GBB3_HUMAN - dbPTM
GBB3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GBB3_HUMAN
UniProt AC P16520
Protein Name Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-3
Gene Name GNB3
Organism Homo sapiens (Human).
Sequence Length 340
Subcellular Localization
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 MGEMEQLRQEAEQLKKQIADARKACADVTLAELVSGLEVVGRVQMRTRRTLRGHLAKIYAMHWATDSKLLVSASQDGKLIVWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNMCSIYNLKSREGNVKVSRELSAHTGYLSCCRFLDDNNIVTSSGDTTCALWDIETGQQKTVFVGHTGDCMSLAVSPDFNLFISGACDASAKLWDVREGTCRQTFTGHESDINAICFFPNGEAICTGSDDASCRLFDLRADQELICFSHESIICGITSVAFSLSGRLLFAGYDDFNCNVWDSMKSERVGILSGHDNRVSCLGVTADGMAVATGSWDSFLKIWN
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
16AcetylationQEAEQLKKQIADARK
HHHHHHHHHHHHHHH
56.3721466224
23AcetylationKQIADARKACADVTL
HHHHHHHHHHHHCHH
49.9221466224
57AcetylationTLRGHLAKIYAMHWA
HHHHHHHHHHHHHHH
42.4826051181
59PhosphorylationRGHLAKIYAMHWATD
HHHHHHHHHHHHHCC
9.36-
68AcetylationMHWATDSKLLVSASQ
HHHHCCCCEEEEECC
48.9619413330
72PhosphorylationTDSKLLVSASQDGKL
CCCCEEEEECCCCCE
23.36-
74PhosphorylationSKLLVSASQDGKLIV
CCEEEEECCCCCEEE
22.6919060867
78AcetylationVSASQDGKLIVWDSY
EEECCCCCEEEEEEC
43.2430588975
85PhosphorylationKLIVWDSYTTNKVHA
CEEEEEECCCCEEEE
18.3419413330
86PhosphorylationLIVWDSYTTNKVHAI
EEEEEECCCCEEEEE
28.0419413330
87PhosphorylationIVWDSYTTNKVHAIP
EEEEECCCCEEEEEE
25.4719413330
89UbiquitinationWDSYTTNKVHAIPLR
EEECCCCEEEEEECC
33.0521906983
89AcetylationWDSYTTNKVHAIPLR
EEECCCCEEEEEECC
33.0526051181
129ADP-ribosylationSIYNLKSREGNVKVS
EEEECCCCCCCCEEC
55.01-
140PhosphorylationVKVSRELSAHTGYLS
CEECHHHHHCCCEEE
17.1622461510
143PhosphorylationSRELSAHTGYLSCCR
CHHHHHCCCEEEEEE
27.5222461510
145PhosphorylationELSAHTGYLSCCRFL
HHHHCCCEEEEEEEE
9.1522461510
177UbiquitinationDIETGQQKTVFVGHT
EECCCCEEEEEEECC
38.48-
207PhosphorylationISGACDASAKLWDVR
EECCCCCCCCEEEEC
16.8222817900
209AcetylationGACDASAKLWDVREG
CCCCCCCCEEEECCC
47.8426051181
309PhosphorylationSERVGILSGHDNRVS
CCCEEEEECCCCCEE
31.96-
334PhosphorylationVATGSWDSFLKIWN-
EEECCHHHHHHHCC-
26.6424719451

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 GBB3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GBB3_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 GBB3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PHLP_HUMANPDCLphysical
19376773
GBG2_HUMANGNG2physical
19376773
GBG2_HUMANGNG2physical
22940628
GBG5_HUMANGNG5physical
22940628
GBG8_HUMANGNG8physical
22940628
GBG10_HUMANGNG10physical
22940628
GBG12_HUMANGNG12physical
22940628
GNAI3_HUMANGNAI3physical
22940628
GNAQ_HUMANGNAQphysical
22940628
GNA12_HUMANGNA12physical
22940628
GBB3_HUMANGNB3physical
21125662

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 GBB3_HUMAN

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Related Literatures of Post-Translational Modification

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