COG4_HUMAN - dbPTM
COG4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COG4_HUMAN
UniProt AC Q9H9E3
Protein Name Conserved oligomeric Golgi complex subunit 4
Gene Name COG4
Organism Homo sapiens (Human).
Sequence Length 785
Subcellular Localization Golgi apparatus membrane
Peripheral membrane protein
Cytoplasmic side .
Protein Description Required for normal Golgi function. Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with SCFD1..
Protein Sequence MADLDSPPKLSGVQQPSEGVGGGRCSEISAELIRSLTELQELEAVYERLCGEEKVVERELDALLEQQNTIESKMVTLHRMGPNLQLIEGDAKQLAGMITFTCNLAENVSSKVRQLDLAKNRLYQAIQRADDILDLKFCMDGVQTALRSEDYEQAAAHTHRYLCLDKSVIELSRQGKEGSMIDANLKLLQEAEQRLKAIVAEKFAIATKEGDLPQVERFFKIFPLLGLHEEGLRKFSEYLCKQVASKAEENLLMVLGTDMSDRRAAVIFADTLTLLFEGIARIVETHQPIVETYYGPGRLYTLIKYLQVECDRQVEKVVDKFIKQRDYHQQFRHVQNNLMRNSTTEKIEPRELDPILTEVTLMNARSELYLRFLKKRISSDFEVGDSMASEEVKQEHQKCLDKLLNNCLLSCTMQELIGLYVTMEEYFMRETVNKAVALDTYEKGQLTSSMVDDVFYIVKKCIGRALSSSSIDCLCAMINLATTELESDFRDVLCNKLRMGFPATTFQDIQRGVTSAVNIMHSSLQQGKFDTKGIESTDEAKMSFLVTLNNVEVCSENISTLKKTLESDCTKLFSQGIGGEQAQAKFDSCLSDLAAVSNKFRDLLQEGLTELNSTAIKPQVQPWINSFFSVSHNIEEEEFNDYEANDPWVQQFILNLEQQMAEFKASLSPVIYDSLTGLMTSLVAVELEKVVLKSTFNRLGGLQFDKELRSLIAYLTTVTTWTIRDKFARLSQMATILNLERVTEILDYWGPNSGPLTWRLTPAEVRQVLALRIDFRSEDIKRLRL
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------MADLDSPPK
------CCCCCCCCC		26.5222814378
6Phosphorylation--MADLDSPPKLSGV
--CCCCCCCCCCCCC		50.8529255136
10PhosphorylationDLDSPPKLSGVQQPS
CCCCCCCCCCCCCCC		7.1219413330
11PhosphorylationLDSPPKLSGVQQPSE
CCCCCCCCCCCCCCC		42.9422167270
17PhosphorylationLSGVQQPSEGVGGGR
CCCCCCCCCCCCCCC		42.5225159151
21PhosphorylationQQPSEGVGGGRCSEI
CCCCCCCCCCCHHHH		43.6320058876
26PhosphorylationGVGGGRCSEISAELI
CCCCCCHHHHHHHHH		36.2825627689
37PhosphorylationAELIRSLTELQELEA
HHHHHHHHHHHHHHH		35.58-
46PhosphorylationLQELEAVYERLCGEE
HHHHHHHHHHHHCCH		11.4628796482
50PhosphorylationEAVYERLCGEEKVVE
HHHHHHHHCCHHHHH		8.9227642862
54AcetylationERLCGEEKVVERELD
HHHHCCHHHHHHHHH		47.4825953088
54UbiquitinationERLCGEEKVVERELD
HHHHCCHHHHHHHHH		47.48-
58UbiquitinationGEEKVVERELDALLE
CCHHHHHHHHHHHHH		37.86-
73 (in isoform 1)Ubiquitination-25.3021890473
73 (in isoform 2)Ubiquitination-25.3021890473
73UbiquitinationQQNTIESKMVTLHRM
HHCCHHHHHHHHHHC		25.3021890473
73UbiquitinationQQNTIESKMVTLHRM
HHCCHHHHHHHHHHC		25.3021890473
77UbiquitinationIESKMVTLHRMGPNL
HHHHHHHHHHCCCCC		1.32-
77 (in isoform 3)Ubiquitination-1.3221890473
99PhosphorylationKQLAGMITFTCNLAE
HHHHHHHHHHHCCHH		12.1929978859
101PhosphorylationLAGMITFTCNLAENV
HHHHHHHHHCCHHHH		7.5829978859
109PhosphorylationCNLAENVSSKVRQLD
HCCHHHHHHHHHHHH		35.7029978859
110PhosphorylationNLAENVSSKVRQLDL
CCHHHHHHHHHHHHH		30.7829978859
121MethylationQLDLAKNRLYQAIQR
HHHHHHHHHHHHHHH		33.78-
