ELP2_HUMAN
ID ELP2_HUMAN Reviewed; 826 AA.
AC Q6IA86; A8KAI6; B4DTG0; B4DXP0; E7EP23; E9PCX0; Q53GZ0; Q687Y8; Q8N5C2;
AC Q96GV4; Q96PI7; Q9H9N0; Q9NV81;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Elongator complex protein 2;
DE Short=ELP2;
DE AltName: Full=SHINC-2;
DE AltName: Full=STAT3-interacting protein 1;
DE Short=StIP1;
GN Name=ELP2; Synonyms=STATIP1;
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 2).
RC TISSUE=Hematopoietic;
RA Zhao C.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA Sakabe I., Suy S., Kumar D., Ahmad I., Kasid U.;
RT "Shinc-2 gene expression is modulated in human prostate cancer cells
RT treated with biological anticancer agents.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 5; 6 AND 7), AND
RP VARIANTS PRO-128 AND MET-305.
RC TISSUE=Placenta, Testis, and Uterus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS PRO-128
RP AND MET-305.
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Ovary, and Uterus;
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 [8]
RP IDENTIFICATION IN THE ELONGATOR COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11714725; DOI=10.1074/jbc.m110445200;
RA Hawkes N.A., Otero G., Winkler G.S., Marshall N., Dahmus M.E.,
RA Krappmann D., Scheidereit C., Thomas C.L., Schiavo G.,
RA Erdjument-Bromage H., Tempst P., Svejstrup J.Q.;
RT "Purification and characterization of the human elongator complex.";
RL J. Biol. Chem. 277:3047-3052(2002).
RN [9]
RP IDENTIFICATION IN THE ELONGATOR CORE COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11818576; DOI=10.1073/pnas.251672198;
RA Kim J.H., Lane W.S., Reinberg D.;
RT "Human Elongator facilitates RNA polymerase II transcription through
RT chromatin.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:1241-1246(2002).
RN [10]
RP IDENTIFICATION IN THE ELONGATOR COMPLEX.
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 [11]
RP INTERACTION WITH ELP1 AND ELP3, AND MUTAGENESIS OF 1-MET--ARG-17; ARG-634;
RP ARG-636; ARG-670 AND ARG-689.
RX PubMed=25960406; DOI=10.1016/j.str.2015.03.018;
RA Dong C., Lin Z., Diao W., Li D., Chu X., Wang Z., Zhou H., Xie Z., Shen Y.,
RA Long J.;
RT "The Elp2 subunit is essential for elongator complex assembly and
RT functional regulation.";
RL Structure 23:1078-1086(2015).
RN [12]
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).
RN [13]
RP VARIANTS MRT58 ARG-206 AND TRP-462, AND INVOLVEMENT IN MRT58.
RX PubMed=25847581; DOI=10.1002/ajmg.a.36935;
RA Cohen J.S., Srivastava S., Farwell K.D., Lu H.M., Zeng W., Lu H.,
RA Chao E.C., Fatemi A.;
RT "ELP2 is a novel gene implicated in neurodevelopmental disabilities.";
RL Am. J. Med. Genet. A 167:1391-1395(2015).
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 the formation of carboxymethyluridine in the wobble base at
CC position 34 in tRNAs (PubMed:29332244). {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 (PubMed:11714725, PubMed:11818576,
CC PubMed:22854966, PubMed:25960406). Interacts with STAT3 and JAKs (By
CC similarity). {ECO:0000250|UniProtKB:Q91WG4,
CC ECO:0000269|PubMed:11714725, ECO:0000269|PubMed:11818576,
CC ECO:0000269|PubMed:22854966}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11714725,
CC ECO:0000269|PubMed:11818576}. Nucleus {ECO:0000269|PubMed:11714725,
CC ECO:0000269|PubMed:11818576}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q6IA86-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6IA86-2; Sequence=VSP_016531, VSP_016532;
CC Name=3;
CC IsoId=Q6IA86-3; Sequence=VSP_016531;
CC Name=4;
CC IsoId=Q6IA86-4; Sequence=VSP_016533;
CC Name=5;
CC IsoId=Q6IA86-5; Sequence=VSP_043410, VSP_016532;
CC Name=6;
CC IsoId=Q6IA86-6; Sequence=VSP_044979;
CC Name=7;
CC IsoId=Q6IA86-7; Sequence=VSP_044978;
CC -!- DOMAIN: Folds into a two seven-bladed beta-propeller structure which is
CC required for elongator complex assembly.
