GOG6A_HUMAN - dbPTM
GOG6A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GOG6A_HUMAN
UniProt AC Q9NYA3
Protein Name Golgin subfamily A member 6A
Gene Name GOLGA6A
Organism Homo sapiens (Human).
Sequence Length 693
Subcellular Localization
Protein Description
Protein Sequence MWPQPYLPPHPMMLEESRQNKLAAAKKKLKEYQQRKSPGIPAGAKTKKKKTDSSPETTTSGGCHSPGDSQYQELAVALESSSVTISQLNENIESLKQQKKQVEHQLEEAKKTNNEIHKAQMERLETINILTLEKADLKTTLYHTKRAARHFEEESKDLAGRLQYSLQRIQELERALCAVSTQQQEEDRSSSCREAVLQRWLQQTIKERALLNAHVTQVTESLKQVQLERDEYAKHIKGERARWQERMWKMSVEARTLKEEKKRDIHRIQELERSLSELKNQMAEPPSLAPPAVTSVVEQLQDEAKHLRQEVEGLEGKLQSQVENNQALSLLSKEQKQRLQEQEEMLREQEAQRVREQERLCEQNERLREQQKTLQEQGERLRKQEQRLRKQEERLRKEEERLQKQEKRLWDQEERLWKKEERLQKQEERLALSQNHKLDKQLAEPQCSFEDLNNEKKSALQLEQQVKELQEKLDEEHLEAASHQNQQLETQLSLVALPGEGDGGQHLDSEEEEAPRPTPNIPEDLESREATSSFMDLPKEKADGTEQVERRELGFVQPSGVTDGMRESFTVYESQGAVPNTRHQEMEDVIRLAQKEEEMKVKLLELQELVLPLVGNHEGHGKFLIAAQNPADEPTPGAPAPQELGAAGEQDVFYEVSLDNNVEPAPGAAREGSPHDNPTVQQIVQLSPVMQDT
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
6Phosphorylation--MWPQPYLPPHPMM
--CCCCCCCCCCCCC
26.9624043423
17PhosphorylationHPMMLEESRQNKLAA
CCCCCHHHHHHHHHH
29.7724043423
37PhosphorylationKEYQQRKSPGIPAGA
HHHHHHHCCCCCCCC
30.4626714015
45AcetylationPGIPAGAKTKKKKTD
CCCCCCCCCCCCCCC
61.02-
47AcetylationIPAGAKTKKKKTDSS
CCCCCCCCCCCCCCC
62.9918584635
47UbiquitinationIPAGAKTKKKKTDSS
CCCCCCCCCCCCCCC
62.99-
48AcetylationPAGAKTKKKKTDSSP
CCCCCCCCCCCCCCC
65.8118584641
48UbiquitinationPAGAKTKKKKTDSSP
CCCCCCCCCCCCCCC
65.81-
49AcetylationAGAKTKKKKTDSSPE
CCCCCCCCCCCCCCC
63.5618584647
49UbiquitinationAGAKTKKKKTDSSPE
CCCCCCCCCCCCCCC
63.56-
131PhosphorylationLETINILTLEKADLK
HHHCEEEEEECCCHH
29.13-
144PhosphorylationLKTTLYHTKRAARHF
HHHHHHHHHHHHHHC
14.52-
155PhosphorylationARHFEEESKDLAGRL
HHHCHHHHHHHHHHH
34.4521815630
189PhosphorylationQQQEEDRSSSCREAV
HHHHHHHCHHHHHHH
38.64-
190PhosphorylationQQEEDRSSSCREAVL
HHHHHHCHHHHHHHH
34.06-
329PhosphorylationVENNQALSLLSKEQK
HHHHHHHHHHCHHHH
30.2224719451
433PhosphorylationQEERLALSQNHKLDK
HHHHHHHHHHHHHHH
24.2722817900
448PhosphorylationQLAEPQCSFEDLNNE
HHCCCCCCHHHCCHH
26.8230622161
458PhosphorylationDLNNEKKSALQLEQQ
HCCHHHHHHHHHHHH
45.3330622161
531PhosphorylationDLESREATSSFMDLP
HHHCCHHCCCCCCCC
21.8330622161
532PhosphorylationLESREATSSFMDLPK
HHCCHHCCCCCCCCH
28.7330622161
533PhosphorylationESREATSSFMDLPKE
HCCHHCCCCCCCCHH
21.8930622161
673PhosphorylationPGAAREGSPHDNPTV
CCCCCCCCCCCCCCH
17.8225693802
679PhosphorylationGSPHDNPTVQQIVQL
CCCCCCCCHHHHHHH
36.8825693802

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 GOG6A_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GOG6A_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 GOG6A_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GOG6A_HUMAN !!

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 GOG6A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-433, AND MASSSPECTROMETRY.

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