ID RHOA_BOVIN Reviewed; 193 AA. AC P61585; P06749; Q3ZC72; Q9UEJ4; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 04-NOV-2026, entry version 184. DE RecName: Full=Transforming protein RhoA; DE EC=3.6.5.2 {ECO:0000250|UniProtKB:P61586}; DE AltName: Full=Gb; DE AltName: Full=p21; DE Flags: Precursor; GN Name=RHOA; Synonyms=ARHA, RHO12; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2506852; DOI=10.1016/0006-291x(89)92344-9; RA Ogorochi T., Nemoto Y., Nakajima M., Nakamura E., Fujiwara M., Narumiya S.; RT "cDNA cloning of Gb, the substrate for botulinum ADP-ribosyltransferase RT from bovine adrenal gland and its identification as a rho gene product."; RL Biochem. Biophys. Res. Commun. 163:1175-1181(1989). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 19-25; 42-50; 52-57; 59-97; 99-104; 134-162 AND RP 169-176. RC TISSUE=Adrenal gland; RX PubMed=3141419; DOI=10.1016/s0021-9258(19)77828-4; RA Narumiya S., Sekine A., Fujiwara M.; RT "Substrate for botulinum ADP-ribosyltransferase, Gb, has an amino acid RT sequence homologous to a putative rho gene product."; RL J. Biol. Chem. 263:17255-17257(1988). RN [4] RP PROTEIN SEQUENCE OF 28-70 AND 99-194, AND ADP-RIBOSYLATION AT ASN-41. RX PubMed=2174426; DOI=10.1016/s0021-9258(17)45287-2; RA Williamson K.C., Smith L.A., Moss J., Vaughan M.; RT "Guanine nucleotide-dependent ADP-ribosylation of soluble rho catalyzed by RT Clostridium botulinum C3 ADP-ribosyltransferase. Isolation and RT characterization of a newly recognized form of rhoA."; RL J. Biol. Chem. 265:20807-20812(1990). RN [5] RP PROTEIN SEQUENCE OF 37-47, AND ADP-RIBOSYLATION AT ASN-41. RX PubMed=2498316; DOI=10.1016/s0021-9258(18)81834-8; RA Sekine A., Fujiwara M., Narumiya S.; RT "Asparagine residue in the rho gene product is the modification site for RT botulinum ADP-ribosyltransferase."; RL J. Biol. Chem. 264:8602-8605(1989). RN [6] RP ISOPRENYLATION AT CYS-190, AND METHYLATION AT CYS-190. RC TISSUE=Aortic smooth muscle; RX PubMed=1905729; DOI=10.1016/s0021-9258(18)98947-7; RA Katayama M., Kawata M., Yoshida Y., Horiuchi H., Yamamoto T., Matsuura Y., RA Takai Y.; RT "The posttranslationally modified C-terminal structure of bovine aortic RT smooth muscle rhoA p21."; RL J. Biol. Chem. 266:12639-12645(1991). CC -!- FUNCTION: Small GTPase which cycles between an active GTP-bound and an CC inactive GDP-bound state. Mainly associated with cytoskeleton CC organization, in active state binds to a variety of effector proteins CC to regulate cellular responses such as cytoskeletal dynamics, cell CC migration and cell cycle. Regulates a signal transduction pathway CC linking plasma membrane receptors to the assembly of focal adhesions CC and actin stress fibers. Involved in a microtubule-dependent signal CC that is required for the myosin contractile ring formation during cell CC cycle cytokinesis. Plays an essential role in cleavage furrow CC formation. Required for the apical junction formation of keratinocyte CC cell-cell adhesion. Essential for the SPATA13-mediated regulation of CC cell migration and adhesion assembly and disassembly. The MEMO1-RHOA- CC DIAPH1 signaling pathway plays an important role in ERBB2-dependent CC stabilization of microtubules at the cell cortex. It controls the CC localization of APC and CLASP2 to the cell membrane, via the regulation CC of GSK3B activity. In turn, membrane-bound APC allows the localization CC of the MACF1 to the cell membrane, which is required for microtubule CC capture and stabilization. Involved in the reorientation of endothelial CC cells and their actin stress fibers in response to cellular CC mechantransduction-mediated activation by ARHGEF40 (By similarity). CC Regulates KCNA2 potassium