AGFG1_MOUSE - dbPTM
AGFG1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AGFG1_MOUSE
UniProt AC Q8K2K6
Protein Name Arf-GAP domain and FG repeat-containing protein 1
Gene Name Agfg1
Organism Mus musculus (Mouse).
Sequence Length 561
Subcellular Localization Nucleus . Cytoplasmic vesicle . Associated with the cytosolic surface of proacrosomic vesicles of early round spermatids.
Protein Description Required for vesicle docking or fusion during acrosome biogenesis. May play a role in RNA trafficking or localization..
Protein Sequence MAASAKRKQEEKHLKMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPPHRVKSISMTTFTQQEIEFLQKHGNEVCKQIWLGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRWYVPPEQAKVVASVHASISGSSASSTSSTPEVKPLKSLLGESAPALHLNKGTPSQSPVVGRSQGQQQEKKQFDLLSDLGSDIFAAPAPQSTATANFANFAHFNSHAAQNSANADFANFDAFGQSSGSSNFGGFPTASHSSFQPQTTGGSAGSVNANFAHFDNFPKSSSADFGTFSTSQSHQTASTVSKVSTNKAGLQTADKYAALANLDNIFSAGQGGDQGSGFGTTGKAPVGSVVSVPSHSSASSDKYAALAELDSVFSSAATSSNAYTPTSNASSSVFGTVPVGASAQTQPASSGPAPFGATPSTNPFVAATGPSAASSTNPFQTNARGATAATFGTASMSMPAGFGTPAQYSLPTSFSGSFQQPAFPAQAAFPQQTAFSQQPNGAGFATFGQTKPVVTPFGQVAAAGVSSNPFMTGAPTGQLPTGSSSTNPFL
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
69PhosphorylationPHRVKSISMTTFTQQ
CCCCCEEEEEECHHH		19.7129899451
71PhosphorylationRVKSISMTTFTQQEI
CCCEEEEEECHHHHH		16.3929899451
72PhosphorylationVKSISMTTFTQQEIE
CCEEEEEECHHHHHH		18.9529899451
114UbiquitinationFRDPQKVKEFLQEKY
CCCHHHHHHHHHHHH		50.1922790023
138PhosphorylationEQAKVVASVHASISG
HHCCEEEEEEEEECC		11.6523984901
138O-linked_GlycosylationEQAKVVASVHASISG
HHCCEEEEEEEEECC		11.6530059200
142PhosphorylationVVASVHASISGSSAS
EEEEEEEEECCCCCC		11.4726643407
144PhosphorylationASVHASISGSSASST
EEEEEEECCCCCCCC		30.0826643407
146O-linked_GlycosylationVHASISGSSASSTSS
EEEEECCCCCCCCCC		18.8830059200
146PhosphorylationVHASISGSSASSTSS
EEEEECCCCCCCCCC		18.8823984901
147PhosphorylationHASISGSSASSTSST
EEEECCCCCCCCCCC		35.3825266776
149PhosphorylationSISGSSASSTSSTPE
EECCCCCCCCCCCCC		35.7826643407
150PhosphorylationISGSSASSTSSTPEV
ECCCCCCCCCCCCCC		31.8326643407
151PhosphorylationSGSSASSTSSTPEVK
CCCCCCCCCCCCCCH		24.9726643407
152PhosphorylationGSSASSTSSTPEVKP
CCCCCCCCCCCCCHH		33.8826643407
153PhosphorylationSSASSTSSTPEVKPL
CCCCCCCCCCCCHHH		48.3326643407
154PhosphorylationSASSTSSTPEVKPLK
CCCCCCCCCCCHHHH		24.2026643407
162 (in isoform 1)Phosphorylation-36.1924719451
162PhosphorylationPEVKPLKSLLGESAP
CCCHHHHHHHCCCCC		36.1925521595
167 (in isoform 1)Phosphorylation-37.4424719451
167PhosphorylationLKSLLGESAPALHLN
HHHHHCCCCCCEECC		37.4427742792
175AcetylationAPALHLNKGTPSQSP
CCCEECCCCCCCCCC		71.2123236377
175UbiquitinationAPALHLNKGTPSQSP
CCCEECCCCCCCCCC		71.2122790023
177PhosphorylationALHLNKGTPSQSPVV
