ID ELL_HUMAN Reviewed; 621 AA. AC P55199; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 04-NOV-2026, entry version 200. DE RecName: Full=RNA polymerase II elongation factor ELL; DE AltName: Full=Eleven-nineteen lysine-rich leukemia protein; GN Name=ELL; Synonyms=C19orf17; 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], AND CHROMOSOMAL TRANSLOCATION. RC TISSUE=Fetal brain; RX PubMed=7991593; DOI=10.1073/pnas.91.25.12110; RA Thirman M.J., Levitan D.A., Kobayashi H., Simon M.C., Rowley J.D.; RT "Cloning of ELL, a gene that fuses to MLL in a t(11;19)(q23;p13.1) in acute RT myeloid leukemia."; RL Proc. Natl. Acad. Sci. U.S.A. 91:12110-12114(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; 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 [3] RP FUNCTION IN TRANSCRIPTION ELONGATION. RX PubMed=8596958; DOI=10.1126/science.271.5257.1873; RA Shilatifard A., Lane W.S., Jackson K.W., Conaway R.C., Conaway J.W.; RT "An RNA polymerase II elongation factor encoded by the human ELL gene."; RL Science 271:1873-1876(1996). RN [4] RP INTERACTION WITH EAF1, AND SUBCELLULAR LOCATION. RX PubMed=11418481; DOI=10.1182/blood.v98.1.201; RA Simone F., Polak P.E., Kaberlein J.J., Luo R.T., Levitan D.A., RA Thirman M.J.; RT "EAF1, a novel ELL-associated factor that is delocalized by expression of RT the MLL-ELL fusion protein."; RL Blood 98:201-209(2001). RN [5] RP INTERACTION WITH EAF2, AND SUBCELLULAR LOCATION. RX PubMed=12446457; DOI=10.1182/blood-2002-06-1664; RA Simone F., Luo R.T., Polak P.E., Kaberlein J.J., Thirman M.J.; RT "ELL-associated factor 2 (EAF2), a functional homolog of EAF1 with RT alternative ELL binding properties."; RL Blood 101:2355-2362(2003). RN [6] RP SUBCELLULAR LOCATION. RX PubMed=12686606; DOI=10.1091/mbc.e02-07-0394; RA Polak P.E., Simone F., Kaberlein J.J., Luo R.T., Thirman M.J.; RT "ELL and EAF1 are Cajal body components that are disrupted in MLL-ELL RT leukemia."; RL Mol. Biol. Cell 14:1517-1528(2003). RN [7] RP FUNCTION IN TRANSCRIPTION. RX PubMed=16006523; DOI=10.1073/pnas.0503017102; RA Kong S.E., Banks C.A., Shilatifard A., Conaway J.W., Conaway R.C.; RT "ELL-associated factors 1 and 2 are positive regulators of RNA polymerase RT II elongation factor ELL."; RL Proc. Natl. Acad. Sci. U.S.A. 102:10094-10098(2005). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-561, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [10] RP FUNCTION, AND IDENTIFICATION IN THE SEC COMPLEX. RX PubMed=20471948; DOI=10.1016/j.molcel.2010.04.013; RA He N., Liu M., Hsu J., Xue Y., Chou S., Burlingame A., Krogan N.J., RA Alber T., Zhou Q.; RT "HIV-1 Tat and host AFF4 recruit two transcription elongation factors into RT a bifunctional complex for coordinated activation of HIV-1 transcription."; RL Mol. Cell 38:428-438(2010). RN [11] RP FUNCTION, AND IDENTIFICATION IN THE SEC COMPLEX. RX PubMed=20159561; DOI=10.1016/j.molcel.2010.01.026; RA Lin C., Smith E.R., Takahashi H., Lai K.C., Martin-Brown S., Florens L., RA Washburn M.P., Conaway J.W., Conaway R.C., Shilatifard A.; RT "AFF4, a component of the ELL/P-TEFb elongation complex and a shared RT subunit of MLL chimeras, can link transcription elongation to leukemia."; RL Mol. Cell 37:429-437(2010). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE SEC COMPLEX, RP IDENTIFICATION IN THE LEC COMPLEX, AND INTERACTION WITH ICE1 AND ICE2. RX PubMed=22195968; DOI=10.1016/j.molcel.2011.12.008; RA Smith E.R., Lin C., Garrett A.S., Thornton J., Mohaghegh N., Hu D., RA Jackson J., Saraf A., Swanson S.K., Seidel C., Florens L., Washburn M.P., RA Eissenberg J.C., Shilatifard A.; RT "The little elongation complex regulates small nuclear RNA transcription."; RL Mol. Cell 44:954-965(2011). RN [14] RP FUNCTION. RX PubMed=22252557; DOI=10.1038/ncomms1652; RA Byun J.S., Fufa T.D., Wakano C., Fernandez A., Haggerty C.M., Sung M.H., RA Gardner K.; RT "ELL facilitates RNA polymerase II pause site entry and release."; RL Nat. Commun. 