COG3_HUMAN - dbPTM
COG3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID COG3_HUMAN
UniProt AC Q96JB2
Protein Name Conserved oligomeric Golgi complex subunit 3
Gene Name COG3
Organism Homo sapiens (Human).
Sequence Length 828
Subcellular Localization Golgi apparatus, Golgi stack membrane
Peripheral membrane protein . Associated with the peripheral membrane of cis/medial cisternae.
Protein Description Involved in ER-Golgi transport..
Protein Sequence MAEAALLLLPEAAAERDAREKLALWDRRPDTTAPLTDRQTDSVLELKAAAENLPVPAELPIEDLCSLTSQSLPIELTSVVPESTEDILLKGFTSLGMEEERIETAQQFFSWFAKLQTQMDQDEGTKYRQMRDYLSGFQEQCDAILNDVNSALQHLESLQKQYLFVSNKTGTLHEACEQLLKEQSELVDLAENIQQKLSYFNELETINTKLNSPTLSVNSDGFIPMLAKLDDCITYISSHPNFKDYPIYLLKFKQCLSKALHLMKTYTVNTLQTLTSQLLKRDPSSVPNADNAFTLFYVKFRAAAPKVRTLIEQIELRSEKIPEYQQLLNDIHQCYLDQRELLLGPSIACTVAELTSQNNRDHCALVRSGCAFMVHVCQDEHQLYNEFFTKPTSKLDELLEKLCVSLYDVFRPLIIHVIHLETLSELCGILKNEVLEDHVQNNAEQLGAFAAGVKQMLEDVQERLVYRTHIYIQTDITGYKPAPGDLAYPDKLVMMEQIAQSLKDEQKKVPSEASFSDVHLEEGESNSLTKSGSTESLNPRPQTTISPADLHGMWYPTVRRTLVCLSKLYRCIDRAVFQGLSQEALSACIQSLLGASESISKNKTQIDGQLFLIKHLLILREQIAPFHTEFTIKEISLDLKKTRDAAFKILNPMTVPRFFRLNSNNALIEFLLEGTPEIREHYLDSKKDVDRHLKSACEQFIQQQTKLFVEQLEEFMTKVSALKTMASQGGPKYTLSQQPWAQPAKVNDLAATAYKTIKTKLPVTLRSMSLYLSNKDTEFILFKPVRNNIQQVFQKFHALLKEEFSPEDIQIIACPSMEQLSLLLLVSK
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------MAEAALLLL
------CHHHHHHHC		18.3522814378
21UbiquitinationAERDAREKLALWDRR
HCCHHHHHHHHCCCC		33.2429967540
42PhosphorylationLTDRQTDSVLELKAA
CCCCCCCCHHHHHHH		31.80-
93O-linked_GlycosylationDILLKGFTSLGMEEE
HHHHHCHHHCCCCHH		31.5429237092
125PhosphorylationQMDQDEGTKYRQMRD
HCCCCCCHHHHHHHH		23.9029449344
126AcetylationMDQDEGTKYRQMRDY
CCCCCCHHHHHHHHH		49.6620167786
212PhosphorylationTINTKLNSPTLSVNS
HHCCCCCCCCCCCCC		29.6927050516
214PhosphorylationNTKLNSPTLSVNSDG
CCCCCCCCCCCCCCC		31.3327050516
216PhosphorylationKLNSPTLSVNSDGFI
CCCCCCCCCCCCCCH		23.0221406692
219PhosphorylationSPTLSVNSDGFIPML
CCCCCCCCCCCHHHH		36.6321406692
273PhosphorylationYTVNTLQTLTSQLLK
CHHHHHHHHHHHHHH		34.81-
424UbiquitinationVIHLETLSELCGILK
HHCHHHHHHHHHHHH		35.6224816145
468O-linked_GlycosylationQERLVYRTHIYIQTD
HHHHHHEEEEEEEEC		8.5729237092
477O-linked_GlycosylationIYIQTDITGYKPAPG
EEEEECCCCCCCCCC		36.9529237092
511PhosphorylationDEQKKVPSEASFSDV
HHHHCCCCCCCCCCC		49.1021712546
514PhosphorylationKKVPSEASFSDVHLE
HCCCCCCCCCCCCCC		22.6423401153
516PhosphorylationVPSEASFSDVHLEEG
CCCCCCCCCCCCCCC		35.9126657352
525PhosphorylationVHLEEGESNSLTKSG
CCCCCCCCCCCCCCC		42.4428450419
527PhosphorylationLEEGESNSLTKSGST
CCCCCCCCCCCCCCC		46.8526074081
529PhosphorylationEGESNSLTKSGSTES
CCCCCCCCCCCCCCC		24.0028450419
531PhosphorylationESNSLTKSGSTESLN
CCCCCCCCCCCCCCC		32.5129255136
533PhosphorylationNSLTKSGSTESLNPR
CCCCCCCCCCCCCCC		35.7729255136
534PhosphorylationSLTKSGSTESLNPRP
CCCCCCCCCCCCCCC		32.8729255136
536PhosphorylationTKSGSTESLNPRPQT
CCCCCCCCCCCCCCC		33.2723927012
543PhosphorylationSLNPRPQTTISPADL
CCCCCCCCCCCHHHH		28.8726657352
544PhosphorylationLNPRPQTTISPADLH
