EAF1_HUMAN
ID EAF1_HUMAN Reviewed; 268 AA.
AC Q96JC9; B4E3F5; Q8IW10;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=ELL-associated factor 1;
GN Name=EAF1;
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), FUNCTION, INTERACTION WITH ELL AND
RP ELL2, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Bone marrow;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
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 [6]
RP FUNCTION.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, 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 IDENTIFICATION IN THE SEC COMPLEX.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND IDENTIFICATION BY
RP 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Acts as a transcriptional transactivator of ELL and ELL2
CC elongation activities. {ECO:0000269|PubMed:11418481,
CC ECO:0000269|PubMed:16006523}.
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). Interacts with ELL and ELL2.
CC {ECO:0000269|PubMed:11418481, ECO:0000269|PubMed:22195968}.
CC -!- INTERACTION:
CC Q96JC9; Q96CW1: AP2M1; NbExp=5; IntAct=EBI-769261, EBI-297683;
CC Q96JC9; Q4LE39-3: ARID4B; NbExp=3; IntAct=EBI-769261, EBI-11957452;
CC Q96JC9; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-769261, EBI-10181188;
CC Q96JC9; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-769261, EBI-11519926;
CC Q96JC9; Q8NCX0-3: CCDC150; NbExp=3; IntAct=EBI-769261, EBI-12235840;
CC Q96JC9; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-769261, EBI-739624;
CC Q96JC9; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-769261, EBI-742887;
CC Q96JC9; Q9H147: DNTTIP1; NbExp=3; IntAct=EBI-769261, EBI-2795449;
CC Q96JC9; Q7L190: DPPA4; NbExp=3; IntAct=EBI-769261, EBI-710457;
CC Q96JC9; O00472: ELL2; NbExp=6; IntAct=EBI-769261, EBI-395274;
CC Q96JC9; Q9HB65: ELL3; NbExp=5; IntAct=EBI-769261, EBI-715224;
CC Q96JC9; Q86W67: FAM228A; NbExp=3; IntAct=EBI-769261, EBI-12958227;
CC Q96JC9; Q8TAE8: GADD45GIP1; NbExp=3; IntAct=EBI-769261, EBI-372506;
CC Q96JC9; O95995: GAS8; NbExp=3; IntAct=EBI-769261, EBI-1052570;
CC Q96JC9; Q5JQS6: GCSAML; NbExp=3; IntAct=EBI-769261, EBI-17857617;
CC Q96JC9; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-769261, EBI-5916454;
CC Q96JC9; Q8TE85-2: GRHL3; NbExp=3; IntAct=EBI-769261, EBI-12827521;
CC Q96JC9; P32780: GTF2H1; NbExp=3; IntAct=EBI-769261, EBI-715539;
CC Q96JC9; Q92759: GTF2H4; NbExp=3; IntAct=EBI-769261, EBI-6380495;
CC Q96JC9; Q9NSC5: HOMER3; NbExp=7; IntAct=EBI-769261, EBI-748420;
CC Q96JC9; O75031: HSF2BP; NbExp=3; IntAct=EBI-769261, EBI-7116203;
CC Q96JC9; Q14145: KEAP1; NbExp=3; IntAct=EBI-769261, EBI-751001;
CC Q96JC9; Q86T90: KIAA1328; NbExp=3; IntAct=EBI-769261, EBI-3437878;
CC Q96JC9; Q8N8X9: MAB21L3; NbExp=3; IntAct=EBI-769261, EBI-10268010;
CC Q96JC9; O95402: MED26; NbExp=5; IntAct=EBI-769261, EBI-394392;
CC Q96JC9; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-769261, EBI-2548751;
CC Q96JC9; P26367: PAX6; NbExp=3; IntAct=EBI-769261, EBI-747278;
CC Q96JC9; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-769261, EBI-79165;
