GGA1_HUMAN - dbPTM
GGA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GGA1_HUMAN
UniProt AC Q9UJY5
Protein Name ADP-ribosylation factor-binding protein GGA1
Gene Name GGA1
Organism Homo sapiens (Human).
Sequence Length 639
Subcellular Localization Golgi apparatus, trans-Golgi network membrane
Peripheral membrane protein. Endosome membrane
Peripheral membrane protein.
Protein Description Plays a role in protein sorting and trafficking between the trans-Golgi network (TGN) and endosomes. Mediates the ARF-dependent recruitment of clathrin to the TGN and binds ubiquitinated proteins and membrane cargo molecules with a cytosolic acidic cluster-dileucine (AC-LL) motif..
Protein Sequence MEPAMEPETLEARINRATNPLNKELDWASINGFCEQLNEDFEGPPLATRLLAHKIQSPQEWEAIQALTVLETCMKSCGKRFHDEVGKFRFLNELIKVVSPKYLGSRTSEKVKNKILELLYSWTVGLPEEVKIAEAYQMLKKQGIVKSDPKLPDDTTFPLPPPRPKNVIFEDEEKSKMLARLLKSSHPEDLRAANKLIKEMVQEDQKRMEKISKRVNAIEEVNNNVKLLTEMVMSHSQGGAAAGSSEDLMKELYQRCERMRPTLFRLASDTEDNDEALAEILQANDNLTQVINLYKQLVRGEEVNGDATAGSIPGSTSALLDLSGLDLPPAGTTYPAMPTRPGEQASPEQPSASVSLLDDELMSLGLSDPTPPSGPSLDGTGWNSFQSSDATEPPAPALAQAPSMESRPPAQTSLPASSGLDDLDLLGKTLLQQSLPPESQQVRWEKQQPTPRLTLRDLQNKSSSCSSPSSSATSLLHTVSPEPPRPPQQPVPTELSLASITVPLESIKPSNILPVTVYDQHGFRILFHFARDPLPGRSDVLVVVVSMLSTAPQPIRNIVFQSAVPKVMKVKLQPPSGTELPAFNPIVHPSAITQVLLLANPQKEKVRLRYKLTFTMGDQTYNEMGDVDQFPPPETWGSL
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-------MEPAMEPE
-------CCCCCCHH
14.5422814378
15UbiquitinationETLEARINRATNPLN
HHHHHHHHHHCCCCH
23.2121963094
23UbiquitinationRATNPLNKELDWASI
HHCCCCHHCCCHHHH
68.30-
23UbiquitinationRATNPLNKELDWASI
HHCCCCHHCCCHHHH
68.3023000965
28UbiquitinationLNKELDWASINGFCE
CHHCCCHHHHHHHHH
10.5321890473
28UbiquitinationLNKELDWASINGFCE
CHHCCCHHHHHHHHH
10.5323000965
46UbiquitinationEDFEGPPLATRLLAH
CCCCCCHHHHHHHHH
9.5225015289
54 (in isoform 2)Ubiquitination-36.5121890473
54UbiquitinationATRLLAHKIQSPQEW
HHHHHHHHCCCHHHH
36.51-
57 (in isoform 6)Phosphorylation-31.8324043423
57 (in isoform 5)Phosphorylation-31.8324043423
68 (in isoform 6)Phosphorylation-26.5124043423
68 (in isoform 5)Phosphorylation-26.5124043423
69UbiquitinationEAIQALTVLETCMKS
HHHHHHHHHHHHHHH
4.7724816145
73GlutathionylationALTVLETCMKSCGKR
HHHHHHHHHHHCCHH
2.0622555962
88UbiquitinationFHDEVGKFRFLNELI
HHHHHHHHHHHHHHH
5.7023000965
92UbiquitinationVGKFRFLNELIKVVS
HHHHHHHHHHHHHHC
39.0421890473
92UbiquitinationVGKFRFLNELIKVVS
HHHHHHHHHHHHHHC
39.0422817900
93UbiquitinationGKFRFLNELIKVVSP
HHHHHHHHHHHHHCH
54.7621890473
96UbiquitinationRFLNELIKVVSPKYL
HHHHHHHHHHCHHHC
49.5623000965
99PhosphorylationNELIKVVSPKYLGSR
HHHHHHHCHHHCCCC
20.75-
101UbiquitinationLIKVVSPKYLGSRTS