channel activity by reducing its location at CC the cell surface in response to CHRM1 activation; promotes KCNA2 CC endocytosis. Acts as an allosteric activator of guanine nucleotide CC exchange factor ECT2 by binding in its activated GTP-bound form to the CC PH domain of ECT2 which stimulates the release of PH inhibition and CC promotes the binding of substrate RHOA to the ECT2 catalytic center. CC May be an activator of PLCE1. In neurons, involved in the inhibition of CC the initial spine growth. Upon activation by CaMKII, modulates CC dendritic spine structural plasticity by relaying CaMKII transient CC activation to synapse-specific, long-term signaling. Acts as a CC regulator of platelet alpha-granule release during activation and CC aggregation of platelets (By similarity). When activated by DAAM1 may CC signal centrosome maturation and chromosomal segregation during cell CC division. May also be involved in contractile ring formation during CC cytokinesis. {ECO:0000250|UniProtKB:P24406, CC ECO:0000250|UniProtKB:P61586, ECO:0000250|UniProtKB:P61589, CC ECO:0000250|UniProtKB:Q9QUI0}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + phosphate + H(+); Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; CC Evidence={ECO:0000250|UniProtKB:P61586}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:P61586}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P61586}; CC -!- ACTIVITY REGULATION: Regulated by guanine nucleotide exchange factors CC (GEFs) which promote the exchange of bound GDP for free GTP, GTPase CC activating proteins (GAPs) which increase the GTP hydrolysis activity CC and GDP dissociation inhibitors which inhibit the dissociation of the CC nucleotide from the GTPase. Activated by GEFs such as ARHGEF2, ARHGEF3, CC ARHGEF28 and BCR. Activated by ARHGEF40 in response to CC mechanotransduction in endothelial cells (By similarity). Inhibited by CC GAPs such as ARHGAP30. Inhibited by GDP dissociation inhibitors such as CC ARHGDIA. {ECO:0000250|UniProtKB:P24406, ECO:0000250|UniProtKB:P61586}. CC -!- SUBUNIT: Interacts with ARHGEF28 (By similarity). Interacts (via GTP- CC bound form) with RIPOR1 (via N-terminus); this interaction links RHOA CC to STK24 and STK26 kinases. Interacts with RIPOR2 (via active GTP- or CC inactive GDP-bound forms) isoform 1 and isoform 2; these interactions CC are direct, block the loading of GTP to RHOA and decrease upon CC chemokine CCL19 stimulation in primary T lymphocytes. Binds PRKCL1, CC ROCK1 and ROCK2. Interacts with ARHGEF2, ARHGEF3, NET1 and RTKN. CC Interacts with PLCE1 and AKAP13. Interacts with DIAPH1. Interacts (in CC the constitutively activated, GTP-bound form) with DGKQ. Interacts with CC RACK1; enhances RHOA activation. Interacts with PKP4; the interaction CC is detected at the midbody. Interacts (GTP-bound form preferentially) CC with PKN2; the interaction stimulates autophosphorylation and CC phosphorylation of PKN2. Interacts with ARHGDIA; this interaction CC inactivates and stabilizes RHOA. Interacts with ARHGDIB. Interacts CC (GTP-bound form) with KCNA2 (via cytoplasmic N-terminal domain) (By CC similarity). Interacts (GTP-bound form) with ECT2; the interaction CC results in allosteric activation of ECT2. Interacts with RAP1GDS1; the CC interaction is direct and in a 1:1 stoichiometry (By similarity). CC Interacts with ARHGAP19 (By similarity). {ECO:0000250|UniProtKB:P61586, CC ECO:0000250|UniProtKB:Q9QUI0}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P61586}; CC Lipid-anchor {ECO:0000250|UniProtKB:P61586}; Cytoplasmic side CC {ECO:0000250|UniProtKB:P61586}. Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:P61586}. Cleavage furrow CC {ECO:0000250|UniProtKB:P61586}. Cytoplasm, cell cortex CC {ECO:0000250|UniProtKB:P61586}. Midbody {ECO:0000250|UniProtKB:P61586}. CC Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q9QUI0}. Cell CC projection, dendrite {ECO:0000250|UniProtKB:Q9QUI0}. Nucleus CC {ECO:0000250|UniProtKB:P61586}. Cytoplasm CC {ECO:0000250|UniProtKB:P61586}. Note=Localized to cell-cell contacts in CC calcium-treated keratinocytes (By similarity). Translocates to the CC equatorial region before furrow formation in a ECT2-dependent manner. CC Localizes to the equatorial cell cortex (at the site of the presumptive CC furrow) in early anaphase in an activated form and in a myosin- and CC actin-independent manner. Colocalizes with KANK1 at the contractile CC ring. Colocalizes with DAAM1 and KANK1 around centrosomes. CC {ECO:0000250|UniProtKB:Q9QUI0}. CC -!- PTM: Phosphorylation by PRKG1 at Ser-188 inactivates RHOA signaling (By CC similarity). Phosphorylation by SLK at Ser-188 in response to AGTR2 CC activation (By similarity). {ECO:0000250|UniProtKB:P61586, CC ECO:0000250|UniProtKB:P61589}. CC -!- PTM: Ubiquitinated by the BCR(KCTD13) and BCR(TNFAIP1) E3 ubiquitin CC ligase complexes, leading to its degradation by the proteasome, thereby CC regulating the actin cytoskeleton and synaptic transmission in neurons. CC Ubiquitinated at Lys-135 in a FBXL19-mediated manner; leading to CC proteasomal degradation. {ECO:0000250|UniProtKB:P61586, CC ECO:0000250|UniProtKB:Q9QUI0}. CC -!- PTM: Serotonylation of Gln-63 by TGM2 during activation and aggregation CC of platelets leads to constitutive activation of GTPase activity. CC {ECO:0000250|UniProtKB:Q9QUI0}. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M27278; AAA30409.1; -; mRNA. DR EMBL; BC102880; AAI02881.1; -; mRNA. DR PIR; A33518; TVBO12. DR RefSeq; NP_788818.1; NM_176645.3. DR AlphaFoldDB; P61585; -. DR BMRB; P61585; -. DR SMR; P61585; -. DR CORUM; P61585; -. DR FunCoup; P61585; 4092. DR IntAct; P61585; 8. DR STRING; 9913.ENSBTAP00000005600; -. DR iPTMnet; P61585; -. DR PaxDb; 9913-ENSBTAP00000005600; -. DR PeptideAtlas; P61585; -. DR Ensembl; ENSBTAT00000005600.7; ENSBTAP00000005600.5; ENSBTAG00000004279.7. DR Ensembl; ENSBTAT00085071837; ENSBTAP00085016257; ENSBTAG00085040842. DR Ensembl; ENSBTAT00090067552; ENSBTAP00090037027; ENSBTAG00090031916. DR GeneID; 338049; -. DR KEGG; bta:338049; -. DR CTD; 387; -. DR VEuPathDB; HostDB:ENSBTAG00000004279; -. DR VGNC; VGNC:33943; RHOA. DR eggNOG; KOG0393; Eukaryota. DR GeneTree; ENSGT00950000182945; -. DR HOGENOM; CLU_041217_21_2_1; -. DR InParanoid; P61585; -. DR OMA; AAHIYDK; -. DR OrthoDB; 8830751at2759; -. DR Reactome; R-BTA-114604; GPVI-mediated activation cascade. DR Reactome; R-BTA-193634; Axonal growth inhibition (RHOA activation). DR Reactome; R-BTA-198203; PI3K/AKT activation. DR Reactome; R-BTA-209563; Axonal growth stimulation. DR Reactome; R-BTA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition). DR Reactome; R-BTA-392451; G beta:gamma signalling through PI3Kgamma. DR Reactome; R-BTA-3928662; EPHB-mediated forward signaling. DR Reactome; R-BTA-3928663; EPHA-mediated growth cone collapse. DR Reactome; R-BTA-4086400; PCP/CE pathway. DR Reactome; R-BTA-416482; G alpha (12/13) signalling events. DR Reactome; R-BTA-416550; Sema4D mediated inhibition of cell attachment and migration. DR Reactome; R-BTA-416572; Sema4D induced cell migration and growth-cone collapse. DR Reactome; R-BTA-4420097; VEGFA-VEGFR2 Pathway. DR Reactome; R-BTA-5625740; RHO GTPases activate PKNs. DR Reactome; R-BTA-5625900; RHO GTPases activate CIT. DR Reactome; R-BTA-5625970; RHO GTPases activate KTN1. DR Reactome; R-BTA-5627117; RHO GTPases Activate ROCKs. DR Reactome; R-BTA-5663220; RHO GTPases Activate Formins. DR