CEECCCCCCCCCCCC		22.7527087446
177 (in isoform 1)Phosphorylation-22.7524719451
179PhosphorylationHLNKGTPSQSPVVGR
ECCCCCCCCCCCCCC		43.0325521595
179 (in isoform 1)Phosphorylation-43.0324719451
181PhosphorylationNKGTPSQSPVVGRSQ
CCCCCCCCCCCCCCC		24.8127087446
187PhosphorylationQSPVVGRSQGQQQEK
CCCCCCCCCCCHHHH		32.5023375375
291O-linked_GlycosylationHFDNFPKSSSADFGT
CCCCCCCCCCCCCCC		29.7530059200
291PhosphorylationHFDNFPKSSSADFGT
CCCCCCCCCCCCCCC		29.7526160508
292PhosphorylationFDNFPKSSSADFGTF
CCCCCCCCCCCCCCC		35.3526160508
293PhosphorylationDNFPKSSSADFGTFS
CCCCCCCCCCCCCCC		38.6627742792
298O-linked_GlycosylationSSSADFGTFSTSQSH
CCCCCCCCCCCCCCC		17.8830059200
298PhosphorylationSSSADFGTFSTSQSH
CCCCCCCCCCCCCCC		17.8827742792
300O-linked_GlycosylationSADFGTFSTSQSHQT
CCCCCCCCCCCCCCC		27.3030059200
300PhosphorylationSADFGTFSTSQSHQT
CCCCCCCCCCCCCCC		27.3027742792
301PhosphorylationADFGTFSTSQSHQTA
CCCCCCCCCCCCCCH		26.9627742792
302O-linked_GlycosylationDFGTFSTSQSHQTAS
CCCCCCCCCCCCCHH		28.6130059200
304O-linked_GlycosylationGTFSTSQSHQTASTV
CCCCCCCCCCCHHHE		19.8230059200
318MalonylationVSKVSTNKAGLQTAD
EEEHHCCCHHCCHHH		43.8726320211
323PhosphorylationTNKAGLQTADKYAAL
CCCHHCCHHHHHHHH		41.7022499769
327PhosphorylationGLQTADKYAALANLD
HCCHHHHHHHHHCCC		9.5426824392
338PhosphorylationANLDNIFSAGQGGDQ
HCCCCCCCCCCCCCC		27.9123984901
347PhosphorylationGQGGDQGSGFGTTGK
CCCCCCCCCCCCCCC		25.8923984901
351PhosphorylationDQGSGFGTTGKAPVG
CCCCCCCCCCCCCCC		30.0723984901
352PhosphorylationQGSGFGTTGKAPVGS
CCCCCCCCCCCCCCC		36.7423984901
359PhosphorylationTGKAPVGSVVSVPSH
CCCCCCCCEEECCCC		21.4126643407
362O-linked_GlycosylationAPVGSVVSVPSHSSA
CCCCCEEECCCCCCC		26.5930059200
362PhosphorylationAPVGSVVSVPSHSSA
CCCCCEEECCCCCCC		26.5927087446
365PhosphorylationGSVVSVPSHSSASSD
CCEEECCCCCCCCCH		33.5726643407
367O-linked_GlycosylationVVSVPSHSSASSDKY
EEECCCCCCCCCHHH		31.7530059200
367PhosphorylationVVSVPSHSSASSDKY
EEECCCCCCCCCHHH		31.7526643407
368PhosphorylationVSVPSHSSASSDKYA
EECCCCCCCCCHHHH		27.0926643407
370PhosphorylationVPSHSSASSDKYAAL
CCCCCCCCCHHHHHH		40.8026643407
371PhosphorylationPSHSSASSDKYAALA
CCCCCCCCHHHHHHH		37.5329899451
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 AGFG1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AGFG1_MOUSE !!
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 AGFG1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EPS15_MOUSEEps15physical
9303539
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AGFG1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177 AND SER-181, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-177; SER-179 ANDSER-181, AND MASS SPECTROMETRY.

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