GNAS2_HUMAN - dbPTM
GNAS2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GNAS2_HUMAN
UniProt AC P63092
Protein Name Guanine nucleotide-binding protein G(s) subunit alpha isoforms short
Gene Name GNAS
Organism Homo sapiens (Human).
Sequence Length 394
Subcellular Localization Cell membrane
Lipid-anchor .
Protein Description Guanine nucleotide-binding proteins (G proteins) function as transducers in numerous signaling pathways controlled by G protein-coupled receptors (GPCRs). [PubMed: 17110384 Signaling involves the activation of adenylyl cyclases, resulting in increased levels of the signaling molecule cAMP]
Protein Sequence MGCLGNSKTEDQRNEEKAQREANKKIEKQLQKDKQVYRATHRLLLLGAGESGKSTIVKQMRILHVNGFNGEGGEEDPQAARSNSDGEKATKVQDIKNNLKEAIETIVAAMSNLVPPVELANPENQFRVDYILSVMNVPDFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDLLAEKVLAGKSKIEDYFPEFARYTTPEDATPEPGEDPRVTRAKYFIRDEFLRISTASGDGRHYCYPHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL
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
2N-palmitoylation------MGCLGNSKT
------CCCCCCCCC		18.50-
3S-palmitoylation-----MGCLGNSKTE
-----CCCCCCCCCH		4.2029575903
8UbiquitinationMGCLGNSKTEDQRNE
CCCCCCCCCHHHHHH		60.99-
8 (in isoform 3)Ubiquitination-60.99-
9PhosphorylationGCLGNSKTEDQRNEE
CCCCCCCCHHHHHHH		44.6129759185
9 (in isoform 2)Phosphorylation-44.6129759185
9 (in isoform 3)Phosphorylation-44.6129759185
9 (in isoform 4)Phosphorylation-44.6129759185
17UbiquitinationEDQRNEEKAQREANK
HHHHHHHHHHHHHHH		43.5721906983
17 (in isoform 2)Ubiquitination-43.5721890473
17 (in isoform 1)Ubiquitination-43.5721890473
28UbiquitinationEANKKIEKQLQKDKQ
HHHHHHHHHHHHHHH		60.83-
51PhosphorylationLLLGAGESGKSTIVK
HHHCCCCCCCCHHHE		51.07-
53UbiquitinationLGAGESGKSTIVKQM
HCCCCCCCCHHHEEE		54.4221890473
53 (in isoform 3)Ubiquitination-54.4221890473
53 (in isoform 2)Ubiquitination-54.4221890473
53UbiquitinationLGAGESGKSTIVKQM
HCCCCCCCCHHHEEE		54.4221890473
53 (in isoform 1)Ubiquitination-54.4221890473
58UbiquitinationSGKSTIVKQMRILHV
CCCCHHHEEEEEEEE		34.2321890473
58 (in isoform 3)Ubiquitination-34.2321890473
58 (in isoform 2)Ubiquitination-34.2321890473
58UbiquitinationSGKSTIVKQMRILHV
CCCCHHHEEEEEEEE		34.2321890473
58 (in isoform 1)Ubiquitination-34.2321890473
73 (in isoform 3)Ubiquitination-30.7121890473
74 (in isoform 2)Ubiquitination-70.8121890473
76 (in isoform 3)Ubiquitination-35.9921890473
77 (in isoform 2)Ubiquitination-29.0521890473
81 (in isoform 3)Ubiquitination-39.1121890473
82 (in isoform 4)Phosphorylation-35.6422210691
82 (in isoform 2)Ubiquitination-35.6421890473
84 (in isoform 4)Phosphorylation-48.5222210691
88UbiquitinationRSNSDGEKATKVQDI
HCCCCCCCCHHHHHH		67.8721906983
88 (in isoform 1)Ubiquitination-67.8721890473
91UbiquitinationSDGEKATKVQDIKNN
CCCCCCHHHHHHHHH		42.6421890473
91 (in isoform 1)Ubiquitination-42.6421890473
96UbiquitinationATKVQDIKNNLKEAI
CHHHHHHHHHHHHHH		48.3421890473
96 (in isoform 1)Ubiquitination-48.3421890473
97UbiquitinationTKVQDIKNNLKEAIE
HHHHHHHHHHHHHHH		60.4421890473
100UbiquitinationQDIKNNLKEAIETIV
HHHHHHHHHHHHHHH		47.42-
166 (in isoform 3)Ubiquitination-23.2921890473
167 (in isoform 2)Ubiquitination-59.2121890473
171 (in isoform 3)Ubiquitination-3.3121890473
172 (in isoform 2)Ubiquitination-2.1121890473
177PhosphorylationQLIDCAQYFLDKIDV
