GBB2_HUMAN - dbPTM
GBB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GBB2_HUMAN
UniProt AC P62879
Protein Name Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-2
Gene Name GNB2
Organism Homo sapiens (Human).
Sequence Length 340
Subcellular Localization Cytoplasm, perinuclear region .
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 MSELEQLRQEAEQLRNQIRDARKACGDSTLTQITAGLDPVGRIQMRTRRTLRGHLAKIYAMHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNFVACGGLDNICSIYSLKTREGNVRVSRELPGHTGYLSCCRFLDDNQIITSSGDTTCALWDIETGQQTVGFAGHSGDVMSLSLAPDGRTFVSGACDASIKLWDVRDSMCRQTFIGHESDINAVAFFPNGYAFTTGSDDATCRLFDLRADQELLMYSHDNIICGITSVAFSRSGRLLLAGYDDFNCNIWDAMKGDRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN
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
2Phosphorylation------MSELEQLRQ
------CHHHHHHHH
51.3825159151
2Acetylation------MSELEQLRQ
------CHHHHHHHH
51.3819413330
15MethylationRQEAEQLRNQIRDAR
HHHHHHHHHHHHHHH
32.47-
23UbiquitinationNQIRDARKACGDSTL
HHHHHHHHHHCCCHH
50.1521906983
25S-nitrosylationIRDARKACGDSTLTQ
HHHHHHHHCCCHHHH
7.5421278135
25S-nitrosocysteineIRDARKACGDSTLTQ
HHHHHHHHCCCHHHH
7.54-
28PhosphorylationARKACGDSTLTQITA
HHHHHCCCHHHHHHC
15.5929255136
29PhosphorylationRKACGDSTLTQITAG
HHHHCCCHHHHHHCC
38.2729255136
31PhosphorylationACGDSTLTQITAGLD
HHCCCHHHHHHCCCC
20.2929255136
34PhosphorylationDSTLTQITAGLDPVG
CCHHHHHHCCCCCCC
12.5925850435
50PhosphorylationIQMRTRRTLRGHLAK
CHHHCHHHHHHHHHH
19.9524719451
57AcetylationTLRGHLAKIYAMHWG
HHHHHHHHHHHHHCC
42.48-
57UbiquitinationTLRGHLAKIYAMHWG
HHHHHHHHHHHHHCC
42.4821890473
59PhosphorylationRGHLAKIYAMHWGTD
HHHHHHHHHHHCCCC
9.3629496907
67PhosphorylationAMHWGTDSRLLVSAS
HHHCCCCCEEEEEEC
25.3524719451
72PhosphorylationTDSRLLVSASQDGKL
CCCEEEEEECCCCCE
23.36-
74PhosphorylationSRLLVSASQDGKLII
CEEEEEECCCCCEEE
22.6921712546
78AcetylationVSASQDGKLIIWDSY
EEECCCCCEEEEECC
44.8130588969
84PhosphorylationGKLIIWDSYTTNKVH
CCEEEEECCCCCEEE
14.9128152594
85PhosphorylationKLIIWDSYTTNKVHA
CEEEEECCCCCEEEE
18.3428152594
86PhosphorylationLIIWDSYTTNKVHAI
EEEEECCCCCEEEEE
28.0428152594
87PhosphorylationIIWDSYTTNKVHAIP
EEEECCCCCEEEEEE
25.4728152594
89UbiquitinationWDSYTTNKVHAIPLR
EECCCCCEEEEEECC
33.0521890473
109UbiquitinationTCAYAPSGNFVACGG
EEEECCCCCEEEECC
30.45-
125PhosphorylationDNICSIYSLKTREGN
HHCCEEEEEECCCCC
23.0124719451
136PhosphorylationREGNVRVSRELPGHT
CCCCEEEEEECCCCC
14.9627794612
145PhosphorylationELPGHTGYLSCCRFL
ECCCCCCEEEEEEEE
9.1529496907
201UbiquitinationPDGRTFVSGACDASI
CCCCCCCCCCCCCEE
19.24-
204S-nitrosylationRTFVSGACDASIKLW
CCCCCCCCCCEEEEH
5.2521278135
204S-nitrosocysteineRTFVSGACDASIKLW
CCCCCCCCCCEEEEH
5.25-
207PhosphorylationVSGACDASIKLWDVR
CCCCCCCEEEEHHHC
13.6528857561
209AcetylationGACDASIKLWDVRDS
CCCCCEEEEHHHCHH
40.8226051181
209UbiquitinationGACDASIKLWDVRDS
CCCCCEEEEHHHCHH
40.8221906983
