SH23A_HUMAN - dbPTM
SH23A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SH23A_HUMAN
UniProt AC Q9BRG2
Protein Name SH2 domain-containing protein 3A
Gene Name SH2D3A
Organism Homo sapiens (Human).
Sequence Length 576
Subcellular Localization
Protein Description May play a role in JNK activation..
Protein Sequence MQVPQDGEDLAGQPWYHGLLSRQKAEALLQQNGDFLVRASGSRGGNPVISCRWRGSALHFEVFRVALRPRPGRPTALFQLEDEQFPSIPALVHSYMTGRRPLSQATGAVVSRPVTWQGPLRRSFSEDTLMDGPARIEPLRARKWSNSQPADLAHMGRSREDPAGMEASTMPISALPRTSSDPVLLKAPAPLGTVADSLRASDGQLQAKAPTKPPRTPSFELPDASERPPTYCELVPRVPSVQGTSPSQSCPEPEAPWWEAEEDEEEENRCFTRPQAEISFCPHDAPSCLLGPQNRPLEPQVLHTLRGLFLEHHPGSTALHLLLVDCQATGLLGVTRDQRGNMGVSSGLELLTLPHGHHLRLELLERHQTLALAGALAVLGCSGPLEERAAALRGLVELALALRPGAAGDLPGLAAVMGALLMPQVSRLEHTWRQLRRSHTEAALAFEQELKPLMRALDEGAGPCDPGEVALPHVAPMVRLLEGEEVAGPLDESCERLLRTLHGARHMVRDAPKFRKVAAQRLRGFRPNPELREALTTGFVRRLLWGSRGAGAPRAERFEKFQRVLGVLSQRLEPDR
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
16PhosphorylationDLAGQPWYHGLLSRQ
CCCCCCCHHHHHCHH		7.8410187783
24UbiquitinationHGLLSRQKAEALLQQ
HHHHCHHHHHHHHHH		47.27-
25 (in isoform 2)Phosphorylation-10.0425056879
40PhosphorylationGDFLVRASGSRGGNP
CCEEEEECCCCCCCC		27.0824719451
56PhosphorylationISCRWRGSALHFEVF
EEEEECCCCEEEEEE		21.0527251275
95PhosphorylationIPALVHSYMTGRRPL
HHHHHHHHHCCCCCH		5.4822817900
97PhosphorylationALVHSYMTGRRPLSQ
HHHHHHHCCCCCHHH		21.2124719451
123PhosphorylationWQGPLRRSFSEDTLM
CCCCCCCCCCCCCCC		27.0423927012
125PhosphorylationGPLRRSFSEDTLMDG
CCCCCCCCCCCCCCC		35.4919664994
128PhosphorylationRRSFSEDTLMDGPAR
CCCCCCCCCCCCCCC		21.6723663014
145PhosphorylationPLRARKWSNSQPADL
HHHCCCCCCCCCCHH		29.6425159151
147PhosphorylationRARKWSNSQPADLAH
HCCCCCCCCCCHHHH		31.8328731282
158PhosphorylationDLAHMGRSREDPAGM
HHHHCCCCCCCCCCC		34.0025159151
173PhosphorylationEASTMPISALPRTSS
CCCCCCCCCCCCCCC		20.2024719451
178PhosphorylationPISALPRTSSDPVLL
CCCCCCCCCCCCEEE		30.5523927012
179PhosphorylationISALPRTSSDPVLLK
CCCCCCCCCCCEEEE		33.7423927012
180PhosphorylationSALPRTSSDPVLLKA
CCCCCCCCCCEEEEC		45.3719664994
193PhosphorylationKAPAPLGTVADSLRA
ECCCCCCHHHHHHCC		21.8730278072
197PhosphorylationPLGTVADSLRASDGQ
CCCHHHHHHCCCCCC		15.2622167270
201PhosphorylationVADSLRASDGQLQAK
HHHHHCCCCCCCCCC		35.5222167270
211PhosphorylationQLQAKAPTKPPRTPS
CCCCCCCCCCCCCCC		62.1323532336
216PhosphorylationAPTKPPRTPSFELPD
CCCCCCCCCCCCCCC		29.1121945579
218PhosphorylationTKPPRTPSFELPDAS
CCCCCCCCCCCCCCC		30.6421945579
225PhosphorylationSFELPDASERPPTYC
CCCCCCCCCCCCCCE		41.3321945579
230PhosphorylationDASERPPTYCELVPR
CCCCCCCCCEEEECC		43.4121945579
231PhosphorylationASERPPTYCELVPRV
CCCCCCCCEEEECCC		6.9521945579
245PhosphorylationVPSVQGTSPSQSCPE
CCCCCCCCCCCCCCC		29.4021712546
358UbiquitinationLTLPHGHHLRLELLE
EECCCCCHHHHHHHH		19.76-
451UbiquitinationLAFEQELKPLMRALD
HHHHHHHHHHHHHHH		35.0421906983
467UbiquitinationGAGPCDPGEVALPHV
CCCCCCHHCCCHHHH		28.85-
493PhosphorylationVAGPLDESCERLLRT
CCCCCCHHHHHHHHH		22.4229523821
547PhosphorylationVRRLLWGSRGAGAPR
HHHHHHCCCCCCCCH		18.8924719451
548MethylationRRLLWGSRGAGAPRA
HHHHHCCCCCCCCHH		34.7354559279
560UbiquitinationPRAERFEKFQRVLGV
CHHHHHHHHHHHHHH		44.05-
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 SH23A_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SH23A_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 SH23A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BCAR1_HUMANBCAR1physical
10187783
EGFR_HUMANEGFRphysical
10187783
CENPB_HUMANCENPBphysical
25814554
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 SH23A_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-180, 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-123; SER-125 ANDSER-180, AND MASS SPECTROMETRY.

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