ID RABL6_HUMAN Reviewed; 729 AA. AC Q3YEC7; A8QVZ7; A8QVZ8; C6K8I4; C6K8I5; Q4F968; Q5T5R7; Q8IWK1; Q8TCL4; AC Q8WU94; Q96SR8; Q9BU21; Q9H935; DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 2. DT 02-SEP-2026, entry version 173. DE RecName: Full=Rab-like protein 6; DE EC=3.6.5.2 {ECO:0000305|PubMed:17962191, ECO:0000305|PubMed:19433581}; DE AltName: Full=GTP-binding protein Parf; DE AltName: Full=Partner of ARF; DE AltName: Full=Rab-like protein 1; DE Short=RBEL1; GN Name=RABL6 {ECO:0000312|HGNC:HGNC:24703}; Synonyms=C9orf86, PARF; 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), VARIANT GLN-382, FUNCTION, RP SUBCELLULAR LOCATION, AND INTERACTION WITH CDKN2A. RX PubMed=16582619; DOI=10.4161/cc.5.6.2560; RA Tompkins V., Hagen J., Zediak V.P., Quelle D.E.; RT "Identification of novel ARF binding proteins by two-hybrid screening."; RL Cell Cycle 5:641-646(2006). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), ALTERNATIVE SPLICING, RP GLYCOSYLATION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY. RX PubMed=17962191; DOI=10.1074/jbc.m704760200; RA Montalbano J., Jin W., Sheikh M.S., Huang Y.; RT "RBEL1 is a novel gene that encodes a nucleocytoplasmic Ras superfamily RT GTP-binding protein and is overexpressed in breast cancer."; RL J. Biol. Chem. 282:37640-37649(2007). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4 AND 6), SUBCELLULAR LOCATION, RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=19433581; DOI=10.1074/jbc.m109.009597; RA Montalbano J., Lui K., Sheikh M.S., Huang Y.; RT "Identification and characterization of RBEL1 subfamily of GTPases in the RT Ras superfamily involved in cell growth regulation."; RL J. Biol. Chem. 284:18129-18142(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-382. RA Lin L., Nong W., Li H., Ke R., Shen C., Zhong G., Zheng Z., Liang M., RA Wen S., Zhou G., Yang S.; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANT RP GLN-382. RC TISSUE=Brain, and Kidney; 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 45-729 (ISOFORM 5), NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 103-729 (ISOFORM 1), AND VARIANT GLN-382. RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 251-719. RC TISSUE=Brain; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-577; SER-596 AND THR-599, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425; SER-427; SER-596 AND RP THR-599, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425; SER-427; SER-596 AND RP THR-599, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-402; SER-492; SER-525; RP SER-596; THR-599; SER-640 AND SER-641, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-596 AND THR-599, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Small GTPase involved in the regulation of cell growth and CC survival (PubMed:19433581). Promotes cellular proliferation CC (PubMed:16582619, PubMed:19433581). May reduce growth inhibitory CC activity of CDKN2A (PubMed:16582619). {ECO:0000269|PubMed:16582619, CC ECO:0000269|PubMed:19433581}. 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:0000305|PubMed:17962191, ECO:0000305|PubMed:19433581}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000305|PubMed:17962191, ECO:0000305|PubMed:19433581}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P62820}; CC -!