ELP6_HUMAN
ID ELP6_HUMAN Reviewed; 266 AA.
AC Q0PNE2; Q9BW57; Q9NXJ3;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Elongator complex protein 6 {ECO:0000303|PubMed:22854966};
DE AltName: Full=Angiotonin-transactivated protein 1;
DE AltName: Full=Protein TMEM103;
GN Name=ELP6 {ECO:0000303|PubMed:22854966, ECO:0000312|HGNC:HGNC:25976};
GN Synonyms=ATP1, C3orf75, TMEM103;
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).
RC TISSUE=Liver;
RA Liu X., Wei H., Chen J.;
RT "Screening the cirrhosis related genes by microarray.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon mucosa;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 IDENTIFICATION IN THE ELONGATOR COMPLEX, FUNCTION, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
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 [5]
RP IDENTIFICATION BY MASS 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 [6]
RP REVIEW.
RX PubMed=29332244; DOI=10.1007/s00018-018-2747-6;
RA Dalwadi U., Yip C.K.;
RT "Structural insights into the function of Elongator.";
RL Cell. Mol. Life Sci. 75:1613-1622(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) (PubMed:29332244). The elongator complex
CC catalyzes formation of carboxymethyluridine in the wobble base at
CC position 34 in tRNAs (PubMed:22854966, PubMed:29332244). Involved in
CC cell migration (By similarity). {ECO:0000250|UniProtKB:Q8BK75,
CC ECO:0000269|PubMed:22854966, ECO:0000303|PubMed:29332244}.
CC -!- PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA
CC biosynthesis. {ECO:0000303|PubMed:29332244}.
CC -!- SUBUNIT: Component of the elongator complex which consists of ELP1,
CC ELP2, ELP3, ELP4, ELP5 and ELP6. {ECO:0000269|PubMed:22854966}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q0PNE2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q0PNE2-2; Sequence=VSP_022721, VSP_022722;
CC -!- SIMILARITY: Belongs to the ELP6 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:0000305|PubMed:29332244}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH00623.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH14204.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ787088; ABG79574.1; -; mRNA.
DR EMBL; AK000218; BAA91017.1; -; mRNA.
DR EMBL; BC000623; AAH00623.1; ALT_FRAME; mRNA.
DR EMBL; BC014204; AAH14204.1; ALT_FRAME; mRNA.
DR CCDS; CCDS43082.1; -. [Q0PNE2-1]
DR RefSeq; NP_001026873.2; NM_001031703.2. [Q0PNE2-1]
DR AlphaFoldDB; Q0PNE2; -.
DR SMR; Q0PNE2; -.
DR BioGRID; 120209; 40.
DR ComplexPortal; CPX-1949; Elongator holoenzyme complex.
DR CORUM; Q0PNE2; -.
DR IntAct; Q0PNE2; 11.
DR STRING; 9606.ENSP00000296149; -.
DR iPTMnet; Q0PNE2; -.
DR PhosphoSitePlus; Q0PNE2; -.
DR BioMuta; ELP6; -.
DR DMDM; 121940398; -.
DR EPD; Q0PNE2; -.
DR jPOST; Q0PNE2; -.
DR MassIVE; Q0PNE2; -.
DR MaxQB; Q0PNE2; -.
DR PaxDb; Q0PNE2; -.
DR PeptideAtlas; Q0PNE2; -.
DR PRIDE; Q0PNE2; -.
DR ProteomicsDB; 58781; -. [Q0PNE2-1]
DR ProteomicsDB; 58782; -. [Q0PNE2-2]
DR Antibodypedia; 48948; 95 antibodies from 14 providers.
DR DNASU; 54859; -.
DR Ensembl; ENST00000296149.9; ENSP00000296149.4; ENSG00000163832.16. [Q0PNE2-1]
DR GeneID; 54859; -.
DR KEGG; hsa:54859; -.
DR MANE-Select; ENST00000296149.9; ENSP00000296149.4; NM_001031703.3; NP_001026873.2.
DR UCSC; uc003crk.4; human. [Q0PNE2-1]
DR CTD; 54859; -.
DR DisGeNET; 54859; -.
DR GeneCards; ELP6; -.
DR HGNC; HGNC:25976; ELP6.
DR HPA; ENSG00000163832; Low tissue specificity.
DR MIM; 615020; gene.
DR neXtProt; NX_Q0PNE2; -.
DR OpenTargets; ENSG00000163832; -.
DR PharmGKB; PA164717260; -.
DR VEuPathDB; HostDB:ENSG00000163832; -.
DR eggNOG; KOG4723; Eukaryota.
DR GeneTree; ENSGT00390000011734; -.
DR HOGENOM; CLU_092581_2_0_1; -.
DR InParanoid; Q0PNE2; -.
DR OMA; MFTELNS; -.
DR OrthoDB; 1272502at2759; -.
DR PhylomeDB; Q0PNE2; -.
DR TreeFam; TF331346; -.
DR PathwayCommons; Q0PNE2; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q0PNE2; -.
DR UniPathway; UPA00988; -.
DR BioGRID-ORCS; 54859; 565 hits in 1088 CRISPR screens.
DR ChiTaRS; ELP6; human.
DR GenomeRNAi; 54859; -.
DR Pharos; Q0PNE2; Tbio.
DR PRO; PR:Q0PNE2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q0PNE2; protein.
DR Bgee; ENSG00000163832; Expressed in right adrenal gland and 172 other tissues.
DR ExpressionAtlas; Q0PNE2; baseline and differential.
DR Genevisible; Q0PNE2; HS.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0033588; C:elongator holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IC:ComplexPortal.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IC:ComplexPortal.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR018627; ELP6.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR16184; PTHR16184; 1.
DR Pfam; PF09807; ELP6; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Reference proteome; tRNA processing.
FT CHAIN 1..266
FT /note="Elongator complex protein 6"
FT /id="PRO_0000274360"
FT VAR_SEQ 225..250
FT /note="LRILWRRPSQPAVHRDQSFTYQYKIQ -> VCRGLLGNGLLARVPVILDYIG
FT ESQA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022721"
FT VAR_SEQ 251..266
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022722"
SQ SEQUENCE 266 AA; 29793 MW; 49D96C1484446FB0 CRC64;
MFVELNNLLN TTPDRAEQGK LTLLCDAKTD GSFLVHHFLS FYLKANCKVC FVALIQSFSH
YSIVGQKLGV SLTMARERGQ LVFLEGLKSA VDVVFQAQKE PHPLQFLREA NAGNLKPLFE
FVREALKPVD SGEARWTYPV LLVDDLSVLL SLGMGAVAVL DFIHYCRATV CWELKGNMVV
LVHDSGDAED EENDILLNGL SHQSHLILRA EGLATGFCRD VHGQLRILWR RPSQPAVHRD
QSFTYQYKIQ DKSVSFFAKG MSPAVL
