNX1_HUMANLNX1physical
25814554
LRRF1_HUMANLRRFIP1physical
25814554
PKHB1_HUMANPLEKHB1physical
25814554
FSBP_HUMANRAD54Bphysical
25814554
RA54B_HUMANRAD54Bphysical
25814554
DC121_HUMANDCAF12L1physical
25814554
ZHX3_HUMANZHX3physical
25814554
ZSCA1_HUMANZSCAN1physical
25814554
P85A_HUMANPIK3R1physical
25814554
P55G_HUMANPIK3R3physical
25814554
FAK1_HUMANPTK2physical
25814554
SPTB1_HUMANSPTBphysical
25814554
TSC1_HUMANTSC1physical
25814554
ARI5A_HUMANARID5Aphysical
25814554
CQ082_HUMANC17orf82physical
25814554
NAA16_HUMANNAA16physical
25814554
LASP1_HUMANLASP1physical
25814554
SRC_HUMANSRCphysical
22689825
VGFR2_HUMANKDRphysical
22689825
KDM1B_HUMANKDM1Bphysical
28514442
PEAK1_HUMANPEAK1physical
28514442
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SH22A_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-217 AND SER-296, ANDMASS SPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-39; TYR-216 AND TYR-305,AND MASS SPECTROMETRY.

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