ID ARL2_HUMAN Reviewed; 184 AA. AC P36404; G3V184; Q9BUK8; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 4. DT 10-FEB-2021, entry version 194. DE RecName: Full=ADP-ribosylation factor-like protein 2; GN Name=ARL2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-141. RX PubMed=8415637; DOI=10.1073/pnas.90.19.8952; RA Clark J., Moore L., Krasinskas A., Way J., Battey J.F., Tamkun J.W., RA Kahn R.A.; RT "Selective amplification of additional members of the ADP-ribosylation RT factor (ARF) family: cloning of additional human and Drosophila ARF-like RT genes."; RL Proc. Natl. Acad. Sci. U.S.A. 90:8952-8956(1993). RN [2] RP SEQUENCE REVISION TO 11. RA Kahn R.A.; RL Submitted (NOV-1997) to UniProtKB. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-141. RC TISSUE=Brain; RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.; RT "cDNA clones of human proteins involved in signal transduction sequenced by RT the Guthrie cDNA resource center (www.cdna.org)."; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT ALA-141. RX PubMed=15146197; DOI=10.1038/nbt971; RA Brandenberger R., Wei H., Zhang S., Lei S., Murage J., Fisk G.J., Li Y., RA Xu C., Fang R., Guegler K., Rao M.S., Mandalam R., Lebkowski J., RA Stanton L.W.; RT "Transcriptome characterization elucidates signaling networks that control RT human ES cell growth and differentiation."; RL Nat. Biotechnol. 22:707-716(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP INTERACTION WITH ARL2BP. RX PubMed=10488091; DOI=10.1074/jbc.274.39.27553; RA Sharer J.D., Kahn R.A.; RT "The ARF-like 2 (ARL2)-binding protein, BART. Purification, cloning, and RT initial characterization."; RL J. Biol. Chem. 274:27553-27561(1999). RN [9] RP FUNCTION, INTERACTION WITH TBCD, AND MUTAGENESIS OF THR-30; THR-47; PHE-50 RP AND GLN-70. RX PubMed=10831612; DOI=10.1083/jcb.149.5.1087; RA Bhamidipati A., Lewis S.A., Cowan N.J.; RT "ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of RT tubulin-folding cofactor D with native tubulin."; RL J. Cell Biol. 149:1087-1096(2000). RN [10] RP INTERACTION WITH ARL2BP AND PDE6D, AND MUTAGENESIS OF GLN-70. RX PubMed=11303027; DOI=10.1074/jbc.m102359200; RA Van Valkenburgh H., Shern J.F., Sharer J.D., Zhu X., Kahn R.A.; RT "ADP-ribosylation factors (ARFs) and ARF-like 1 (ARL1) have both specific RT and shared effectors: characterizing ARL1-binding proteins."; RL J. Biol. Chem. 276:22826-22837(2001). RN [11] RP INTERACTION WITH ARL2BP. RX PubMed=11847227; DOI=10.1074/jbc.m200128200; RA Bartolini F., Bhamidipati A., Thomas S., Schwahn U., Lewis S.A., RA Cowan N.J.; RT "Functional overlap between retinitis pigmentosa 2 protein and the tubulin- RT specific chaperone cofactor C."; RL J. Biol. Chem. 277:14629-14634(2002). RN [12] RP SUBCELLULAR LOCATION, AND LACK OF N-MYRISTOYLATION. RX PubMed=11809823; DOI=10.1091/mbc.01-05-0245; RA Sharer J.D., Shern J.F., Van Valkenburgh H., Wallace D.C., Kahn R.A.; RT "ARL2 and BART enter mitochondria and bind the adenine nucleotide RT transporter."; RL Mol. Biol. Cell 13:71-83(2002). RN [13] RP FUNCTION, MUTAGENESIS OF GLN-70, AND SUBCELLULAR LOCATION. RX PubMed=16525022; DOI=10.1091/mbc.e05-10-0929; RA Zhou C., Cunningham L., Marcus A.I., Li Y., Kahn R.A.; RT "Arl2 and Arl3 regulate different microtubule-dependent processes."; RL Mol. Biol. Cell 17:2476-2487(2006). RN [14] RP INTERACTION WITH ELMOD2. RX PubMed=17452337; DOI=10.1074/jbc.m701347200; RA