GOPC_HUMAN - dbPTM
GOPC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GOPC_HUMAN
UniProt AC Q9HD26
Protein Name Golgi-associated PDZ and coiled-coil motif-containing protein
Gene Name GOPC
Organism Homo sapiens (Human).
Sequence Length 462
Subcellular Localization Cytoplasm. Golgi apparatus membrane
Peripheral membrane protein. Golgi apparatus, trans-Golgi network membrane
Peripheral membrane protein. Cell junction, synapse. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density. Cell projection
Protein Description Plays a role in intracellular protein trafficking and degradation. May regulate CFTR chloride currents and acid-induced ASIC3 currents by modulating cell surface expression of both channels. May also regulate the intracellular trafficking of the ADR1B receptor. May play a role in autophagy. Overexpression results in CFTR intracellular retention and degradation in the lysosomes..
Protein Sequence MSAGGPCPAAAGGGPGGASCSVGAPGGVSMFRWLEVLEKEFDKAFVDVDLLLGEIDPDQADITYEGRQKMTSLSSCFAQLCHKAQSVSQINHKLEAQLVDLKSELTETQAEKVVLEKEVHDQLLQLHSIQLQLHAKTGQSADSGTIKAKLSGPSVEELERELEANKKEKMKEAQLEAEVKLLRKENEALRRHIAVLQAEVYGARLAAKYLDKELAGRVQQIQLLGRDMKGPAHDKLWNQLEAEIHLHRHKTVIRACRGRNDLKRPMQAPPGHDQDSLKKSQGVGPIRKVLLLKEDHEGLGISITGGKEHGVPILISEIHPGQPADRCGGLHVGDAILAVNGVNLRDTKHKEAVTILSQQRGEIEFEVVYVAPEVDSDDENVEYEDESGHRYRLYLDELEGGGNPGASCKDTSGEIKVLQGFNKKAVTDTHENGDLGTASETPLDDGASKLDDLHTLYHKKSY
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
2Acetylation------MSAGGPCPA
------CCCCCCCCC
35.3019413330
2Phosphorylation------MSAGGPCPA
------CCCCCCCCC
35.3019413330
19PhosphorylationGGGPGGASCSVGAPG
CCCCCCCCCCCCCCC
15.3628348404
21PhosphorylationGPGGASCSVGAPGGV
CCCCCCCCCCCCCCC
22.5328348404
39UbiquitinationRWLEVLEKEFDKAFV
HHHHHHHHHHHHHHC
60.5629967540
86PhosphorylationQLCHKAQSVSQINHK
HHHHHHHCHHHHCHH
28.7025849741
88PhosphorylationCHKAQSVSQINHKLE
HHHHHCHHHHCHHHH
30.5030622161
93UbiquitinationSVSQINHKLEAQLVD
CHHHHCHHHHHHHCH
43.4632015554
93MalonylationSVSQINHKLEAQLVD
CHHHHCHHHHHHHCH
43.4626320211
93AcetylationSVSQINHKLEAQLVD
CHHHHCHHHHHHHCH
43.4620167786
102SumoylationEAQLVDLKSELTETQ
HHHHCHHHHHCCHHH
37.10-
102 (in isoform 3)Ubiquitination-37.1021906983
102 (in isoform 2)Ubiquitination-37.1021906983
102SumoylationEAQLVDLKSELTETQ
HHHHCHHHHHCCHHH
37.10-
102 (in isoform 1)Ubiquitination-37.1021906983
102UbiquitinationEAQLVDLKSELTETQ
HHHHCHHHHHCCHHH
37.1021906983
103PhosphorylationAQLVDLKSELTETQA
HHHCHHHHHCCHHHH
45.1726074081
106PhosphorylationVDLKSELTETQAEKV
CHHHHHCCHHHHHHH
32.7026074081
108PhosphorylationLKSELTETQAEKVVL
HHHHCCHHHHHHHHH
28.0426074081
1122-HydroxyisobutyrylationLTETQAEKVVLEKEV
CCHHHHHHHHHCHHH
40.43-
112UbiquitinationLTETQAEKVVLEKEV
CCHHHHHHHHHCHHH
40.4329967540
136UbiquitinationIQLQLHAKTGQSADS
EEEEEECCCCCCCCC
42.3029967540
143PhosphorylationKTGQSADSGTIKAKL
CCCCCCCCCEEEEEC
37.2427251275
145PhosphorylationGQSADSGTIKAKLSG
