| UniProt ID | RAC1_HUMAN | |
|---|---|---|
| UniProt AC | P63000 | |
| Protein Name | Ras-related C3 botulinum toxin substrate 1 | |
| Gene Name | RAC1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 192 | |
| Subcellular Localization |
Cell membrane Lipid-anchor Cytoplasmic side. Melanosome . Cytoplasm. Inner surface of plasma membrane possibly with attachment requiring prenylation of the C-terminal cysteine (By similarity). Identified by mass spectrometry in melanosome fractions |
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| Protein Description | Plasma membrane-associated small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins to regulate cellular responses such as secretory processes, phagocytosis of apoptotic cells, epithelial cell polarization, neurons adhesion, migration and differentiation, and growth-factor induced formation of membrane ruffles. Rac1 p21/rho GDI heterodimer is the active component of the cytosolic factor sigma 1, which is involved in stimulation of the NADPH oxidase activity in macrophages. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. Stimulates PKN2 kinase activity. In concert with RAB7A, plays a role in regulating the formation of RBs (ruffled borders) in osteoclasts. In podocytes, promotes nuclear shuttling of NR3C2; this modulation is required for a proper kidney functioning. Required for atypical chemokine receptor ACKR2-induced LIMK1-PAK1-dependent phosphorylation of cofilin (CFL1) and for up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3.; Isoform B has an accelerated GEF-independent GDP/GTP exchange and an impaired GTP hydrolysis, which is restored partially by GTPase-activating proteins. It is able to bind to the GTPase-binding domain of PAK but not full-length PAK in a GTP-dependent manner, suggesting that the insertion does not completely abolish effector interaction.. | |
| Protein Sequence | MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAIRAVLCPPPVKKRKRKCLLL | |
| 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 |
|---|---|---|---|---|---|
| 5 | Ubiquitination | ---MQAIKCVVVGDG ---CCCCEEEEECCC | 24.80 | - | |
| 6 | S-palmitoylation | --MQAIKCVVVGDGA --CCCCEEEEECCCC | 1.99 | 29575903 | |
| 32 | Phosphorylation | TNAFPGEYIPTVFDN CCCCCCCCCCCEECC | 20.37 | 22817900 | |
| 32 | AMPylation | TNAFPGEYIPTVFDN CCCCCCCCCCCEECC | 20.37 | 19362538 | |
| 32 | O-AMP-tyrosine | TNAFPGEYIPTVFDN CCCCCCCCCCCEECC | 20.37 | - | |
| 32 | O-linked_Glycosylation | TNAFPGEYIPTVFDN CCCCCCCCCCCEECC | 20.37 | 24141704 | |
| 35 | O-AMP-threonine | FPGEYIPTVFDNYSA CCCCCCCCEECCCEE | 25.01 | - | |
| 35 | AMPylation | FPGEYIPTVFDNYSA CCCCCCCCEECCCEE | 25.01 | 19039103 | |
| 35 | O-linked_Glycosylation | FPGEYIPTVFDNYSA CCCCCCCCEECCCEE | 25.01 | 24905543 | |
| 39 | ADP-ribosylation | YIPTVFDNYSANVMV CCCCEECCCEEEEEE | 22.61 | - | |
| 39 | ADP-ribosylation | YIPTVFDNYSANVMV CCCCEECCCEEEEEE | 22.61 | - | |
| 64 | Phosphorylation | DTAGQEDYDRLRPLS CCCCCCCHHHCCCCC | 11.38 | 28796482 | |
| 71 | Phosphorylation | YDRLRPLSYPQTDVF HHHCCCCCCCCCCEE | 37.13 | 16831194 | |
