ELP5_MOUSE
ID ELP5_MOUSE Reviewed; 300 AA.
AC Q99L85; O08973; Q9CUX2;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Elongator complex protein 5;
DE AltName: Full=Dermal papilla-derived protein 6 homolog;
DE AltName: Full=Retinoic acid-induced protein 12;
GN Name=Elp5; Synonyms=Derp6, Rai12;
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 [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Melanoma;
RX PubMed=9371513;
RA Spanjaard R.A., Lee P.J., Sarkar S., Goedegebuure P.S., Eberlein T.J.;
RT "Clone 10d/BM28 (CDCL1), an early S-phase protein, is an important growth
RT regulator of melanoma.";
RL Cancer Res. 57:5122-5128(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Hippocampus;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [5]
RP FUNCTION.
RX PubMed=22854966; DOI=10.1074/jbc.m112.402727;
RA Close P., Gillard M., Ladang A., Jiang Z., Papuga J., Hawkes N., Nguyen L.,
RA Chapelle J.P., Bouillenne F., Svejstrup J., Fillet M., Chariot A.;
RT "DERP6 (ELP5) and C3ORF75 (ELP6) regulate tumorigenicity and migration of
RT melanoma cells as subunits of Elongator.";
RL J. Biol. Chem. 287:32535-32545(2012).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=30097576; DOI=10.1038/s41467-018-05765-6;
RA Kojic M., Gaik M., Kiska B., Salerno-Kochan A., Hunt S., Tedoldi A.,
RA Mureev S., Jones A., Whittle B., Genovesi L.A., Adolphe C., Brown D.L.,
RA Stow J.L., Alexandrov K., Sah P., Glatt S., Wainwright B.J.;
RT "Elongator mutation in mice induces neurodegeneration and ataxia-like
RT behavior.";
RL Nat. Commun. 9:3195-3195(2018).
CC -!- FUNCTION: Component of the elongator complex which is required for
CC multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl
CC uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U
CC (5-carbamoylmethyl uridine) (By similarity). The elongator complex
CC catalyzes the formation of carboxymethyluridine in the wobble base at
CC position 34 in tRNAs (By similarity). Involved in cell migration
CC (PubMed:22854966). {ECO:0000250|UniProtKB:Q8TE02,
CC ECO:0000269|PubMed:22854966}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000250|UniProtKB:Q8TE02}.
CC -!- SUBUNIT: Component of the elongator complex which consists of ELP1,
CC ELP2, ELP3, ELP4, ELP5 and ELP6; in the complex, is required for
CC optimal binding of ELP3 to ELP4. {ECO:0000250|UniProtKB:Q8TE02}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8TE02}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8TE02}.
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in testis
CC (PubMed:9371513). Expressed throughout the cerebellum
CC (PubMed:30097576). {ECO:0000269|PubMed:30097576,
CC ECO:0000269|PubMed:9371513}.
CC -!- PTM: Tyrosine-phosphorylated. {ECO:0000250|UniProtKB:Q8TE02}.
CC -!- SIMILARITY: Belongs to the ELP5 family. {ECO:0000305}.
CC -!- CAUTION: The elongator complex was originally thought to play a role in
CC transcription elongation. However, it is no longer thought to play a
CC direct role in this process and its primary function is thought to be
CC in tRNA modification. {ECO:0000250|UniProtKB:Q8TE02}.
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DR EMBL; AF004107; AAC16252.1; -; mRNA.
DR EMBL; AK152582; BAE31332.1; -; mRNA.
DR EMBL; AK013662; BAB28944.1; -; mRNA.
DR EMBL; AL596185; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003752; AAH03752.1; -; mRNA.
DR CCDS; CCDS24926.1; -.
DR RefSeq; NP_061210.2; NM_018740.2.
DR RefSeq; XP_006533815.1; XM_006533752.3.
DR AlphaFoldDB; Q99L85; -.
DR BioGRID; 207617; 3.
DR STRING; 10090.ENSMUSP00000104235; -.
DR iPTMnet; Q99L85; -.
DR PhosphoSitePlus; Q99L85; -.
DR EPD; Q99L85; -.
DR MaxQB; Q99L85; -.
DR PaxDb; Q99L85; -.
DR PeptideAtlas; Q99L85; -.
DR PRIDE; Q99L85; -.
DR ProteomicsDB; 275748; -.
DR Antibodypedia; 11862; 84 antibodies from 20 providers.
DR DNASU; 54351; -.
DR Ensembl; ENSMUST00000108594; ENSMUSP00000104235; ENSMUSG00000018565.
DR GeneID; 54351; -.
DR KEGG; mmu:54351; -.
DR UCSC; uc007jtc.3; mouse.
DR CTD; 23587; -.
DR MGI; MGI:1859017; Elp5.
DR VEuPathDB; HostDB:ENSMUSG00000018565; -.
DR eggNOG; ENOG502QQ2R; Eukaryota.
DR GeneTree; ENSGT00390000009210; -.
DR HOGENOM; CLU_076374_0_0_1; -.
DR InParanoid; Q99L85; -.
DR OMA; SICHLAT; -.
DR OrthoDB; 805928at2759; -.
DR PhylomeDB; Q99L85; -.
DR TreeFam; TF314636; -.
DR UniPathway; UPA00988; -.
DR BioGRID-ORCS; 54351; 23 hits in 71 CRISPR screens.
DR ChiTaRS; Elp5; mouse.
DR PRO; PR:Q99L85; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q99L85; protein.
DR Bgee; ENSMUSG00000018565; Expressed in spermatocyte and 253 other tissues.
DR ExpressionAtlas; Q99L85; baseline and differential.
DR Genevisible; Q99L85; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0033588; C:elongator holoenzyme complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0006400; P:tRNA modification; IBA:GO_Central.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR019519; Elp5.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR15641; PTHR15641; 1.
DR Pfam; PF10483; Elong_Iki1; 2.
PE 2: Evidence at transcript level;
KW Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; tRNA processing.
FT CHAIN 1..300
FT /note="Elongator complex protein 5"
FT /id="PRO_0000280818"
FT REGION 279..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..300
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TE02"
FT CONFLICT 146
FT /note="R -> H (in Ref. 1; AAC16252)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="H -> R (in Ref. 1; AAC16252)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="P -> Q (in Ref. 1; AAC16252)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 300 AA; 33498 MW; 09D1277BFD67A767 CRC64;
MLDSLLAIGG LVLLRDSVEW EGRSLLKALI KKSALRGEQV HVLGCEVSEE EFREGFDSDV
NSRLVYHDLF RDPLNWSKPG EAVPEGPLKA LRSMCKRTDH GSVTIALDSL SWLLCHIPCV
TLCQALHALS QQNGDPGDNS LVEQVRVLGL LHEELHGPGS MGALNTLAHT EVTLSGKVDQ
TSASILCRRP QQRATYQTWW FSVLPDFSLT LHEGLPLRSE LHPDHHTTQV DPTAHLTFNL
HLSKKEREAR DSLTLPFQFS SEKQKALLHP VPSRTTGHIF YEPDAFDDVD PEDPDDDLDI