CC {ECO:0000250|UniProtKB:P42935}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 58
CC (MRT58) [MIM:617270]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRT58
CC transmission pattern is consistent with autosomal recessive
CC inheritance. {ECO:0000269|PubMed:25847581}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the WD repeat ELP2 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:11714725,
CC ECO:0000305|PubMed:11818576, ECO:0000305|PubMed:29332244}.
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DR EMBL; AF332505; AAK97355.1; -; mRNA.
DR EMBL; AF403223; AAQ03093.1; -; mRNA.
DR EMBL; AK001741; BAA91874.1; -; mRNA.
DR EMBL; AK022709; BAB14193.1; -; mRNA.
DR EMBL; AK293051; BAF85740.1; -; mRNA.
DR EMBL; AK300201; BAG61972.1; -; mRNA.
DR EMBL; AK302062; BAG63452.1; -; mRNA.
DR EMBL; CR457269; CAG33550.1; -; mRNA.
DR EMBL; AK222791; BAD96511.1; -; mRNA.
DR EMBL; AC023043; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009211; AAH09211.2; -; mRNA.
DR EMBL; BC032553; AAH32553.1; -; mRNA.
DR CCDS; CCDS11918.1; -. [Q6IA86-1]
DR CCDS; CCDS56065.1; -. [Q6IA86-6]
DR CCDS; CCDS56066.1; -. [Q6IA86-5]
DR CCDS; CCDS56067.1; -. [Q6IA86-3]
DR CCDS; CCDS56068.1; -. [Q6IA86-2]
DR CCDS; CCDS56069.1; -. [Q6IA86-7]
DR RefSeq; NP_001229804.1; NM_001242875.2. [Q6IA86-6]
DR RefSeq; NP_001229805.1; NM_001242876.2. [Q6IA86-5]
DR RefSeq; NP_001229806.1; NM_001242877.2. [Q6IA86-3]
DR RefSeq; NP_001229807.1; NM_001242878.2. [Q6IA86-2]
DR RefSeq; NP_001229808.1; NM_001242879.2. [Q6IA86-7]
DR RefSeq; NP_060725.1; NM_018255.3. [Q6IA86-1]
DR AlphaFoldDB; Q6IA86; -.
DR SMR; Q6IA86; -.
DR BioGRID; 120541; 70.
DR ComplexPortal; CPX-1949; Elongator holoenzyme complex.
DR CORUM; Q6IA86; -.
DR DIP; DIP-56235N; -.
DR IntAct; Q6IA86; 17.
DR MINT; Q6IA86; -.
DR STRING; 9606.ENSP00000414851; -.
DR GlyGen; Q6IA86; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6IA86; -.
DR PhosphoSitePlus; Q6IA86; -.
DR SwissPalm; Q6IA86; -.
DR BioMuta; ELP2; -.
DR DMDM; 83305834; -.
DR EPD; Q6IA86; -.
DR jPOST; Q6IA86; -.
DR MassIVE; Q6IA86; -.
DR MaxQB; Q6IA86; -.
DR PeptideAtlas; Q6IA86; -.
DR PRIDE; Q6IA86; -.
DR ProteomicsDB; 17271; -.
DR ProteomicsDB; 19532; -.
