RABL6_HUMAN
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 03-AUG-2022, entry version 154.
DE RecName: Full=Rab-like protein 6;
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; 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;
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, AND SUBCELLULAR LOCATION.
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), AND SUBCELLULAR LOCATION.
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: May enhance cellular proliferation. May reduce growth
CC inhibitory activity of CDKN2A. {ECO:0000269|PubMed:16582619}.
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};
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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_001173988.1. [Q3YEC7-2]
DR RefSeq; NP_001167460.1; NM_001173989.2. [Q3YEC7-6]
DR RefSeq; NP_078994.3; NM_024718.4. [Q3YEC7-1]
DR AlphaFoldDB; Q3YEC7; -.
DR SMR; Q3YEC7; -.
DR BioGRID; 120812; 94.
DR IntAct; Q3YEC7; 46.
DR MINT; Q3YEC7; -.
DR STRING; 9606.ENSP00000360727; -.
DR GlyGen; Q3YEC7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q3YEC7; -.
DR PhosphoSitePlus; Q3YEC7; -.
DR BioMuta; RABL6; -.
DR DMDM; 125957950; -.
DR EPD; Q3YEC7; -.
DR jPOST; Q3YEC7; -.
DR MassIVE; Q3YEC7; -.
DR MaxQB; Q3YEC7; -.
DR PaxDb; Q3YEC7; -.
DR PeptideAtlas; Q3YEC7; -.
DR PRIDE; Q3YEC7; -.
DR Antibodypedia; 32247; 112 antibodies from 22 providers.
DR DNASU; 55684; -.
DR Ensembl; ENST00000311502.12; ENSP00000311134.7; ENSG00000196642.19. [Q3YEC7-1]
DR Ensembl; ENST00000357466.6; ENSP00000350056.2; ENSG00000196642.19. [Q3YEC7-3]
DR Ensembl; ENST00000371663.10; ENSP00000360727.6; ENSG00000196642.19. [Q3YEC7-2]
DR Ensembl; ENST00000371671.9; ENSP00000360736.4; ENSG00000196642.19. [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 CTD; 55684; -.
DR DisGeNET; 55684; -.
DR GeneCards; RABL6; -.
DR HGNC; HGNC:24703; RABL6.
DR HPA; ENSG00000196642; Low tissue specificity.
DR MIM; 610615; gene.
DR neXtProt; NX_Q3YEC7; -.
DR OpenTargets; ENSG00000196642; -.
DR PharmGKB; PA134868176; -.
DR VEuPathDB; HostDB:ENSG00000196642; -.
DR eggNOG; KOG0084; Eukaryota.
DR GeneTree; ENSGT00390000016002; -.
DR HOGENOM; CLU_012780_0_0_1; -.
DR InParanoid; Q3YEC7; -.
DR OMA; SKWRQSP; -.
DR PhylomeDB; Q3YEC7; -.
DR TreeFam; TF313974; -.
DR PathwayCommons; Q3YEC7; -.
DR SignaLink; Q3YEC7; -.
DR BioGRID-ORCS; 55684; 14 hits in 1086 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 166 other tissues.
DR ExpressionAtlas; Q3YEC7; baseline and differential.
DR Genevisible; Q3YEC7; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
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:0005525; F:GTP binding; IDA:MGI.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR040385; RABL6.
DR InterPro; IPR001806; Small_GTPase.
DR PANTHER; PTHR14932; PTHR14932; 1.
DR Pfam; PF00071; Ras; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Glycoprotein; GTP-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; 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 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 285..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..351
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 50..57
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 100..104
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT BINDING 177..179
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
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
