AP1G1_HUMAN - dbPTM
AP1G1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP1G1_HUMAN
UniProt AC O43747
Protein Name AP-1 complex subunit gamma-1
Gene Name AP1G1
Organism Homo sapiens (Human).
Sequence Length 822
Subcellular Localization Golgi apparatus . Cytoplasmic vesicle, clathrin-coated vesicle membrane
Peripheral membrane protein
Cytoplasmic side . Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex.
Protein Description Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules..
Protein Sequence MPAPIRLRELIRTIRTARTQAEEREMIQKECAAIRSSFREEDNTYRCRNVAKLLYMHMLGYPAHFGQLECLKLIASQKFTDKRIGYLGAMLLLDERQDVHLLMTNCIKNDLNHSTQFVQGLALCTLGCMGSSEMCRDLAGEVEKLLKTSNSYLRKKAALCAVHVIRKVPELMEMFLPATKNLLNEKNHGVLHTSVVLLTEMCERSPDMLAHFRKLVPQLVRILKNLIMSGYSPEHDVSGISDPFLQVRILRLLRILGRNDDDSSEAMNDILAQVATNTETSKNVGNAILYETVLTIMDIKSESGLRVLAINILGRFLLNNDKNIRYVALTSLLKTVQTDHNAVQRHRSTIVDCLKDLDVSIKRRAMELSFALVNGNNIRGMMKELLYFLDSCEPEFKADCASGIFLAAEKYAPSKRWHIDTIMRVLTTAGSYVRDDAVPNLIQLITNSVEMHAYTVQRLYKAILGDYSQQPLVQVAAWCIGEYGDLLVSGQCEEEEPIQVTEDEVLDILESVLISNMSTSVTRGYALTAIMKLSTRFTCTVNRIKKVVSIYGSSIDVELQQRAVEYNALFKKYDHMRSALLERMPVMEKVTTNGPTEIVQTNGETEPAPLETKPPPSGPQPTSQANDLLDLLGGNDITPVIPTAPTSKPSSAGGELLDLLGDINLTGAPAAAPAPASVPQISQPPFLLDGLSSQPLFNDIAAGIPSITAYSKNGLKIEFTFERSNTNPSVTVITIQASNSTELDMTDFVFQAAVPKTFQLQLLSPSSSIVPAFNTGTITQVIKVLNPQKQQLRMRIKLTYNHKGSAMQDLAEVNNFPPQSWQ
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
29UbiquitinationEEREMIQKECAAIRS
HHHHHHHHHHHHHHH		43.78-
29AcetylationEEREMIQKECAAIRS
HHHHHHHHHHHHHHH		43.7823236377
37PhosphorylationECAAIRSSFREEDNT
HHHHHHHHHCCCCCC		20.6217081983
45PhosphorylationFREEDNTYRCRNVAK
HCCCCCCHHHHHHHH		17.6125839225
55PhosphorylationRNVAKLLYMHMLGYP
HHHHHHHHHHHHCCC		8.7318083107
61PhosphorylationLYMHMLGYPAHFGQL
HHHHHHCCCCHHCHH		8.0318083107
76PhosphorylationECLKLIASQKFTDKR
HHHHHHHCCCCCCCC		27.2326437602
78AcetylationLKLIASQKFTDKRIG
HHHHHCCCCCCCCHH		47.9719608861
782-HydroxyisobutyrylationLKLIASQKFTDKRIG
HHHHHCCCCCCCCHH		47.97-
78UbiquitinationLKLIASQKFTDKRIG
HHHHHCCCCCCCCHH		47.9719608861
80PhosphorylationLIASQKFTDKRIGYL
HHHCCCCCCCCHHHH		47.8826437602
104PhosphorylationQDVHLLMTNCIKNDL
HHHHHHHHHHHHCCC		27.2329083192
144UbiquitinationDLAGEVEKLLKTSNS
HHHHHHHHHHHHCCH		65.3819608861
144AcetylationDLAGEVEKLLKTSNS
HHHHHHHHHHHHCCH		65.3819608861
147MalonylationGEVEKLLKTSNSYLR
HHHHHHHHHCCHHHH		61.4126320211
147UbiquitinationGEVEKLLKTSNSYLR
HHHHHHHHHCCHHHH		61.41-
147AcetylationGEVEKLLKTSNSYLR
HHHHHHHHHCCHHHH		61.4125953088