DR ProteomicsDB; 66359; -. [Q6IA86-1]
DR ProteomicsDB; 66360; -. [Q6IA86-2]
DR ProteomicsDB; 66361; -. [Q6IA86-3]
DR ProteomicsDB; 66362; -. [Q6IA86-4]
DR ProteomicsDB; 66363; -. [Q6IA86-5]
DR Antibodypedia; 657; 129 antibodies from 24 providers.
DR DNASU; 55250; -.
DR Ensembl; ENST00000350494.10; ENSP00000316051.6; ENSG00000134759.14. [Q6IA86-5]
DR Ensembl; ENST00000351393.10; ENSP00000257191.7; ENSG00000134759.14. [Q6IA86-3]
DR Ensembl; ENST00000358232.11; ENSP00000350967.6; ENSG00000134759.14. [Q6IA86-1]
DR Ensembl; ENST00000423854.6; ENSP00000391202.2; ENSG00000134759.14. [Q6IA86-7]
DR Ensembl; ENST00000442325.6; ENSP00000414851.2; ENSG00000134759.14. [Q6IA86-6]
DR Ensembl; ENST00000539560.5; ENSP00000443555.1; ENSG00000134759.14. [Q6IA86-4]
DR Ensembl; ENST00000542824.5; ENSP00000443800.1; ENSG00000134759.14. [Q6IA86-2]
DR GeneID; 55250; -.
DR KEGG; hsa:55250; -.
DR MANE-Select; ENST00000358232.11; ENSP00000350967.6; NM_018255.4; NP_060725.1.
DR UCSC; uc002kzk.4; human. [Q6IA86-1]
DR CTD; 55250; -.
DR DisGeNET; 55250; -.
DR GeneCards; ELP2; -.
DR HGNC; HGNC:18248; ELP2.
DR HPA; ENSG00000134759; Low tissue specificity.
DR MalaCards; ELP2; -.
DR MIM; 616054; gene.
DR MIM; 617270; phenotype.
DR neXtProt; NX_Q6IA86; -.
DR OpenTargets; ENSG00000134759; -.
DR PharmGKB; PA162385051; -.
DR VEuPathDB; HostDB:ENSG00000134759; -.
DR eggNOG; KOG1063; Eukaryota.
DR GeneTree; ENSGT00390000000916; -.
DR HOGENOM; CLU_006430_1_0_1; -.
DR InParanoid; Q6IA86; -.
DR OMA; EHTKRVN; -.
DR OrthoDB; 461632at2759; -.
DR PhylomeDB; Q6IA86; -.
DR TreeFam; TF105985; -.
DR PathwayCommons; Q6IA86; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q6IA86; -.
DR UniPathway; UPA00988; -.
DR BioGRID-ORCS; 55250; 544 hits in 1096 CRISPR screens.
DR ChiTaRS; ELP2; human.
DR GeneWiki; ELP2; -.
DR GenomeRNAi; 55250; -.
DR Pharos; Q6IA86; Tbio.
DR PRO; PR:Q6IA86; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q6IA86; protein.
DR Bgee; ENSG00000134759; Expressed in left ovary and 181 other tissues.
DR ExpressionAtlas; Q6IA86; baseline and differential.
DR Genevisible; Q6IA86; HS.
DR GO; GO:0005737; C:cytoplasm; NAS:HGNC-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0033588; C:elongator holoenzyme complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0008023; C:transcription elongation factor complex; IDA:HGNC-UCL.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0046425; P:regulation of receptor signaling pathway via JAK-STAT; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:HGNC-UCL.
DR GO; GO:0006417; P:regulation of translation; IC:ComplexPortal.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:BHF-UCL.
DR GO; GO:0002098; P:tRNA wobble uridine modification; IC:ComplexPortal.
DR Gene3D; 2.130.10.10; -; 5.
DR InterPro; IPR037289; Elp2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR44111; PTHR44111; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 12.
