GBG5_HUMAN - dbPTM
GBG5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GBG5_HUMAN
UniProt AC P63218
Protein Name Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5
Gene Name GNG5
Organism Homo sapiens (Human).
Sequence Length 68
Subcellular Localization Cell membrane
Lipid-anchor
Cytoplasmic side .
Protein Description Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction..
Protein Sequence MSGSSSVAAMKKVVQQLRLEAGLNRVKVSQAAADLKQFCLQNAQHDPLLTGVSSSTNPFRPQKVCSFL
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
2Phosphorylation------MSGSSSVAA
------CCCHHHHHH
47.5929255136
2Acetylation------MSGSSSVAA
------CCCHHHHHH
47.5920068231
4Phosphorylation----MSGSSSVAAMK
----CCCHHHHHHHH
16.4829255136
5Phosphorylation---MSGSSSVAAMKK
---CCCHHHHHHHHH
32.1529255136
6Phosphorylation--MSGSSSVAAMKKV
--CCCHHHHHHHHHH
19.9223401153
11AcetylationSSSVAAMKKVVQQLR
HHHHHHHHHHHHHHH
37.3825953088
11UbiquitinationSSSVAAMKKVVQQLR
HHHHHHHHHHHHHHH
37.3833845483
12UbiquitinationSSVAAMKKVVQQLRL
HHHHHHHHHHHHHHH
34.2624816145
18MethylationKKVVQQLRLEAGLNR
HHHHHHHHHHHCCCC
26.58-
27UbiquitinationEAGLNRVKVSQAAAD
HHCCCCHHHHHHHHH
32.6921906983
36UbiquitinationSQAAADLKQFCLQNA
HHHHHHHHHHHHHHC
41.7123000965
53PhosphorylationDPLLTGVSSSTNPFR
CCCCCCCCCCCCCCC
21.6628348404
54PhosphorylationPLLTGVSSSTNPFRP
CCCCCCCCCCCCCCC
38.4826657352
55PhosphorylationLLTGVSSSTNPFRPQ
CCCCCCCCCCCCCCH
25.3828348404
56PhosphorylationLTGVSSSTNPFRPQK
CCCCCCCCCCCCCHH
49.1926657352
65MethylationPFRPQKVCSFL----
CCCCHHHHHCC----
2.83-
65GeranylgeranylationPFRPQKVCSFL----
CCCCHHHHHCC----
2.83-

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 GBG5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GBG5_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 GBG5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GNB5_HUMANGNB5physical
8636150
GBB1_HUMANGNB1physical
8636150
GBB2_HUMANGNB2physical
8636150
GBB3_HUMANGNB3physical
8636150
GBB4_HUMANGNB4physical
8636150
GBB1_HUMANGNB1physical
19168127
GBB2_HUMANGNB2physical
19168127
GBB3_HUMANGNB3physical
19168127
GBB3_HUMANGNB3physical
22940628
GOGA2_HUMANGOLGA2physical
25416956
K1H1_HUMANKRT31physical
25416956
MDFI_HUMANMDFIphysical
25416956
TRAF1_HUMANTRAF1physical
25416956
AMOL2_HUMANAMOTL2physical
25416956
EP15R_HUMANEPS15L1physical
25416956
K1C40_HUMANKRT40physical
25416956

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 GBG5_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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 2-18, AND ACETYLATION AT SER-2.

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