| UniProt ID | RAB1A_HUMAN | |
|---|---|---|
| UniProt AC | P62820 | |
| Protein Name | Ras-related protein Rab-1A | |
| Gene Name | RAB1A | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 205 | |
| Subcellular Localization | Golgi apparatus . Endoplasmic reticulum . Early endosome . Cytoplasm, cytosol . Membrane . Melanosome . Alternates between membrane-associated and cytosolic forms. | |
| Protein Description | The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. RAB1A regulates vesicular protein transport from the endoplasmic reticulum (ER) to the Golgi compartment and on to the cell surface, and plays a role in IL-8 and growth hormone secretion. Regulates the level of CASR present at the cell membrane. Plays a role in cell adhesion and cell migration, via its role in protein trafficking. Plays a role in autophagosome assembly and cellular defense reactions against pathogenic bacteria. Plays a role in microtubule-dependent protein transport by early endosomes and in anterograde melanosome transport.. | |
| Protein Sequence | MSSMNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESFNNVKQWLQEIDRYASENVNKLLVGNKCDLTTKKVVDYTTAKEFADSLGIPFLETSAKNATNVEQSFMTMAAEIKKRMGPGATAGGAEKSNVKIQSTPVKQSGGGCC | |
| 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 | Phosphorylation | ------MSSMNPEYD ------CCCCCHHHH | 37.99 | 25849741 | |
| 2 | Acetylation | ------MSSMNPEYD ------CCCCCHHHH | 37.99 | 22223895 | |
| 3 | Phosphorylation | -----MSSMNPEYDY -----CCCCCHHHHH | 22.68 | 25849741 | |
| 8 | Phosphorylation | MSSMNPEYDYLFKLL CCCCCHHHHHHHHHH | 15.90 | 25627689 | |
| 10 | Phosphorylation | SMNPEYDYLFKLLLI CCCHHHHHHHHHHHH | 17.09 | 28348404 | |
| 20 | Phosphorylation | KLLLIGDSGVGKSCL HHHHHCCCCCCCCCE | 30.11 | - | |
| 26 | S-palmitoylation | DSGVGKSCLLLRFAD CCCCCCCCEEEEECC | 3.37 | 29575903 | |
| 35 | Phosphorylation | LLRFADDTYTESYIS EEEECCCCCCHHHHH | 32.65 | 20068231 | |
| 36 | Phosphorylation | LRFADDTYTESYIST EEECCCCCCHHHHHE | 18.59 | 28796482 | |
| 37 | Phosphorylation | RFADDTYTESYISTI EECCCCCCHHHHHEE | 22.13 | 28796482 | |
| 39 | Phosphorylation | ADDTYTESYISTIGV CCCCCCHHHHHEEEC | 21.70 | 28796482 | |
| 40 | Phosphorylation | DDTYTESYISTIGVD CCCCCHHHHHEEECC | 7.83 | 28796482 | |
| 42 | Phosphorylation | TYTESYISTIGVDFK CCCHHHHHEEECCEE | 13.02 | 28796482 | |
| 43 | Phosphorylation | YTESYISTIGVDFKI CCHHHHHEEECCEEE | 16.52 | 28796482 | |
| 52 | Phosphorylation | GVDFKIRTIELDGKT ECCEEEEEEEECCEE | 23.44 | 22985185 | |
| 55 (in isoform 2) | Ubiquitination | - | 10.46 | 21890473 | |