DR SUPFAM; SSF50978; SSF50978; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Disease variant; Intellectual disability;
KW Nucleus; Reference proteome; Repeat; tRNA processing; WD repeat.
FT CHAIN 1..826
FT /note="Elongator complex protein 2"
FT /id="PRO_0000051241"
FT REPEAT 13..53
FT /note="WD 1"
FT REPEAT 56..100
FT /note="WD 2"
FT REPEAT 105..152
FT /note="WD 3"
FT REPEAT 158..200
FT /note="WD 4"
FT REPEAT 205..246
FT /note="WD 5"
FT REPEAT 281..329
FT /note="WD 6"
FT REPEAT 339..378
FT /note="WD 7"
FT REPEAT 386..425
FT /note="WD 8"
FT REPEAT 436..474
FT /note="WD 9"
FT REPEAT 565..609
FT /note="WD 10"
FT REPEAT 612..651
FT /note="WD 11"
FT REPEAT 667..706
FT /note="WD 12"
FT REPEAT 712..753
FT /note="WD 13"
FT REPEAT 777..826
FT /note="WD 14"
FT VAR_SEQ 149..218
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044978"
FT VAR_SEQ 149..174
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_016531"
FT VAR_SEQ 150..175
FT /note="MCLQTLNFGNGFALALCLSFLPNTDV -> TWKTGQVERGRAWKPPASLALC
FT SRSCDSMVSCYASILCKALWKEKLHTFWHHNRISFLPSAFRPI (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043410"
FT VAR_SEQ 175
FT /note="V -> VTWKTGQVERGRAWKPPASLALCSRSCDSMVSCYASILCKALWKEKL
FT HTFWHHNRISFLPSAFRPI (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044979"
FT VAR_SEQ 332..375
FT /note="Missing (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.1"
FT /id="VSP_016532"
FT VAR_SEQ 652..826
FT /note="EPVFSLFAFTNKITSVHSRIIWSCDWSPDSKYFFTGSRDKKVVVWGECDSTD
FT DCIEHNIGPCSSVLDVGGAVTAVSVCPVLHPSQRYVVAVGLECGKICLYTWKKTDQVPE
FT INDWTHCVETSQSQSHTLAIRKLCWKNCSGKTEQKEAEGAEWLHFASCGEDHTVKIHRV
FT NKCAL -> VELFGLVIGVLTASISSLGVETKRWLSGVSATPLMTVLSTTLAPAPQSWT
FT WVGL (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_016533"
FT VARIANT 128
FT /note="T -> P (in dbSNP:rs1785934)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.5"
FT /id="VAR_024072"
FT VARIANT 206
FT /note="H -> R (in MRT58; unknown pathological significance;
FT dbSNP:rs773432002)"
FT /evidence="ECO:0000269|PubMed:25847581"
FT /id="VAR_077989"
FT VARIANT 305
FT /note="V -> M (in dbSNP:rs1785928)"
FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.5"
FT /id="VAR_024073"
FT VARIANT 359
FT /note="H -> R (in dbSNP:rs16967474)"
FT /id="VAR_024074"
FT VARIANT 462
FT /note="R -> W (in MRT58; unknown pathological significance;
FT dbSNP:rs767713084)"
FT /evidence="ECO:0000269|PubMed:25847581"
FT /id="VAR_077990"
FT VARIANT 541
FT /note="I -> T (in dbSNP:rs28463092)"
FT /id="VAR_033804"
FT VARIANT 543
FT /note="T -> P (in dbSNP:rs17563617)"
FT /id="VAR_033805"
FT VARIANT 795
FT /note="E -> G (in dbSNP:rs12607773)"
FT /id="VAR_024075"
FT VARIANT 806
FT /note="H -> P (in dbSNP:rs1044128)"
FT /id="VAR_024076"
FT VARIANT 815
FT /note="T -> P (in dbSNP:rs1044134)"
FT /id="VAR_033806"
FT MUTAGEN 1..17
FT /note="Missing: Abolishes interaction with ELP1 and ELP3."