| 71 (in isoform 2) | Phosphorylation | - | 37.13 | 23927012 | |
| 72 (in isoform 2) | Phosphorylation | - | 13.67 | 26657352 | |
| 75 (in isoform 2) | Phosphorylation | - | 29.62 | 28387310 | |
| 79 (in isoform 2) | Phosphorylation | - | 3.15 | 28442448 | |
| 80 (in isoform 2) | Phosphorylation | - | 1.19 | 28442448 | |
| 85 (in isoform 2) | Phosphorylation | - | 6.62 | 28442448 | |
| 86 (in isoform 2) | Phosphorylation | - | 21.75 | 28442448 | |
| 89 | Phosphorylation | FSLVSPASFENVRAK EECCCHHHHHCHHHH | 36.16 | - | |
| 96 (in isoform 1) | Ubiquitination | - | 36.37 | 21890473 | |
| 96 | Ubiquitination | SFENVRAKWYPEVRH HHHCHHHHCCHHHHH | 36.37 | 21890473 | |
| 98 | Phosphorylation | ENVRAKWYPEVRHHC HCHHHHCCHHHHHHC | 6.71 | 28152594 | |
| 102 | Methylation | AKWYPEVRHHCPNTP HHCCHHHHHHCCCCC | 16.51 | 115490013 | |
| 108 | Phosphorylation | VRHHCPNTPIILVGT HHHHCCCCCEEEEEE | 10.87 | 23312004 | |
| 115 (in isoform 2) | Ubiquitination | - | 22.43 | 21890473 | |
| 115 | Phosphorylation | TPIILVGTKLDLRDD CCEEEEEECCCCCCC | 22.43 | 23312004 | |
| 116 | Ubiquitination | PIILVGTKLDLRDDK CEEEEEECCCCCCCH | 33.79 | 22053931 | |
| 116 (in isoform 1) | Ubiquitination | - | 33.79 | 21890473 | |
| 123 | Methylation | KLDLRDDKDTIEKLK CCCCCCCHHHHHHHH | 62.15 | - | |
| 123 | Acetylation | KLDLRDDKDTIEKLK CCCCCCCHHHHHHHH | 62.15 | 72664873 | |
| 123 | Ubiquitination | KLDLRDDKDTIEKLK CCCCCCCHHHHHHHH | 62.15 | 21906983 | |
| 123 (in isoform 1) | Ubiquitination | - | 62.15 | 21890473 | |
| 125 | Phosphorylation | DLRDDKDTIEKLKEK CCCCCHHHHHHHHHC | 36.45 | 24961811 | |
| 128 | Ubiquitination | DDKDTIEKLKEKKLT CCHHHHHHHHHCCCC | 62.09 | - | |
| 130 | Trimethylation | KDTIEKLKEKKLTPI HHHHHHHHHCCCCCC | 77.79 | - | |
| 130 | Methylation | KDTIEKLKEKKLTPI HHHHHHHHHCCCCCC | 77.79 | - | |
| 133 | Ubiquitination | IEKLKEKKLTPITYP HHHHHHCCCCCCCCH | 59.70 | 21890473 | |
| 133 (in isoform 1) | Ubiquitination | - | 59.70 | 21890473 | |
| 135 (in isoform 2) | Ubiquitination | - | 22.86 | 21890473 | |
| 142 (in isoform 2) | Ubiquitination | - | 15.76 | 21890473 | |
| 145 | Sulfoxidation | TYPQGLAMAKEIGAV CCHHHHHHHHHHCCE | 7.05 | 30846556 | |
| 147 | Succinylation | PQGLAMAKEIGAVKY HHHHHHHHHHCCEEE | 36.46 | 23954790 | |
| 147 | Acetylation | PQGLAMAKEIGAVKY HHHHHHHHHHCCEEE | 36.46 | 25953088 | |
| 147 | Ubiquitination | PQGLAMAKEIGAVKY HHHHHHHHHHCCEEE | 36.46 | 18093184 | |
| 147 (in isoform 1) | Ubiquitination | - | 36.46 | 21890473 | |
| 152 (in isoform 2) | Ubiquitination | - | 3.36 | 21890473 | |
| 153 (in isoform 1) | Ubiquitination | - | 43.51 | 21890473 | |
| 153 | Ubiquitination | AKEIGAVKYLECSAL HHHHCCEEEEECHHH | 43.51 | 21890473 | |
| 153 | Acetylation | AKEIGAVKYLECSAL HHHHCCEEEEECHHH | 43.51 | 25953088 | |
| 154 | Phosphorylation | KEIGAVKYLECSALT HHHCCEEEEECHHHH | 10.92 | 28152594 | |
| 157 | S-palmitoylation | GAVKYLECSALTQRG CCEEEEECHHHHHHC | 2.38 | 29575903 | |
| 161 | Phosphorylation | YLECSALTQRGLKTV EEECHHHHHHCHHHH | 18.88 | 25850435 | |
| 163 | Methylation | ECSALTQRGLKTVFD ECHHHHHHCHHHHHH | 47.37 | - | |
