GNAI3_HUMAN - dbPTM
GNAI3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GNAI3_HUMAN
UniProt AC P08754
Protein Name Guanine nucleotide-binding protein G(k) subunit alpha {ECO:0000303|PubMed:2452165}
Gene Name GNAI3
Organism Homo sapiens (Human).
Sequence Length 354
Subcellular Localization Cytoplasm . Cell membrane . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Membrane
Lipid-anchor . Localizes in the centrosomes of interphase and mitotic cells. Detected at the cleavage furrow and/or the midbody.
Protein Description Heterotrimeric guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Signaling by an activated GPCR promotes GDP release and GTP binding. The alpha subunit has a low GTPase activity that converts bound GTP to GDP, thereby terminating the signal. Both GDP release and GTP hydrolysis are modulated by numerous regulatory proteins. [PubMed: 8774883]
Protein Sequence MGCTLSAEDKAAVERSKMIDRNLREDGEKAAKEVKLLLLGAGESGKSTIVKQMKIIHEDGYSEDECKQYKVVVYSNTIQSIIAIIRAMGRLKIDFGEAARADDARQLFVLAGSAEEGVMTPELAGVIKRLWRDGGVQACFSRSREYQLNDSASYYLNDLDRISQSNYIPTQQDVLRTRVKTTGIVETHFTFKDLYFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTETSIILFLNKKDLFEEKIKRSPLTICYPEYTGSNTYEEAAAYIQCQFEDLNRRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKECGLY
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------MGCTLSAED
------CCCCCCHHH		17.0825255805
3S-palmitoylation-----MGCTLSAEDK
-----CCCCCCHHHH		3.14-
17UbiquitinationKAAVERSKMIDRNLR
HHHHHHHHHHCHHHH		46.2029967540
29UbiquitinationNLREDGEKAAKEVKL
HHHHHHHHHHHHHHH		60.2121906983
32UbiquitinationEDGEKAAKEVKLLLL
HHHHHHHHHHHHHEE		68.8222817900
35UbiquitinationEKAAKEVKLLLLGAG
HHHHHHHHHHEECCC		34.2121906983
35UbiquitinationEKAAKEVKLLLLGAG
HHHHHHHHHHEECCC		34.2121890473
35AcetylationEKAAKEVKLLLLGAG
HHHHHHHHHHEECCC		34.2126051181
44PhosphorylationLLLGAGESGKSTIVK
HEECCCCCCCCHHHH		51.0720873877
46UbiquitinationLGAGESGKSTIVKQM
ECCCCCCCCHHHHEE		54.4223000965
47PhosphorylationGAGESGKSTIVKQMK
CCCCCCCCHHHHEEE		27.2220873877
48PhosphorylationAGESGKSTIVKQMKI
CCCCCCCHHHHEEEE		33.0229514088
51UbiquitinationSGKSTIVKQMKIIHE
CCCCHHHHEEEEECC		40.6023000965
54AcetylationSTIVKQMKIIHEDGY
CHHHHEEEEECCCCC		35.6927452117
54UbiquitinationSTIVKQMKIIHEDGY
CHHHHEEEEECCCCC		35.6922817900
61PhosphorylationKIIHEDGYSEDECKQ
EEECCCCCCHHHHCE		22.6221082442
62PhosphorylationIIHEDGYSEDECKQY
EECCCCCCHHHHCEE		44.0628152594
67AcetylationGYSEDECKQYKVVVY
CCCHHHHCEEEEEEE		55.4026051181
67UbiquitinationGYSEDECKQYKVVVY
CCCHHHHCEEEEEEE		55.4029967540
69PhosphorylationSEDECKQYKVVVYSN
CHHHHCEEEEEEECC		7.4025884760
70AcetylationEDECKQYKVVVYSNT
HHHHCEEEEEEECCH		26.517367651
75O-linked_GlycosylationQYKVVVYSNTIQSII
EEEEEEECCHHHHHH		18.8528411811
77O-linked_GlycosylationKVVVYSNTIQSIIAI
EEEEECCHHHHHHHH		17.9128411811