- INTERACTION: CC Q3YEC7; Q99750: MDFI; NbExp=2; IntAct=EBI-742029, EBI-724076; CC Q3YEC7; P58062: SPINK7; NbExp=3; IntAct=EBI-742029, EBI-1182445; CC Q3YEC7-3; Q92993: KAT5; NbExp=3; IntAct=EBI-25885259, EBI-399080; CC Q3YEC7-3; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-25885259, EBI-11742507; CC Q3YEC7-3; P17252: PRKCA; NbExp=3; IntAct=EBI-25885259, EBI-1383528; CC Q3YEC7-3; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-25885259, EBI-9090795; CC Q3YEC7-3; P61981: YWHAG; NbExp=3; IntAct=EBI-25885259, EBI-359832; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm CC {ECO:0000269|PubMed:17962191}. Note=Predominantly cytoplasmic CC (PubMed:17962191). CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus CC {ECO:0000269|PubMed:17962191}. Note=Predominantly nuclear CC (PubMed:17962191). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; Synonyms=RBEL1A; CC IsoId=Q3YEC7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q3YEC7-2; Sequence=VSP_022646; CC Name=3; Synonyms=RBEL1B; CC IsoId=Q3YEC7-3; Sequence=VSP_022649; CC Name=4; Synonyms=RBEL1D; CC IsoId=Q3YEC7-4; Sequence=VSP_022647, VSP_022648; CC Name=5; CC IsoId=Q3YEC7-5; Sequence=VSP_022646, VSP_022647, VSP_022648; CC Name=6; Synonyms=RBEL1C; CC IsoId=Q3YEC7-6; Sequence=VSP_042559, VSP_042560; CC -!- PTM: Isoform 1 is O-glycosylated, while other isoforms are not. CC {ECO:0000269|PubMed:17962191}. CC -!- MISCELLANEOUS: [Isoform 1]: Predominant isoform. Overexpressed in about CC 67% of primary breast tumors. CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH02945.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH21095.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAH35786.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB14408.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB55213.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; DQ141240; AAZ73768.1; -; mRNA. DR EMBL; EF156752; ABO84837.1; -; mRNA. DR EMBL; EF156753; ABO84838.1; -; mRNA. DR EMBL; GQ169126; ACS45171.1; -; mRNA. DR EMBL; GQ169127; ACS45172.1; -; mRNA. DR EMBL; AL355987; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; DQ099383; AAZ13759.1; -; mRNA. DR EMBL; BC002945; AAH02945.2; ALT_INIT; mRNA. DR EMBL; BC021095; AAH21095.2; ALT_INIT; mRNA. DR EMBL; BC035786; AAH35786.1; ALT_INIT; mRNA. DR EMBL; AK023107; BAB14408.1; ALT_INIT; mRNA. DR EMBL; AK027586; BAB55213.1; ALT_INIT; mRNA. DR EMBL; AL713707; CAD28504.1; -; mRNA. DR CCDS; CCDS48058.1; -. [Q3YEC7-1] DR CCDS; CCDS55352.1; -. [Q3YEC7-2] DR CCDS; CCDS55353.1; -. [Q3YEC7-6] DR RefSeq; NP_001167459.1; NM_001173988.2. [Q3YEC7-2] DR RefSeq; NP_001167460.1; NM_001173989.4. [Q3YEC7-6] DR RefSeq; NP_078994.3; NM_024718.5. [Q3YEC7-1] DR AlphaFoldDB; Q3YEC7; -. DR SMR; Q3YEC7; -. DR BioGRID; 120812; 155. DR FunCoup; Q3YEC7; 2957. DR IntAct; Q3YEC7; 71. DR MINT; Q3YEC7; -. DR STRING; 9606.ENSP00000360727; -. DR BindingDB; Q3YEC7; -. DR ChEMBL; CHEMBL6067258; -. DR GlyGen; Q3YEC7; 5 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (4 sites). DR iPTMnet; Q3YEC7; -. DR PhosphoSitePlus; Q3YEC7; -. DR BioMuta; RABL6; -. DR DMDM; 125957950; -. DR jPOST; Q3YEC7; -. DR MassIVE; Q3YEC7; -. DR PaxDb; 9606-ENSP00000360727; -. DR PeptideAtlas; Q3YEC7; -. DR Pumba; Q3YEC7; -. DR Antibodypedia; 32247; 108 antibodies from 22 providers. DR DNASU; 55684; -. DR Ensembl; ENST00000311502.12; ENSP00000311134.7; ENSG00000196642.20. [Q3YEC7-1] DR Ensembl; ENST00000357466.6; ENSP00000350056.2; ENSG00000196642.20. [Q3YEC7-3] DR Ensembl; ENST00000371663.10; ENSP00000360727.6; ENSG00000196642.20. [Q3YEC7-2] DR Ensembl; ENST00000371671.9; ENSP00000360736.4; ENSG00000196642.20. [Q3YEC7-6] DR GeneID; 55684; -. DR KEGG; hsa:55684; -. DR MANE-Select; ENST00000311502.12; ENSP00000311134.7; NM_024718.5; NP_078994.3. DR