HHHHHCHHHCCCCCC
45.6723000965
101UbiquitinationLIKVVSPKYLGSRTS
HHHHHCHHHCCCCCC
45.6721890473
101 (in isoform 1)Ubiquitination-45.6721890473
101MalonylationLIKVVSPKYLGSRTS
HHHHHCHHHCCCCCC
45.6730639696
101MalonylationLIKVVSPKYLGSRTS
HHHHHCHHHCCCCCC
45.6726320211
101AcetylationLIKVVSPKYLGSRTS
HHHHHCHHHCCCCCC
45.6725953088
105UbiquitinationVSPKYLGSRTSEKVK
HCHHHCCCCCCHHHH
29.7723000965
105PhosphorylationVSPKYLGSRTSEKVK
HCHHHCCCCCCHHHH
29.7722798277
108PhosphorylationKYLGSRTSEKVKNKI
HHCCCCCCHHHHHHH
34.0222798277
110UbiquitinationLGSRTSEKVKNKILE
CCCCCCHHHHHHHHH
59.2723000965
113UbiquitinationRTSEKVKNKILELLY
CCCHHHHHHHHHHHH
39.3223000965
118UbiquitinationVKNKILELLYSWTVG
HHHHHHHHHHHHHCC
4.9523000965
122UbiquitinationILELLYSWTVGLPEE
HHHHHHHHHCCCCHH
4.9929967540
125UbiquitinationLLYSWTVGLPEEVKI
HHHHHHCCCCHHHHH
28.3032015554
132 (in isoform 2)Ubiquitination-5.1721890473
133UbiquitinationLPEEVKIAEAYQMLK
CCHHHHHHHHHHHHH
6.9424816145
140AcetylationAEAYQMLKKQGIVKS
HHHHHHHHHCCCCCC
37.3925953088
141AcetylationEAYQMLKKQGIVKSD
HHHHHHHHCCCCCCC
50.2025953088
141 (in isoform 2)Ubiquitination-50.2021890473
141UbiquitinationEAYQMLKKQGIVKSD
HHHHHHHHCCCCCCC
50.20-
147PhosphorylationKKQGIVKSDPKLPDD
HHCCCCCCCCCCCCC
48.5328348404
155PhosphorylationDPKLPDDTTFPLPPP
CCCCCCCCCCCCCCC
37.4028348404
156PhosphorylationPKLPDDTTFPLPPPR
CCCCCCCCCCCCCCC
30.1920068231
157UbiquitinationKLPDDTTFPLPPPRP
CCCCCCCCCCCCCCC
6.7621890473
158UbiquitinationLPDDTTFPLPPPRPK
CCCCCCCCCCCCCCC
41.69-
165 (in isoform 2)Ubiquitination-66.1921890473
165UbiquitinationPLPPPRPKNVIFEDE
CCCCCCCCCCCCCCH
66.1921890473
165UbiquitinationPLPPPRPKNVIFEDE
CCCCCCCCCCCCCCH
66.1922817900
165 (in isoform 1)Ubiquitination-66.1921890473
174 (in isoform 1)Ubiquitination-54.0221890473
174UbiquitinationVIFEDEEKSKMLARL
CCCCCHHHHHHHHHH
54.0221906983
175UbiquitinationIFEDEEKSKMLARLL
CCCCHHHHHHHHHHH
26.9525015289
182UbiquitinationSKMLARLLKSSHPED
HHHHHHHHHCCCHHH
4.1622817900
183UbiquitinationKMLARLLKSSHPEDL
HHHHHHHHCCCHHHH
55.2833845483
183MethylationKMLARLLKSSHPEDL
HHHHHHHHCCCHHHH
55.28-
184PhosphorylationMLARLLKSSHPEDLR
HHHHHHHCCCHHHHH
33.5730108239
185PhosphorylationLARLLKSSHPEDLRA
HHHHHHCCCHHHHHH
41.2830108239
191UbiquitinationSSHPEDLRAANKLIK
CCCHHHHHHHHHHHH
43.9333845483
191UbiquitinationSSHPEDLRAANKLIK
CCCHHHHHHHHHHHH
43.9321890473
192UbiquitinationSHPEDLRAANKLIKE
CCHHHHHHHHHHHHH
23.7625015289
195AcetylationEDLRAANKLIKEMVQ
HHHHHHHHHHHHHHH
47.0325953088
195UbiquitinationEDLRAANKLIKEMVQ
HHHHHHHHHHHHHHH
47.0329967540
198UbiquitinationRAANKLIKEMVQEDQ
HHHHHHHHHHHHHHH
50.6333845483
198 (in isoform 1)Ubiquitination-50.6321890473
200UbiquitinationANKLIKEMVQEDQKR