CCCCCCCCCCHHHHC		17.7623927012
546PhosphorylationPRPQTTISPADLHGM
CCCCCCCCHHHHCCC		16.3726657352
557PhosphorylationLHGMWYPTVRRTLVC
HCCCCHHHHHHHHHH		15.7923927012
604PhosphorylationESISKNKTQIDGQLF
HHHCCCCCCCCHHHH		39.9021406692
636PhosphorylationEFTIKEISLDLKKTR
EEEEEEECCCCHHHH		19.5427251275
648UbiquitinationKTRDAAFKILNPMTV
HHHHHHHHHHCCCCC		41.3724816145
654PhosphorylationFKILNPMTVPRFFRL
HHHHCCCCCCEEEEE		28.7223612710
663PhosphorylationPRFFRLNSNNALIEF
CEEEEECCCCHHHHH		35.7328355574
675PhosphorylationIEFLLEGTPEIREHY
HHHHHCCCHHHHHHH		14.3623532336
694UbiquitinationKDVDRHLKSACEQFI
HHHHHHHHHHHHHHH		29.8629967540
717PhosphorylationEQLEEFMTKVSALKT
HHHHHHHHHHHHHHH		33.35-
723UbiquitinationMTKVSALKTMASQGG
HHHHHHHHHHHHCCC		35.6529967540
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 COG3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of COG3_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 COG3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
COG1_HUMANCOG1physical
11929878
COG8_HUMANCOG8physical
11929878
COG4_HUMANCOG4physical
11929878
COG2_HUMANCOG2physical
11929878
COG6_HUMANCOG6physical
11929878
COG6_HUMANCOG6physical
22939629
COG4_HUMANCOG4physical
22939629
COG8_HUMANCOG8physical
22939629
COG7_HUMANCOG7physical
22939629
COG5_HUMANCOG5physical
22939629
SC24C_HUMANSEC24Cphysical
22939629
ACTZ_HUMANACTR1Aphysical
22863883
CDC73_HUMANCDC73physical
22863883
ML12A_HUMANMYL12Aphysical
22863883
RABL6_HUMANRABL6physical
22863883
COG4_HUMANCOG4physical
26186194
COG6_HUMANCOG6physical
26186194
COG7_HUMANCOG7physical
26186194
HAUS1_HUMANHAUS1physical
26186194
COG8_HUMANCOG8physical
26186194
COG5_HUMANCOG5physical
26186194
COG2_HUMANCOG2physical
26186194
CCD18_HUMANCCDC18physical
26186194
COG1_HUMANCOG1physical
26186194
TBCC_HUMANTBCCphysical
26186194
HAUS4_HUMANHAUS4physical
26186194
CP250_HUMANCEP250physical
26186194
HAUS3_HUMANHAUS3physical
26186194
NEUA_HUMANCMASphysical
26186194
CLIC1_HUMANCLIC1physical
26344197
COG1_HUMANCOG1physical
26344197
COG4_HUMANCOG4physical
26344197
COG6_HUMANCOG6physical
26344197
COG7_HUMANCOG7physical
26344197
COG6_HUMANCOG6physical
28514442
CCD18_HUMANCCDC18physical
28514442
COG1_HUMANCOG1physical
28514442
COG8_HUMANCOG8physical
28514442
COG7_HUMANCOG7physical
28514442
COG2_HUMANCOG2physical
28514442
COG4_HUMANCOG4physical
28514442
TBCC_HUMANTBCCphysical
28514442
HAUS3_HUMANHAUS3physical
28514442
HAUS4_HUMANHAUS4physical
28514442
CP250_HUMANCEP250physical
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 COG3_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.
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides.";
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.;
Nat. Biotechnol. 21:566-569(2003).
Cited for: PROTEIN SEQUENCE OF 2-16, AND ACETYLATION AT ALA-2.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, 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-533 AND SER-663, ANDMASS SPECTROMETRY.

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