CCCCCCCEEEEECCC
24.2128857561
145 (in isoform 2)Phosphorylation-24.21-
147UbiquitinationSADSGTIKAKLSGPS
CCCCCEEEEECCCCC
39.0327667366
147 (in isoform 1)Ubiquitination-39.0321906983
147 (in isoform 2)Ubiquitination-39.0321906983
147 (in isoform 3)Ubiquitination-39.0321906983
149UbiquitinationDSGTIKAKLSGPSVE
CCCEEEEECCCCCHH
37.8830230243
151PhosphorylationGTIKAKLSGPSVEEL
CEEEEECCCCCHHHH
48.2026657352
154PhosphorylationKAKLSGPSVEELERE
EEECCCCCHHHHHHH
45.7622985185
170SulfoxidationEANKKEKMKEAQLEA
HHHHHHHHHHHHHHH
5.0721406390
171UbiquitinationANKKEKMKEAQLEAE
HHHHHHHHHHHHHHH
62.05-
172UbiquitinationNKKEKMKEAQLEAEV
HHHHHHHHHHHHHHH
37.8429967540
180UbiquitinationAQLEAEVKLLRKENE
HHHHHHHHHHHHHHH
33.0529967540
200UbiquitinationIAVLQAEVYGARLAA
HHHHHHHHHHHHHHH
6.3129967540
201PhosphorylationAVLQAEVYGARLAAK
HHHHHHHHHHHHHHH
9.1418083107
204UbiquitinationQAEVYGARLAAKYLD
HHHHHHHHHHHHHHC
22.0929967540
208UbiquitinationYGARLAAKYLDKELA
HHHHHHHHHHCHHHH
40.5129967540
209PhosphorylationGARLAAKYLDKELAG
HHHHHHHHHCHHHHH
18.5318083107
212UbiquitinationLAAKYLDKELAGRVQ
HHHHHHCHHHHHHHH
52.6229967540
270UbiquitinationKRPMQAPPGHDQDSL
CCCCCCCCCCCHHHH
56.6229967540
271UbiquitinationRPMQAPPGHDQDSLK
CCCCCCCCCCHHHHH
35.6229967540
276PhosphorylationPPGHDQDSLKKSQGV
CCCCCHHHHHHHCCC
36.1328985074
278UbiquitinationGHDQDSLKKSQGVGP
CCCHHHHHHHCCCCC
55.0929967540
279UbiquitinationHDQDSLKKSQGVGPI
CCHHHHHHHCCCCCC
53.9929967540
280PhosphorylationDQDSLKKSQGVGPIR
CHHHHHHHCCCCCCC
30.4929743597
302PhosphorylationDHEGLGISITGGKEH
CCCCCEEEECCCHHH
16.5828348404
342UbiquitinationAILAVNGVNLRDTKH
EEEEECCCCCCCCCC
5.2733845483
350UbiquitinationNLRDTKHKEAVTILS
CCCCCCCHHHHHHHH
49.2633845483
369PhosphorylationEIEFEVVYVAPEVDS
EEEEEEEEEECCCCC
8.9626657352
376PhosphorylationYVAPEVDSDDENVEY
EEECCCCCCCCCCEE
52.7327362937
383PhosphorylationSDDENVEYEDESGHR
CCCCCCEEECCCCCE
25.1326074081
387PhosphorylationNVEYEDESGHRYRLY
CCEEECCCCCEEEEE
52.8226074081
391PhosphorylationEDESGHRYRLYLDEL
ECCCCCEEEEEEEEC
10.1726074081
394PhosphorylationSGHRYRLYLDELEGG
CCCEEEEEEEECCCC
11.7828796482
401UbiquitinationYLDELEGGGNPGASC
EEEECCCCCCCCCCC
24.2729967540
407PhosphorylationGGGNPGASCKDTSGE
CCCCCCCCCCCCCCC
27.8429507054
408UbiquitinationGGNPGASCKDTSGEI
CCCCCCCCCCCCCCE
4.6032015554
409UbiquitinationGNPGASCKDTSGEIK
CCCCCCCCCCCCCEE
62.6429967540
411PhosphorylationPGASCKDTSGEIKVL
CCCCCCCCCCCEEEE
24.9121712546
412PhosphorylationGASCKDTSGEIKVLQ
CCCCCCCCCCEEEEE
44.5629214152
415UbiquitinationCKDTSGEIKVLQGFN
CCCCCCCEEEEECCC
4.2229967540
416SumoylationKDTSGEIKVLQGFNK
CCCCCCEEEEECCCC
32.37-
416UbiquitinationKDTSGEIKVLQGFNK
CCCCCCEEEEECCCC
32.3732015554
416SumoylationKDTSGEIKVLQGFNK
CCCCCCEEEEECCCC
32.37-
4232-HydroxyisobutyrylationKVLQGFNKKAVTDTH
EEEECCCCCCCCCCC
39.59-
423UbiquitinationKVLQGFNKKAVTDTH
EEEECCCCCCCCCCC
39.5929967540
437PhosphorylationHENGDLGTASETPLD
CCCCCCCCCCCCCCC
