AGAP1_HUMAN - dbPTM
AGAP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AGAP1_HUMAN
UniProt AC Q9UPQ3
Protein Name Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 1
Gene Name AGAP1
Organism Homo sapiens (Human).
Sequence Length 857
Subcellular Localization Cytoplasm . Associates with the endocytic compartment.
Protein Description GTPase-activating protein for ARF1 and, to a lesser extent, ARF5. Directly and specifically regulates the adapter protein 3 (AP-3)-dependent trafficking of proteins in the endosomal-lysosomal system..
Protein Sequence MNYQQQLANSAAIRAEIQRFESVHPNIYSIYELLERVEEPVLQNQIREHVIAIEDAFVNSQEWTLSRSVPELKVGIVGNLASGKSALVHRYLTGTYVQEESPEGGRFKKEIVVDGQSYLLLIRDEGGPPEAQFAMWVDAVIFVFSLEDEISFQTVYHYYSRMANYRNTSEIPLVLVGTQDAISSANPRVIDDARARKLSNDLKRCTYYETCATYGLNVERVFQDVAQKIVATRKKQQLSIGPCKSLPNSPSHSSVCSAQVSAVHISQTSNGGGSLSDYSSSVPSTPSTSQKELRIDVPPTANTPTPVRKQSKRRSNLFTSRKGSDPDKEKKGLESRADSIGSGRAIPIKQGMLLKRSGKSLNKEWKKKYVTLCDNGVLTYHPSLHDYMQNVHGKEIDLLRTTVKVPGKRPPRATSACAPISSPKTNGLSKDMSSLHISPNSGNVTSASGSQMASGISLVSFNSRPDGMHQRSYSVSSADQWSEATVIANSAISSDTGLGDSVCSSPSISSTTSPKLDPPPSPHANRKKHRRKKSTSNFKADGLSGTAEEQEENFEFIIVSLTGQTWHFEATTYEERDAWVQAIESQILASLQSCESSKNKSRLTSQSEAMALQSIRNMRGNSHCVDCETQNPNWASLNLGALMCIECSGIHRNLGTHLSRVRSLDLDDWPVELIKVMSSIGNELANSVWEESSQGRTKPSVDSTREEKERWIRAKYEQKLFLAPLPCTELSLGQHLLRATADEDLRTAILLLAHGSRDEVNETCGEGDGRTALHLACRKGNVVLAQLLIWYGVDVTARDAHGNTALAYARQASSQECIDVLLQYGCPDERFVLMATPNLSRRNNNRNNSSGRVPTII
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
1Acetylation-------MNYQQQLA
-------CCHHHHHH		10.7222814378
3Phosphorylation-----MNYQQQLANS
-----CCHHHHHHHH		13.34-
10PhosphorylationYQQQLANSAAIRAEI
HHHHHHHHHHHHHHH		17.3030622161
60PhosphorylationIEDAFVNSQEWTLSR
EEHHHCCCCHHHHCC		24.9527732954
64PhosphorylationFVNSQEWTLSRSVPE
HCCCCHHHHCCCCCC		17.6928111955
66PhosphorylationNSQEWTLSRSVPELK
CCCHHHHCCCCCCCE		18.3528111955
91PhosphorylationKSALVHRYLTGTYVQ
CCHHHHHHHHCCEEE		8.1720068231
93PhosphorylationALVHRYLTGTYVQEE
HHHHHHHHCCEEEEE		20.6720068231
95PhosphorylationVHRYLTGTYVQEESP
HHHHHHCCEEEEECC		18.4520068231
96PhosphorylationHRYLTGTYVQEESPE
HHHHHCCEEEEECCC		11.0720068231
101PhosphorylationGTYVQEESPEGGRFK
CCEEEEECCCCCCCE		27.7421815630
232PhosphorylationVAQKIVATRKKQQLS
HHHHHHHHHCCCCCC		31.93-
300PhosphorylationLRIDVPPTANTPTPV
ECCCCCCCCCCCCCC		26.8629255136
303PhosphorylationDVPPTANTPTPVRKQ
CCCCCCCCCCCCCCC		26.5229255136
305PhosphorylationPPTANTPTPVRKQSK
CCCCCCCCCCCCCCH		32.1729255136
311PhosphorylationPTPVRKQSKRRSNLF
CCCCCCCCHHHHCCC		31.0323882029
315PhosphorylationRKQSKRRSNLFTSRK
CCCCHHHHCCCCCCC		41.7530576142
320PhosphorylationRRSNLFTSRKGSDPD
HHHCCCCCCCCCCCH		25.35-
335PhosphorylationKEKKGLESRADSIGS
HHHHCHHHHHHHCCC		37.5029514088
339PhosphorylationGLESRADSIGSGRAI
CHHHHHHHCCCCCCE		28.0625159151
342PhosphorylationSRADSIGSGRAIPIK
HHHHHCCCCCCEECH		24.3629514088
369PhosphorylationNKEWKKKYVTLCDNG
CHHHHHHEEEECCCC		13.93-
380PhosphorylationCDNGVLTYHPSLHDY
CCCCEEEECHHHHHH		13.94-
387PhosphorylationYHPSLHDYMQNVHGK
ECHHHHHHHHHCCCC		7.00-
404UbiquitinationDLLRTTVKVPGKRPP
EEEEEEEECCCCCCC		40.39-
414PhosphorylationGKRPPRATSACAPIS
CCCCCCCCCCCCCCC		20.3829396449
415PhosphorylationKRPPRATSACAPISS
CCCCCCCCCCCCCCC		21.9925850435
421PhosphorylationTSACAPISSPKTNGL
CCCCCCCCCCCCCCC		39.2630266825