EEHHHHHHHHHHCHH		6.38-
181UbiquitinationCAQYFLDKIDVIKQA
HHHHHHHHCHHHHHC		42.8421906983
181 (in isoform 1)Ubiquitination-42.8421890473
186UbiquitinationLDKIDVIKQADYVPS
HHHCHHHHHCCCCCC		39.0020639865
186 (in isoform 1)Ubiquitination-39.0021890473
187UbiquitinationDKIDVIKQADYVPSD
HHCHHHHHCCCCCCC		28.4821890473
190PhosphorylationDVIKQADYVPSDQDL
HHHHHCCCCCCCHHH		19.78-
193PhosphorylationKQADYVPSDQDLLRC
HHCCCCCCCHHHHHH		37.55-
196 (in isoform 3)Ubiquitination-53.3021890473
197 (in isoform 2)Ubiquitination-2.4321890473
201ADP-ribosylationDQDLLRCRVLTSGIF
CHHHHHHEEECCCCC		21.75-
201 (in isoform 3)Ubiquitination-21.7521890473
201ADP-ribosylationDQDLLRCRVLTSGIF
CHHHHHHEEECCCCC		21.75-
202 (in isoform 2)Ubiquitination-8.6121890473
204PhosphorylationLLRCRVLTSGIFETK
HHHHEEECCCCCEEE		23.27-
210PhosphorylationLTSGIFETKFQVDKV
ECCCCCEEEEEEEEE		26.81-
211UbiquitinationTSGIFETKFQVDKVN
CCCCCEEEEEEEEEE		26.9721890473
211 (in isoform 1)Ubiquitination-26.9721890473
212UbiquitinationSGIFETKFQVDKVNF
CCCCEEEEEEEEEEE		12.8121890473
216UbiquitinationETKFQVDKVNFHMFD
EEEEEEEEEEEEEEE		39.9721890473
216 (in isoform 1)Ubiquitination-39.9721890473
217UbiquitinationTKFQVDKVNFHMFDV
EEEEEEEEEEEEEEC		8.8321890473
259 (in isoform 3)Ubiquitination-50.6321890473
260 (in isoform 2)Ubiquitination-42.5621890473
274UbiquitinationQEALNLFKSIWNNRW
HHHHHHHHHHHCCHH		44.1720639865
274 (in isoform 1)Ubiquitination-44.1721890473
275UbiquitinationEALNLFKSIWNNRWL
HHHHHHHHHHCCHHH		26.0421890473
278 (in isoform 3)Ubiquitination-26.9021890473
279 (in isoform 2)Ubiquitination-22.8521890473
285 (in isoform 3)Ubiquitination-2.2121890473
286 (in isoform 2)Ubiquitination-11.5121890473
290 (in isoform 3)Ubiquitination-4.9321890473
291 (in isoform 2)Ubiquitination-7.5921890473
292 (in isoform 3)Ubiquitination-32.3821890473
293UbiquitinationSVILFLNKQDLLAEK
HHHHHCCHHHHHHHH		47.5421906983
293 (in isoform 2)Ubiquitination-47.5421890473
293 (in isoform 1)Ubiquitination-47.5421890473
300UbiquitinationKQDLLAEKVLAGKSK
HHHHHHHHHHCCCHH		36.6218781797
300 (in isoform 1)Ubiquitination-36.6221890473
301UbiquitinationQDLLAEKVLAGKSKI
HHHHHHHHHCCCHHH		3.1321890473
305UbiquitinationAEKVLAGKSKIEDYF
HHHHHCCCHHHHHHC		42.8621890473
305 (in isoform 1)Ubiquitination-42.8621890473
306UbiquitinationEKVLAGKSKIEDYFP
HHHHCCCHHHHHHCH		37.6421890473
307UbiquitinationKVLAGKSKIEDYFPE
HHHCCCHHHHHHCHH		54.3120639865
307 (in isoform 1)Ubiquitination-54.3121890473
308UbiquitinationVLAGKSKIEDYFPEF
HHCCCHHHHHHCHHH		6.6821890473
311PhosphorylationGKSKIEDYFPEFARY
CCHHHHHHCHHHHCC		14.29-
323 (in isoform 3)Ubiquitination-57.8721890473
324 (in isoform 2)Ubiquitination-24.3221890473
338UbiquitinationDPRVTRAKYFIRDEF
CCCCCEEEEEECCCH		37.0921890473
338 (in isoform 1)Ubiquitination-37.0921890473
339UbiquitinationPRVTRAKYFIRDEFL
CCCCEEEEEECCCHH		11.8521890473
347MethylationFIRDEFLRISTASGD
EECCCHHEEEECCCC		26.57-
349PhosphorylationRDEFLRISTASGDGR
CCCHHEEEECCCCCC		16.1020068231
352PhosphorylationFLRISTASGDGRHYC
HHEEEECCCCCCCCE		37.1920068231
358PhosphorylationASGDGRHYCYPHFTC
CCCCCCCCEECCEEE		7.72-
360PhosphorylationGDGRHYCYPHFTCAV
CCCCCCEECCEEEEE		7.80-
391PhosphorylationQRMHLRQYELL----
HHHHHHHHHCC----		11.34-