UCSC; uc004cjh.4; human. [Q3YEC7-1] DR AGR; HGNC:24703; -. DR ClinPGx; PA134868176; -. DR CTD; 55684; -. DR DisGeNET; 55684; -. DR GeneCards; RABL6; -. DR HGNC; HGNC:24703; RABL6. DR HPA; ENSG00000196642; Low tissue specificity. DR MIM; 610615; gene. DR OpenTargets; ENSG00000196642; -. DR VEuPathDB; HostDB:ENSG00000196642; -. DR eggNOG; KOG0084; Eukaryota. DR GeneTree; ENSGT00390000016002; -. DR HOGENOM; CLU_012780_0_0_1; -. DR InParanoid; Q3YEC7; -. DR OMA; DHVTYFI; -. DR OrthoDB; 207081at2759; -. DR PAN-GO; Q3YEC7; 3 GO annotations based on evolutionary models. DR PhylomeDB; Q3YEC7; -. DR PathwayCommons; Q3YEC7; -. DR SignaLink; Q3YEC7; -. DR Agora; ENSG00000196642; -. DR BioGRID-ORCS; 55684; 30 hits in 1164 CRISPR screens. DR ChiTaRS; RABL6; human. DR GeneWiki; C9orf86; -. DR GenomeRNAi; 55684; -. DR Pharos; Q3YEC7; Tbio. DR PRO; PR:Q3YEC7; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q3YEC7; protein. DR Bgee; ENSG00000196642; Expressed in right hemisphere of cerebellum and 168 other cell types or tissues. DR ExpressionAtlas; Q3YEC7; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0003925; F:G protein activity; IC:UniProtKB. DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB. DR FunFam; 3.40.50.300:FF:000781; RAB, member RAS oncogene family like 6; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR040385; RABL6. DR PANTHER; PTHR14932:SF1; RAB-LIKE PROTEIN 6; 1. DR PANTHER; PTHR14932; RAS GTPASE-RELATED; 1. DR Pfam; PF08477; Roc; 1. DR PRINTS; PR00449; RASTRNSFRMNG. DR SMART; SM00175; RAB; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51419; RAB; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cytoplasm; Glycoprotein; GTP-binding; KW Hydrolase; Magnesium; Metal-binding; Nucleotide-binding; Nucleus; KW Phosphoprotein; Proteomics identification; Reference proteome. FT CHAIN 1..729 FT /note="Rab-like protein 6" FT /id="PRO_0000274223" FT REGION 39..279 FT /note="Small GTPase-like" FT REGION 70..83 FT /note="Switch-I" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00753" FT REGION 123..141 FT /note="Switch-II" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00753" FT REGION 281..729 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 655..693 FT /note="Interaction with CDKN2A" FT /evidence="ECO:0000269|PubMed:16582619" FT COMPBIAS 290..315 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 331..351 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 395..416 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 489..502 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 581..595 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 596..605 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 606..615 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 635..652 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 669..678 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 679..689 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 711..729 FT /note="Gly residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 55 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 56 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 57 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 57 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 70 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 75 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 75 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 100 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 176 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 179 