422PhosphorylationSACAPISSPKTNGLS
CCCCCCCCCCCCCCC		31.0025159151
433 (in isoform 2)Phosphorylation-39.6229978859
434 (in isoform 2)Phosphorylation-19.8229978859
441 (in isoform 2)Phosphorylation-34.8229978859
443 (in isoform 2)Phosphorylation-33.4429978859
448 (in isoform 2)Phosphorylation-38.4529978859
451 (in isoform 2)Phosphorylation-34.6829978859
452 (in isoform 2)Phosphorylation-3.2529978859
454 (in isoform 2)Phosphorylation-31.1729978859
456 (in isoform 2)Phosphorylation-2.3929978859
457 (in isoform 2)Phosphorylation-26.6629978859
458 (in isoform 2)Phosphorylation-3.3629978859
459 (in isoform 2)Phosphorylation-4.9829978859
460 (in isoform 2)Phosphorylation-24.8128387310
505PhosphorylationLGDSVCSSPSISSTT
CCCCCCCCCCCCCCC		19.96-
507PhosphorylationDSVCSSPSISSTTSP
CCCCCCCCCCCCCCC		36.73-
513PhosphorylationPSISSTTSPKLDPPP
CCCCCCCCCCCCCCC		21.81-
521PhosphorylationPKLDPPPSPHANRKK
CCCCCCCCCCCCCHH		34.7829255136
534PhosphorylationKKHRRKKSTSNFKAD
HHHCCCCCCCCCCCC		39.8524719451
535PhosphorylationKHRRKKSTSNFKADG
HHCCCCCCCCCCCCC		36.2523312004
601PhosphorylationCESSKNKSRLTSQSE
HHHCCCHHHCCCHHH		41.7523090842
604PhosphorylationSKNKSRLTSQSEAMA
CCCHHHCCCHHHHHH		24.4929255136
605PhosphorylationKNKSRLTSQSEAMAL
CCHHHCCCHHHHHHH		35.9829255136
607PhosphorylationKSRLTSQSEAMALQS
HHHCCCHHHHHHHHH		27.3929255136
614PhosphorylationSEAMALQSIRNMRGN
HHHHHHHHHHHHCCC		25.1024117733
663PhosphorylationTHLSRVRSLDLDDWP
HHHHHCCCCCCCCCC		24.31-
836PhosphorylationERFVLMATPNLSRRN
HHEEEEECCCCHHCC		9.9519664994
840PhosphorylationLMATPNLSRRNNNRN
EEECCCCHHCCCCCC		35.5222617229
849PhosphorylationRNNNRNNSSGRVPTI
CCCCCCCCCCCCCCC		37.4122617229
850PhosphorylationNNNRNNSSGRVPTII
CCCCCCCCCCCCCCC		32.5130243723
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 AGAP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AGAP1_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 AGAP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
SQSTM_HUMANSQSTM1physical
9564850
RHOA_HUMANRHOAphysical
22453919
ARF1_HUMANARF1physical
22453919
ARF6_HUMANARF6physical
22453919
RAC1_HUMANRAC1physical
22453919
CDC42_HUMANCDC42physical
22453919
KI13B_HUMANKIF13Bphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
LRFN1_HUMANLRFN1physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
LIMA1_HUMANLIMA1physical
27173435
MAGI1_HUMANMAGI1physical
27173435
TESK2_HUMANTESK2physical
27173435
DCLK1_HUMANDCLK1physical
27173435
SRS12_HUMANSRSF12physical
27173435
SYDE1_HUMANSYDE1physical
27173435
F110B_HUMANFAM110Bphysical
27173435
F110A_HUMANFAM110Aphysical
27173435
TBC25_HUMANTBC1D25physical
27173435
HDAC4_HUMANHDAC4physical
27173435
NADK_HUMANNADKphysical
27173435
CBY1_HUMANCBY1physical
27173435
CING_HUMANCGNphysical
27173435
NGAP_HUMANRASAL2physical
27173435
MELK_HUMANMELKphysical
27173435
AFAD_HUMANMLLT4physical
27173435
KIF1C_HUMANKIF1Cphysical
27173435
SH3B4_HUMANSH3BP4physical
27173435
NAV1_HUMANNAV1physical
27173435
ARF1_HUMANARF1physical
16332543
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 AGAP1_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-315, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-836, AND MASSSPECTROMETRY.

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