3:633-633(2012). RN [15] RP REVIEW ON THE SUPER ELONGATION COMPLEX. RX PubMed=22895430; DOI=10.1038/nrm3417; RA Luo Z., Lin C., Shilatifard A.; RT "The super elongation complex (SEC) family in transcriptional control."; RL Nat. Rev. Mol. Cell Biol. 13:543-547(2012). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND SER-309, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [18] RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE LEC COMPLEX, AND RP INTERACTION WITH ICE1. RX PubMed=23932780; DOI=10.1016/j.molcel.2013.07.003; RA Hu D., Smith E.R., Garruss A.S., Mohaghegh N., Varberg J.M., Lin C., RA Jackson J., Gao X., Saraf A., Florens L., Washburn M.P., Eissenberg J.C., RA Shilatifard A.; RT "The little elongation complex functions at initiation and elongation RT phases of snRNA gene transcription."; RL Mol. Cell 51:493-505(2013). RN [19] RP INTERACTION WITH USPL1. RX PubMed=24413172; DOI=10.1242/jcs.141788; RA Hutten S., Chachami G., Winter U., Melchior F., Lamond A.I.; RT "A role for the Cajal-body-associated SUMO isopeptidase USPL1 in snRNA RT transcription mediated by RNA polymerase II."; RL J. Cell Sci. 127:1065-1078(2014). RN [20] RP STRUCTURE BY NMR OF 197-297. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the helical domain in human eleven-nineteen lysine- RT rich leukemia protein ELL."; RL Submitted (MAY-2007) to the PDB data bank. CC -!- FUNCTION: Elongation factor component of the super elongation complex CC (SEC), a complex required to increase the catalytic rate of RNA CC polymerase II transcription by suppressing transient pausing by the CC polymerase at multiple sites along the DNA. Elongation factor component CC of the little elongation complex (LEC), a complex required to regulate CC small nuclear RNA (snRNA) gene transcription by RNA polymerase II and CC III (PubMed:22195968, PubMed:23932780). Specifically required for CC stimulating the elongation step of RNA polymerase II- and III-dependent CC snRNA gene transcription (PubMed:23932780). ELL also plays an early CC role before its assembly into in the SEC complex by stabilizing RNA CC polymerase II recruitment/initiation and entry into the pause site. CC Required to stabilize the pre-initiation complex and early elongation. CC {ECO:0000269|PubMed:16006523, ECO:0000269|PubMed:20159561, CC ECO:0000269|PubMed:20471948, ECO:0000269|PubMed:22195968, CC ECO:0000269|PubMed:22252557, ECO:0000269|PubMed:23932780, CC ECO:0000269|PubMed:8596958}. CC -!- SUBUNIT: Component of the super elongation complex (SEC), at least CC composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb CC complex and ELL (ELL, ELL2 or ELL3). Component of the little elongation CC complex (LEC), at least composed of ELL (ELL, ELL2 or ELL3), ZC3H8, CC ICE1 and ICE2. Interacts with AFF4; the interaction is direct. CC Interacts with EAF1 and EAF2. Interacts with ICE1 (via N-terminus CC domain). Interacts with ICE2. Interacts with USPL1 (PubMed:24413172). CC {ECO:0000269|PubMed:11418481, ECO:0000269|PubMed:12446457, CC ECO:0000269|PubMed:20159561, ECO:0000269|PubMed:20471948, CC ECO:0000269|PubMed:22195968, ECO:0000269|PubMed:23932780, CC ECO:0000269|PubMed:24413172}. CC -!- INTERACTION: CC P55199; Q659A1: ICE2; NbExp=5; IntAct=EBI-1245868, EBI-4322746; CC P55199; P62136: PPP1CA; NbExp=2; IntAct=EBI-1245868, EBI-357253; CC P55199; Q96H20: SNF8; NbExp=3; IntAct=EBI-1245868, EBI-747719; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11418481, CC ECO:0000269|PubMed:12446457}. Nucleus speckle CC {ECO:0000269|PubMed:11418481, ECO:0000269|PubMed:12446457}. Nucleus, CC Cajal body {ECO:0000269|PubMed:12686606, ECO:0000269|PubMed:22195968, CC ECO:0000269|PubMed:23932780}. Note=Colocalizes with EAF2 to nuclear CC speckles (PubMed:12446457). Colocalizes with coilin in subnuclear cajal CC and histone locus bodies (PubMed:12686606). Translocates in the CC LEC complex to cajal and histone locus bodies at snRNA genes in a ICE1- CC dependent manner. Associates to transcriptionally active chromatin at CC snRNA genes (PubMed:23932780). {ECO:0000269|PubMed:12446457, CC ECO:0000269|PubMed:12686606, ECO:0000269|PubMed:23932780}. CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested. Highest levels CC found in placenta, skeletal muscle, testis and peripheral blood CC leukocytes. CC -!