34.0226657352
439PhosphorylationNGDLGTASETPLDDG
CCCCCCCCCCCCCCC
41.6725159151
441PhosphorylationDLGTASETPLDDGAS
CCCCCCCCCCCCCCC
27.0228985074
451UbiquitinationDDGASKLDDLHTLYH
CCCCCCHHHHHHHHC
61.2329967540
455PhosphorylationSKLDDLHTLYHKKSY
CCHHHHHHHHCCCCC
35.9929978859
457PhosphorylationLDDLHTLYHKKSY--
HHHHHHHHCCCCC--
16.8514729942
459UbiquitinationDLHTLYHKKSY----
HHHHHHCCCCC----
29.8329967540
461PhosphorylationHTLYHKKSY------
HHHHCCCCC------
40.6624719451
462PhosphorylationTLYHKKSY-------
HHHCCCCC-------
31.3014729942

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
-KUbiquitinationE3 ubiquitin ligaseUBE3AQ05086
PMID:16878151

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GOPC_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 GOPC_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSPG5_HUMANCSPG5physical
12885772
BECN1_HUMANBECN1physical
12372286
GRID2_HUMANGRID2physical
12372286
RHOQ_HUMANRHOQphysical
11162552
GOPC_HUMANGOPCphysical
11162552
CLCN3_HUMANCLCN3physical
12471024
CFTR_HUMANCFTRphysical
12471024
STX6_RATStx6physical
11384996
GRM5_RATGrm5physical
19860857
MARH2_HUMANMARCH2physical
23818989
IMA5_HUMANKPNA1physical
21988832
TF65_HUMANRELAphysical
21988832
TGFR2_HUMANTGFBR2physical
21988832
NUP62_HUMANNUP62physical
21988832
ARI1_HUMANARIH1physical
22863883
NC2B_HUMANDR1physical
22863883
HSF1_HUMANHSF1physical
22863883
LRSM1_HUMANLRSAM1physical
22863883
2A5D_HUMANPPP2R5Dphysical
22863883
SEM4G_HUMANSEMA4Gphysical
25416956
RM01_HUMANMRPL1physical
25416956
AKIR1_HUMANAKIRIN1physical
25416956
C102B_HUMANCCDC102Bphysical
25416956
GHC2_HUMANSLC25A18physical
25416956
ZN587_HUMANZNF587physical
25416956
MUM1_HUMANMUM1physical
25416956
MYCD_HUMANMYOCDphysical
25416956
MORN4_HUMANMORN4physical
25416956
RN183_HUMANRNF183physical
25416956
SPAT8_HUMANSPATA8physical
25416956
ZN564_HUMANZNF564physical
25416956
ZBT49_HUMANZBTB49physical
25416956
FAM9B_HUMANFAM9Bphysical
25416956
LCLT1_HUMANLCLAT1physical
25416956
ZSCA1_HUMANZSCAN1physical
25416956
CQ067_HUMANC17orf67physical
25416956
ZBTB5_HUMANZBTB5physical
28514442
RTL6_HUMANLDOC1Lphysical
28514442
FCSD2_HUMANFCHSD2physical
28514442
ATG4D_HUMANATG4Dphysical
28514442
BAP1_HUMANBAP1physical
28514442
CNTLN_HUMANCNTLNphysical
28514442
M18BP_HUMANMIS18BP1physical
28514442
KIF1B_HUMANKIF1Bphysical
28514442
GOGA3_HUMANGOLGA3physical
28514442
CENPF_HUMANCENPFphysical
28514442
PKN2_HUMANPKN2physical
28514442
C102A_HUMANCCDC102Aphysical
28514442
SSNA1_HUMANSSNA1physical
28514442
LIMA1_HUMANLIMA1physical
28514442
CCDC8_HUMANCCDC8physical
28514442
TFAM_HUMANTFAMphysical
28514442
GRK6_HUMANGRK6physical
28514442
CABL1_HUMANCABLES1physical
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 GOPC_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-457 AND TYR-462, ANDMASS SPECTROMETRY.

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