216PhosphorylationKLWDVRDSMCRQTFI
EEHHHCHHHHCCCCC
14.8224719451
239PhosphorylationVAFFPNGYAFTTGSD
EEECCCCEEEECCCC
12.75-
301AcetylationCNIWDAMKGDRAGVL
CCHHHHCCCCCCEEE
60.4226051181
301UbiquitinationCNIWDAMKGDRAGVL
CCHHHHCCCCCCEEE
60.422190698
317S-nitrosylationGHDNRVSCLGVTDDG
CCCCCEEEEEECCCC
3.3321278135
317S-nitrosocysteineGHDNRVSCLGVTDDG
CCCCCEEEEEECCCC
3.33-
329PhosphorylationDDGMAVATGSWDSFL
CCCEEEEECCHHHHH
25.7528348404
331PhosphorylationGMAVATGSWDSFLKI
CEEEEECCHHHHHHH
24.2924719451
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 GBB2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GBB2_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 GBB2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CPNS1_HUMANCAPNS1physical
16169070
GBG10_HUMANGNG10physical
7665596
RAF1_HUMANRAF1physical
7782277
ATX10_HUMANATXN10physical
16498633
PHLP_HUMANPDCLphysical
19376773
GBG2_HUMANGNG2physical
19376773
GBG3_HUMANGNG3physical
19376773
GBG4_HUMANGNG4physical
19376773
GBG5_HUMANGNG5physical
19376773
GBG7_HUMANGNG7physical
19376773
GBG8_HUMANGNG8physical
19376773
GBGT2_HUMANGNGT2physical
19376773
GBG10_HUMANGNG10physical
19376773
GBG12_HUMANGNG12physical
19376773
GNAI1_HUMANGNAI1physical
16371464
GNAI2_HUMANGNAI2physical
16371464
GNAI3_HUMANGNAI3physical
16371464
ID3_HUMANID3physical
18255255
ODPB_HUMANPDHBphysical
21988832
ACTN4_HUMANACTN4physical
23326349
HDAC5_HUMANHDAC5physical
23326349
MEF2A_HUMANMEF2Aphysical
23326349
H2B2E_HUMANHIST2H2BEphysical
23326349
TBP_HUMANTBPphysical
23326349
TAF8_HUMANTAF8physical
23326349
NFAC2_HUMANNFATC2physical
23326349
STAT1_HUMANSTAT1physical
23326349
STAT3_HUMANSTAT3physical
23326349
AT2B1_HUMANATP2B1physical
26344197
VA0D1_HUMANATP6V0D1physical
26344197
GNA11_HUMANGNA11physical
26344197
GNAQ_HUMANGNAQphysical
26344197
PYC_HUMANPCphysical
26344197
GBG2_HUMANGNG2physical
25982117
CUL4A_HUMANCUL4Aphysical
25982117
ARBK1_HUMANADRBK1physical
25982117
DDB1_HUMANDDB1physical
25982117
GNAS3_HUMANGNASphysical
28514442
GNAS2_HUMANGNASphysical
28514442
ALEX_HUMANGNASphysical
28514442
GNAS1_HUMANGNASphysical
28514442
PHLP_HUMANPDCLphysical
28514442
PFD5_HUMANPFDN5physical
28514442
PFD1_HUMANPFDN1physical
28514442
ANXA1_HUMANANXA1physical
28514442
PFD4_HUMANPFDN4physical
28514442
PFD6_HUMANPFDN6physical
28514442
TCPB_HUMANCCT2physical
28514442
TCPG_HUMANCCT3physical
28514442
GBG5_HUMANGNG5physical
28514442
TCPA_HUMANTCP1physical
28514442
TADBP_HUMANTARDBPphysical
28514442
TCPD_HUMANCCT4physical
28514442
TCPZ_HUMANCCT6Aphysical
28514442
PFD3_HUMANVBP1physical
28514442
TCPW_HUMANCCT6Bphysical
28514442

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 GBB2_HUMAN

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Related Literatures of Post-Translational Modification

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