148PhosphorylationEVEKLLKTSNSYLRK
HHHHHHHHCCHHHHH		32.8623403867
149PhosphorylationVEKLLKTSNSYLRKK
HHHHHHHCCHHHHHH		23.3823403867
151PhosphorylationKLLKTSNSYLRKKAA
HHHHHCCHHHHHHHH		25.8823403867
152PhosphorylationLLKTSNSYLRKKAAL
HHHHCCHHHHHHHHH		18.1223403867
156UbiquitinationSNSYLRKKAALCAVH
CCHHHHHHHHHHHHH		32.24-
1562-HydroxyisobutyrylationSNSYLRKKAALCAVH
CCHHHHHHHHHHHHH		32.24-
167UbiquitinationCAVHVIRKVPELMEM
HHHHHHHHCHHHHHH		51.52-
180UbiquitinationEMFLPATKNLLNEKN
HHHHHHHHHHHHHCC		47.94-
214MalonylationDMLAHFRKLVPQLVR
HHHHHHHHHHHHHHH		53.5526320211
228SulfoxidationRILKNLIMSGYSPEH
HHHHHHHHCCCCCCC		2.6131801345
229PhosphorylationILKNLIMSGYSPEHD
HHHHHHHCCCCCCCC		27.8224076635
231PhosphorylationKNLIMSGYSPEHDVS
HHHHHCCCCCCCCCC		17.4724076635
232PhosphorylationNLIMSGYSPEHDVSG
HHHHCCCCCCCCCCC		27.6024076635
238PhosphorylationYSPEHDVSGISDPFL
CCCCCCCCCCCCHHH		36.1424076635
263PhosphorylationLGRNDDDSSEAMNDI
HCCCCCCCHHHHHHH		36.7521406692
264PhosphorylationGRNDDDSSEAMNDIL
CCCCCCCHHHHHHHH		36.0521406692
276PhosphorylationDILAQVATNTETSKN
HHHHHHHHCCCCCCC		43.7621406692
278PhosphorylationLAQVATNTETSKNVG
HHHHHHCCCCCCCHH		35.9621406692
280PhosphorylationQVATNTETSKNVGNA
HHHHCCCCCCCHHHH		42.8521406692
281PhosphorylationVATNTETSKNVGNAI
HHHCCCCCCCHHHHH		18.9221406692
322UbiquitinationRFLLNNDKNIRYVAL
HHHHCCCCCHHHHHH		57.29-
322AcetylationRFLLNNDKNIRYVAL
HHHHCCCCCHHHHHH		57.2925953088
326PhosphorylationNNDKNIRYVALTSLL
CCCCCHHHHHHHHHH		6.0528152594
331PhosphorylationIRYVALTSLLKTVQT
HHHHHHHHHHHHHHC		32.3324719451
348PhosphorylationNAVQRHRSTIVDCLK
HHHHHHHHHHHHHHH		19.1627273156
355UbiquitinationSTIVDCLKDLDVSIK
HHHHHHHHCCCHHHH		63.68-
362UbiquitinationKDLDVSIKRRAMELS
HCCCHHHHHHHHHHH		28.4621906983
3622-HydroxyisobutyrylationKDLDVSIKRRAMELS
HCCCHHHHHHHHHHH		28.46-
392GlutathionylationLLYFLDSCEPEFKAD
HHHHHHHCCHHHHHH		11.4622555962
525PhosphorylationSTSVTRGYALTAIMK
CCHHHHHHHHHHHHH		8.647386487
546UbiquitinationCTVNRIKKVVSIYGS
EEHHHHHHHHEEECC		45.5621906983
549PhosphorylationNRIKKVVSIYGSSID
HHHHHHHEEECCCCC		17.0620860994
566PhosphorylationLQQRAVEYNALFKKY
HHHHHHHHHHHHHHH		10.1128796482
573PhosphorylationYNALFKKYDHMRSAL
HHHHHHHHHHHHHHH		16.2121253578
757PhosphorylationFQAAVPKTFQLQLLS
HHHCCCCEEEEEECC		15.5628450419
764PhosphorylationTFQLQLLSPSSSIVP
EEEEEECCCCCCCCC		31.1829496963
766PhosphorylationQLQLLSPSSSIVPAF
EEEECCCCCCCCCCC		33.0829523821
767PhosphorylationLQLLSPSSSIVPAFN
EEECCCCCCCCCCCC		27.7128450419
768PhosphorylationQLLSPSSSIVPAFNT