Bowzard J.B., Cheng D., Peng J., Kahn R.A.; RT "ELMOD2 is an Arl2 GTPase-activating protein that also acts on Arfs."; RL J. Biol. Chem. 282:17568-17580(2007). RN [15] RP FUNCTION, AND GTP/GDP BINDING. RX PubMed=18588884; DOI=10.1016/j.febslet.2008.05.053; RA Veltel S., Kravchenko A., Ismail S., Wittinghofer A.; RT "Specificity of Arl2/Arl3 signaling is mediated by a ternary Arl3-effector- RT GAP complex."; RL FEBS Lett. 582:2501-2507(2008). RN [16] RP FUNCTION, INTERACTION WITH ARL2BP, MUTAGENESIS OF THR-30 AND GLN-70, AND RP SUBCELLULAR LOCATION. RX PubMed=18234692; DOI=10.1093/intimm/dxm154; RA Muromoto R., Sekine Y., Imoto S., Ikeda O., Okayama T., Sato N., RA Matsuda T.; RT "BART is essential for nuclear retention of STAT3."; RL Int. Immunol. 20:395-403(2008). RN [17] RP INTERACTION WITH ARL2BP. RX PubMed=18981177; DOI=10.1074/jbc.m806167200; RA Bailey L.K., Campbell L.J., Evetts K.A., Littlefield K., Rajendra E., RA Nietlispach D., Owen D., Mott H.R.; RT "The structure of binder of Arl2 (BART) reveals a novel G protein binding RT domain: implications for function."; RL J. Biol. Chem. 284:992-999(2009). RN [18] RP FUNCTION. RX PubMed=20740604; DOI=10.1002/cm.20480; RA Tian G., Thomas S., Cowan N.J.; RT "Effect of TBCD and its regulatory interactor Arl2 on tubulin and RT microtubule integrity."; RL Cytoskeleton 67:706-714(2010). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP INTERACTION WITH TBCD. RX PubMed=27666374; DOI=10.1016/j.ajhg.2016.08.005; RA Miyake N., Fukai R., Ohba C., Chihara T., Miura M., Shimizu H., Kakita A., RA Imagawa E., Shiina M., Ogata K., Okuno-Yuguchi J., Fueki N., Ogiso Y., RA Suzumura H., Watabe Y., Imataka G., Leong H.Y., Fattal-Valevski A., RA Kramer U., Miyatake S., Kato M., Okamoto N., Sato Y., Mitsuhashi S., RA Nishino I., Kaneko N., Nishiyama A., Tamura T., Mizuguchi T., Nakashima M., RA Tanaka F., Saitsu H., Matsumoto N.; RT "Biallelic TBCD mutations cause early-onset neurodegenerative RT encephalopathy."; RL Am. J. Hum. Genet. 99:950-961(2016). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 1-184 IN A COMPLEX WITH ARL2BP; RP GTP AND MAGNESIUM IONS, INTERACTION WITH ARL2BP, AND MUTAGENESIS OF LEU-3; RP LEU-4; ILE-6; LEU-7; PHE-50; TYR-76 AND TYR-80. RX PubMed=19368893; DOI=10.1016/j.str.2009.01.014; RA Zhang T., Li S., Zhang Y., Zhong C., Lai Z., Ding J.; RT "Crystal structure of the ARL2-GTP-BART complex reveals a novel recognition RT and binding mode of small GTPase with effector."; RL Structure 17:602-610(2009). CC -!- FUNCTION: Small GTP-binding protein which cycles between an inactive CC GDP-bound and an active GTP-bound form, and the rate of cycling is CC regulated by guanine nucleotide exchange factors (GEF) and GTPase- CC activating proteins (GAP). GTP-binding protein that does not act as an CC allosteric activator of the cholera toxin catalytic subunit. Regulates CC formation of new microtubules and centrosome integrity. Prevents the CC TBCD-induced microtubule destruction. Participates in association with CC TBCD, in the disassembly of the apical junction complexes. Antagonizes CC the effect of TBCD on epithelial cell detachment and tight and adherens CC junctions disassembly. Together with ARL2, plays a role in the nuclear CC translocation, retention and transcriptional activity of STAT3. CC Component of a regulated secretory pathway involved in Ca(2+)-dependent CC release of acetylcholine. Required for normal progress through the cell CC cycle. {ECO:0000269|PubMed:10831612, ECO:0000269|PubMed:16525022, CC ECO:0000269|PubMed:18234692, ECO:0000269|PubMed:18588884, CC ECO:0000269|PubMed:20740604}. CC -!