| 166 (in isoform 2) | Ubiquitination | - | 45.53 | 21890473 | |
| 166 | Ubiquitination | ALTQRGLKTVFDEAI HHHHHCHHHHHHHHH | 45.53 | 21890473 | |
| 166 (in isoform 1) | Ubiquitination | - | 45.53 | 21890473 | |
| 167 | Phosphorylation | LTQRGLKTVFDEAIR HHHHCHHHHHHHHHH | 31.29 | 21082442 | |
| 172 (in isoform 2) | Ubiquitination | - | 9.83 | 21890473 | |
| 178 | S-palmitoylation | EAIRAVLCPPPVKKR HHHHHHCCCCCCCCC | 3.70 | 22157745 | |
| 178 | S-nitrosylation | EAIRAVLCPPPVKKR HHHHHHCCCCCCCCC | 3.70 | 19483679 | |
| 178 | S-nitrosocysteine | EAIRAVLCPPPVKKR HHHHHHCCCCCCCCC | 3.70 | - | |
| 183 | Sumoylation | VLCPPPVKKRKRKCL HCCCCCCCCCCCCEE | 53.27 | - | |
| 183 (in isoform 1) | Ubiquitination | - | 53.27 | 21890473 | |
| 183 | Ubiquitination | VLCPPPVKKRKRKCL HCCCCCCCCCCCCEE | 53.27 | 22053931 | |
| 184 | Sumoylation | LCPPPVKKRKRKCLL CCCCCCCCCCCCEEC | 64.48 | - | |
| 184 | Ubiquitination | LCPPPVKKRKRKCLL CCCCCCCCCCCCEEC | 64.48 | - | |
| 185 (in isoform 2) | Ubiquitination | - | 37.99 | 21890473 | |
| 186 | Sumoylation | PPPVKKRKRKCLLL- CCCCCCCCCCEECC- | 66.15 | - | |
| 188 | Sumoylation | PVKKRKRKCLLL--- CCCCCCCCEECC--- | 32.06 | - | |
| 189 | Geranylgeranylation | VKKRKRKCLLL---- CCCCCCCEECC---- | 3.62 | 1903399 | |
| 189 | Methylation | VKKRKRKCLLL---- CCCCCCCEECC---- | 3.62 | - | |
| 189 | Geranylgeranylation | VKKRKRKCLLL---- CCCCCCCEECC---- | 3.62 | 1903399 | |
| 202 (in isoform 2) | Ubiquitination | - | 21890473 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 64 | Y | Phosphorylation | Kinase | PTK2 | Q05397 | GPS |
| 64 | Y | Phosphorylation | Kinase | SRC | P12931 | PSP |
| 71 | S | Phosphorylation | Kinase | AKT1 | P31749 | PSP |
| 71 | S | Phosphorylation | Kinase | AKT-FAMILY | - | GPS |
| 71 | S | Phosphorylation | Kinase | PKB_GROUP | - | PhosphoELM |
| 108 | T | Phosphorylation | Kinase | MAPK3 | P27361 | GPS |
| - | K | Ubiquitination | E3 ubiquitin ligase | HACE1 | Q8IYU2 | PMID:22036506 |
| - | K | Ubiquitination | E3 ubiquitin ligase | BIRC2 | Q13490 | PMID:22117219 |
| - | K | Ubiquitination | E3 ubiquitin ligase | FBXL19 | Q6PCT2 | PMID:24658274 |
| - | K | Ubiquitination | E3 ubiquitin ligase | SMURF1 | Q9HCE7 | PMID:16472676 |
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 35 | T | Glycosylation |
| 8810274 |
* 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 RAC1_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 |
| "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 SER-71, AND MASSSPECTROMETRY. | |
| Prenylation | |
| Reference | PubMed |
| "Carboxyl-terminal isoprenylation of ras-related GTP-binding proteinsencoded by rac1, rac2, and ralA."; Kinsella B.T., Erdman R.A., Maltese W.A.; J. Biol. Chem. 266:9786-9794(1991). Cited for: ISOPRENYLATION AT CYS-189. | |
| Ubiquitylation | |
| Reference | PubMed |
| "Activated Rac1, but not the tumorigenic variant Rac1b, isubiquitinated on Lys 147 through a JNK-regulated process."; Visvikis O., Lores P., Boyer L., Chardin P., Lemichez E., Gacon G.; FEBS J. 275:386-396(2008). Cited for: UBIQUITINATION AT LYS-147. | |