CC Q96JC9; Q9NWS0: PIH1D1; NbExp=3; IntAct=EBI-769261, EBI-357318;
CC Q96JC9; P61289: PSME3; NbExp=9; IntAct=EBI-769261, EBI-355546;
CC Q96JC9; Q8N488: RYBP; NbExp=3; IntAct=EBI-769261, EBI-752324;
CC Q96JC9; O00560: SDCBP; NbExp=3; IntAct=EBI-769261, EBI-727004;
CC Q96JC9; P04279-2: SEMG1; NbExp=3; IntAct=EBI-769261, EBI-12272118;
CC Q96JC9; P37108: SRP14; NbExp=3; IntAct=EBI-769261, EBI-353399;
CC Q96JC9; Q96MF2: STAC3; NbExp=5; IntAct=EBI-769261, EBI-745680;
CC Q96JC9; Q15560: TCEA2; NbExp=3; IntAct=EBI-769261, EBI-710310;
CC Q96JC9; Q12800: TFCP2; NbExp=3; IntAct=EBI-769261, EBI-717422;
CC Q96JC9; Q08117: TLE5; NbExp=4; IntAct=EBI-769261, EBI-717810;
CC Q96JC9; O95379: TNFAIP8; NbExp=3; IntAct=EBI-769261, EBI-1049336;
CC Q96JC9; P19237: TNNI1; NbExp=3; IntAct=EBI-769261, EBI-746692;
CC Q96JC9; Q12933: TRAF2; NbExp=3; IntAct=EBI-769261, EBI-355744;
CC Q96JC9; Q9BVG3: TRIM62; NbExp=3; IntAct=EBI-769261, EBI-6929619;
CC Q96JC9; Q5SQQ9-2: VAX1; NbExp=3; IntAct=EBI-769261, EBI-12227803;
CC Q96JC9; Q8IY57-5: YAF2; NbExp=5; IntAct=EBI-769261, EBI-12111538;
CC Q96JC9; O43829: ZBTB14; NbExp=3; IntAct=EBI-769261, EBI-10176632;
CC Q96JC9; P52747: ZNF143; NbExp=3; IntAct=EBI-769261, EBI-2849334;
CC Q96JC9; O95125: ZNF202; NbExp=3; IntAct=EBI-769261, EBI-751960;
CC Q96JC9; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-769261, EBI-4395669;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:11418481}.
CC Nucleus, Cajal body {ECO:0000269|PubMed:12686606}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96JC9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96JC9-2; Sequence=VSP_056193, VSP_056194;
CC -!- TISSUE SPECIFICITY: Strongly expressed in heart, brain, placenta, lung,
CC liver, skeletal muscle, kidney, pancreas, spleen, prostate, testis,
CC small intestine and colon. Poorly expressed in thymus.
CC {ECO:0000269|PubMed:11418481}.
CC -!- SIMILARITY: Belongs to the EAF family. {ECO:0000305}.
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DR EMBL; AF272973; AAK58687.1; -; mRNA.
DR EMBL; AK304697; BAG65467.1; -; mRNA.
DR EMBL; AC027125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041329; AAH41329.1; -; mRNA.
DR CCDS; CCDS2626.1; -. [Q96JC9-1]
DR RefSeq; NP_149074.3; NM_033083.6. [Q96JC9-1]
DR RefSeq; XP_005265575.1; XM_005265518.1. [Q96JC9-2]
DR RefSeq; XP_011532467.1; XM_011534165.1. [Q96JC9-2]
DR RefSeq; XP_011532468.1; XM_011534166.1. [Q96JC9-2]
DR PDB; 7OKX; EM; 3.30 A; O=1-268.
DR PDB; 7OKY; EM; 4.14 A; O=1-268.
DR PDBsum; 7OKX; -.
DR PDBsum; 7OKY; -.
DR AlphaFoldDB; Q96JC9; -.
DR SMR; Q96JC9; -.
DR BioGRID; 124514; 119.
DR CORUM; Q96JC9; -.
DR IntAct; Q96JC9; 95.
DR MINT; Q96JC9; -.
DR STRING; 9606.ENSP00000380054; -.
DR GlyGen; Q96JC9; 1 site.
DR iPTMnet; Q96JC9; -.
DR PhosphoSitePlus; Q96JC9; -.
DR BioMuta; EAF1; -.
DR DMDM; 73919265; -.
DR EPD; Q96JC9; -.
DR jPOST; Q96JC9; -.
DR MassIVE; Q96JC9; -.
DR MaxQB; Q96JC9; -.
DR PaxDb; Q96JC9; -.
DR PeptideAtlas; Q96JC9; -.
DR PRIDE; Q96JC9; -.
DR ProteomicsDB; 5897; -.
