ID ELP5_HUMAN Reviewed; 316 AA. AC Q8TE02; A8K1M5; D3DTN9; Q659B6; Q7Z2T4; Q8TDR9; Q9BUB2; Q9Y2Q4; DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 2. DT 01-OCT-2014, entry version 84. DE RecName: Full=Elongator complex protein 5; DE AltName: Full=Dermal papilla-derived protein 6; DE AltName: Full=S-phase 2 protein; GN Name=ELP5; Synonyms=C17orf81, DERP6; ORFNames=HSPC002, MSTP071; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR RP LOCATION. RX PubMed=16850183; DOI=10.1007/s11033-006-6273-5; RA Yuan J., Tang W., Luo K., Chen X., Gu X., Wan B., Yu L.; RT "Cloning and characterization of the human gene DERP6, which activates RT transcriptional activities of p53."; RL Mol. Biol. Rep. 33:151-158(2006). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LYS-14. RC TISSUE=Hair follicle dermal papilla; RA Ikeda A., Yoshimoto M.; RT "Molecular cloning of a dermal papilla derived gene."; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Hippocampus; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in RT the human lineage."; RL Nature 440:1045-1049(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP TYR-303. RC TISSUE=Placenta; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-316 (ISOFORM 3). RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for RT 300 previously undefined genes expressed in CD34+ hematopoietic RT stem/progenitor cells."; RL Genome Res. 10:1546-1560(2000). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-316 (ISOFORM 2). RC TISSUE=Aorta; RA Zhao B., Xu Y.Y., Liu Y.Q., Wang X.Y., Liu B., Sheng H., Ye J., RA Song L., Gao Y., Zhang C.L., Zhang J., Gao R.L., Wu Q.Y., Hui R.T.; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 149-316 (ISOFORM 4). RC TISSUE=Amygdala; 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., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [10] RP IDENTIFICATION IN THE RNA POLYMERASE II ELONGATOR COMPLEX, SUBCELLULAR RP LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=22854966; DOI=10.1074/jbc.M112.402727; RA Close P., Gillard M., Ladang A., Jiang Z., Papuga J., Hawkes N., RA Nguyen L., Chapelle J.P., Bouillenne F., Svejstrup J., Fillet M., RA Chariot A.; RT "DERP6 (ELP5) and C3ORF75 (ELP6) regulate tumorigenicity and migration RT of melanoma cells as subunits of Elongator."; RL J. Biol. Chem. 287:32535-32545(2012). CC -!- FUNCTION: Acts as subunit of the RNA polymerase II elongator CC complex, which is a histone acetyltransferase component of the RNA CC polymerase II (Pol II) holoenzyme and is involved in CC transcriptional elongation. Elongator may play a role in chromatin CC remodeling and is involved in acetylation of histones H3 and CC probably H4. Involved in cell migration (By similarity). May be CC involved in TP53-mediated transcriptional regulation. CC {ECO:0000250, ECO:0000269|PubMed:16850183}. CC -!- SUBUNIT: Component of the RNA polymerase II elongator complex CC (Elongator), which consists of IKBKAP/ELP1, STIP1/ELP2, ELP3, CC ELP4, ELP5 and ELP6; in the complex, is required for optimal CC binding of ELP3 to ELP4. {ECO:0000269|PubMed:22854966}. CC -!- INTERACTION: CC P54253:ATXN1; NbExp=2; IntAct=EBI-946189, EBI-930964; CC Q96EB1:ELP4; NbExp=4; IntAct=EBI-946189, EBI-3951755; CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q8TE02-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8TE02-2; Sequence=VSP_023923; CC Note=Ref.8 (AAQ13591) sequence is in conflict in position: CC 263:H->Q. {ECO:0000305}; CC Name=3; CC IsoId=Q8TE02-3; Sequence=VSP_023920, VSP_023921; CC Name=4; CC IsoId=Q8TE02-4; Sequence=VSP_023922; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with high levels in CC heart, brain, liver, skeletal muscle and testis. CC -!- SIMILARITY: Belongs to the ELP5 family. {ECO:0000305}. CC -!- CAUTION: It is uncertain whether Met-1 or Met-17 is the initiator. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAD20964.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC Sequence=AAQ13591.