- SUBUNIT: Found in a complex with ARL2, ARL2BP and SLC25A6. Found in a CC complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. CC Found in a complex with ARL2, ARL2BP and SLC25A4. The GTP-bound form CC interacts with PDE6D. Interacts with ELMOD2. The GTP-bound form CC interacts with ARL2BP. Interacts, preferentially in its GDP-bound CC state, with TBCD. Interacts with UNC119. {ECO:0000269|PubMed:10488091, CC ECO:0000269|PubMed:10831612, ECO:0000269|PubMed:11303027, CC ECO:0000269|PubMed:11847227, ECO:0000269|PubMed:17452337, CC ECO:0000269|PubMed:18234692, ECO:0000269|PubMed:18981177, CC ECO:0000269|PubMed:19368893, ECO:0000269|PubMed:27666374}. CC -!- INTERACTION: CC P36404; Q9Y2Y0: ARL2BP; NbExp=24; IntAct=EBI-752365, EBI-3449344; CC P36404; Q969G2: LHX4; NbExp=3; IntAct=EBI-752365, EBI-2865388; CC P36404; O43924: PDE6D; NbExp=18; IntAct=EBI-752365, EBI-712685; CC P36404; Q9BZK7: TBL1XR1; NbExp=4; IntAct=EBI-752365, EBI-765729; CC P36404; Q13432: UNC119; NbExp=11; IntAct=EBI-752365, EBI-711260; CC -!- SUBCELLULAR LOCATION: Mitochondrion intermembrane space. Cytoplasm, CC cytoskeleton, microtubule organizing center, centrosome. Nucleus. CC Cytoplasm. Note=The complex formed with ARL2BP, ARL2 and SLC25A6 is CC expressed in mitochondria. The complex formed with ARL2BP, ARL2 and CC SLC25A4 is expressed in mitochondria (By similarity). Not detected in CC the Golgi, nucleus and on the mitotic spindle. Centrosome-associated CC throughout the cell cycle. Not detected to interphase microtubules. CC {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P36404-1; Sequence=Displayed; CC Name=2; CC IsoId=P36404-2; Sequence=VSP_047278; CC -!- PTM: Not N-myristoylated. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Arf 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; L13687; AAC37606.1; -; mRNA. DR EMBL; AF493888; AAM12602.1; -; mRNA. DR EMBL; CN338497; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AP000436; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471076; EAW74333.1; -; Genomic_DNA. DR EMBL; BC002530; AAH02530.1; -; mRNA. DR CCDS; CCDS55770.1; -. [P36404-2] DR CCDS; CCDS8088.1; -. [P36404-1] DR PIR; A48259; A48259. DR RefSeq; NP_001186674.1; NM_001199745.1. [P36404-2] DR RefSeq; NP_001658.2; NM_001667.3. [P36404-1] DR PDB; 3DOE; X-ray; 2.25 A; A=1-184. DR PDB; 3DOF; X-ray; 3.30 A; A=1-184. DR PDBsum; 3DOE; -. DR PDBsum; 3DOF; -. DR SMR; P36404; -. DR BioGRID; 106895; 87. DR CORUM; P36404; -. DR DIP; DIP-47535N; -. DR IntAct; P36404; 24. DR MINT; P36404; -. DR STRING; 9606.ENSP00000246747; -. DR ChEMBL; CHEMBL4295751; -. DR DrugBank; DB14731; Tagraxofusp. DR iPTMnet; P36404; -. DR PhosphoSitePlus; P36404; -. DR BioMuta; ARL2; -. DR DMDM; 116241255; -. DR EPD; P36404; -. DR jPOST; P36404; -. DR MassIVE; P36404; -. DR PaxDb; P36404; -. DR PeptideAtlas; P36404; -. DR PRIDE; P36404; -. DR ProteomicsDB; 32289; -. DR ProteomicsDB; 55198; -. [P36404-1] DR Antibodypedia; 29583; 356 antibodies. DR DNASU; 402; -. DR Ensembl; ENST00000246747; ENSP00000246747; ENSG00000213465. [P36404-1] DR Ensembl; ENST00000529384; ENSP00000436021; ENSG00000213465. [P36404-1] DR Ensembl; ENST00000533729; ENSP00000432971; ENSG00000213465. [P36404-2] DR