GNAI2_HUMAN - dbPTM
GNAI2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GNAI2_HUMAN
UniProt AC P04899
Protein Name Guanine nucleotide-binding protein G(i) subunit alpha-2
Gene Name GNAI2
Organism Homo sapiens (Human).
Sequence Length 355
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cell membrane . Membrane
Lipid-anchor . Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody.
Protein Description Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. May play a role in cell division.; Isoform sGi2: Regulates the cell surface density of dopamine receptors DRD2 by sequestrating them as an intracellular pool..
Protein Sequence MGCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEDGYSEEECRQYRAVVYSNTIQSIMAIVKAMGNLQIDFADPSRADDARQLFALSCTAEEQGVLPDDLSGVIRRLWADHGVQACFGRSREYQLNDSAAYYLNDLERIAQSDYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSAYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKITHSPLTICFPEYTGANKYDEAASYIQSKFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF
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------MGCTVSAED
------CCCCCCHHH		18.7922223895
3S-palmitoylation-----MGCTVSAEDK
-----CCCCCCHHHH		3.07-
4Phosphorylation----MGCTVSAEDKA
----CCCCCCHHHHH		16.2728258704
6O-linked_Glycosylation--MGCTVSAEDKAAA
--CCCCCCHHHHHHH		14.0525367160
6Phosphorylation--MGCTVSAEDKAAA
--CCCCCCHHHHHHH		14.0529083192
16O-linked_GlycosylationDKAAAERSKMIDKNL
HHHHHHHHHHHCHHH		20.3425367160
17UbiquitinationKAAAERSKMIDKNLR
HHHHHHHHHHCHHHH		46.20-
21AcetylationERSKMIDKNLREDGE
HHHHHHCHHHHHHHH		47.1325953088
21UbiquitinationERSKMIDKNLREDGE
HHHHHHCHHHHHHHH		47.13-
29AcetylationNLREDGEKAAREVKL
HHHHHHHHHHHHHHH		53.5325953088
29UbiquitinationNLREDGEKAAREVKL
HHHHHHHHHHHHHHH		53.5321906983
29 (in isoform 1)Ubiquitination-53.5321890473
35AcetylationEKAAREVKLLLLGAG
HHHHHHHHHHEECCC		28.7625953088
35UbiquitinationEKAAREVKLLLLGAG
HHHHHHHHHHEECCC		28.76-
35 (in isoform 1)Ubiquitination-28.7621890473
35 (in isoform 2)Ubiquitination-28.7621890473
38UbiquitinationAREVKLLLLGAGESG
HHHHHHHEECCCCCC		6.33-
44PhosphorylationLLLGAGESGKSTIVK
HEECCCCCCCCHHHH		51.0720873877
46UbiquitinationLGAGESGKSTIVKQM
ECCCCCCCCHHHHEE		54.4221890473
46 (in isoform 1)Ubiquitination-54.4221890473
47PhosphorylationGAGESGKSTIVKQMK
CCCCCCCCHHHHEEE		27.2220873877
48PhosphorylationAGESGKSTIVKQMKI
CCCCCCCHHHHEEEE		33.0229514088
51UbiquitinationSGKSTIVKQMKIIHE
CCCCHHHHEEEEECC		40.6021906983
51 (in isoform 1)Ubiquitination-40.6021890473
54AcetylationSTIVKQMKIIHEDGY
CHHHHEEEEECCCCC		35.6926051181