- DISEASE: Note=A chromosomal aberration involving ELL is found in acute CC leukemias. Translocation t(11;19)(q23;p13.1) with KMT2A/MLL1. The CC result is a rogue activator protein. {ECO:0000269|PubMed:7991593}. CC -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/10/ELL"; 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; U16282; AAA57120.1; -; mRNA. DR EMBL; BC049195; AAH49195.1; -; mRNA. DR CCDS; CCDS12380.1; -. DR PIR; I38880; I38880. DR RefSeq; NP_006523.1; NM_006532.4. DR PDB; 2DOA; NMR; -; A=200-292. DR SMR; P55199; -. DR BioGRID; 113828; 95. DR ComplexPortal; CPX-2712; Little elongation complex, ELL variant. DR CORUM; P55199; -. DR IntAct; P55199; 53. DR STRING; 9606.ENSP00000262809; -. DR NDEx; IQUERY-CP-ELL; 1 NDEx IQuery Curated Pathway. DR BindingDB; P55199; -. DR ChEMBL; CHEMBL5725004; -. DR GlyGen; P55199; 2 sites, 1 N-linked glycan (1 site). DR iPTMnet; P55199; -. DR PhosphoSitePlus; P55199; -. DR BioMuta; ELL; -. DR DMDM; 1706635; -. DR PaxDb; 9606-ENSP00000262809; -. DR PeptideAtlas; P55199; -. DR ProteomicsDB; 56805; -. DR Pumba; P55199; -. DR jPOST; P55199; -. DR MassIVE; P55199; -. DR DNASU; 8178; -. DR Ensembl; ENST00000262809.9; ENSP00000262809.3; ENSG00000105656.14. DR GeneID; 8178; -. DR KEGG; hsa:8178; -. DR MANE-Select; ENST00000262809.9; ENSP00000262809.3; NM_006532.4; NP_006523.1. DR UCSC; uc002njh.3; human. DR CTD; 8178; -. DR DisGeNET; 8178; -. DR VEuPathDB; HostDB:ENSG00000105656; -. DR GeneCards; ELL; -. DR HGNC; HGNC:23114; ELL. DR AGR; HGNC:23114; -. DR HPA; ENSG00000105656; Low tissue specificity. DR MIM; 600284; gene. DR OpenTargets; ENSG00000105656; -. DR ClinPGx; PA134939610; -. DR eggNOG; KOG4796; Eukaryota. DR GeneTree; ENSGT00940000155914; -. DR HOGENOM; CLU_021268_0_0_1; -. DR InParanoid; P55199; -. DR OMA; AAPCWVQ; -. DR OrthoDB; 6284217at2759; -. DR PhylomeDB; P55199; -. DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex. DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat. DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat. DR Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation. DR Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery. DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript. DR Reactome; R-HSA-167287; HIV elongation arrest and recovery. DR Reactome; R-HSA-167290; Pausing and recovery of HIV elongation. DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events. DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER). DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes. DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes. DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation. DR Reactome; R-HSA-9938024; Somatic hypermutation of immunoglobulin genes. DR SignaLink; P55199; -. DR SIGNOR; P55199; -. DR ChiTaRS; ELL; human. DR EvolutionaryTrace; P55199; -. DR Agora; ENSG00000105656; -. DR GeneWiki; ELL_(gene); -. DR GenomeRNAi; 8178; -. DR PRO; PR:P55199; -. DR Bgee; ENSG00000105656; Expressed in right testis and 110 other cell types or tissues. DR ExpressionAtlas; P55199; baseline and differential. DR FunFam; 1.10.10.2670:FF:000002; RNA polymerase II elongation factor ELL2; 1. DR Gene3D; 6.10.140.340; -; 1. DR Gene3D; 1.10.10.2670; E3 ubiquitin-protein ligase; 1. DR InterPro; IPR042065; E3_ELL-like. DR InterPro; IPR031176; ELL/occludin. DR InterPro; IPR019464; ELL_N. DR InterPro; IPR010844; Occludin_ELL. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR23288; OCCLUDIN AND RNA POLYMERASE II ELONGATION FACTOR ELL; 1. DR PANTHER; PTHR23288:SF9; RNA POLYMERASE II ELONGATION FACTOR ELL; 1. DR Pfam; PF10390; ELL; 1. DR Pfam; PF07303; Occludin_ELL; 1. DR SUPFAM; SSF144292; occludin/ELL-like; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS51980; OCEL; 1. DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB. DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB. DR GO; GO:0035363; C:histone locus body; IDA:UniProtKB. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB. DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0019902; F:phosphatase binding; IDA:UniProtKB. DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; TAS:ProtInc. DR GO; GO:1905382; P:positive regulation of snRNA transcription by RNA polymerase II; NAS:ComplexPortal. DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IMP:UniProtKB. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IMP:UniProtKB. DR GO; GO:0042795; P:snRNA transcription by RNA polymerase II; IMP:UniProtKB. DR GO; GO:0042796; P:snRNA transcription by RNA polymerase III; IMP:UniProtKB. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; TAS:ProtInc. DR Proteomes; UP000005640; Chromosome 19. DR PathwayCommons; P55199; -. DR Pharos; P55199; Tbio. DR Antibodypedia; 15081; 453 antibodies from 35 providers. DR RNAct; P55199; protein. DR BioGRID-ORCS; 8178; 781 hits in 1167 CRISPR screens. DR AlphaFoldDB; P55199; -. DR CD-CODE; 804901D1; Nuclear speckle. DR FunCoup; P55199; 3843. DR PAN-GO; P55199; 4 GO annotations based on evolutionary models. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Chromosomal rearrangement; Nucleus; KW Phosphoprotein; Proteomics identification; Proto-oncogene; KW Reference proteome; Transcription; Transcription regulation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..621 FT /note="RNA polymerase II elongation factor ELL" FT /id="PRO_0000146733" FT DOMAIN 507..617 FT /note="OCEL" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01324" FT REGION 296..417 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 431..504 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 445..459 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 374..383 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 406..415 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 436..445 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 446..457 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 458..467 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 474..504 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 46 FT /note="KMT2A/MLL1 fusion point (in acute myeloid leukemia FT patient)" FT /evidence="ECO:0000269|PubMed:7991593" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 180 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 309 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 561 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT VARIANT 297 FT /note="S -> N (in dbSNP:rs2303694)" FT /id="VAR_053072" FT VARIANT 387 FT /note="R -> W (in dbSNP:rs35245196)" FT /id="VAR_053073" FT HELIX 207..217 FT /evidence="ECO:0007829|PDB:2DOA" FT HELIX 222..232 FT /evidence="ECO:0007829|PDB:2DOA" FT HELIX 236..248 FT /evidence="ECO:0007829|PDB:2DOA" FT STRAND 249..252 FT /evidence="ECO:0007829|PDB:2DOA" FT STRAND 254..256 FT /evidence="ECO:0007829|PDB:2DOA" FT STRAND 258..260 FT /evidence="ECO:0007829|PDB:2DOA" FT HELIX 265..268 FT /evidence="ECO:0007829|PDB:2DOA" FT HELIX 279..291 FT /evidence="ECO:0007829|PDB:2DOA" SQ SEQUENCE 621 AA; 68265 MW; EB4A3F94CA8A411F CRC64; MAALKEDRSY GLSCGRVSDG SKVSVFHVKL TDSALRAFES YRARQDSVSL RPSIRFQGSQ GHISIPQPDC PAEARTFSFY LSNIGRDNPQ GSFDCIQQYV SSHGEVHLDC LGSIQDKITV CATDDSYQKA RQSMAQAEEE TRSRSAIVIK AGGRYLGKKV QFRKPAPGAT DAVPSRKRAT PINLASAIRK SGASAVSGGS GVSQRPFRDR VLHLLALRPY RKAELLLRLQ KDGLTQADKD ALDGLLQQVA NMSAKDGTCT LQDCMYKDVQ KDWPGYSEGD QQLLKRVLVR KLCQPQSTGS LLGDPAASSP PGERGRSASP PQKRLQPPDF IDPLANKKPR ISHFTQRAQP AVNGKLGVPN GREALLPTPG PPASTDTLSS STHLPPRLEP PRAHDPLADV SNDLGHSGRD CEHGEAAAPA PTVRLGLPLL TDCAQPSRPH GSPSRSKPKK KSKKHKDKER AAEDKPRAQL PDCAPATHAT PGAPADTPGL NGTCSVSSVP TSTSETPDYL LKYAAISSSE QRQSYKNDFN AEYSEYRDLH ARIERITRRF TQLDAQLRQL SQGSEEYETT RGQILQEYRK IKKTNTNYSQ EKHRCEYLHS KLAHIKRLIA EYDQRQLQAW P //