GeneID; 402; -. DR KEGG; hsa:402; -. DR UCSC; uc021qlc.2; human. [P36404-1] DR CTD; 402; -. DR DisGeNET; 402; -. DR GeneCards; ARL2; -. DR HGNC; HGNC:693; ARL2. DR HPA; ENSG00000213465; Low tissue specificity. DR MIM; 601175; gene. DR neXtProt; NX_P36404; -. DR OpenTargets; ENSG00000213465; -. DR PharmGKB; PA24986; -. DR VEuPathDB; HostDB:ENSG00000213465.7; -. DR eggNOG; KOG0073; Eukaryota. DR GeneTree; ENSGT00940000157941; -. DR HOGENOM; CLU_040729_12_3_1; -. DR InParanoid; P36404; -. DR OMA; EHRGYKL; -. DR PhylomeDB; P36404; -. DR TreeFam; TF105462; -. DR PathwayCommons; P36404; -. DR Reactome; R-HSA-389977; Post-chaperonin tubulin folding pathway. DR Reactome; R-HSA-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane. DR Reactome; R-HSA-9648002; RAS processing. DR BioGRID-ORCS; 402; 747 hits in 879 CRISPR screens. DR EvolutionaryTrace; P36404; -. DR GeneWiki; ARL2; -. DR GenomeRNAi; 402; -. DR Pharos; P36404; Tbio. DR PRO; PR:P36404; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P36404; protein. DR Bgee; ENSG00000213465; Expressed in nucleus accumbens and 226 other tissues. DR ExpressionAtlas; P36404; baseline and differential. DR Genevisible; P36404; HS. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005925; C:focal adhesion; IDA:HPA. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0016328; C:lateral plasma membrane; ISS:UniProtKB. DR GO; GO:0015630; C:microtubule cytoskeleton; IBA:GO_Central. DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:UniProtKB. DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0019003; F:GDP binding; IEA:Ensembl. DR GO; GO:0005525; F:GTP binding; IMP:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IMP:UniProtKB. DR GO; GO:0005095; F:GTPase inhibitor activity; TAS:ProtInc. DR GO; GO:0070830; P:bicellular tight junction assembly; ISS:UniProtKB. DR GO; GO:0007098; P:centrosome cycle; IMP:UniProtKB. DR GO; GO:0051457; P:maintenance of protein location in nucleus; IDA:UniProtKB. DR GO; GO:0034260; P:negative regulation of GTPase activity; IDA:UniProtKB. DR GO; GO:0010811; P:positive regulation of cell-substrate adhesion; ISS:UniProtKB. DR GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:UniProtKB. DR GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome. DR GO; GO:0031113; P:regulation of microtubule polymerization; IMP:UniProtKB. DR GO; GO:0007021; P:tubulin complex assembly; TAS:ProtInc. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR006689; Small_GTPase_ARF/SAR. DR Pfam; PF00025; Arf; 1. DR PRINTS; PR00328; SAR1GTPBP. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51417; ARF; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell cycle; Cytoplasm; Cytoskeleton; KW GTP-binding; Isopeptide bond; Lipoprotein; Mitochondrion; Myristate; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000255" FT CHAIN 2..184 FT /note="ADP-ribosylation factor-like protein 2" FT /id="PRO_0000207453" FT NP_BIND 23..30 FT /note="GTP" FT /evidence="ECO:0000250" FT NP_BIND 66..70 FT /note="GTP" FT /evidence="ECO:0000250" FT NP_BIND 125..128 FT /note="GTP" FT /evidence="ECO:0000250" FT BINDING 68 FT /note="GTP; via amide nitrogen" FT /evidence="ECO:0000250" FT MOD_RES 45 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D0J4" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000255" FT CROSSLNK 71 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT VAR_SEQ 113..139 