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; 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; AF087868; AAM10496.1; -; mRNA. DR EMBL; AB013910; BAB87800.1; -; mRNA. DR EMBL; AK289940; BAF82629.1; -; mRNA. DR EMBL; AC003688; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471108; EAW90230.1; -; Genomic_DNA. DR EMBL; CH471108; EAW90231.1; -; Genomic_DNA. DR EMBL; BC002762; AAH02762.2; -; mRNA. DR EMBL; AF070658; AAD20964.1; ALT_INIT; mRNA. DR EMBL; AF163262; AAQ13591.1; ALT_INIT; mRNA. DR EMBL; AL713741; CAH56280.1; -; mRNA. DR CCDS; CCDS11094.1; -. [Q8TE02-1] DR CCDS; CCDS11095.1; -. [Q8TE02-2] DR RefSeq; NP_056177.3; NM_015362.4. [Q8TE02-1] DR RefSeq; NP_981958.1; NM_203413.2. [Q8TE02-2] DR RefSeq; NP_981959.1; NM_203414.2. [Q8TE02-1] DR RefSeq; NP_981960.1; NM_203415.1. [Q8TE02-1] DR UniGene; Hs.417029; -. DR ProteinModelPortal; Q8TE02; -. DR BioGrid; 117122; 5. DR IntAct; Q8TE02; 5. DR MINT; MINT-2856032; -. DR STRING; 9606.ENSP00000346412; -. DR PhosphoSite; Q8TE02; -. DR DMDM; 134034093; -. DR MaxQB; Q8TE02; -. DR PaxDb; Q8TE02; -. DR PRIDE; Q8TE02; -. DR DNASU; 23587; -. DR Ensembl; ENST00000354429; ENSP00000346412; ENSG00000170291. [Q8TE02-1] DR Ensembl; ENST00000356683; ENSP00000349111; ENSG00000170291. [Q8TE02-2] DR Ensembl; ENST00000396627; ENSP00000379868; ENSG00000170291. [Q8TE02-1] DR Ensembl; ENST00000396628; ENSP00000379869; ENSG00000170291. [Q8TE02-1] DR Ensembl; ENST00000573657; ENSP00000459633; ENSG00000170291. [Q8TE02-3] DR Ensembl; ENST00000574255; ENSP00000461489; ENSG00000170291. [Q8TE02-3] DR Ensembl; ENST00000574993; ENSP00000459835; ENSG00000170291. [Q8TE02-2] DR GeneID; 23587; -. DR KEGG; hsa:23587; -. DR UCSC; uc002gfg.1; human. [Q8TE02-1] DR UCSC; uc002gfj.3; human. [Q8TE02-2] DR UCSC; uc002gfk.1; human. [Q8TE02-3] DR CTD; 23587; -. DR GeneCards; GC17P007154; -. DR HGNC; HGNC:30617; ELP5. DR HPA; HPA023279; -. DR MIM; 615019; gene. DR neXtProt; NX_Q8TE02; -. DR PharmGKB; PA143485405; -. DR eggNOG; NOG41404; -. DR HOGENOM; HOG000013029; -. DR HOVERGEN; HBG081433; -. DR InParanoid; Q8TE02; -. DR OMA; NSRLVYH; -. DR OrthoDB; EOG70PBZX; -. DR PhylomeDB; Q8TE02; -. DR TreeFam; TF314636; -. DR Reactome; REACT_172610; HATs acetylate histones. DR GeneWiki; C17orf81; -. DR GenomeRNAi; 23587; -. DR NextBio; 46212; -. DR PRO; PR:Q8TE02; -. DR ArrayExpress; Q8TE02; -. DR Bgee; Q8TE02; -. DR CleanEx; HS_C17orf81; -. DR Genevestigator; Q8TE02; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0033588; C:Elongator holoenzyme complex; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0006325; P:chromatin organization; TAS:Reactome. DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR019519; Elp5. DR Pfam; PF10483; Elong_Iki1; 1. PE 1: Evidence at protein level; KW Alternative splicing; Complete proteome; Cytoplasm; Nucleus; KW Polymorphism; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 316 Elongator complex protein 5. FT /FTId=PRO_0000280817. FT VAR_SEQ 154 179 DSSSVGKVSVLGLLHEELHGPGPVGA -> ETPPSLFPLIH FT LPLPRSVPLFLSTLE (in isoform 3). FT {ECO:0000303|PubMed:11042152}. FT /FTId=VSP_023920. FT VAR_SEQ 180 316 Missing (in isoform 3). FT {ECO:0000303|PubMed:11042152}. FT /FTId=VSP_023921. FT VAR_SEQ 246 246 V -> VHPLYLQV (in isoform 4). FT {ECO:0000303|PubMed:17974005}. FT /FTId=VSP_023922. FT VAR_SEQ 247 316 DPTTHLTFNLHLSKKEREARDSLILPFQFSSEKQQALLRPR FT PGQATSHIFYEPDAYDDLDQEDPDDDLDI -> SKNAKART FT RKCSLVSGHGRENKSCRGWGWGQGF (in isoform 2). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|Ref.8}. FT /FTId=VSP_023923. FT VARIANT 14 14 E -> K (in dbSNP:rs2521988). FT {ECO:0000269|Ref.2}. FT /FTId=VAR_053882. FT VARIANT 303 303 D -> Y (in dbSNP:rs17849664). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_031205. FT CONFLICT 151 151 C -> R (in Ref. 1; AAM10496). FT {ECO:0000305}. FT CONFLICT 175 175 G -> S (in Ref. 1; AAM10496). FT {ECO:0000305}. FT CONFLICT 181 181 S -> N (in Ref. 1; AAM10496). FT {ECO:0000305}. FT CONFLICT 228 228 Q -> K (in Ref. 1; AAM10496). FT {ECO:0000305}. FT CONFLICT 245 245 P -> R (in Ref. 1; AAM10496). FT {ECO:0000305}. SQ SEQUENCE 316 AA; 34841 MW; C96F86C6B99CE7CE CRC64; MTPSEGARAG TGRELEMLDS LLALGGLVLL RDSVEWEGRS LLKALVKKSA LCGEQVHILG CEVSEEEFRE GFDSDINNRL VYHDFFRDPL NWSKTEEAFP GGPLGALRAM CKRTDPVPVT IALDSLSWLL LRLPCTTLCQ VLHAVSHQDS CPGDSSSVGK VSVLGLLHEE LHGPGPVGAL SSLAQTEVTL GGTMGQASAH ILCRRPRQRP TDQTQWFSIL PDFSLDLQEG PSVESQPYSD PHIPPVDPTT HLTFNLHLSK KEREARDSLI LPFQFSSEKQ QALLRPRPGQ ATSHIFYEPD AYDDLDQEDP DDDLDI //