HHHHHHHHHHHHHHH
2.9933845483
200UbiquitinationANKLIKEMVQEDQKR
HHHHHHHHHHHHHHH
2.99-
206UbiquitinationEMVQEDQKRMEKISK
HHHHHHHHHHHHHHH
67.0624816145
215UbiquitinationMEKISKRVNAIEEVN
HHHHHHHHHHHHHHH
6.9721890473
215UbiquitinationMEKISKRVNAIEEVN
HHHHHHHHHHHHHHH
6.9733845483
223UbiquitinationNAIEEVNNNVKLLTE
HHHHHHHHHHHHHHH
60.9024816145
223UbiquitinationNAIEEVNNNVKLLTE
HHHHHHHHHHHHHHH
60.90-
236PhosphorylationTEMVMSHSQGGAAAG
HHHHHHCCCCCCCCC
24.1817525332
244PhosphorylationQGGAAAGSSEDLMKE
CCCCCCCCHHHHHHH
26.3128348404
245PhosphorylationGGAAAGSSEDLMKEL
CCCCCCCHHHHHHHH
33.9228348404
262PhosphorylationRCERMRPTLFRLASD
HHHHHCHHHHHHHCC
28.32-
268PhosphorylationPTLFRLASDTEDNDE
HHHHHHHCCCCCCHH
50.0528348404
270PhosphorylationLFRLASDTEDNDEAL
HHHHHCCCCCCHHHH
42.6227273156
355PhosphorylationEQPSASVSLLDDELM
CCCCCEEEECCHHHH
22.2512060753
359UbiquitinationASVSLLDDELMSLGL
CEEEECCHHHHHCCC
51.3929967540
373UbiquitinationLSDPTPPSGPSLDGT
CCCCCCCCCCCCCCC
65.6229967540
412PhosphorylationESRPPAQTSLPASSG
CCCCCCCCCCCCCCC
34.0524275569
418PhosphorylationQTSLPASSGLDDLDL
CCCCCCCCCCCHHHH
45.5414702039
434PhosphorylationGKTLLQQSLPPESQQ
HHHHHHHCCCHHHHH
29.8628857561
446UbiquitinationSQQVRWEKQQPTPRL
HHHCHHHHCCCCCCE
47.4729967540
450PhosphorylationRWEKQQPTPRLTLRD
HHHHCCCCCCEEHHH
19.39-
463UbiquitinationRDLQNKSSSCSSPSS
HHHCCCCCCCCCCCH
36.65-
478PhosphorylationSATSLLHTVSPEPPR
HHHHHHHHCCCCCCC
23.7326074081
480PhosphorylationTSLLHTVSPEPPRPP
HHHHHHCCCCCCCCC
25.3826074081
493PhosphorylationPPQQPVPTELSLASI
CCCCCCCCEEEEEEE
50.2030243723
496PhosphorylationQPVPTELSLASITVP
CCCCCEEEEEEEEEE
18.6930243723
499PhosphorylationPTELSLASITVPLES
CCEEEEEEEEEEHHH
24.8830243723
501PhosphorylationELSLASITVPLESIK
EEEEEEEEEEHHHCC
17.3630243723
506PhosphorylationSITVPLESIKPSNIL
EEEEEHHHCCHHHEE
43.5330243723
546PhosphorylationDVLVVVVSMLSTAPQ
CEEEEEEECCCCCCC
11.4619276368
550PhosphorylationVVVSMLSTAPQPIRN
EEEECCCCCCCCHHH
38.0919276368

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
355SPhosphorylationKinaseCSNK2A1P68400
GPS
355SPhosphorylationKinaseCK2-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GGA1_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 GGA1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NECP2_HUMANNECAP2physical
14665628
ARF1_HUMANARF1physical
12636914
CLH1_HUMANCLTCphysical
11301005
SYNRG_HUMANSYNRGphysical
10814529
RABE1_HUMANRABEP1physical
12505986
RABX5_HUMANRABGEF1physical
12505986
BACE2_HUMANBACE2physical
12135764
ARF3_HUMANARF3physical
10749927
VPS18_HUMANVPS18physical
16996030
UBC_HUMANUBCphysical
14660606
RABX5_HUMANRABGEF1physical
15143060
ARF1_HUMANARF1physical
15143060