123PhosphorylationDLAKNRLYQAIQRAD
HHHHHHHHHHHHHHH		7.8328796482
123UbiquitinationDLAKNRLYQAIQRAD
HHHHHHHHHHHHHHH		7.83-
125MethylationAKNRLYQAIQRADDI
HHHHHHHHHHHHHHH		6.06-
127PhosphorylationNRLYQAIQRADDILD
HHHHHHHHHHHHHHC		37.2127642862
166UbiquitinationHRYLCLDKSVIELSR
CHHEEECHHHHHHHH		33.40-
170UbiquitinationCLDKSVIELSRQGKE
EECHHHHHHHHCCCC		38.24-
176 (in isoform 1)Ubiquitination-51.0321890473
176UbiquitinationIELSRQGKEGSMIDA
HHHHHCCCCCCCHHH		51.0321906983
176 (in isoform 2)Ubiquitination-51.0321890473
179PhosphorylationSRQGKEGSMIDANLK
HHCCCCCCCHHHHHH		17.4120363803
180UbiquitinationRQGKEGSMIDANLKL
HCCCCCCCHHHHHHH		4.77-
183PhosphorylationKEGSMIDANLKLLQE
CCCCCHHHHHHHHHH		16.60-
186UbiquitinationSMIDANLKLLQEAEQ
CCHHHHHHHHHHHHH		47.13-
190UbiquitinationANLKLLQEAEQRLKA
HHHHHHHHHHHHHHH		54.89-
200UbiquitinationQRLKAIVAEKFAIAT
HHHHHHHHHHHHHHC		14.24-
207PhosphorylationAEKFAIATKEGDLPQ
HHHHHHHCCCCCCHH		24.4220860994
208UbiquitinationEKFAIATKEGDLPQV
HHHHHHCCCCCCHHH		51.1621906983
208 (in isoform 2)Ubiquitination-51.1621890473
208 (in isoform 1)Ubiquitination-51.1621890473
211PhosphorylationAIATKEGDLPQVERF
HHHCCCCCCHHHHHH		57.1624719451
212UbiquitinationIATKEGDLPQVERFF
HHCCCCCCHHHHHHH		4.74-
234UbiquitinationLHEEGLRKFSEYLCK
CCHHHHHHHHHHHHH		59.28-
238UbiquitinationGLRKFSEYLCKQVAS
HHHHHHHHHHHHHHH		19.05-
245UbiquitinationYLCKQVASKAEENLL
HHHHHHHHHHHHCHH		33.28-
260PhosphorylationMVLGTDMSDRRAAVI
HHHCCCCCHHHHHHH		30.6725332170
320UbiquitinationQVEKVVDKFIKQRDY
HHHHHHHHHHHCCHH		37.06-
323UbiquitinationKVVDKFIKQRDYHQQ
HHHHHHHHCCHHHHH		42.27-
324UbiquitinationVVDKFIKQRDYHQQF
HHHHHHHCCHHHHHH		38.37-
327UbiquitinationKFIKQRDYHQQFRHV
HHHHCCHHHHHHHHH		12.06-
346 (in isoform 1)Ubiquitination-50.7221890473
346UbiquitinationMRNSTTEKIEPRELD
HCCCCCCCCCHHHCC		50.7221906983
350UbiquitinationTTEKIEPRELDPILT
CCCCCCHHHCCHHHH		44.30-
378PhosphorylationRFLKKRISSDFEVGD
HHHHHHCCCCCCCCC		28.08-
379PhosphorylationFLKKRISSDFEVGDS
HHHHHCCCCCCCCCC		43.9028258704
382PhosphorylationKRISSDFEVGDSMAS
HHCCCCCCCCCCCCC		51.05-
383PhosphorylationRISSDFEVGDSMASE
HCCCCCCCCCCCCCH		11.87-
393UbiquitinationSMASEEVKQEHQKCL
CCCCHHHHHHHHHHH		53.93-
397UbiquitinationEEVKQEHQKCLDKLL
HHHHHHHHHHHHHHH		37.09-
443AcetylationVALDTYEKGQLTSSM
HHCCCCCCCCCCHHH		41.3619608861
447AcetylationTYEKGQLTSSMVDDV
CCCCCCCCHHHHHHH		15.7419608861
447PhosphorylationTYEKGQLTSSMVDDV
CCCCCCCCHHHHHHH		15.7429978859
448PhosphorylationYEKGQLTSSMVDDVF
CCCCCCCHHHHHHHH		25.6529978859
449PhosphorylationEKGQLTSSMVDDVFY
CCCCCCHHHHHHHHH		20.0029978859
456PhosphorylationSMVDDVFYIVKKCIG
HHHHHHHHHHHHHHH		12.4929978859
514PhosphorylationQDIQRGVTSAVNIMH
HHHHHCHHHHHHHHH		17.5025693802
515PhosphorylationDIQRGVTSAVNIMHS
HHHHCHHHHHHHHHH		28.0125693802
519PhosphorylationGVTSAVNIMHSSLQQ
