COG5_HUMAN - dbPTM
COG5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COG5_HUMAN
UniProt AC Q9UP83
Protein Name Conserved oligomeric Golgi complex subunit 5
Gene Name COG5
Organism Homo sapiens (Human).
Sequence Length 839
Subcellular Localization Cytoplasm, cytosol . Golgi apparatus membrane
Peripheral membrane protein .
Protein Description Required for normal Golgi function..
Protein Sequence MGWVGGRRRDSASPPGRSRSAADDINPAPANMEGGGGSVAVAGLGARGSGAAAATVRELLQDGCYSDFLNEDFDVKTYTSQSIHQAVIAEQLAKLAQGISQLDRELHLQVVARHEDLLAQATGIESLEGVLQMMQTRIGALQGAVDRIKAKIVEPYNKIVARTAQLARLQVACDLLRRIIRILNLSKRLQGQLQGGSREITKAAQSLNELDYLSQGIDLSGIEVIENDLLFIARARLEVENQAKRLLEQGLETQNPTQVGTALQVFYNLGTLKDTITSVVDGYCATLEENINSALDIKVLTQPSQSAVRGGPGRSTMPTPGNTAALRASFWTNMEKLMDHIYAVCGQVQHLQKVLAKKRDPVSHICFIEEIVKDGQPEIFYTFWNSVTQALSSQFHMATNSSMFLKQAFEGEYPKLLRLYNDLWKRLQQYSQHIQGNFNASGTTDLYVDLQHMEDDAQDIFIPKKPDYDPEKALKDSLQPYEAAYLSKSLSRLFDPINLVFPPGGRNPPSSDELDGIIKTIASELNVAAVDTNLTLAVSKNVAKTIQLYSVKSEQLLSTQGDASQVIGPLTEGQRRNVAVVNSLYKLHQSVTKAIHALMENAVQPLLTSVGDAIEAIIITMHQEDFSGSLSSSGKPDVPCSLYMKELQGFIARVMSDYFKHFECLDFVFDNTEAIAQRAVELFIRHASLIRPLGEGGKMRLAADFAQMELAVGPFCRRVSDLGKSYRMLRSFRPLLFQASEHVASSPALGDVIPFSIIIQFLFTRAPAELKSPFQRAEWSHTRFSQWLDDHPSEKDRLLLIRGALEAYVQSVRSREGKEFAPVYPIMVQLLQKAMSALQ
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
11PhosphorylationVGGRRRDSASPPGRS
CCCCCCCCCCCCCCC		28.9126425664
13PhosphorylationGRRRDSASPPGRSRS
CCCCCCCCCCCCCCC		35.2630576142
18PhosphorylationSASPPGRSRSAADDI
CCCCCCCCCCCHHCC		36.1833259812
20PhosphorylationSPPGRSRSAADDINP
CCCCCCCCCHHCCCC		29.1127690223
38PhosphorylationNMEGGGGSVAVAGLG
CCCCCCCCEEEECCC		15.3527690223
49 (in isoform 2)Phosphorylation-21.5024719451
49PhosphorylationAGLGARGSGAAAATV
ECCCCCCCCHHHHHH		21.5025849741
55PhosphorylationGSGAAAATVRELLQD
CCCHHHHHHHHHHHC		18.5023927012
65 (in isoform 2)Phosphorylation-19.4627642862
76UbiquitinationLNEDFDVKTYTSQSI
CCCCCCCCCCCCCHH		37.3429967540
78 (in isoform 2)Phosphorylation-9.9327642862
94AcetylationVIAEQLAKLAQGISQ
HHHHHHHHHHHHHHH		53.6123236377
147MethylationALQGAVDRIKAKIVE
HHHHHHHHHHHHHHC		26.21-
151UbiquitinationAVDRIKAKIVEPYNK
HHHHHHHHHHCCHHH		42.1327667366
158 (in isoform 2)Ubiquitination-32.49-
158UbiquitinationKIVEPYNKIVARTAQ
HHHCCHHHHHHHHHH		32.49-
187UbiquitinationIRILNLSKRLQGQLQ
HHHHCHHHHHHHHCC		61.3627667366
197PhosphorylationQGQLQGGSREITKAA
HHHCCCCHHHHHHHH		33.3023401153
197 (in isoform 2)Phosphorylation-33.3024719451
201PhosphorylationQGGSREITKAAQSLN
CCCHHHHHHHHHHHH		15.1823403867
2442-HydroxyisobutyrylationLEVENQAKRLLEQGL
HHHHHHHHHHHHCCC		33.54-
244UbiquitinationLEVENQAKRLLEQGL
HHHHHHHHHHHHCCC		33.5424816145
304PhosphorylationIKVLTQPSQSAVRGG
EEEECCCCCCCCCCC		27.2723312004
306PhosphorylationVLTQPSQSAVRGGPG
EECCCCCCCCCCCCC		32.8223312004
309MethylationQPSQSAVRGGPGRST
CCCCCCCCCCCCCCC		44.03-
315PhosphorylationVRGGPGRSTMPTPGN
CCCCCCCCCCCCCCC		34.6728857561
316PhosphorylationRGGPGRSTMPTPGNT
CCCCCCCCCCCCCCH		26.3028857561
317SulfoxidationGGPGRSTMPTPGNTA
CCCCCCCCCCCCCHH		3.5221406390
319PhosphorylationPGRSTMPTPGNTAAL
CCCCCCCCCCCHHHH		32.7628555341
353UbiquitinationGQVQHLQKVLAKKRD
HHHHHHHHHHHCCCC		45.6429967540
358UbiquitinationLQKVLAKKRDPVSHI
HHHHHHCCCCCCCEE		57.3229967540
465 (in isoform 2)Ubiquitination-37.45-
465UbiquitinationQDIFIPKKPDYDPEK
HHCCCCCCCCCCHHH		37.45-
472UbiquitinationKPDYDPEKALKDSLQ
CCCCCHHHHHHHCCC		65.4929967540