| 58 | Malonylation | RTIELDGKTIKLQIW EEEEECCEEEEEEEE | 46.90 | 26320211 | |
| 58 | Ubiquitination | RTIELDGKTIKLQIW EEEEECCEEEEEEEE | 46.90 | - | |
| 59 | Phosphorylation | TIELDGKTIKLQIWD EEEECCEEEEEEEEC | 28.95 | 26307563 | |
| 61 | Ubiquitination | ELDGKTIKLQIWDTA EECCEEEEEEEECCC | 39.30 | - | |
| 61 | Malonylation | ELDGKTIKLQIWDTA EECCEEEEEEEECCC | 39.30 | 26320211 | |
| 61 | Acetylation | ELDGKTIKLQIWDTA EECCEEEEEEEECCC | 39.30 | 23954790 | |
| 67 | Phosphorylation | IKLQIWDTAGQERFR EEEEEECCCCHHHHH | 20.07 | 28857561 | |
| 75 | Phosphorylation | AGQERFRTITSSYYR CCHHHHHHHHHHHHC | 26.37 | 22617229 | |
| 77 | Phosphorylation | QERFRTITSSYYRGA HHHHHHHHHHHHCCC | 15.82 | 30108239 | |
| 78 | Phosphorylation | ERFRTITSSYYRGAH HHHHHHHHHHHCCCC | 16.70 | 21130716 | |
| 79 | Phosphorylation | RFRTITSSYYRGAHG HHHHHHHHHHCCCCE | 19.96 | 28348404 | |
| 79 | O-(2-cholinephosphoryl)serine | RFRTITSSYYRGAHG HHHHHHHHHHCCCCE | 19.96 | - | |
| 79 | Other | RFRTITSSYYRGAHG HHHHHHHHHHCCCCE | 19.96 | 22158903 | |
| 80 | Phosphorylation | FRTITSSYYRGAHGI HHHHHHHHHCCCCEE | 9.28 | 23663014 | |
| 81 | Phosphorylation | RTITSSYYRGAHGII HHHHHHHHCCCCEEE | 12.43 | 28060719 | |
| 91 | Phosphorylation | AHGIIVVYDVTDQES CCEEEEEEECCCHHH | 8.19 | 28985074 | |
| 94 | Phosphorylation | IIVVYDVTDQESFNN EEEEEECCCHHHHHH | 29.12 | 28985074 | |
| 98 | Phosphorylation | YDVTDQESFNNVKQW EECCCHHHHHHHHHH | 27.86 | 28985074 | |
| 103 (in isoform 1) | Ubiquitination | - | 37.57 | 21890473 | |
| 103 | Ubiquitination | QESFNNVKQWLQEID HHHHHHHHHHHHHHH | 37.57 | 21906983 | |
| 111 (in isoform 3) | Ubiquitination | - | 34.28 | 21906983 | |
| 111 | Methylation | QWLQEIDRYASENVN HHHHHHHHHHCCCHH | 34.28 | - | |
| 112 | Phosphorylation | WLQEIDRYASENVNK HHHHHHHHHCCCHHH | 15.67 | 26657352 | |
| 114 | Phosphorylation | QEIDRYASENVNKLL HHHHHHHCCCHHHHH | 22.29 | 25849741 | |
| 115 (in isoform 3) | Ubiquitination | - | 57.96 | 21906983 | |
| 119 | Ubiquitination | YASENVNKLLVGNKC HHCCCHHHHHCCCCC | 38.63 | 21890473 | |
| 119 | Acetylation | YASENVNKLLVGNKC HHCCCHHHHHCCCCC | 38.63 | 26051181 | |
| 119 (in isoform 1) | Ubiquitination | - | 38.63 | 21890473 | |
| 123 (in isoform 2) | Ubiquitination | - | 28.05 | 21890473 | |
| 125 | Ubiquitination | NKLLVGNKCDLTTKK HHHHCCCCCCCCCCC | 24.17 | - | |
| 126 | S-nitrosocysteine | KLLVGNKCDLTTKKV HHHCCCCCCCCCCCC | 6.34 | - | |
| 126 | S-nitrosylation | KLLVGNKCDLTTKKV HHHCCCCCCCCCCCC | 6.34 | 19483679 | |
| 127 (in isoform 2) | Ubiquitination | - | 48.97 | 21890473 | |