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15146197" FT /id="VSP_047278" FT VARIANT 141 FT /note="V -> A (in dbSNP:rs664226)" FT /evidence="ECO:0000269|PubMed:15146197, FT ECO:0000269|PubMed:8415637, ECO:0000269|Ref.3" FT /id="VAR_028056" FT MUTAGEN 3 FT /note="L->A: Reduces interaction with ARL2BP." FT /evidence="ECO:0000269|PubMed:19368893" FT MUTAGEN 3 FT /note="L->D: Reduces interaction with ARL2BP." FT /evidence="ECO:0000269|PubMed:19368893" FT MUTAGEN 4 FT /note="L->A: Does not reduce interaction with ARL2BP." FT /evidence="ECO:0000269|PubMed:19368893" FT MUTAGEN 4 FT /note="L->D: Reduces interaction with ARL2BP." FT /evidence="ECO:0000269|PubMed:19368893" FT MUTAGEN 6 FT /note="I->R: Reduces interaction with ARL2BP." FT /evidence="ECO:0000269|PubMed:19368893" FT MUTAGEN 7 FT /note="L->A: Does not reduce interaction with ARL2BP." FT /evidence="ECO:0000269|PubMed:19368893" FT MUTAGEN 7 FT /note="L->D: Reduces interaction with ARL2BP." FT /evidence="ECO:0000269|PubMed:19368893" FT MUTAGEN 30 FT /note="T->N: Does not inhibit the interaction with TBCD and FT rescues the TBCD-induced microtubule destruction. Reduces FT interaction with ARL2BP. Inhibits accumulation of STAT3 in FT the nucleus." FT /evidence="ECO:0000269|PubMed:10831612, FT ECO:0000269|PubMed:18234692" FT MUTAGEN 47 FT /note="T->A: Does not inhibit the interaction with TBCD and FT rescues the TBCD-induced microtubule destruction." FT /evidence="ECO:0000269|PubMed:10831612" FT MUTAGEN 50 FT /note="F->A: Reduces interaction with ARL2BP. Inhibits the FT interaction with TBCD and rescues the TBCD-induced FT microtubule destruction." FT /evidence="ECO:0000269|PubMed:10831612, FT ECO:0000269|PubMed:19368893" FT MUTAGEN 70 FT /note="Q->L: Induces cell cycle arrest, reduces ability to FT form microtubules and centrosome fragmentation. Inhibits FT the interaction with TBCD and does not rescue the TBCD- FT induced microtubule destruction. Interacts with ARL2BP and FT PDE6D." FT /evidence="ECO:0000269|PubMed:10831612, FT ECO:0000269|PubMed:11303027, ECO:0000269|PubMed:16525022, FT ECO:0000269|PubMed:18234692" FT MUTAGEN 76 FT /note="Y->A: Does not reduce interaction with ARL2BP." FT /evidence="ECO:0000269|PubMed:19368893" FT MUTAGEN 80 FT /note="Y->A: Reduces interaction with ARL2BP." FT /evidence="ECO:0000269|PubMed:19368893" FT HELIX 3..9 FT /evidence="ECO:0000244|PDB:3DOE" FT STRAND 16..22 FT /evidence="ECO:0000244|PDB:3DOE" FT HELIX 29..37 FT /evidence="ECO:0000244|PDB:3DOE" FT STRAND 48..54 FT /evidence="ECO:0000244|PDB:3DOE" FT STRAND 60..67 FT /evidence="ECO:0000244|PDB:3DOE" FT HELIX 71..80 FT /evidence="ECO:0000244|PDB:3DOE" FT STRAND 85..92 FT /evidence="ECO:0000244|PDB:3DOE" FT HELIX 96..98 FT /evidence="ECO:0000244|PDB:3DOE" FT HELIX 99..110 FT /evidence="ECO:0000244|PDB:3DOE" FT HELIX 113..115 FT /evidence="ECO:0000244|PDB:3DOE" FT STRAND 119..125 FT /evidence="ECO:0000244|PDB:3DOE" FT HELIX 135..140 FT /evidence="ECO:0000244|PDB:3DOE" FT HELIX 141..146 FT /evidence="ECO:0000244|PDB:3DOE" FT STRAND 152..156 FT /evidence="ECO:0000244|PDB:3DOE" FT TURN 159..162 FT /evidence="ECO:0000244|PDB:3DOE" FT HELIX 165..184 FT /evidence="ECO:0000244|PDB:3DOE" SQ SEQUENCE 184 AA; 20878 MW; 0823F005719C17F9 CRC64; MGLLTILKKM KQKERELRLL MLGLDNAGKT TILKKFNGED IDTISPTLGF NIKTLEHRGF KLNIWDVGGQ KSLRSYWRNY FESTDGLIWV VDSADRQRMQ DCQRELQSLL VEERLAGATL LIFANKQDLP GALSSNAIRE VLELDSIRSH HWCIQGCSAV TGENLLPGID WLLDDISSRI FTAD //