54UbiquitinationSTIVKQMKIIHEDGY
CHHHHEEEEECCCCC		35.69-
61PhosphorylationKIIHEDGYSEEECRQ
EEECCCCCCHHHHHH		25.8225884760
62PhosphorylationIIHEDGYSEEECRQY
EECCCCCCHHHHHHH		44.0226356563
66S-palmitoylationDGYSEEECRQYRAVV
CCCCHHHHHHHHHHH		3.5829575903
69PhosphorylationSEEECRQYRAVVYSN
CHHHHHHHHHHHCHH		4.9222817900
88SulfoxidationIMAIVKAMGNLQIDF
HHHHHHHHCCCEEEE		2.7921406390
111O-linked_GlycosylationARQLFALSCTAEEQG
HHHHHHHHCCHHHCC		13.1425367160
112GlutathionylationRQLFALSCTAEEQGV
HHHHHHHCCHHHCCC		4.3222555962
112S-palmitoylationRQLFALSCTAEEQGV
HHHHHHHCCHHHCCC		4.3229575903
113O-linked_GlycosylationQLFALSCTAEEQGVL
HHHHHHCCHHHCCCC		33.4625367160
125O-linked_GlycosylationGVLPDDLSGVIRRLW
CCCCCCHHHHHHHHH		37.7025367160
141UbiquitinationDHGVQACFGRSREYQ
HHCHHHHCCCCCCEE		11.6121890473
144PhosphorylationVQACFGRSREYQLND
HHHHCCCCCCEECCC		29.8222817900
146UbiquitinationACFGRSREYQLNDSA
HHCCCCCCEECCCCH		38.5921890473
147PhosphorylationCFGRSREYQLNDSAA
HCCCCCCEECCCCHH		19.72-
155PhosphorylationQLNDSAAYYLNDLER
ECCCCHHHHHHHHHH		14.27-
156UbiquitinationLNDSAAYYLNDLERI
CCCCHHHHHHHHHHH		8.3621890473
161UbiquitinationAYYLNDLERIAQSDY
HHHHHHHHHHHHCCC		44.9221890473
168PhosphorylationERIAQSDYIPTQQDV
HHHHHCCCCCCHHHH		17.6622817900
177UbiquitinationPTQQDVLRTRVKTTG
CCHHHHHHHHHCCCC		21.9721890473
177 (in isoform 2)Ubiquitination-21.9721890473
179ADP-ribosylationQQDVLRTRVKTTGIV
HHHHHHHHHCCCCEE		22.85-
179ADP-ribosylationQQDVLRTRVKTTGIV
HHHHHHHHHCCCCEE		22.85-
182UbiquitinationVLRTRVKTTGIVETH
HHHHHHCCCCEEEEE		27.6521890473
182 (in isoform 2)Ubiquitination-27.6521890473
193UbiquitinationVETHFTFKDLHFKMF
EEEEEEECCEEEEEE		57.21-
193 (in isoform 1)Ubiquitination-57.2121890473
193UbiquitinationVETHFTFKDLHFKMF
EEEEEEECCEEEEEE		57.2121890473
197UbiquitinationFTFKDLHFKMFDVGG
EEECCEEEEEEECCC		8.7921890473
198AcetylationTFKDLHFKMFDVGGQ
EECCEEEEEEECCCC		28.1026822725
198UbiquitinationTFKDLHFKMFDVGGQ
EECCEEEEEEECCCC		28.10-
198 (in isoform 1)Ubiquitination-28.1021890473
198UbiquitinationTFKDLHFKMFDVGGQ
EECCEEEEEEECCCC		28.1021890473
205Deamidated glutamineKMFDVGGQRSERKKW
EEEECCCCCCCHHHH		39.54-
205DeamidationKMFDVGGQRSERKKW
EEEECCCCCCCHHHH		39.5424141704
207PhosphorylationFDVGGQRSERKKWIH
EECCCCCCCHHHHHH		33.5923401153
212UbiquitinationQRSERKKWIHCFEGV
CCCCHHHHHHHHHHH		6.6521890473
233UbiquitinationVALSAYDLVLAEDEE
HHHHHHHHHHHCHHH		1.9021890473
233 (in isoform 2)Ubiquitination-1.9021890473
249AcetylationNRMHESMKLFDSICN
HHHHHHHHHHHHHHC		56.1125953088
249UbiquitinationNRMHESMKLFDSICN
HHHHHHHHHHHHHHC		56.1121890473
