GGNB2_HUMAN - dbPTM
GGNB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GGNB2_HUMAN
UniProt AC Q9H3C7
Protein Name Gametogenetin-binding protein 2
Gene Name GGNBP2
Organism Homo sapiens (Human).
Sequence Length 697
Subcellular Localization Cytoplasmic vesicle. Associated with vesicular structures..
Protein Description May be involved in spermatogenesis..
Protein Sequence MARLVAVCRDGEEEFPFERRQIPLYIDDTLTMVMEFPDNVLNLDGHQNNGAQLKQFIQRHGMLKQQDLSIAMVVTSREVLSALSQLVPCVGCRRSVERLFSQLVESGNPALEPLTVGPKGVLSVTRSCMTDAKKLYTLFYVHGSKLNDMIDAIPKSKKNKRCQLHSLDTHKPKPLGGCWMDVWELMSQECRDEVVLIDSSCLLETLETYLRKHRFCTDCKNKVLRAYNILIGELDCSKEKGYCAALYEGLRCCPHERHIHVCCETDFIAHLLGRAEPEFAGGRRERHAKTIDIAQEEVLTCLGIHLYERLHRIWQKLRAEEQTWQMLFYLGVDALRKSFEMTVEKVQGISRLEQLCEEFSEEERVRELKQEKKRQKRKNRRKNKCVCDIPTPLQTADEKEVSQEKETDFIENSSCKACGSTEDGNTCVEVIVTNENTSCTCPSSGNLLGSPKIKKGLSPHCNGSDCGYSSSMEGSETGSREGSDVACTEGICNHDEHGDDSCVHHCEDKEDDGDSCVECWANSEENDTKGKNKKKKKKSKILKCDEHIQKLGSCITDPGNRETSGNTMHTVFHRDKTKDTHPESCCSSEKGGQPLPWFEHRKNVPQFAEPTETLFGPDSGKGAKSLVELLDESECTSDEEIFISQDEIQSFMANNQSFYSNREQYRQHLKEKFNKYCRLNDHKRPICSGWLTTAGAN
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
76PhosphorylationSIAMVVTSREVLSAL
CEEEEECCHHHHHHH		18.1624719451
88UbiquitinationSALSQLVPCVGCRRS
HHHHHHHHHHCCHHH		18.7022817900
115PhosphorylationNPALEPLTVGPKGVL
CCCCCCCCCCCCCEE		33.85-
119UbiquitinationEPLTVGPKGVLSVTR
CCCCCCCCCEEEEEH		56.5822817900
119 (in isoform 3)Ubiquitination-56.5821906983
119 (in isoform 2)Ubiquitination-56.5821906983
119 (in isoform 1)Ubiquitination-56.5821906983
125PhosphorylationPKGVLSVTRSCMTDA
CCCEEEEEHHHHCCH		17.31-
136PhosphorylationMTDAKKLYTLFYVHG
HCCHHHHHHEEEECC		15.4124719451
137PhosphorylationTDAKKLYTLFYVHGS
CCHHHHHHEEEECCH		22.3424719451
140PhosphorylationKKLYTLFYVHGSKLN
HHHHHEEEECCHHHH		8.4728348404
171UbiquitinationLHSLDTHKPKPLGGC
EECCCCCCCCCCCCC		57.7529967540
238UbiquitinationIGELDCSKEKGYCAA
HCCCCCCCCCCHHHH		70.5429967540
240UbiquitinationELDCSKEKGYCAALY
CCCCCCCCCHHHHHH		59.94-
242PhosphorylationDCSKEKGYCAALYEG
CCCCCCCHHHHHHCC		7.0325884760
309UbiquitinationLGIHLYERLHRIWQK
HHHHHHHHHHHHHHH		23.4122817900
314UbiquitinationYERLHRIWQKLRAEE
HHHHHHHHHHHHHHH		6.8222817900
316UbiquitinationRLHRIWQKLRAEEQT
HHHHHHHHHHHHHHH		25.5822817900
345 (in isoform 1)Ubiquitination-35.2121906983
345 (in isoform 3)Ubiquitination-35.2121906983
345UbiquitinationSFEMTVEKVQGISRL
HHHHHHHHHHHHHHH		35.2122817900
347UbiquitinationEMTVEKVQGISRLEQ
HHHHHHHHHHHHHHH		55.3522817900
360PhosphorylationEQLCEEFSEEERVRE
HHHHHHCCHHHHHHH		47.5919664994
413PhosphorylationETDFIENSSCKACGS
