COG1_HUMAN - dbPTM
COG1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COG1_HUMAN
UniProt AC Q8WTW3
Protein Name Conserved oligomeric Golgi complex subunit 1
Gene Name COG1
Organism Homo sapiens (Human).
Sequence Length 980
Subcellular Localization Golgi apparatus membrane
Peripheral membrane protein
Cytoplasmic side .
Protein Description Required for normal Golgi function..
Protein Sequence MATAATSPALKRLDLRDPAALFETHGAEEIRGLERQVRAEIEHKKEELRQMVGERYRDLIEAADTIGQMRRCAVGLVDAVKATDQYCARLRQAGSAAPRPPRAQQPQQPSQEKFYSMAAQIKLLLEIPEKIWSSMEASQCLHATQLYLLCCHLHSLLQLDSSSSRYSPVLSRFPILIRQVAAASHFRSTILHESKMLLKCQGVSDQAVAEALCSIMLLEESSPRQALTDFLLARKATIQKLLNQPHHGAGIKAQICSLVELLATTLKQAHALFYTLPEGLLPDPALPCGLLFSTLETITGQHPAGKGTGVLQEEMKLCSWFKHLPASIVEFQPTLRTLAHPISQEYLKDTLQKWIHMCNEDIKNGITNLLMYVKSMKGLAGIRDAMWELLTNESTNHSWDVLCRRLLEKPLLFWEDMMQQLFLDRLQTLTKEGFDSISSSSKELLVSALQELESSTSNSPSNKHIHFEYNMSLFLWSESPNDLPSDAAWVSVANRGQFASSGLSMKAQAISPCVQNFCSALDSKLKVKLDDLLAYLPSDDSSLPKDVSPTQAKSSAFDRYADAGTVQEMLRTQSVACIKHIVDCIRAELQSIEEGVQGQQDALNSAKLHSVLFMARLCQSLGELCPHLKQCILGKSESSEKPAREFRALRKQGKVKTQEIIPTQAKWQEVKEVLLQQSVMGYQVWSSAVVKVLIHGFTQSLLLDDAGSVLATATSWDELEIQEEAESGSSVTSKIRLPAQPSWYVQSFLFSLCQEINRVGGHALPKVTLQEMLKSCMVQVVAAYEKLSEEKQIKKEGAFPVTQNRALQLLYDLRYLNIVLTAKGDEVKSGRSKPDSRIEKVTDHLEALIDPFDLDVFTPHLNSNLHRLVQRTSVLFGLVTGTENQLAPRSSTFNSQEPHNILPLASSQIRFGLLPLSMTSTRKAKSTRNIETKAQVVPPARSTAGDPTVPGSLFRQLVSEEDNTSAPSLFKLGWLSSMTK
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------MATAATSPA
------CCCCCCCHH		13.1222814378
3Phosphorylation-----MATAATSPAL
-----CCCCCCCHHH		18.6121406692
6Phosphorylation--MATAATSPALKRL
--CCCCCCCHHHHHC		32.5529255136
7Phosphorylation-MATAATSPALKRLD
-CCCCCCCHHHHHCC		11.9329255136
11AcetylationAATSPALKRLDLRDP
CCCCHHHHHCCCCCH		53.6925953088
11UbiquitinationAATSPALKRLDLRDP
CCCCHHHHHCCCCCH		53.6922505724
442-HydroxyisobutyrylationVRAEIEHKKEELRQM
HHHHHHHHHHHHHHH		49.44-
44UbiquitinationVRAEIEHKKEELRQM
HHHHHHHHHHHHHHH		49.4424816145
45UbiquitinationRAEIEHKKEELRQMV
HHHHHHHHHHHHHHH		59.33-
81UbiquitinationVGLVDAVKATDQYCA
HHHHHHHHHHHHHHH		47.49-
95PhosphorylationARLRQAGSAAPRPPR
HHHHHCCCCCCCCCC		25.0327174698
110PhosphorylationAQQPQQPSQEKFYSM
CCCCCCCCHHHHHHH		46.7829978859
116PhosphorylationPSQEKFYSMAAQIKL
CCHHHHHHHHHHHHH		12.7029978859
167PhosphorylationDSSSSRYSPVLSRFP
CCCCCCCCCHHHHHH		13.8626699800
240UbiquitinationARKATIQKLLNQPHH
HHHHHHHHHHCCCCC		51.6029967540
316UbiquitinationGVLQEEMKLCSWFKH
CCHHHHHHHHHHHHH		50.0132015554
377MethylationLMYVKSMKGLAGIRD
HHHHHHHCHHHCHHH		58.8423644510
431UbiquitinationDRLQTLTKEGFDSIS
HHHHHHCHHCHHCCC		59.9821906983
442UbiquitinationDSISSSSKELLVSAL
HCCCCCCHHHHHHHH		55.0929967540
447PhosphorylationSSKELLVSALQELES
CCHHHHHHHHHHHHH		24.1920873877
454PhosphorylationSALQELESSTSNSPS
HHHHHHHHCCCCCCC		52.0926329039
455PhosphorylationALQELESSTSNSPSN
HHHHHHHCCCCCCCC		26.8630278072
456PhosphorylationLQELESSTSNSPSNK
HHHHHHCCCCCCCCC		41.0030278072
457PhosphorylationQELESSTSNSPSNKH
HHHHHCCCCCCCCCE		36.9430278072
459PhosphorylationLESSTSNSPSNKHIH