80O-linked_GlycosylationVYSNTIQSIIAIIRA
EECCHHHHHHHHHHH		16.4728411811
92UbiquitinationIRAMGRLKIDFGEAA
HHHHCCCCCCHHHHH		38.5823000965
92UbiquitinationIRAMGRLKIDFGEAA
HHHHCCCCCCHHHHH		38.5821890473
92AcetylationIRAMGRLKIDFGEAA
HHHHCCCCCCHHHHH		38.5826051181
92SumoylationIRAMGRLKIDFGEAA
HHHHCCCCCCHHHHH		38.58-
128UbiquitinationPELAGVIKRLWRDGG
HHHHHHHHHHHHCCC		38.7521906983
144MethylationQACFSRSREYQLNDS
EEEEECCCCEECCCC		45.60-
161MethylationYYLNDLDRISQSNYI
HHHCCHHHHHHCCCC		37.44-
163PhosphorylationLNDLDRISQSNYIPT
HCCHHHHHHCCCCCC		28.5725850435
165PhosphorylationDLDRISQSNYIPTQQ
CHHHHHHCCCCCCHH		25.4728152594
167PhosphorylationDRISQSNYIPTQQDV
HHHHHCCCCCCHHHH		17.3328152594
178ADP-ribosylationQQDVLRTRVKTTGIV
HHHHHHHHHCCCCEE		22.85-
178ADP-ribosylationQQDVLRTRVKTTGIV
HHHHHHHHHCCCCEE		22.85-
180UbiquitinationDVLRTRVKTTGIVET
HHHHHHHCCCCEEEE		36.7630230243
192UbiquitinationVETHFTFKDLYFKMF
EEEEEEEHHHEEEEE		43.7121890473
192UbiquitinationVETHFTFKDLYFKMF
EEEEEEEHHHEEEEE		43.7123000965
197AcetylationTFKDLYFKMFDVGGQ
EEHHHEEEEEECCCC		25.7127452117
197UbiquitinationTFKDLYFKMFDVGGQ
EEHHHEEEEEECCCC		25.7123000965
204Deamidated glutamineKMFDVGGQRSERKKW
EEEECCCCCCCHHHH		39.54-
204DeamidationKMFDVGGQRSERKKW
EEEECCCCCCCHHHH		39.5424141704
206PhosphorylationFDVGGQRSERKKWIH
EECCCCCCCHHHHHH		33.5923401153
248UbiquitinationNRMHESMKLFDSICN
HHHHHHHHHHHHHHC		56.1121890473
248UbiquitinationNRMHESMKLFDSICN
HHHHHHHHHHHHHHC		56.1123000965
252PhosphorylationESMKLFDSICNNKWF
HHHHHHHHHHCCCCC		23.0025159151
257UbiquitinationFDSICNNKWFTETSI
HHHHHCCCCCCHHEE		29.6823503661
271UbiquitinationIILFLNKKDLFEEKI
EEEEECHHHHHHHHH		59.60-
277UbiquitinationKKDLFEEKIKRSPLT
HHHHHHHHHHCCCCE		46.4521890473
277AcetylationKKDLFEEKIKRSPLT
HHHHHHHHHHCCCCE		46.4527452117
317UbiquitinationLNRRKDTKEIYTHFT
HCCCCCCCHHCCEEE		52.8530230243
317AcetylationLNRRKDTKEIYTHFT
HCCCCCCCHHCCEEE		52.8526051181
320PhosphorylationRKDTKEIYTHFTCAT
CCCCCHHCCEEEECC		8.6828152594
330UbiquitinationFTCATDTKNVQFVFD
EEECCCCCCCEEEHH		58.9133845483
345UbiquitinationAVTDVIIKNNLKECG
HHHHHHHHCCCHHCC		28.7632015554
349UbiquitinationVIIKNNLKECGLY--
HHHHCCCHHCCCC--		53.7527667366
351ADP-ribosylationIKNNLKECGLY----
HHCCCHHCCCC----		4.32-
351ADP-ribosylationIKNNLKECGLY----
HHCCCHHCCCC----		4.32-
354PhosphorylationNLKECGLY-------
CCHHCCCC-------		11.2025884760
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
-KUbiquitinationE3 ubiquitin ligaseOSTM1Q86WC4
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
204QAmidation

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 GNAI3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUCB1_RATNucb1physical
9647645
RGS10_HUMANRGS10physical
8774883
RGS14_HUMANRGS14physical
11387333
RGS12_HUMANRGS12physical
11387333