UBC_HUMANUBCphysical
15143060
TS101_HUMANTSG101physical
15143060
BACE1_HUMANBACE1physical
15466887
RABE1_HUMANRABEP1physical
15457209
RABE1_HUMANRABEP1physical
14636058
CCD91_HUMANCCDC91physical
12808037
MPRD_HUMANM6PRphysical
15044437
ADIPO_MOUSEAdipoqphysical
16407204
MPRI_HUMANIGF2Rphysical
11859376
SORT_HUMANSORT1physical
11859376
BACE1_HUMANBACE1physical
15117318
MPRI_HUMANIGF2Rphysical
15117318
CLH1_HUMANCLTCphysical
17344219
CLH1_HUMANCLTCphysical
17052248
CCD91_HUMANCCDC91physical
12858163
SYNRG_HUMANSYNRGphysical
12858163
BACE1_HUMANBACE1physical
15886016
ARF3_HUMANARF3physical
14690499
A4_HUMANAPPphysical
17151287
RABE1_HUMANRABEP1physical
16473621
SORT_HUMANSORT1physical
20015111
SORL_HUMANSORL1physical
20015111
GGA1_HUMANGGA1physical
17506864
SYNRG_HUMANSYNRGphysical
17506864
EPN4_HUMANCLINT1physical
17506864
RABE1_HUMANRABEP1physical
17506864
CLH1_HUMANCLTCphysical
17506864
GGA2_HUMANGGA2physical
14638859
GGA3_HUMANGGA3physical
14638859
LRP3_HUMANLRP3physical
11390366
SORT_HUMANSORT1physical
11390366
MPRI_HUMANIGF2Rphysical
11390366
MON2_YEASTMON2physical
18418388
MON2_HUMANMON2physical
18418388
ARF1_MOUSEArf1physical
12679809
MAP1A_HUMANMAP1Aphysical
10747088
RABE1_HUMANRABEP1physical
10747088
SYNRG_HUMANSYNRGphysical
10747088
RNF11_HUMANRNF11physical
25195858
ARF1_HUMANARF1physical
11950392
ARF3_HUMANARF3physical
11950392
ARF5_HUMANARF5physical
11950392
ARF6_HUMANARF6physical
11950392
CA216_HUMANC1orf216physical
25416956
UBC_HUMANUBCphysical
17494868
TOLIP_HUMANTOLLIPphysical
15047686
DHX15_HUMANDHX15physical
26344197
4EBP1_HUMANEIF4EBP1physical
26344197
GIPC1_HUMANGIPC1physical
26344197
LIX1L_HUMANLIX1Lphysical
26344197
RABEK_HUMANRABEPKphysical
26344197
SORL_HUMANSORL1physical
26053850
ARF6_HUMANARF6physical
21198641
ARF1_HUMANARF1physical
21198641
CEP72_HUMANCEP72physical
28514442
CLCN3_HUMANCLCN3physical
28514442
E2F5_HUMANE2F5physical
28514442
TFDP1_HUMANTFDP1physical
28514442
CEP44_HUMANCEP44physical
28514442
CCD91_HUMANCCDC91physical
28514442
RBGP1_HUMANRABGAP1physical
28514442
FP100_HUMANC17orf70physical
28514442
DTBP1_HUMANDTNBP1physical
28514442
LRP10_HUMANLRP10physical
28514442
MAP1S_HUMANMAP1Sphysical
28514442
RBG10_HUMANRABGAP1Lphysical
28514442
RBG1L_HUMANRABGAP1Lphysical
28514442
TMM9B_HUMANTMEM9Bphysical
28514442
EXOC4_HUMANEXOC4physical
28514442
CENPH_HUMANCENPHphysical
28514442
SNP47_HUMANSNAP47physical
27173435
ECHD1_HUMANECHDC1physical
27173435

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 GGA1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-236, AND MASSSPECTROMETRY.

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