HHHCCCCCCCCCEEE		29.4928355574
461PhosphorylationSSTSNSPSNKHIHFE
HCCCCCCCCCEEEEE		59.3330278072
524UbiquitinationFCSALDSKLKVKLDD
HHHHHCHHHCCCHHH		52.58-
526UbiquitinationSALDSKLKVKLDDLL
HHHCHHHCCCHHHHH		40.85-
528UbiquitinationLDSKLKVKLDDLLAY
HCHHHCCCHHHHHHH		44.6129967540
528AcetylationLDSKLKVKLDDLLAY
HCHHHCCCHHHHHHH		44.6119824333
545UbiquitinationSDDSSLPKDVSPTQA
CCCCCCCCCCCHHHC		75.8629967540
548PhosphorylationSSLPKDVSPTQAKSS
CCCCCCCCHHHCCHH		32.1529255136
550PhosphorylationLPKDVSPTQAKSSAF
CCCCCCHHHCCHHHH		33.3828060719
553UbiquitinationDVSPTQAKSSAFDRY
CCCHHHCCHHHHHHH		34.8221906983
559MethylationAKSSAFDRYADAGTV
CCHHHHHHHCCHHHH		23.29-
572PhosphorylationTVQEMLRTQSVACIK
HHHHHHHHCCHHHHH		22.64-
574PhosphorylationQEMLRTQSVACIKHI
HHHHHHCCHHHHHHH		15.86-
607UbiquitinationQDALNSAKLHSVLFM
HHHHHHHHHHHHHHH		46.70-
610PhosphorylationLNSAKLHSVLFMARL
HHHHHHHHHHHHHHH		30.8324043423
657PhosphorylationRKQGKVKTQEIIPTQ
HHCCCCCCCCCCCCH		34.1322817900
666UbiquitinationEIIPTQAKWQEVKEV
CCCCCHHHHHHHHHH		39.3222817900
671UbiquitinationQAKWQEVKEVLLQQS
HHHHHHHHHHHHHCC		41.1622817900
775PhosphorylationTLQEMLKSCMVQVVA
CHHHHHHHHHHHHHH		11.9524532841
811PhosphorylationNRALQLLYDLRYLNI
HHHHHHHHHHHHCEE		22.8620071362
890PhosphorylationENQLAPRSSTFNSQE
CCCCCCCCCCCCCCC		32.44-
891PhosphorylationNQLAPRSSTFNSQEP
CCCCCCCCCCCCCCC		37.99-
892PhosphorylationQLAPRSSTFNSQEPH
CCCCCCCCCCCCCCC		28.2528555341
906PhosphorylationHNILPLASSQIRFGL
CCCHHHCCCCCCCCC		30.38-
907PhosphorylationNILPLASSQIRFGLL
CCHHHCCCCCCCCCC		24.82-
917PhosphorylationRFGLLPLSMTSTRKA
CCCCCCCCCCCCCCC		20.3428857561
933UbiquitinationSTRNIETKAQVVPPA
CCCCCCCCCEECCCC		24.8327667366
952PhosphorylationGDPTVPGSLFRQLVS
CCCCCCHHHHHHHHC		20.4728857561
959PhosphorylationSLFRQLVSEEDNTSA
HHHHHHHCCCCCCCC		43.8129396449
964PhosphorylationLVSEEDNTSAPSLFK
HHCCCCCCCCCHHHH		38.2927251275
965PhosphorylationVSEEDNTSAPSLFKL
HCCCCCCCCCHHHHH		44.4229396449
968PhosphorylationEDNTSAPSLFKLGWL
CCCCCCCHHHHHHHH		46.2724719451
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 COG1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COG1_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 COG1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COG4_HUMANCOG4physical
15047703
COG4_HUMANCOG4physical
22939629
COG3_HUMANCOG3physical
22939629
COG7_HUMANCOG7physical
22939629
COG5_HUMANCOG5physical
22939629
COG6_HUMANCOG6physical
22939629
COG8_HUMANCOG8physical
22939629
COG2_HUMANCOG2physical
22939629
COG7_HUMANCOG7physical
26344197
Drug and Disease Associations
Kegg Disease
H00119 Congenital disorders of glycosylation (CDG) type II
OMIM Disease
611209Congenital disorder of glycosylation 2G (CDG2G)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of COG1_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, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459, AND MASSSPECTROMETRY.
"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-7 AND SER-459, AND MASSSPECTROMETRY.

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