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 GNAS2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GNAS2_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 GNAS2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FSCN1_HUMANFSCN1physical
17353931
PUR6_HUMANPAICSphysical
17353931
RUVB1_HUMANRUVBL1physical
17353931
GLYM_HUMANSHMT2physical
17353931
ADCY6_HUMANADCY6genetic
9228084
GNAS3_HUMANGNASphysical
7797570
GNAS2_HUMANGNASphysical
7797570
ALEX_HUMANGNASphysical
7797570
GNAS1_HUMANGNASphysical
7797570
NUCB1_HUMANNUCB1physical
21988832
NUCB2_HUMANNUCB2physical
21988832
1A02_HUMANHLA-Aphysical
9914489
1A03_HUMANHLA-Aphysical
9914489
1A01_HUMANHLA-Aphysical
9914489
1A26_HUMANHLA-Aphysical
9914489
AXIN1_HUMANAXIN1physical
16293724
PANX1_HUMANPANX1physical
16293724
GNAL_HUMANGNALphysical
26186194
GBG4_HUMANGNG4physical
26186194
TROP_HUMANTROphysical
26186194
MAGD2_HUMANMAGED2physical
26186194
GBB1_HUMANGNB1physical
26186194
GBB2_HUMANGNB2physical
26186194
GBB4_HUMANGNB4physical
26186194
C1QBP_HUMANC1QBPphysical
26186194
MAP2_HUMANMETAP2physical
26186194
CPT2_HUMANCPT2physical
26186194
YBEY_HUMANYBEYphysical
26186194
GBG10_HUMANGNG10physical
26186194
OCAD1_HUMANOCIAD1physical
26186194
GNA12_HUMANGNA12physical
26186194
ARMX3_HUMANARMCX3physical
26186194
GBG5_HUMANGNG5physical
26186194
IF4H_HUMANEIF4Hphysical
26344197
EMAL2_HUMANEML2physical
26344197
GIPC1_HUMANGIPC1physical
26344197
PUR4_HUMANPFASphysical
26344197
RIC8B_HUMANRIC8Bphysical
12652642
ADCY2_HUMANADCY2physical
25241761
GPA1_YEASTGPA1genetic
8943324
GBB_YEASTSTE4genetic
8943324
GNAL_HUMANGNALphysical
28514442
TROP_HUMANTROphysical
28514442
OCAD1_HUMANOCIAD1physical
28514442
MAGD2_HUMANMAGED2physical
28514442
GBB4_HUMANGNB4physical
28514442
CPT2_HUMANCPT2physical
28514442
GBG5_HUMANGNG5physical
28514442
MAP2_HUMANMETAP2physical
28514442
GNA12_HUMANGNA12physical
28514442
C1QBP_HUMANC1QBPphysical
28514442
GBB1_HUMANGNB1physical
28514442
Drug and Disease Associations
Kegg Disease
H00244 Pseudohypoparathyroidism
H00441 Progressive osseous heteroplasia (POH)
H00501 Fibrous dysplasia, polyostotic; Albright hereditary osteodystrophy
OMIM Disease
103580Albright hereditary osteodystrophy (AHO)
103580Pseudohypoparathyroidism 1A (PHP1A)
174800McCune-Albright syndrome (MAS)
102200Pituitary adenoma, growth hormone-secreting, 1 (PAGH1)
166350Progressive osseous heteroplasia (POH)
219080ACTH-independent macronodular adrenal hyperplasia 1 (AIMAH1)
603233Pseudohypoparathyroidism 1B (PHP1B)
139320GNAS hyperfunction (GNASHYP)
612462Pseudohypoparathyroidism 1C (PHP1C)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GNAS2_HUMAN

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Related Literatures of Post-Translational Modification
Palmitoylation
ReferencePubMed
"Site-specific analysis of protein S-acylation by resin-assistedcapture.";
Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A.,Stamler J.S., Casey P.J.;
J. Lipid Res. 52:393-398(2011).
Cited for: PALMITOYLATION AT CYS-3.
Ubiquitylation
ReferencePubMed
"Quantitative analysis of global ubiquitination in HeLa cells by massspectrometry.";
Meierhofer D., Wang X., Huang L., Kaiser P.;
J. Proteome Res. 7:4566-4576(2008).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-300, AND MASSSPECTROMETRY.

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