EECCCCCCCCCCCCC		31.7628450419
770PhosphorylationLSPSSSIVPAFNTGT
CCCCCCCCCCCCCCH		2.7824719451
771PhosphorylationSPSSSIVPAFNTGTI
CCCCCCCCCCCCCHH		29.4827251275
789UbiquitinationIKVLNPQKQQLRMRI
HHHHCHHHHHHHEEE		41.07-
797AcetylationQQLRMRIKLTYNHKG
HHHHEEEEEEECCCC		25.1425953088
799PhosphorylationLRMRIKLTYNHKGSA
HHEEEEEEECCCCCH		19.7824719451
800PhosphorylationRMRIKLTYNHKGSAM
HEEEEEEECCCCCHH		26.2146164915
802PhosphorylationRIKLTYNHKGSAMQD
EEEEEECCCCCHHHH		25.9924719451
803PhosphorylationIKLTYNHKGSAMQDL
EEEEECCCCCHHHHH		51.4224719451
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 AP1G1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP1G1_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 AP1G1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NECP1_HUMANNECAP1physical
14665628
NECP2_HUMANNECAP2physical
14665628
ARF1_HUMANARF1physical
11926829
SYNRG_HUMANSYNRGphysical
12042876
RABE1_HUMANRABEP1physical
12042876
SYNRG_HUMANSYNRGphysical
10814529
RABE1_HUMANRABEP1physical
12505986
AP1M2_HUMANAP1M2physical
10535737
AP1M1_HUMANAP1M1physical
10535737
AP1S1_HUMANAP1S1physical
10535737
AP1B1_HUMANAP1B1physical
10535737
SYPH_HUMANSYPphysical
12498786
AP2M1_HUMANAP2M1physical
7593184
AP1B1_HUMANAP1B1physical
7593184
AP2S1_HUMANAP2S1physical
7593184
AP1M1_HUMANAP1M1physical
7593184
AP1S1_HUMANAP1S1physical
7593184
GAG_HV1H2gagphysical
17538020
JUN_HUMANJUNphysical
17538020
CLH1_HUMANCLTCphysical
11387476
RABE1_HUMANRABEP1physical
11387476
AP1M1_HUMANAP1M1physical
22939629
AP1S1_HUMANAP1S1physical
22939629
AP1S2_HUMANAP1S2physical
22939629
AP1M1_HUMANAP1M1physical
10747088
AP2M1_HUMANAP2M1physical
10747088
SYNRG_HUMANSYNRGphysical
10747088
AP1S1_HUMANAP1S1physical
10747088
AP1B1_HUMANAP1B1physical
10747088
MAP1A_HUMANMAP1Aphysical
10747088
RABE1_HUMANRABEP1physical
10747088
NPM3_HUMANNPM3physical
22863883
OSB11_HUMANOSBPL11physical
22863883
PRRC1_HUMANPRRC1physical
22863883
CIP4_HUMANTRIP10physical
22863883
AP1S2_HUMANAP1S2physical
25416956
UBL7_HUMANUBL7physical
25416956
CORO7_HUMANCORO7physical
16905771
AP1B1_HUMANAP1B1physical
26344197
AP2B1_HUMANAP2B1physical
26344197
DCPS_HUMANDCPSphysical
26344197
GGA1_HUMANGGA1physical
14973137
RABE1_HUMANRABEP1physical
14973137
CLH1_HUMANCLTCphysical
21411634
EPS15_HUMANEPS15physical
18524853
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 AP1G1_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-144, AND MASS SPECTROMETRY.

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