GNAT2_HUMAN - dbPTM
GNAT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GNAT2_HUMAN
UniProt AC P19087
Protein Name Guanine nucleotide-binding protein G(t) subunit alpha-2
Gene Name GNAT2
Organism Homo sapiens (Human).
Sequence Length 354
Subcellular Localization
Protein Description Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Transducin is an amplifier and one of the transducers of a visual impulse that performs the coupling between rhodopsin and cGMP-phosphodiesterase..
Protein Sequence MGSGASAEDKELAKRSKELEKKLQEDADKEAKTVKLLLLGAGESGKSTIVKQMKIIHQDGYSPEECLEFKAIIYGNVLQSILAIIRAMTTLGIDYAEPSCADDGRQLNNLADSIEEGTMPPELVEVIRRLWKDGGVQACFERAAEYQLNDSASYYLNQLERITDPEYLPSEQDVLRSRVKTTGIIETKFSVKDLNFRMFDVGGQRSERKKWIHCFEGVTCIIFCAALSAYDMVLVEDDEVNRMHESLHLFNSICNHKFFAATSIVLFLNKKDLFEEKIKKVHLSICFPEYDGNNSYDDAGNYIKSQFLDLNMRKDVKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF
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
2Myristoylation------MGSGASAED
------CCCCCCHHH
34.48-
3Phosphorylation-----MGSGASAEDK
-----CCCCCCHHHH
29.8624719451
6Phosphorylation--MGSGASAEDKELA
--CCCCCCHHHHHHH
35.4024719451
17AcetylationKELAKRSKELEKKLQ
HHHHHHHHHHHHHHH
71.0530588951
21AcetylationKRSKELEKKLQEDAD
HHHHHHHHHHHHHHH
71.9930588957
35AcetylationDKEAKTVKLLLLGAG
HHHHHHHHHHHHCCC
38.357219281
44PhosphorylationLLLGAGESGKSTIVK
HHHCCCCCCCCHHHH
51.0720873877
46UbiquitinationLGAGESGKSTIVKQM
HCCCCCCCCHHHHEE
54.4221890473
47PhosphorylationGAGESGKSTIVKQMK
CCCCCCCCHHHHEEE
27.2220873877
48PhosphorylationAGESGKSTIVKQMKI
CCCCCCCHHHHEEEE
33.0229514088
51UbiquitinationSGKSTIVKQMKIIHQ
CCCCHHHHEEEEECC
40.6021906983
95PhosphorylationMTTLGIDYAEPSCAD
HHHCCCCCCCCCCCC
15.79-
178ADP-ribosylationEQDVLRSRVKTTGII
HHHHHHHHHCCCCEE
27.76-
178ADP-ribosylationEQDVLRSRVKTTGII
HHHHHHHHHCCCCEE
27.76-
192UbiquitinationIETKFSVKDLNFRMF
EEEEEEECCCCEEEE
56.13-
206PhosphorylationFDVGGQRSERKKWIH
EECCCCCCCCHHHHH
33.5923401153
271UbiquitinationIVLFLNKKDLFEEKI
HHHHHCCHHHHHHHH
59.60-
321PhosphorylationKDVKEIYSHMTCATD
CCHHHHHHHCCCCCC
16.6722210691
324PhosphorylationKEIYSHMTCATDTQN
HHHHHHCCCCCCCCC
8.1230576142
327PhosphorylationYSHMTCATDTQNVKF
HHHCCCCCCCCCCCC
41.5522210691
329PhosphorylationHMTCATDTQNVKFVF
HCCCCCCCCCCCCHH
20.0730576142
351ADP-ribosylationIKENLKDCGLF----
HHHHHCCCCCC----
4.95-
351ADP-ribosylationIKENLKDCGLF----
HHHHHCCCCCC----
4.95-

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 GNAT2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GNAT2_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 GNAT2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
U119A_HUMANUNC119physical
26186194
U119B_HUMANUNC119Bphysical
26186194
ACSL3_HUMANACSL3physical
26186194
ACSL4_HUMANACSL4physical
26186194
SNX1_HUMANSNX1physical
26186194
SNX2_HUMANSNX2physical
26186194
SNX5_HUMANSNX5physical
26186194
VP13A_HUMANVPS13Aphysical
26186194
OCAD1_HUMANOCIAD1physical
26186194
EPHA4_HUMANEPHA4physical
26186194
ARMX3_HUMANARMCX3physical
26186194
ACSL4_HUMANACSL4physical
28514442
OCAD1_HUMANOCIAD1physical
28514442
SNX5_HUMANSNX5physical
28514442
U119A_HUMANUNC119physical
28514442
ACSL3_HUMANACSL3physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
613856Achromatopsia 4 (ACHM4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GNAT2_HUMAN

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Related Literatures of Post-Translational Modification

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