UniProt ID | RAP1B_HUMAN | |
---|---|---|
UniProt AC | P61224 | |
Protein Name | Ras-related protein Rap-1b | |
Gene Name | RAP1B | |
Organism | Homo sapiens (Human). | |
Sequence Length | 184 | |
Subcellular Localization | Cell membrane. Cytoplasm, cytosol. Cell junction. May shuttle between plasma membrane and cytosol. Presence of KRIT1 and CDH5 is required for its localization to the cell junction. | |
Protein Description | GTP-binding protein that possesses intrinsic GTPase activity. Contributes to the polarizing activity of KRIT1 and CDH5 in the establishment and maintenance of correct endothelial cell polarity and vascular lumen. Required for the localization of phosphorylated PRKCZ, PARD3 and TIAM1 to the cell junction. Plays a role in the establishment of basal endothelial barrier function.. | |
Protein Sequence | MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDAQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDLEDERVVGKEQGQNLARQWNNCAFLESSAKSKINVNEIFYDLVRQINRKTPVPGKARKKSSCQLL | |
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 |
---|---|---|---|---|---|
5 | Ubiquitination | ---MREYKLVVLGSG ---CCEEEEEEECCC | 30.01 | 21890473 | |
5 | Ubiquitination | ---MREYKLVVLGSG ---CCEEEEEEECCC | 30.01 | 21890473 | |
5 | Acetylation | ---MREYKLVVLGSG ---CCEEEEEEECCC | 30.01 | 25953088 | |
5 | Ubiquitination | ---MREYKLVVLGSG ---CCEEEEEEECCC | 30.01 | 21906983 | |
11 | Phosphorylation | YKLVVLGSGGVGKSA EEEEEECCCCCCCHH | 28.36 | 25159151 | |
17 | Phosphorylation | GSGGVGKSALTVQFV CCCCCCCHHHHHHEE | 23.68 | 20068231 | |
31 | Ubiquitination | VQGIFVEKYDPTIED EEEEEEEECCCCCCH | 50.04 | 21906983 | |
32 | Phosphorylation | QGIFVEKYDPTIEDS EEEEEEECCCCCCHH | 17.41 | 20860994 | |
35 | Phosphorylation | FVEKYDPTIEDSYRK EEEECCCCCCHHHHH | 33.82 | 23403867 | |
39 | Phosphorylation | YDPTIEDSYRKQVEV CCCCCCHHHHHHHEE | 17.66 | 23401153 | |
39 | ADP-ribosylation | YDPTIEDSYRKQVEV CCCCCCHHHHHHHEE | 17.66 | 3141412 | |
39 | ADP-ribosylation | YDPTIEDSYRKQVEV CCCCCCHHHHHHHEE | 17.66 | - | |
40 | Phosphorylation | DPTIEDSYRKQVEVD CCCCCHHHHHHHEEC | 33.86 | 23403867 | |
42 | Ubiquitination | TIEDSYRKQVEVDAQ CCCHHHHHHHEECHH | 50.92 | - | |
58 | Phosphorylation | CMLEILDTAGTEQFT HHHHHHHHCCCHHHH | 24.44 | 27732954 | |
61 | Phosphorylation | EILDTAGTEQFTAMR HHHHHCCCHHHHHHH | 24.93 | 27732954 | |
65 | Phosphorylation | TAGTEQFTAMRDLYM HCCCHHHHHHHHHHH | 21.16 | 27732954 | |
88 | Phosphorylation | VYSITAQSTFNDLQD EEEEEECCCCCCHHH | 32.28 | 26657352 | |
117 | Ubiquitination | PMILVGNKCDLEDER CEEEECCCCCCCCCE | 24.17 | - | |
128 | Ubiquitination | EDERVVGKEQGQNLA CCCEECCHHHHHHHH | 34.94 | - | |
134 | Methylation | GKEQGQNLARQWNNC CHHHHHHHHHHHHCC | 2.98 | 2123345 | |
139 | Methylation | QNLARQWNNCAFLES HHHHHHHHCCHHHHH | 25.93 | 2123345 | |
149 | Ubiquitination | AFLESSAKSKINVNE HHHHHHCCCCCCHHH | 54.98 | - | |
151 | Ubiquitination | LESSAKSKINVNEIF HHHHCCCCCCHHHHH | 37.28 | - | |
159 | Phosphorylation | INVNEIFYDLVRQIN CCHHHHHHHHHHHHC | 17.65 | 23917254 | |
162 | Methylation | NEIFYDLVRQINRKT HHHHHHHHHHHCCCC | 3.75 | 2123345 | |
169 | Phosphorylation | VRQINRKTPVPGKAR HHHHCCCCCCCCCCC | 26.70 | 28060719 | |
174 | Ubiquitination | RKTPVPGKARKKSSC CCCCCCCCCCCCCCC | 38.66 | - | |
179 | Phosphorylation | PGKARKKSSCQLL-- CCCCCCCCCCCCC-- | 39.11 | 12089143 | |
180 | Phosphorylation | GKARKKSSCQLL--- CCCCCCCCCCCC--- | 18.11 | 8463283 | |
181 | Geranylgeranylation | KARKKSSCQLL---- CCCCCCCCCCC---- | 4.22 | 2123345 | |
181 | Methylation | KARKKSSCQLL---- CCCCCCCCCCC---- | 4.22 | 2123345 | |
181 | Geranylgeranylation | KARKKSSCQLL---- CCCCCCCCCCC---- | 4.22 | 2123345 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
179 | S | Phosphorylation | Kinase | PRKACA | P17612 | GPS |
179 | S | Phosphorylation | Kinase | PRKG1 | Q13976 | GPS |
179 | S | Phosphorylation | Kinase | PKA-FAMILY | - | GPS |
179 | S | Phosphorylation | Kinase | PKG-FAMILY | - | GPS |
179 | S | Phosphorylation | Kinase | PKA | - | Uniprot |
179 | S | Phosphorylation | Kinase | PKA_GROUP | - | PhosphoELM |
180 | S | Phosphorylation | Kinase | PKACA | P17612 | PSP |
- | K | Ubiquitination | E3 ubiquitin ligase | SMURF2 | Q9HAU4 | PMID:17318188 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RAP1B_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 RAP1B_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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Prenylation | |
Reference | PubMed |
"Posttranslationally processed structure of the human platelet proteinsmg p21B: evidence for geranylgeranylation and carboxyl methylation ofthe C-terminal cysteine."; Kawata M., Farnsworth C.C., Yoshida Y., Gelb M.H., Glomset J.A.,Takai Y.; Proc. Natl. Acad. Sci. U.S.A. 87:8960-8964(1990). Cited for: ISOPRENYLATION AT CYS-181. |