249 (in isoform 1)Ubiquitination-56.1121890473
249UbiquitinationNRMHESMKLFDSICN
HHHHHHHHHHHHHHC		56.1121890473
253PhosphorylationESMKLFDSICNNKWF
HHHHHHHHHHCCCCC		23.0020873877
255UbiquitinationMKLFDSICNNKWFTD
HHHHHHHHCCCCCCC		5.4821890473
256UbiquitinationKLFDSICNNKWFTDT
HHHHHHHCCCCCCCC		51.99-
261PhosphorylationICNNKWFTDTSIILF
HHCCCCCCCCEEEEE		36.9328857561
263PhosphorylationNNKWFTDTSIILFLN
CCCCCCCCEEEEEEE		20.8328857561
270UbiquitinationTSIILFLNKKDLFEE
CEEEEEEEHHHHHHH		41.8321890473
272UbiquitinationIILFLNKKDLFEEKI
EEEEEEHHHHHHHHC		59.60-
278UbiquitinationKKDLFEEKITHSPLT
HHHHHHHHCCCCCCE		45.78-
280UbiquitinationDLFEEKITHSPLTIC
HHHHHHCCCCCCEEE		27.63-
282PhosphorylationFEEKITHSPLTICFP
HHHHCCCCCCEEECC		16.9825627689
291UbiquitinationLTICFPEYTGANKYD
CEEECCCCCCCCCHH		15.6521890473
291 (in isoform 2)Ubiquitination-15.6521890473
296AcetylationPEYTGANKYDEAASY
CCCCCCCCHHHHHHH		54.2526051181
296UbiquitinationPEYTGANKYDEAASY
CCCCCCCCHHHHHHH		54.25-
297UbiquitinationEYTGANKYDEAASYI
CCCCCCCHHHHHHHH		20.87-
297PhosphorylationEYTGANKYDEAASYI
CCCCCCCHHHHHHHH		20.8729978859
299UbiquitinationTGANKYDEAASYIQS
CCCCCHHHHHHHHHH		42.94-
302UbiquitinationNKYDEAASYIQSKFE
CCHHHHHHHHHHHHH		29.80-
302PhosphorylationNKYDEAASYIQSKFE
CCHHHHHHHHHHHHH		29.8029978859
303PhosphorylationKYDEAASYIQSKFED
CHHHHHHHHHHHHHH		9.7729978859
306PhosphorylationEAASYIQSKFEDLNK
HHHHHHHHHHHHHHH		29.7429978859
307UbiquitinationAASYIQSKFEDLNKR
HHHHHHHHHHHHHHC		36.0821890473
307 (in isoform 1)Ubiquitination-36.0821890473
307UbiquitinationAASYIQSKFEDLNKR
HHHHHHHHHHHHHHC		36.0821890473
313UbiquitinationSKFEDLNKRKDTKEI
HHHHHHHHCCCCCHH		69.03-
315UbiquitinationFEDLNKRKDTKEIYT
HHHHHHCCCCCHHHH		71.94-
318UbiquitinationLNKRKDTKEIYTHFT
HHHCCCCCHHHHHEE		52.85-
321PhosphorylationRKDTKEIYTHFTCAT
CCCCCHHHHHEEECC		8.6828152594
334UbiquitinationATDTKNVQFVFDAVT
CCCCCCCEEEHHHHH		37.87-
350UbiquitinationVIIKNNLKDCGLF--
HHHHCCCCCCCCC--		53.77-
352ADP-ribosylationIKNNLKDCGLF----
HHCCCCCCCCC----		4.95-
352ADP-ribosylationIKNNLKDCGLF----
HHCCCCCCCCC----		4.95-
352S-palmitoylationIKNNLKDCGLF----
HHCCCCCCCCC----		4.9529575903
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
44SPhosphorylationKinasePRKCEQ02156
GPS
144SPhosphorylationKinasePRKCEQ02156
GPS
302SPhosphorylationKinasePRKCEQ02156
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
205QAmidation

24141704
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 GNAI2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MDFI_HUMANMDFIphysical
16189514
PLS1_HUMANPLSCR1physical
16189514
TBA1A_MOUSETuba1aphysical