FT /evidence="ECO:0000269|PubMed:25960406"
FT MUTAGEN 634
FT /note="R->A: No effect on interaction with ELP1 or ELP3;
FT when associated with A-636, A-670 and A-689."
FT /evidence="ECO:0000269|PubMed:25960406"
FT MUTAGEN 636
FT /note="R->A: No effect on interaction with ELP1 or ELP3;
FT when associated with A-634, A-670 and A-689."
FT /evidence="ECO:0000269|PubMed:25960406"
FT MUTAGEN 670
FT /note="R->A: No effect on interaction with ELP1 or ELP3;
FT when associated with A-634, A-636 and A-689."
FT /evidence="ECO:0000269|PubMed:25960406"
FT MUTAGEN 689
FT /note="R->A: No effect on interaction with ELP1 or ELP3;
FT when associated with A-634, A-636 and A-670."
FT /evidence="ECO:0000269|PubMed:25960406"
FT CONFLICT 66
FT /note="W -> R (in Ref. 2; AAQ03093)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="V -> F (in Ref. 4; CAG33550)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="Q -> R (in Ref. 4; CAG33550)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="R -> G (in Ref. 3; BAB14193)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="T -> A (in Ref. 3; BAF85740)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="K -> E (in Ref. 2; AAQ03093)"
FT /evidence="ECO:0000305"
FT CONFLICT 621
FT /note="A -> T (in Ref. 3; BAG63452)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="E -> V (in Ref. 1; AAK97355 and 3; BAB14193)"
FT /evidence="ECO:0000305"
FT CONFLICT 782
FT /note="I -> V (in Ref. 3; BAF85740)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 826 AA; 92500 MW; 949B417D4170B47B CRC64;
MVAPVLETSH VFCCPNRVRG VLNWSSGPRG LLAFGTSCSV VLYDPLKRVV VTNLNGHTAR
VNCIQWICKQ DGSPSTELVS GGSDNQVIHW EIEDNQLLKA VHLQGHEGPV YAVHAVYQRR
TSDPALCTLI VSAAADSAVR LWSKKGPEVM CLQTLNFGNG FALALCLSFL PNTDVPILAC
GNDDCRIHIF AQQNDQFQKV LSLCGHEDWI RGVEWAAFGR DLFLASCSQD CLIRIWKLYI
KSTSLETQDD DNIRLKENTF TIENESVKIA FAVTLETVLA GHENWVNAVH WQPVFYKDGV
LQQPVRLLSA SMDKTMILWA PDEESGVWLE QVRVGEVGGN TLGFYDCQFN EDGSMIIAHA
FHGALHLWKQ NTVNPREWTP EIVISGHFDG VQDLVWDPEG EFIITVGTDQ TTRLFAPWKR
KDQSQVTWHE IARPQIHGYD LKCLAMINRF QFVSGADEKV LRVFSAPRNF VENFCAITGQ
SLNHVLCNQD SDLPEGATVP ALGLSNKAVF QGDIASQPSD EEELLTSTGF EYQQVAFQPS
ILTEPPTEDH LLQNTLWPEV QKLYGHGYEI FCVTCNSSKT LLASACKAAK KEHAAIILWN
TTSWKQVQNL VFHSLTVTQM AFSPNEKFLL AVSRDRTWSL WKKQDTISPE FEPVFSLFAF
TNKITSVHSR IIWSCDWSPD SKYFFTGSRD KKVVVWGECD STDDCIEHNI GPCSSVLDVG
GAVTAVSVCP VLHPSQRYVV AVGLECGKIC LYTWKKTDQV PEINDWTHCV ETSQSQSHTL
AIRKLCWKNC SGKTEQKEAE GAEWLHFASC GEDHTVKIHR VNKCAL