Reactome; R-BTA-5666185; RHO GTPases Activate Rhotekin and Rhophilins. DR Reactome; R-BTA-5689896; Ovarian tumor domain proteases. DR Reactome; R-BTA-6785631; ERBB2 Regulates Cell Motility. DR Reactome; R-BTA-6798695; Neutrophil degranulation. DR Reactome; R-BTA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases. DR Reactome; R-BTA-8980692; RHOA GTPase cycle. DR Reactome; R-BTA-8985586; SLIT2:ROBO1 increases RHOA activity. DR Reactome; R-BTA-9013106; RHOC GTPase cycle. DR PRO; PR:P61585; -. DR Proteomes; UP000009136; Chromosome 22. DR Bgee; ENSBTAG00000004279; Expressed in milk and 102 other cell types or tissues. DR GO; GO:0043296; C:apical junction complex; ISS:UniProtKB. DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB. DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISS:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central. DR GO; GO:0005768; C:endosome; IEA:Ensembl. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB. DR GO; GO:0030496; C:midbody; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0003925; F:G protein activity; IEA:UniProtKB-EC. DR GO; GO:0005525; F:GTP binding; ISS:UniProtKB. DR GO; GO:0003924; F:GTPase activity; ISS:UniProtKB. DR GO; GO:0017022; F:myosin binding; IEA:Ensembl. DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central. DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0002363; P:alpha-beta T cell lineage commitment; IEA:Ensembl. DR GO; GO:0003189; P:aortic valve formation; IEA:Ensembl. DR GO; GO:0043297; P:apical junction assembly; ISS:UniProtKB. DR GO; GO:0038027; P:apolipoprotein A-I-mediated signaling pathway; IEA:Ensembl. DR GO; GO:0043366; P:beta selection; IEA:Ensembl. DR GO; GO:0061430; P:bone trabecula morphogenesis; IEA:Ensembl. DR GO; GO:0034329; P:cell junction assembly; ISS:UniProtKB. DR GO; GO:0016477; P:cell migration; ISS:UniProtKB. DR GO; GO:1990869; P:cellular response to chemokine; ISS:UniProtKB. DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl. DR GO; GO:0036089; P:cleavage furrow formation; ISS:UniProtKB. DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISS:UniProtKB. DR GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISS:UniProtKB. DR GO; GO:1903673; P:mitotic cleavage furrow formation; ISS:UniProtKB. DR GO; GO:0090307; P:mitotic spindle assembly; IEA:Ensembl. DR GO; GO:0050919; P:negative chemotaxis; IEA:Ensembl. DR GO; GO:0045792; P:negative regulation of cell size; IEA:Ensembl. DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl. DR GO; GO:0090324; P:negative regulation of oxidative phosphorylation; IEA:Ensembl. DR GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IEA:Ensembl. DR GO; GO:0042476; P:odontogenesis; IEA:Ensembl. DR GO; GO:0043931; P:ossification involved in bone maturation; IEA:Ensembl. DR GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; IEA:Ensembl. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; ISS:UniProtKB. DR GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB. DR GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; IEA:Ensembl. DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISS:UniProtKB. DR GO; GO:2000406; P:positive regulation of T cell migration; ISS:UniProtKB. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central. DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB. DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:Ensembl. DR GO; GO:1905274; P:regulation of modification of postsynaptic actin cytoskeleton; IEA:Ensembl. DR GO; GO:0033688; P:regulation of osteoblast proliferation; IEA:Ensembl. DR GO; GO:0007266; P:Rho protein signal transduction; ISS:UniProtKB. DR GO; GO:0035385; P:Roundabout signaling pathway; ISS:UniProtKB. DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; IEA:Ensembl. DR GO; GO:1902766; P:skeletal muscle satellite cell migration; ISS:AgBase. DR GO; GO:0043149; P:stress fiber assembly; ISS:UniProtKB. DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISS:UniProtKB. DR GO; GO:0044319; P:wound healing, spreading of cells; ISS:AgBase. DR CDD; cd01870; RhoA_like; 1. DR FunFam; 3.40.50.300:FF:000095; Rho-related GTP-binding protein RhoC; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd. DR InterPro; IPR001806; Small_GTPase. DR InterPro; IPR003578; Small_GTPase_Rho. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR24072; RHO FAMILY GTPASE; 1. DR Pfam; PF00071; Ras; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SMART; SM00173; RAS; 1. DR SMART; SM00174; RHO; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51420; RHO; 1. PE 1: Evidence at protein level; KW ADP-ribosylation; Cell cycle; Cell division; Cell membrane; KW Cell projection; Cytoplasm; Cytoskeleton; Direct protein sequencing; KW GTP-binding; Hydrolase; Isopeptide bond; Lipoprotein; Magnesium; Membrane; KW Metal-binding; Methylation; Nucleotide-binding; Nucleus; Phosphoprotein; KW Prenylation; Proto-oncogene; Reference proteome; Ubl conjugation. FT CHAIN 1..190 FT /note="Transforming protein RhoA" FT /id="PRO_0000030407" FT PROPEP 191..193 FT /note="Removed in mature form" FT /evidence="ECO:0000269|PubMed:1905729" FT /id="PRO_0000457667" FT REGION 61..78 FT /note="Switch II region; involved in RAP1GDS1 isoform 2 FT binding" FT /evidence="ECO:0000250|UniProtKB:P61586" FT MOTIF 34..42 FT /note="Effector region" FT /evidence="ECO:0000255" FT BINDING 15 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61586" FT BINDING 16 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61586" FT BINDING 17 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61586" FT BINDING 18 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61586" FT BINDING 19 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61586" FT BINDING 19 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P61586" FT BINDING 20 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61586" FT BINDING 34 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61586" FT BINDING 37 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61586" FT BINDING 37 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P61586" FT BINDING 59 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P61586" FT BINDING 62 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61586" FT BINDING 118 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61586" FT BINDING 120 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61586" FT BINDING 161 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61586" FT BINDING 162 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P61586" FT MOD_RES 41 FT /note="(Microbial infection) ADP-ribosylasparagine; by FT botulinum toxin" FT /evidence="ECO:0000269|PubMed:2174426, FT ECO:0000269|PubMed:2498316" FT MOD_RES 63 FT /note="5-glutamyl serotonin" FT /evidence="ECO:0000250|UniProtKB:Q9QUI0" FT MOD_RES 188 FT /note="Phosphoserine; by PKG/PRKG1" FT /evidence="ECO:0000250|UniProtKB:P61589" FT MOD_RES 190 FT /note="Cysteine methyl ester" FT /evidence="ECO:0000269|PubMed:1905729" FT LIPID 190 FT /note="S-geranylgeranyl cysteine" FT /evidence="ECO:0000269|PubMed:1905729" FT CROSSLNK 135 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250|UniProtKB:P61586" SQ SEQUENCE 193 AA; 21768 MW; C4DA2DC31FF858BC CRC64; MAAIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG KQVELALWDT AGQEDYDRLR PLSYPDTDVI LMCFSIDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD LRNDEHTRRE LAKMKQEPVK PEEGRDMANR IGAFGYMECS AKTKDGVREV FEMATRAALQ ARRGKKKSGC LVL //