GBB1_HUMANGNB1physical
22186894
KAP3_HUMANPRKAR2Bphysical
22186894
NUCB1_HUMANNUCB1physical
21988832
NUCB2_HUMANNUCB2physical
21988832
RAGP1_HUMANRANGAP1physical
21988832
RGS14_HUMANRGS14physical
21988832
SOX30_HUMANSOX30physical
21988832
CPNS1_HUMANCAPNS1physical
22863883
IF5_HUMANEIF5physical
22863883
UBFD1_HUMANUBFD1physical
22863883
VINC_HUMANVCLphysical
22863883
XPO1_HUMANXPO1physical
22863883
1433F_HUMANYWHAHphysical
22863883
1433T_HUMANYWHAQphysical
22863883
RGS17_HUMANRGS17physical
25416956
GPSM3_HUMANGPSM3physical
25416956
DAPLE_HUMANCCDC88Cphysical
25416956
GPSM1_HUMANGPSM1physical
21209316
GRDN_HUMANCCDC88Aphysical
21209316
GBG4_HUMANGNG4physical
26186194
RPGP1_HUMANRAP1GAPphysical
26186194
GNAI2_HUMANGNAI2physical
26186194
GNAO_HUMANGNAO1physical
26186194
GNAT2_HUMANGNAT2physical
26186194
CLH2_HUMANCLTCL1physical
26186194
AT2A3_HUMANATP2A3physical
26186194
RGS12_HUMANRGS12physical
26186194
RDH13_HUMANRDH13physical
26186194
RIC8A_HUMANRIC8Aphysical
26186194
OSBP1_HUMANOSBPphysical
26186194
GBG10_HUMANGNG10physical
26186194
AAAS_HUMANAAASphysical
26186194
ALG6_HUMANALG6physical
26186194
UBP33_HUMANUSP33physical
26186194
GBB1_HUMANGNB1physical
26186194
GBB2_HUMANGNB2physical
26186194
GBB4_HUMANGNB4physical
26186194
NDC1_HUMANNDC1physical
26186194
GBG5_HUMANGNG5physical
26186194
TM222_HUMANTMEM222physical
26186194
GRDN_HUMANCCDC88Aphysical
26186194
GBG11_HUMANGNG11physical
26186194
RGS14_HUMANRGS14physical
26186194
DCNL5_HUMANDCUN1D5physical
26186194
AN13B_HUMANANKRD13Bphysical
26186194
GPSM1_HUMANGPSM1physical
26186194
GBG7_HUMANGNG7physical
26186194
PSMD3_HUMANPSMD3physical
26344197
GPSM3_HUMANGPSM3physical
21516116
RGS12_HUMANRGS12physical
28514442
GNAO_HUMANGNAO1physical
28514442
RGS14_HUMANRGS14physical
28514442
GPSM1_HUMANGPSM1physical
28514442
GNAT2_HUMANGNAT2physical
28514442
RIC8A_HUMANRIC8Aphysical
28514442
AN13B_HUMANANKRD13Bphysical
28514442
RPGP1_HUMANRAP1GAPphysical
28514442
GBB2_HUMANGNB2physical
28514442
GBG5_HUMANGNG5physical
28514442
GNAI2_HUMANGNAI2physical
28514442
GBG10_HUMANGNG10physical
28514442
TM222_HUMANTMEM222physical
28514442
GBG7_HUMANGNG7physical
28514442
GBB4_HUMANGNB4physical
28514442
AT2A3_HUMANATP2A3physical
28514442
NDC1_HUMANNDC1physical
28514442
DCNL5_HUMANDCUN1D5physical
28514442
GBG11_HUMANGNG11physical
28514442
GBB1_HUMANGNB1physical
28514442
CLH2_HUMANCLTCL1physical
28514442
RASA3_RATRasa3physical
18952607
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
602483Auriculocondylar syndrome 1 (ARCND1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GNAI3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-354, AND MASSSPECTROMETRY.
"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.

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