16169070
NUCB1_HUMANNUCB1physical
9647645
EYA2_HUMANEYA2physical
10906137
ITCH_HUMANITCHphysical
23071112
GNAI3_HUMANGNAI3physical
22939629
SRSF1_HUMANSRSF1physical
22939629
MYH10_HUMANMYH10physical
22939629
PLEC_HUMANPLECphysical
22939629
NCF2_HUMANNCF2physical
16782902
NPM_HUMANNPM1physical
21988832
GDIA_HUMANGDI1physical
22863883
NAGK_HUMANNAGKphysical
22863883
SCRN1_HUMANSCRN1physical
22863883
K1H1_HUMANKRT31physical
25416956
MDFI_HUMANMDFIphysical
25416956
TRIP6_HUMANTRIP6physical
25416956
RGS20_HUMANRGS20physical
25416956
GPSM3_HUMANGPSM3physical
25416956
K1C40_HUMANKRT40physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
CXCR5_HUMANCXCR5physical
23773523
GNAO_HUMANGNAO1physical
26186194
RIC8B_HUMANRIC8Bphysical
26186194
RIC8A_HUMANRIC8Aphysical
26186194
S35B2_HUMANSLC35B2physical
26186194
IQGA2_HUMANIQGAP2physical
26186194
MCU_HUMANMCUphysical
26186194
GBG10_HUMANGNG10physical
26186194
RINT1_HUMANRINT1physical
26186194
ECM29_HUMANKIAA0368physical
26186194
GBG4_HUMANGNG4physical
26186194
MCUB_HUMANCCDC109Bphysical
26186194
LMBD2_HUMANLMBRD2physical
26186194
PM34_HUMANSLC25A17physical
26186194
PAQR1_HUMANADIPOR1physical
26186194
ADCK1_HUMANADCK1physical
26186194
GRDN_HUMANCCDC88Aphysical
26186194
GBB3_HUMANGNB3physical
26186194
GBB4_HUMANGNB4physical
26186194
MFS4B_HUMANKIAA1919physical
26186194
NLRX1_HUMANNLRX1physical
26186194
ARL8A_HUMANARL8Aphysical
26186194
GBG5_HUMANGNG5physical
26186194
S39A6_HUMANSLC39A6physical
26186194
ABCB6_HUMANABCB6physical
26186194
BRAT1_HUMANBRAT1physical
26186194
VAC14_HUMANVAC14physical
26186194
GBG7_HUMANGNG7physical
26186194
4F2_HUMANSLC3A2physical
26344197
GNAO_HUMANGNAO1physical
28514442
RIC8A_HUMANRIC8Aphysical
28514442
GBB3_HUMANGNB3physical
28514442
GBG7_HUMANGNG7physical
28514442
GBB4_HUMANGNB4physical
28514442
GBG10_HUMANGNG10physical
28514442
MFS4B_HUMANKIAA1919physical
28514442
PAQR1_HUMANADIPOR1physical
28514442
MCUB_HUMANCCDC109Bphysical
28514442
MCU_HUMANMCUphysical
28514442
GBG5_HUMANGNG5physical
28514442
ABCB6_HUMANABCB6physical
28514442
LMBD2_HUMANLMBRD2physical
28514442
LMNB1_HUMANLMNB1physical
28514442
GRDN_HUMANCCDC88Aphysical
28514442
ADCK1_HUMANADCK1physical
28514442
ARL8A_HUMANARL8Aphysical
28514442
Drug and Disease Associations
Kegg Disease
H00033 Adrenal carcinoma
H01019 Catecholaminergic polymorphic ventricular tachycardia
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 GNAI2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-69, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory