AGFG2_HUMAN - dbPTM
AGFG2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AGFG2_HUMAN
UniProt AC O95081
Protein Name Arf-GAP domain and FG repeat-containing protein 2
Gene Name AGFG2
Organism Homo sapiens (Human).
Sequence Length 481
Subcellular Localization
Protein Description
Protein Sequence MVMAAKKGPGPGGGVSGGKAEAEAASEVWCRRVRELGGCSQAGNRHCFECAQRGVTYVDITVGSFVCTTCSGLLRGLNPPHRVKSISMTTFTEPEVVFLQSRGNEVCRKIWLGLFDARTSLVPDSRDPQKVKEFLQEKYEKKRWYVPPDQVKGPTYTKGSASTPVQGSIPEGKPLRTLLGDPAPSLSVAASTSSQPVSQSHARTSQARSTQPPPHSSVKKASTDLLADIGGDPFAAPQMAPAFAAFPAFGGQTPSQGGFANFDAFSSGPSSSVFGSLPPAGQASFQAQPTPAGSSQGTPFGATPLAPASQPNSLADVGSFLGPGVPAAGVPSSLFGMAGQVPPLQSVTMGGGGGSSTGLAFGAFTNPFTAPAAQSPLPSTNPFQPNGLAPGPGFGMSSAGPGFPQAVPPTGAFASSFPAPLFPPQTPLVQQQNGSSFGDLGSAKLGQRPLSQPAGISTNPFMTGPSSSPFASKPPTTNPFL
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
6Acetylation--MVMAAKKGPGPGG
--CCCCCCCCCCCCC		49.0412429809
7Acetylation-MVMAAKKGPGPGGG
-CCCCCCCCCCCCCC		66.6626051181
16PhosphorylationPGPGGGVSGGKAEAE
CCCCCCCCCHHHHHH		45.14-
40PhosphorylationVRELGGCSQAGNRHC
HHHHCCCCCCCCCHH		26.7520068231
85PhosphorylationNPPHRVKSISMTTFT
CCCCCCCEEECEECC		19.6227080861
87PhosphorylationPHRVKSISMTTFTEP
CCCCCEEECEECCCC		19.7127080861
92PhosphorylationSISMTTFTEPEVVFL
EEECEECCCCEEEEE		48.8420068231
101PhosphorylationPEVVFLQSRGNEVCR
CEEEEEECCCCHHHH		44.2820068231
132UbiquitinationSRDPQKVKEFLQEKY
CCCHHHHHHHHHHHH		50.19-
138AcetylationVKEFLQEKYEKKRWY
HHHHHHHHHHHCCCC		45.8327452117
138UbiquitinationVKEFLQEKYEKKRWY
HHHHHHHHHHHCCCC		45.83-
141AcetylationFLQEKYEKKRWYVPP
HHHHHHHHCCCCCCH		44.5430589365
142AcetylationLQEKYEKKRWYVPPD
HHHHHHHCCCCCCHH		35.9030589371
145PhosphorylationKYEKKRWYVPPDQVK
HHHHCCCCCCHHHCC		13.70-
152UbiquitinationYVPPDQVKGPTYTKG
CCCHHHCCCCCCCCC		54.24-
158UbiquitinationVKGPTYTKGSASTPV
CCCCCCCCCCCCCCC		40.22-
158AcetylationVKGPTYTKGSASTPV
CCCCCCCCCCCCCCC		40.2226051181
160PhosphorylationGPTYTKGSASTPVQG
CCCCCCCCCCCCCCC		22.1728857561
162PhosphorylationTYTKGSASTPVQGSI
CCCCCCCCCCCCCCC		34.6328857561
163PhosphorylationYTKGSASTPVQGSIP
CCCCCCCCCCCCCCC		27.4826657352
173SumoylationQGSIPEGKPLRTLLG
CCCCCCCCCHHHHHC		38.94-
173SumoylationQGSIPEGKPLRTLLG
CCCCCCCCCHHHHHC		38.9419608861
173UbiquitinationQGSIPEGKPLRTLLG
CCCCCCCCCHHHHHC		38.9419608861
173AcetylationQGSIPEGKPLRTLLG
CCCCCCCCCHHHHHC		38.9419608861
177O-linked_GlycosylationPEGKPLRTLLGDPAP
CCCCCHHHHHCCCCC		33.7428510447
185O-linked_GlycosylationLLGDPAPSLSVAAST
HHCCCCCCCEEECCC		35.0728510447
187O-linked_GlycosylationGDPAPSLSVAASTSS
CCCCCCCEEECCCCC		17.6628510447
191O-linked_GlycosylationPSLSVAASTSSQPVS
CCCEEECCCCCCCCC		21.0528510447
193O-linked_GlycosylationLSVAASTSSQPVSQS
CEEECCCCCCCCCHH		25.2028510447
194O-linked_GlycosylationSVAASTSSQPVSQSH
EEECCCCCCCCCHHH		38.2928510447
198O-linked_GlycosylationSTSSQPVSQSHARTS
CCCCCCCCHHHCCCC		32.4228510447
200O-linked_GlycosylationSSQPVSQSHARTSQA
CCCCCCHHHCCCCCC		16.1728510447
209PhosphorylationARTSQARSTQPPPHS
CCCCCCCCCCCCCCH		34.1218510355
210PhosphorylationRTSQARSTQPPPHSS
CCCCCCCCCCCCCHH		39.2718510355
216PhosphorylationSTQPPPHSSVKKAST
CCCCCCCHHHCHHHH		42.4728348404
217PhosphorylationTQPPPHSSVKKASTD
CCCCCCHHHCHHHHH		34.6218510355
309O-linked_GlycosylationATPLAPASQPNSLAD
CCCCCCCCCCCCCHH		45.1528510447
332O-linked_GlycosylationVPAAGVPSSLFGMAG
CCCCCCCHHHHCCCC		36.9528510447
333O-linked_GlycosylationPAAGVPSSLFGMAGQ
CCCCCCHHHHCCCCC		22.9628510447
451PhosphorylationKLGQRPLSQPAGIST
CCCCCCCCCCCCCCC		36.4828857561
457PhosphorylationLSQPAGISTNPFMTG
CCCCCCCCCCCCCCC		22.6328102081
463PhosphorylationISTNPFMTGPSSSPF
CCCCCCCCCCCCCCC		46.4425627689
466PhosphorylationNPFMTGPSSSPFASK
CCCCCCCCCCCCCCC		44.8025159151
467PhosphorylationPFMTGPSSSPFASKP
CCCCCCCCCCCCCCC		45.2025159151
468PhosphorylationFMTGPSSSPFASKPP
CCCCCCCCCCCCCCC		28.5125159151
472PhosphorylationPSSSPFASKPPTTNP
CCCCCCCCCCCCCCC		46.1827251275
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 AGFG2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AGFG2_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 AGFG2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
EPS15_HUMANEPS15physical
10613896
STAR7_HUMANSTARD7physical
28514442
AGFG1_HUMANAGFG1physical
28514442
TRI68_HUMANTRIM68physical
28514442
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 AGFG2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-173, AND MASS SPECTROMETRY.

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