UniProt ID | PGTB2_HUMAN | |
---|---|---|
UniProt AC | P53611 | |
Protein Name | Geranylgeranyl transferase type-2 subunit beta | |
Gene Name | RABGGTB | |
Organism | Homo sapiens (Human). | |
Sequence Length | 331 | |
Subcellular Localization | ||
Protein Description | Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A.. | |
Protein Sequence | MGTPQKDVIIKSDAPDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGIYWGLTVMDLMGQLHRMNREEILAFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYDSINVIDVNKVVEYVKGLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKLRNFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEEQIKPVNPVFCMPEEVLQRVNVQPELVS | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MGTPQKDVI ------CCCCCCCEE | 46.21 | 19413330 | |
3 | Phosphorylation | -----MGTPQKDVII -----CCCCCCCEEE | 22.65 | 23401153 | |
6 | Acetylation | --MGTPQKDVIIKSD --CCCCCCCEEECCC | 55.98 | 23749302 | |
6 | Ubiquitination | --MGTPQKDVIIKSD --CCCCCCCEEECCC | 55.98 | - | |
11 | Sumoylation | PQKDVIIKSDAPDTL CCCCEEECCCCCCEE | 31.03 | - | |
11 | Ubiquitination | PQKDVIIKSDAPDTL CCCCEEECCCCCCEE | 31.03 | 21906983 | |
11 | Sumoylation | PQKDVIIKSDAPDTL CCCCEEECCCCCCEE | 31.03 | - | |
12 | Phosphorylation | QKDVIIKSDAPDTLL CCCEEECCCCCCEEH | 28.70 | 25850435 | |
17 | Phosphorylation | IKSDAPDTLLLEKHA ECCCCCCEEHHHHHH | 20.46 | 27251275 | |
22 | Ubiquitination | PDTLLLEKHADYIAS CCEEHHHHHHHHHHH | 44.02 | 21906983 | |
22 | Acetylation | PDTLLLEKHADYIAS CCEEHHHHHHHHHHH | 44.02 | 27452117 | |
29 | Phosphorylation | KHADYIASYGSKKDD HHHHHHHHCCCCCCH | 22.07 | 28152594 | |
30 | Phosphorylation | HADYIASYGSKKDDY HHHHHHHCCCCCCHH | 19.18 | 28152594 | |
32 | Phosphorylation | DYIASYGSKKDDYEY HHHHHCCCCCCHHHH | 28.44 | 28152594 | |
33 | Ubiquitination | YIASYGSKKDDYEYC HHHHCCCCCCHHHHH | 56.72 | 21906983 | |
34 | Ubiquitination | IASYGSKKDDYEYCM HHHCCCCCCHHHHHH | 58.49 | - | |
37 | Phosphorylation | YGSKKDDYEYCMSEY CCCCCCHHHHHHHHH | 20.94 | 28674419 | |
39 | Phosphorylation | SKKDDYEYCMSEYLR CCCCHHHHHHHHHHH | 6.29 | 27642862 | |
124 | Acetylation | NKVVEYVKGLQKEDG HHHHHHHHCCCCCCC | 53.66 | 27452117 | |
124 | Ubiquitination | NKVVEYVKGLQKEDG HHHHHHHHCCCCCCC | 53.66 | 21906983 | |
241 | Phosphorylation | EKLPDVCYSWWVLAS HHCCCHHHHHHHHHH | 13.74 | 24719451 | |
248 | Phosphorylation | YSWWVLASLKIIGRL HHHHHHHHHHHHHHC | 26.49 | 24719451 | |
307 | Sumoylation | LLGEEQIKPVNPVFC HCCCHHCCCCCCCEE | 42.48 | - | |
331 | Phosphorylation | NVQPELVS------- CCCHHHCC------- | 47.32 | 28102081 |
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 PGTB2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PGTB2_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 PGTB2_HUMAN !! |
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. |
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Phosphorylation | |
Reference | PubMed |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, AND MASSSPECTROMETRY. | |
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, AND MASSSPECTROMETRY. | |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, AND MASSSPECTROMETRY. | |
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, AND MASSSPECTROMETRY. |