475UbiquitinationYDPEKALKDSLQPYE
CCHHHHHHHCCCHHH		50.5629967540
475 (in isoform 2)Ubiquitination-50.56-
477PhosphorylationPEKALKDSLQPYEAA
HHHHHHHCCCHHHHH		27.5827067055
481PhosphorylationLKDSLQPYEAAYLSK
HHHCCCHHHHHHHHH		12.7720873877
488 (in isoform 1)Ubiquitination-53.4721890473
488 (in isoform 2)Ubiquitination-53.4721890473
488UbiquitinationYEAAYLSKSLSRLFD
HHHHHHHHHHHHHCC		53.4722817900
488 (in isoform 3)Ubiquitination-53.4721890473
510PhosphorylationPGGRNPPSSDELDGI
CCCCCCCCHHHHHHH		52.24-
544 (in isoform 2)Ubiquitination-41.71-
544UbiquitinationAVSKNVAKTIQLYSV
EEEHHHHHHEEEEEE		41.71-
547UbiquitinationKNVAKTIQLYSVKSE
HHHHHHEEEEEECHH		39.3132015554
552UbiquitinationTIQLYSVKSEQLLST
HEEEEEECHHHHHCC		42.19-
586UbiquitinationAVVNSLYKLHQSVTK
HHHHHHHHHHHHHHH		44.8029967540
595UbiquitinationHQSVTKAIHALMENA
HHHHHHHHHHHHHHC		1.7632015554
680UbiquitinationEAIAQRAVELFIRHA
HHHHHHHHHHHHHHH		7.7632015554
698AcetylationRPLGEGGKMRLAADF
EECCCCCCHHHHHHH		31.537972755
698UbiquitinationRPLGEGGKMRLAADF
EECCCCCCHHHHHHH		31.53-
719 (in isoform 2)Ubiquitination-2.42-
719UbiquitinationVGPFCRRVSDLGKSY
HHHHHHHHHHHHHHH		2.42-
724UbiquitinationRRVSDLGKSYRMLRS
HHHHHHHHHHHHHHH		52.16-
727UbiquitinationSDLGKSYRMLRSFRP
HHHHHHHHHHHHHHH		25.4232015554
731UbiquitinationKSYRMLRSFRPLLFQ
HHHHHHHHHHHHHHH		22.9632015554
745UbiquitinationQASEHVASSPALGDV
HHCHHHHCCCCCCCC		35.45-
745 (in isoform 2)Ubiquitination-35.45-
771UbiquitinationTRAPAELKSPFQRAE
HCCCHHHCCHHHCHH		47.8124816145
792UbiquitinationSQWLDDHPSEKDRLL
HHHHHCCCCHHHHHH		51.7024816145
792 (in isoform 2)Ubiquitination-51.70-
795UbiquitinationLDDHPSEKDRLLLIR
HHCCCCHHHHHHHHH		53.1129967540
816 (in isoform 2)Ubiquitination-75.71-
816UbiquitinationVQSVRSREGKEFAPV
HHHHHHCCCCCCCCH		75.7129967540
818UbiquitinationSVRSREGKEFAPVYP
HHHHCCCCCCCCHHH		44.93-
839UbiquitinationQKAMSALQ-------
HHHHHHCC-------		51.49-
839 (in isoform 2)Ubiquitination-51.49-
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 COG5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COG5_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 COG5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MEFV_HUMANMEFVphysical
10782044
COG7_HUMANCOG7physical
15047703
COG4_HUMANCOG4physical
15047703
COG7_HUMANCOG7physical
22939629
COG6_HUMANCOG6physical
22939629
COG8_HUMANCOG8physical
22939629
COG1_HUMANCOG1physical
26344197
COG2_HUMANCOG2physical
26344197
COG3_HUMANCOG3physical
26344197
COG4_HUMANCOG4physical
26344197
COG6_HUMANCOG6physical
26344197
COG7_HUMANCOG7physical
26344197
STK24_HUMANSTK24physical
26344197
COG3_HUMANCOG3physical
28514442
COG6_HUMANCOG6physical
28514442
COG7_HUMANCOG7physical
28514442
COG1_HUMANCOG1physical
28514442
COG8_HUMANCOG8physical
28514442
COG2_HUMANCOG2physical
28514442
COG4_HUMANCOG4physical
28514442
CC136_HUMANCCDC136physical
28514442
ATP7A_HUMANATP7Aphysical
28514442
NIN_HUMANNINphysical
28514442
PCM1_HUMANPCM1physical
28514442
BASI_HUMANBSGphysical
28514442
IFFO1_HUMANIFFO1physical
28514442
STX4_HUMANSTX4physical
28514442
Drug and Disease Associations
Kegg Disease
H00119 Congenital disorders of glycosylation (CDG) type II
OMIM Disease
613612Congenital disorder of glycosylation 2I (CDG2I)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of COG5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND MASSSPECTROMETRY.

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