UniProt ID | GNA12_HUMAN | |
---|---|---|
UniProt AC | Q03113 | |
Protein Name | Guanine nucleotide-binding protein subunit alpha-12 | |
Gene Name | GNA12 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 381 | |
Subcellular Localization |
Cell membrane Lipid-anchor . Lateral cell membrane Lipid-anchor . Cytoplasm . CDH1 enhances cell membrane localization. |
|
Protein Description | Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. [PubMed: 22609986] | |
Protein Sequence | MSGVVRTLSRCLLPAEAGGARERRAGSGARDAEREARRRSRDIDALLARERRAVRRLVKILLLGAGESGKSTFLKQMRIIHGREFDQKALLEFRDTIFDNILKGSRVLVDARDKLGIPWQYSENEKHGMFLMAFENKAGLPVEPATFQLYVPALSALWRDSGIREAFSRRSEFQLGESVKYFLDNLDRIGQLNYFPSKQDILLARKATKGIVEHDFVIKKIPFKMVDVGGQRSQRQKWFQCFDGITSILFMVSSSEYDQVLMEDRRTNRLVESMNIFETIVNNKLFFNVSIILFLNKMDLLVEKVKTVSIKKHFPDFRGDPHRLEDVQRYLVQCFDRKRRNRSKPLFHHFTTAIDTENVRFVFHAVKDTILQENLKDIMLQ | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
11 | S-palmitoylation | VVRTLSRCLLPAEAG HHHHHHHHCCCHHHC | 4.04 | - | |
40 | Phosphorylation | EREARRRSRDIDALL HHHHHHHHHHHHHHH | 32.28 | 22777824 | |
68 | Phosphorylation | LLLGAGESGKSTFLK HHHCCCCCCHHHHHH | 51.07 | 20068231 | |
70 | Ubiquitination | LGAGESGKSTFLKQM HCCCCCCHHHHHHHC | 56.45 | - | |
75 | Ubiquitination | SGKSTFLKQMRIIHG CCHHHHHHHCHHHCC | 37.55 | - | |
105 | Ubiquitination | FDNILKGSRVLVDAR HHHHHCCCEEEEECH | 20.03 | 21906983 | |
114 | Ubiquitination | VLVDARDKLGIPWQY EEEECHHHHCCCCCC | 42.96 | - | |
121 | Phosphorylation | KLGIPWQYSENEKHG HHCCCCCCCCCCCCC | 17.68 | - | |
139 | Ubiquitination | MAFENKAGLPVEPAT EEEECCCCCCCCCCE | 31.93 | - | |
161 | Ubiquitination | LSALWRDSGIREAFS HHHHHHHHCHHHHHH | 27.78 | - | |
198 | Ubiquitination | QLNYFPSKQDILLAR CCCCCCCHHHHHHHH | 52.83 | 21906983 | |
208 | Phosphorylation | ILLARKATKGIVEHD HHHHHHCCCCCCCCC | 32.60 | - | |
219 | Ubiquitination | VEHDFVIKKIPFKMV CCCCEEEEECCCEEE | 39.07 | - | |
220 | Ubiquitination | EHDFVIKKIPFKMVD CCCEEEEECCCEEEE | 44.48 | - | |
235 | Methylation | VGGQRSQRQKWFQCF CCCCCCHHHHHHHHH | 41.09 | - | |
283 | Ubiquitination | IFETIVNNKLFFNVS HHHHHHHCCCCCCHH | 31.36 | 21906983 | |
317 | Ubiquitination | IKKHFPDFRGDPHRL HHHHCCCCCCCHHHH | 10.81 | - | |
343 | Phosphorylation | DRKRRNRSKPLFHHF HHCCCCCCCCCCCCC | 42.02 | 24719451 | |
369 | Phosphorylation | VFHAVKDTILQENLK HHHHHHHHHHHHHHH | 20.19 | 25332170 | |
376 | Ubiquitination | TILQENLKDIMLQ-- HHHHHHHHHHHCC-- | 57.71 | 21906983 |
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 GNA12_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GNA12_HUMAN !! |
* 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 GNA12_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CAD15_HUMAN | CDH15 | physical | 11136230 | |
PPP5_HUMAN | PPP5C | physical | 12176367 | |
ARHGC_HUMAN | ARHGEF12 | physical | 11094164 | |
PAR1_HUMAN | F2R | physical | 8290554 | |
TA2R_HUMAN | TBXA2R | physical | 8290554 | |
HS90A_HUMAN | HSP90AA1 | physical | 11598136 | |
ARHGB_HUMAN | ARHGEF11 | physical | 10026210 | |
M3K5_HUMAN | MAP3K5 | physical | 17595347 | |
ARG28_HUMAN | ARHGEF28 | physical | 17595347 | |
A4_HUMAN | APP | physical | 21832049 | |
IL3RA_HUMAN | IL3RA | physical | 21988832 |
Kegg Disease | ||||||
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OMIM Disease | ||||||
There are no disease associations of PTM sites. | ||||||
Kegg Drug | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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