| 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 | ||
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* 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. | |