HCCCCCCCCCCCCCC		25.0727251275
414PhosphorylationTDFIENSSCKACGST
CCCCCCCCCCCCCCC		31.0825627689
426PhosphorylationGSTEDGNTCVEVIVT
CCCCCCCEEEEEEEE		24.3727251275
433PhosphorylationTCVEVIVTNENTSCT
EEEEEEEECCCCCEE		26.2027251275
437PhosphorylationVIVTNENTSCTCPSS
EEEECCCCCEECCCC		20.9927251275
438PhosphorylationIVTNENTSCTCPSSG
EEECCCCCEECCCCC		21.0027251275
440PhosphorylationTNENTSCTCPSSGNL
ECCCCCEECCCCCCC		27.5027251275
443PhosphorylationNTSCTCPSSGNLLGS
CCCEECCCCCCCCCC		53.6927251275
444PhosphorylationTSCTCPSSGNLLGSP
CCEECCCCCCCCCCC		19.4927251275
450PhosphorylationSSGNLLGSPKIKKGL
CCCCCCCCCCCCCCC		24.0022210691
458PhosphorylationPKIKKGLSPHCNGSD
CCCCCCCCCCCCCCC		22.6728985074
464PhosphorylationLSPHCNGSDCGYSSS
CCCCCCCCCCCCCCC		18.75-
469PhosphorylationNGSDCGYSSSMEGSE
CCCCCCCCCCCCCCC		10.9628348404
470PhosphorylationGSDCGYSSSMEGSET
CCCCCCCCCCCCCCC		25.8130576142
471PhosphorylationSDCGYSSSMEGSETG
CCCCCCCCCCCCCCC		18.2130576142
515PhosphorylationDKEDDGDSCVECWAN
CCCCCCCCCCHHHCC		26.1228985074
537AcetylationGKNKKKKKKSKILKC
CCCCCHHHHHHHHHH		71.7790995
538AcetylationKNKKKKKKSKILKCD
CCCCHHHHHHHHHHH		66.9090999
543UbiquitinationKKKSKILKCDEHIQK
HHHHHHHHHHHHHHH		43.0129967540
550AcetylationKCDEHIQKLGSCITD
HHHHHHHHHHHCCCC		54.9625953088
563PhosphorylationTDPGNRETSGNTMHT
CCCCCCCCCCCCEEE		38.4029978859
564PhosphorylationDPGNRETSGNTMHTV
CCCCCCCCCCCEEEE		25.8729978859
567PhosphorylationNRETSGNTMHTVFHR
CCCCCCCCEEEEEEC		17.5429978859
587PhosphorylationTHPESCCSSEKGGQP
CCHHHHCCCCCCCCC		45.9528985074
602UbiquitinationLPWFEHRKNVPQFAE
CCCHHHCCCCCCCCC		65.2929967540
611PhosphorylationVPQFAEPTETLFGPD
CCCCCCCCCCCCCCC		32.8621060948
613PhosphorylationQFAEPTETLFGPDSG
CCCCCCCCCCCCCCC		29.8421060948
619PhosphorylationETLFGPDSGKGAKSL
CCCCCCCCCCCHHHH		45.6021060948
621UbiquitinationLFGPDSGKGAKSLVE
CCCCCCCCCHHHHHH		60.7029967540
633PhosphorylationLVELLDESECTSDEE
HHHHHCCCCCCCCCE		37.3230576142
637PhosphorylationLDESECTSDEEIFIS
HCCCCCCCCCEEEEC		55.4730576142
657PhosphorylationSFMANNQSFYSNREQ
HHHHCCCCHHCCHHH		28.4230576142
676PhosphorylationLKEKFNKYCRLNDHK
HHHHHHHHHCCCCCC		5.5026657352
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 GGNB2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GGNB2_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 GGNB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GGNB2_HUMAN !!
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 GGNB2_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-360, AND MASSSPECTROMETRY.

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