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT BINDING 215 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250|UniProtKB:P62820" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 402 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:23186163" FT MOD_RES 425 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692" FT MOD_RES 427 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 470 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5U3K5" FT MOD_RES 471 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q5U3K5" FT MOD_RES 492 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 525 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 577 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 596 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 599 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 640 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 641 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 199 FT /note="D -> DS (in isoform 2 and isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_022646" FT VAR_SEQ 236..302 FT /note="RETLLRQLETNQLDMDATLEELSVQQETEDQNYGIFLEMMEARSRGHASPLA FT ANGQSPSPGSQSPVV -> KDVRLAQERGCAVVLVSEEVRMPAGWDCCWGRLGWKEGGS FT QTCPVPALLGRPLLPAEPSPHHWVDYSLESSPLLSCSIP (in isoform 6)" FT /evidence="ECO:0000303|PubMed:19433581" FT /id="VSP_042559" FT VAR_SEQ 236..264 FT /note="RETLLRQLETNQLDMDATLEELSVQQETE -> VSTHHVGWSGCWSLTSFQV FT SPV (in isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:19433581" FT /id="VSP_022647" FT VAR_SEQ 265..729 FT /note="Missing (in isoform 4 and isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:19433581" FT /id="VSP_022648" FT VAR_SEQ 303..729 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:19433581" FT /id="VSP_042560" FT VAR_SEQ 361..729 FT /note="LFGTSPATEAAPPPPEPVPAAEGPATVQSVEDFVPDDRLDRSFLEDTTPARD FT EKKVGAKAAQQDSDSDGEALGGNPMVAGFQDDVDLEDQPRGSPPLPAGPVPSQDITLSS FT EEEAEVAAPTKGPAPAPQQCSEPETKWSSIPASKPRRGTAPTRTAAPPWPGGVSVRTGP FT EKRSSTRPPAEMEPGKGEQASSSESDPEGPIAAQMLSFVMDDPDFESEGSDTQRRADDF FT PVRDDPSDVTDEDEGPAEPPPPPKLPLPAFRLKNDSDLFGLGLEEAGPKESSEEGKEGK FT TPSKEKKKKKKKGKEEEEKAAKKKSKHKKSKDKEEGKEERRRRQQRPPRSRERTAADEL FT EAFLGGGAPGGRHPGGGDYEEL -> PPPWGWRLRGALGRRGQWPPWGGGRACHCLGRH FT LPLYHRLCRCPVAAVCASELEEAGHWWSPGWALQVLGLQAQCEPALQEGRGQLASARLG FT GHPGPLGAEPPVFLRDVTEAQEGPVRVCLQRLGRGRLAVGCALPRHLLALRAHLGPQHA FT YGSASGREP (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:17962191" FT /id="VSP_022649" FT VARIANT 382 FT /note="E -> Q (in dbSNP:rs2811741)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16582619, FT ECO:0000269|Ref.5" FT /id="VAR_030210" FT CONFLICT 137 FT /note="Y -> C (in Ref. 7; BAB14408)" FT /evidence="ECO:0000305" SQ SEQUENCE 729 AA; 79549 MW; 6C3FDB38C7FD7D59 CRC64; MFSALKKLVG SDQAPGRDKN IPAGLQSMNQ ALQRRFAKGV QYNMKIVIRG DRNTGKTALW HRLQGRPFVE EYIPTQEIQV TSIHWSYKTT DDIVKVEVWD VVDKGKCKKR GDGLKMENDP QEAESEMALD AEFLDVYKNC NGVVMMFDIT KQWTFNYILR ELPKVPTHVP VCVLGNYRDM GEHRVILPDD VRDFIDNLDR PPGSSYFRYA ESSMKNSFGL KYLHKFFNIP FLQLQRETLL RQLETNQLDM DATLEELSVQ QETEDQNYGI FLEMMEARSR GHASPLAANG QSPSPGSQSP VVPAGAVSTG SSSPGTPQPA PQLPLNAAPP SSVPPVPPSE ALPPPACPSA PAPRRSIISR LFGTSPATEA APPPPEPVPA AEGPATVQSV EDFVPDDRLD RSFLEDTTPA RDEKKVGAKA AQQDSDSDGE ALGGNPMVAG FQDDVDLEDQ PRGSPPLPAG PVPSQDITLS SEEEAEVAAP TKGPAPAPQQ CSEPETKWSS IPASKPRRGT APTRTAAPPW PGGVSVRTGP EKRSSTRPPA EMEPGKGEQA SSSESDPEGP IAAQMLSFVM DDPDFESEGS DTQRRADDFP VRDDPSDVTD EDEGPAEPPP PPKLPLPAFR LKNDSDLFGL GLEEAGPKES SEEGKEGKTP SKEKKKKKKK GKEEEEKAAK KKSKHKKSKD KEEGKEERRR RQQRPPRSRE RTAADELEAF LGGGAPGGRH PGGGDYEEL //