CHHHHHHHHHHHHHC		1.8027251275
522PhosphorylationSAVNIMHSSLQQGKF
HHHHHHHHHHHCCCC		18.5028857561
523PhosphorylationAVNIMHSSLQQGKFD
HHHHHHHHHHCCCCC		18.6028348404
527PhosphorylationMHSSLQQGKFDTKGI
HHHHHHCCCCCCCCC		21.4527251275
532UbiquitinationQQGKFDTKGIESTDE
HCCCCCCCCCCCCHH		60.792190698
532AcetylationQQGKFDTKGIESTDE
HCCCCCCCCCCCCHH		60.797697129
532 (in isoform 1)Ubiquitination-60.7921890473
536UbiquitinationFDTKGIESTDEAKMS
CCCCCCCCCHHHHHE		38.96-
571UbiquitinationTLESDCTKLFSQGIG
HHHHHHHHHHHCCCC		54.59-
575UbiquitinationDCTKLFSQGIGGEQA
HHHHHHHCCCCHHHH		39.94-
588PhosphorylationQAQAKFDSCLSDLAA
HHHHHHHHHHHHHHH		21.79-
589UbiquitinationAQAKFDSCLSDLAAV
HHHHHHHHHHHHHHH		4.55-
591PhosphorylationAKFDSCLSDLAAVSN
HHHHHHHHHHHHHHH		34.60-
597PhosphorylationLSDLAAVSNKFRDLL
HHHHHHHHHHHHHHH		29.58-
672PhosphorylationASLSPVIYDSLTGLM
HHCCHHHHHHHHHHH		10.34-
697UbiquitinationVVLKSTFNRLGGLQF
HHHHHHHHHCCCCCC		38.05-
706UbiquitinationLGGLQFDKELRSLIA
CCCCCCCHHHHHHHH		60.99-
710PhosphorylationQFDKELRSLIAYLTT
CCCHHHHHHHHHHHH		36.4325954137
710UbiquitinationQFDKELRSLIAYLTT
CCCHHHHHHHHHHHH		36.43-
714PhosphorylationELRSLIAYLTTVTTW
HHHHHHHHHHHHHHH		9.5118083107
717PhosphorylationSLIAYLTTVTTWTIR
HHHHHHHHHHHHHHH		17.1725954137
718PhosphorylationLIAYLTTVTTWTIRD
HHHHHHHHHHHHHHH		3.6518083107
722PhosphorylationLTTVTTWTIRDKFAR
HHHHHHHHHHHHHHH		12.2125954137
753PhosphorylationLDYWGPNSGPLTWRL
HHHHCCCCCCCEEEC		44.9420860994
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 COG4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COG4_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 COG4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COG1_HUMANCOG1physical
15047703
COG2_HUMANCOG2physical
15047703
COG5_HUMANCOG5physical
15047703
COG7_HUMANCOG7physical
15047703
COG7_HUMANCOG7physical
22939629
COG5_HUMANCOG5physical
22939629
COG8_HUMANCOG8physical
22939629
RS20_HUMANRPS20physical
22939629
COG1_HUMANCOG1physical
26344197
COG6_HUMANCOG6physical
26344197
COG7_HUMANCOG7physical
26344197
Drug and Disease Associations
Kegg Disease
H00119 Congenital disorders of glycosylation (CDG) type II
OMIM Disease
613489Congenital disorder of glycosylation 2J (CDG2J)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of COG4_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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-6, AND MASS SPECTROMETRY.
"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-443, AND MASS SPECTROMETRY.
Phosphorylation
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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-6, AND MASS SPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-714, AND MASSSPECTROMETRY.

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