| 131 | Acetylation | NKCDLTTKKVVDYTT CCCCCCCCCCCCHHH | 38.03 | 25953088 | |
| 132 | Acetylation | KCDLTTKKVVDYTTA CCCCCCCCCCCHHHH | 45.45 | 26051181 | |
| 132 | Ubiquitination | KCDLTTKKVVDYTTA CCCCCCCCCCCHHHH | 45.45 | - | |
| 136 | Phosphorylation | TTKKVVDYTTAKEFA CCCCCCCHHHHHHHH | 8.38 | 28152594 | |
| 137 | Phosphorylation | TKKVVDYTTAKEFAD CCCCCCHHHHHHHHH | 18.80 | 28152594 | |
| 138 | Phosphorylation | KKVVDYTTAKEFADS CCCCCHHHHHHHHHH | 29.51 | 28152594 | |
| 145 | Phosphorylation | TAKEFADSLGIPFLE HHHHHHHHHCCCCCC | 25.68 | 21712546 | |
| 153 | Phosphorylation | LGIPFLETSAKNATN HCCCCCCCCCCCCCC | 35.81 | 21712546 | |
| 154 | Phosphorylation | GIPFLETSAKNATNV CCCCCCCCCCCCCCH | 28.06 | 21712546 | |
| 159 | Phosphorylation | ETSAKNATNVEQSFM CCCCCCCCCHHHHHH | 49.55 | 29888752 | |
| 167 | Phosphorylation | NVEQSFMTMAAEIKK CHHHHHHHHHHHHHH | 11.14 | 20068231 | |
| 173 | Ubiquitination | MTMAAEIKKRMGPGA HHHHHHHHHHHCCCC | 26.32 | - | |
| 176 | Sulfoxidation | AAEIKKRMGPGATAG HHHHHHHHCCCCCCC | 11.88 | 30846556 | |
| 181 | O-linked_Glycosylation | KRMGPGATAGGAEKS HHHCCCCCCCCCCCC | 31.58 | OGP | |
| 181 | Phosphorylation | KRMGPGATAGGAEKS HHHCCCCCCCCCCCC | 31.58 | 21406692 | |
| 187 | Ubiquitination | ATAGGAEKSNVKIQS CCCCCCCCCCCEEEC | 46.96 | 21906983 | |
| 187 (in isoform 1) | Ubiquitination | - | 46.96 | 21890473 | |
| 188 | Phosphorylation | TAGGAEKSNVKIQST CCCCCCCCCCEEECC | 38.06 | 28857561 | |
| 191 | Ubiquitination | GAEKSNVKIQSTPVK CCCCCCCEEECCCCC | 39.00 | 2190698 | |
| 191 (in isoform 1) | Ubiquitination | - | 39.00 | 21890473 | |
| 194 | Phosphorylation | KSNVKIQSTPVKQSG CCCCEEECCCCCCCC | 37.85 | 30266825 | |
| 195 | Phosphorylation | SNVKIQSTPVKQSGG CCCEEECCCCCCCCC | 18.74 | 30266825 | |
| 204 | Geranylgeranylation | VKQSGGGCC------ CCCCCCCCC------ | 2.55 | 7991565 | |
| 204 | Geranylgeranylation | VKQSGGGCC------ CCCCCCCCC------ | 2.55 | 7991565 | |
| 205 | Geranylgeranylation | KQSGGGCC------- CCCCCCCC------- | 7.65 | 7991565 | |
| 205 | Geranylgeranylation | KQSGGGCC------- CCCCCCCC------- | 7.65 | 7991565 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RAB1A_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 RAB1A_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 |
| "Rab geranylgeranyl transferase catalyzes the geranylgeranylation ofadjacent cysteines in the small GTPases Rab1A, Rab3A, and Rab5A."; Farnsworth C.C., Seabra M.C., Ericsson L.H., Gelb M.H., Glomset J.A.; Proc. Natl. Acad. Sci. U.S.A. 91:11963-11967(1994). Cited for: ISOPRENYLATION AT CYS-204 AND CYS-205, AND MASS SPECTROMETRY. | |
