RABL6_MOUSE
ID RABL6_MOUSE Reviewed; 725 AA.
AC Q5U3K5; A2AJB0; Q3TAT5; Q3TRU4; Q6PDP8; Q8BFS4; Q8CGJ9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Rab-like protein 6;
DE AltName: Full=GTP-binding protein Parf;
DE AltName: Full=Rab-like protein 1;
DE Short=RBEL1;
GN Name=Rabl6; Synonyms=Parf;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-658.
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Corpora quadrigemina, Embryo, Head, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary gland;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-594 AND THR-597, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 AND SER-483, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436; SER-438; SER-480;
RP SER-482; SER-483; SER-594; THR-597; SER-637; SER-638 AND SER-644, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May enhance cellular proliferation. May reduce growth
CC inhibitory activity of CDKN2A (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q3YEC7}. Note=Predominantly cytoplasmic.
CC {ECO:0000250|UniProtKB:Q3YEC7}.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
CC {ECO:0000305}.
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DR EMBL; AK045520; BAC32404.1; -; mRNA.
DR EMBL; AK081440; BAC38220.1; -; mRNA.
DR EMBL; AK171643; BAE42583.1; -; mRNA.
DR EMBL; AK162461; BAE36932.1; -; mRNA.
DR EMBL; AL732590; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC023692; AAH23692.1; -; mRNA.
DR EMBL; BC058585; AAH58585.1; -; mRNA.
DR EMBL; BC085507; AAH85507.2; -; mRNA.
DR CCDS; CCDS38076.1; -.
DR RefSeq; NP_001019787.2; NM_001024616.1.
DR AlphaFoldDB; Q5U3K5; -.
DR SMR; Q5U3K5; -.
DR BioGRID; 230648; 6.
DR IntAct; Q5U3K5; 2.
DR MINT; Q5U3K5; -.
DR STRING; 10090.ENSMUSP00000058746; -.
DR iPTMnet; Q5U3K5; -.
DR PhosphoSitePlus; Q5U3K5; -.
DR SwissPalm; Q5U3K5; -.
DR EPD; Q5U3K5; -.
DR jPOST; Q5U3K5; -.
DR MaxQB; Q5U3K5; -.
DR PaxDb; Q5U3K5; -.
DR PeptideAtlas; Q5U3K5; -.
DR PRIDE; Q5U3K5; -.
DR ProteomicsDB; 253163; -.
DR Antibodypedia; 32247; 112 antibodies from 22 providers.
DR Ensembl; ENSMUST00000058137; ENSMUSP00000058746; ENSMUSG00000015087.
DR GeneID; 227624; -.
DR KEGG; mmu:227624; -.
DR UCSC; uc008isr.1; mouse.
DR CTD; 55684; -.
DR MGI; MGI:2442633; Rabl6.
DR VEuPathDB; HostDB:ENSMUSG00000015087; -.
DR eggNOG; KOG0084; Eukaryota.
DR GeneTree; ENSGT00390000016002; -.
DR HOGENOM; CLU_012780_1_0_1; -.
DR InParanoid; Q5U3K5; -.
DR OMA; SKWRQSP; -.
DR OrthoDB; 930319at2759; -.
DR PhylomeDB; Q5U3K5; -.
DR TreeFam; TF313974; -.
DR BioGRID-ORCS; 227624; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Rabl6; mouse.
DR PRO; PR:Q5U3K5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q5U3K5; protein.
DR Bgee; ENSMUSG00000015087; Expressed in dorsal pancreas and 255 other tissues.
DR Genevisible; Q5U3K5; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR040385; RABL6.
DR PANTHER; PTHR14932; PTHR14932; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; GTP-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..725
FT /note="Rab-like protein 6"
FT /id="PRO_0000274224"
FT REGION 39..279
FT /note="Small GTPase-like"
FT REGION 281..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..690
FT /note="Interaction with CDKN2A"
FT /evidence="ECO:0000250"
FT COMPBIAS 285..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..648
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:0000250|UniProtKB:Q3YEC7"
FT MOD_RES 414
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3YEC7"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3YEC7"
FT MOD_RES 575
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3YEC7"
FT MOD_RES 594
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 597
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 637
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 520
FT /note="R -> G (in Ref. 1; BAE42583)"
FT /evidence="ECO:0000305"
FT CONFLICT 670
FT /note="S -> K (in Ref. 3; AAH58585)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 725 AA; 79831 MW; B538A8420DC04964 CRC64;
MFSALKKLVG SEQAPGRDKN IPAGLQSMNQ ALQRRFAKGV QYNMKIVIRG DRNTGKTALW
HRLQGKKFVE EYIPTQEIQV TSIHWNYKTT DDVVKVEVWD VVDKGKCKKR GDGLKTENDP
QEAESELALD AEFLDVYKNC NGVVMMFDIT KQWTFNYVLR ELPKVPTHVP VCVLGNYRDM
GEHRVILPDD VRDFIEHLDR PPGSSYFRYA ESSMKNSFGL KYLHKFFNIP FLQLQRETLL
RQLETNQLDI DATLEELSVQ QETEDQNYSI FLEMMEARSR GHASPLAANG QSPSSGSQSP
VVPPSAVSTG SSSPSTPQPA PQLSLGVSST CPSAPSPVPS LEAMPSSVHS SAPAPTPAPA
PAPAQRRSII SRLFGTSPAA EVTPSPPEPA PALEAPARVQ NVEDFVPEDG LDRSFLEDTS
VPKDKKVGAK GPQQDSDSDD GEALGGNPMV AGFQDDVDIE DQTHGKSLLP SDPMPSKNIS
LSSEEEAEGL AGHPRVAPQQ CSEPETKWSS TKVSHPQKKR APTRGTPPWS DGLTTDDSER
PQEGKDKQVS SESDPEGPIA AQMLSFVMDD PDFESDESDT QRRMGRFPVR EDLSDVTDED
TGPAQPPPPS KLPGAFRLKN DSDLFGLGLE EMGPKESSDE DRDSKLPSKE KKKKKKKSKE
EEEKTTKKKS KHKKSKDKEE GKEDRKKKRK PPRSKEQKAA DELEAFLGGG APGSRHPGGG
DYEEL