DR ProteomicsDB; 76942; -. [Q96JC9-1]
DR Antibodypedia; 26754; 131 antibodies from 21 providers.
DR DNASU; 85403; -.
DR Ensembl; ENST00000396842.7; ENSP00000380054.2; ENSG00000144597.14. [Q96JC9-1]
DR GeneID; 85403; -.
DR KEGG; hsa:85403; -.
DR MANE-Select; ENST00000396842.7; ENSP00000380054.2; NM_033083.7; NP_149074.3.
DR UCSC; uc003bzu.4; human. [Q96JC9-1]
DR CTD; 85403; -.
DR DisGeNET; 85403; -.
DR GeneCards; EAF1; -.
DR HGNC; HGNC:20907; EAF1.
DR HPA; ENSG00000144597; Tissue enhanced (bone).
DR MIM; 608315; gene.
DR neXtProt; NX_Q96JC9; -.
DR OpenTargets; ENSG00000144597; -.
DR PharmGKB; PA134897202; -.
DR VEuPathDB; HostDB:ENSG00000144597; -.
DR eggNOG; KOG4795; Eukaryota.
DR GeneTree; ENSGT00390000017724; -.
DR HOGENOM; CLU_025755_0_0_1; -.
DR InParanoid; Q96JC9; -.
DR OMA; YHKECVL; -.
DR OrthoDB; 1269479at2759; -.
DR PhylomeDB; Q96JC9; -.
DR TreeFam; TF320864; -.
DR PathwayCommons; Q96JC9; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR SignaLink; Q96JC9; -.
DR SIGNOR; Q96JC9; -.
DR BioGRID-ORCS; 85403; 257 hits in 1082 CRISPR screens.
DR ChiTaRS; EAF1; human.
DR GeneWiki; EAF1; -.
DR GenomeRNAi; 85403; -.
DR Pharos; Q96JC9; Tbio.
DR PRO; PR:Q96JC9; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q96JC9; protein.
DR Bgee; ENSG00000144597; Expressed in amniotic fluid and 182 other tissues.
DR ExpressionAtlas; Q96JC9; baseline and differential.
DR Genevisible; Q96JC9; HS.
DR GO; GO:0015030; C:Cajal body; IEA:UniProtKB-SubCell.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0032783; C:super elongation complex; IEA:InterPro.
DR GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
DR GO; GO:0003711; F:transcription elongation regulator activity; IMP:ARUK-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IMP:ARUK-UCL.
DR InterPro; IPR027093; EAF_fam.
DR InterPro; IPR019194; Tscrpt_elong_fac_Eaf_N.
DR PANTHER; PTHR15970; PTHR15970; 1.
DR Pfam; PF09816; EAF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..268
FT /note="ELL-associated factor 1"
FT /id="PRO_0000130334"
FT REGION 106..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..262
FT /note="Necessary for transactivation activity"
FT COMPBIAS 106..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..162
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..11
FT /note="MNGTANPLLDR -> MKSQLHCHISL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056193"
FT VAR_SEQ 12..112
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056194"
FT CONFLICT 97
FT /note="Y -> F (in Ref. 4; AAH41329)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="T -> A (in Ref. 4; AAH41329)"
FT /evidence="ECO:0000305"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:7OKX"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:7OKX"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:7OKX"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:7OKX"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:7OKX"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:7OKX"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:7OKX"
FT STRAND 83..91
FT /evidence="ECO:0007829|PDB:7OKX"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:7OKX"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:7OKX"
FT STRAND 102..111
FT /evidence="ECO:0007829|PDB:7OKX"
SQ SEQUENCE 268 AA; 29042 MW; 0D78B586AABB0FA4 CRC64;
MNGTANPLLD REEHCLRLGE SFEKRPRASF HTIRYDFKPA SIDTSCEGEL QVGKGDEVTI
TLPHIPGSTP PMTVFKGNKR PYQKDCVLII NHDTGEYVLE KLSSSIQVKK TRAEGSSKIQ
ARMEQQPTRP PQTSQPPPPP PPMPFRAPTK PPVGPKTSPL KDNPSPEPQL DDIKRELRAE
VDIIEQMSSS SGSSSSDSES SSGSDDDSSS SGGEDNGPAS PPQPSHQQPY NSRPAVANGT
SRPQGSNQLM NTLRNDLQLS ESGSDSDD
