ELL2_HUMAN
ID ELL2_HUMAN Reviewed; 640 AA.
AC O00472; B4DNK7;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=RNA polymerase II elongation factor ELL2;
GN Name=ELL2;
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 [GENOMIC DNA], AND VARIANT THR-298.
RX PubMed=9108030; DOI=10.1073/pnas.94.8.3639;
RA Shilatifard A., Duan D.R., Haque D., Florence C., Schubach W.H.,
RA Conaway J.W., Conaway R.C.;
RT "ELL2, a new member of an ELL family of RNA polymerase II elongation
RT factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3639-3643(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-298.
RC TISSUE=Testis;
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 INTERACTION WITH EAF1.
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 [6]
RP INTERACTION WITH EAF2.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-580, 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 [8]
RP IDENTIFICATION BY 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 [9]
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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, 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 [12]
RP FUNCTION, IDENTIFICATION IN THE SEC COMPLEX, AND IDENTIFICATION IN THE LEC
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, 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 [14]
RP UBIQUITINATION.
RX PubMed=22483617; DOI=10.1016/j.molcel.2012.03.007;
RA Liu M., Hsu J., Chan C., Li Z., Zhou Q.;
RT "The ubiquitin ligase Siah1 controls ELL2 stability and formation of super
RT elongation complexes to modulate gene transcription.";
RL Mol. Cell 46:325-334(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 FUNCTION.
RX PubMed=23251033; DOI=10.1073/pnas.1216971110;
RA Chou S., Upton H., Bao K., Schulze-Gahmen U., Samelson A.J., He N.,
RA Nowak A., Lu H., Krogan N.J., Zhou Q., Alber T.;
RT "HIV-1 Tat recruits transcription elongation factors dispersed along a
RT flexible AFF4 scaffold.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E123-E131(2013).
RN [17]
RP STRUCTURE BY NMR OF 197-292.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ELL_N2 domain of target of RNA polymerase II
RT elongation factor ELL2.";
RL Submitted (JUN-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. Component of the little
CC elongation complex (LEC), a complex required to regulate small nuclear
CC RNA (snRNA) gene transcription by RNA polymerase II and III
CC (PubMed:22195968). Plays a role in immunoglobulin secretion in plasma
CC cells: directs efficient alternative mRNA processing, influencing both
CC proximal poly(A) site choice and exon skipping, as well as
CC immunoglobulin heavy chain (IgH) alternative processing. Probably acts
CC by regulating histone modifications accompanying transition from
CC membrane-specific to secretory IgH mRNA expression.
CC {ECO:0000269|PubMed:20159561, ECO:0000269|PubMed:20471948,
CC ECO:0000269|PubMed:22195968, ECO:0000269|PubMed:23251033}.
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 and leads
CC to stabilize ELL2 and prevent ELL2 ubiquitination. Interacts with EAF1
CC and EAF2. {ECO:0000269|PubMed:11418481, ECO:0000269|PubMed:12446457,
CC ECO:0000269|PubMed:20159561, ECO:0000269|PubMed:20471948,
CC ECO:0000269|PubMed:22195968}.
CC -!- INTERACTION:
CC O00472; P07550: ADRB2; NbExp=3; IntAct=EBI-395274, EBI-491169;
CC O00472; Q8TAX5: AFF4; NbExp=3; IntAct=EBI-395274, EBI-745478;
CC O00472; Q92870-2: APBB2; NbExp=3; IntAct=EBI-395274, EBI-21535880;
CC O00472; P54253: ATXN1; NbExp=6; IntAct=EBI-395274, EBI-930964;
CC O00472; P55212: CASP6; NbExp=3; IntAct=EBI-395274, EBI-718729;
CC O00472; P28329-3: CHAT; NbExp=3; IntAct=EBI-395274, EBI-25837549;
CC O00472; Q96JC9: EAF1; NbExp=6; IntAct=EBI-395274, EBI-769261;
CC O00472; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-395274, EBI-742102;
CC O00472; P22607: FGFR3; NbExp=3; IntAct=EBI-395274, EBI-348399;
CC O00472; P21333-2: FLNA; NbExp=3; IntAct=EBI-395274, EBI-9641086;
CC O00472; Q14957: GRIN2C; NbExp=3; IntAct=EBI-395274, EBI-8285963;
CC O00472; P06396: GSN; NbExp=3; IntAct=EBI-395274, EBI-351506;
CC O00472; P30519: HMOX2; NbExp=3; IntAct=EBI-395274, EBI-712096;
CC O00472; P13473-2: LAMP2; NbExp=3; IntAct=EBI-395274, EBI-21591415;
CC O00472; Q8N2W9: PIAS4; NbExp=3; IntAct=EBI-395274, EBI-473160;
CC O00472; O43741: PRKAB2; NbExp=3; IntAct=EBI-395274, EBI-1053424;
CC O00472; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-395274, EBI-5280197;
CC O00472; P49810: PSEN2; NbExp=3; IntAct=EBI-395274, EBI-2010251;
CC O00472; P62826: RAN; NbExp=3; IntAct=EBI-395274, EBI-286642;
CC O00472; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-395274, EBI-2623095;
CC O00472; P37840: SNCA; NbExp=3; IntAct=EBI-395274, EBI-985879;
CC O00472; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-395274, EBI-741480;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00472-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O00472-2; Sequence=VSP_055476;
CC -!- PTM: Ubiquitinated by SIAH1, leading to its degradation by the
CC proteasome. Interaction with AFF4 stabilizes ELL2 and prevents ELL2
CC ubiquitination. {ECO:0000269|PubMed:22483617}.
CC -!- SIMILARITY: Belongs to the ELL/occludin family. {ECO:0000305}.
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DR EMBL; U88629; AAC51232.1; -; Genomic_DNA.
DR EMBL; AK297956; BAG60269.1; -; mRNA.
DR EMBL; AC008592; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028412; AAH28412.1; -; mRNA.
DR CCDS; CCDS4080.1; -. [O00472-1]
DR RefSeq; NP_036213.2; NM_012081.5. [O00472-1]
DR PDB; 2E5N; NMR; -; A=200-292.
DR PDB; 5JW9; X-ray; 2.00 A; B=519-640.
DR PDB; 7OKX; EM; 3.30 A; M=1-640.
DR PDB; 7OKY; EM; 4.14 A; M=1-640.
DR PDBsum; 2E5N; -.
DR PDBsum; 5JW9; -.
DR PDBsum; 7OKX; -.
DR PDBsum; 7OKY; -.
DR AlphaFoldDB; O00472; -.
DR SMR; O00472; -.
DR BioGRID; 116595; 33.
DR CORUM; O00472; -.
DR IntAct; O00472; 50.
DR STRING; 9606.ENSP00000237853; -.
DR GlyConnect; 1720; 4 N-Linked glycans (1 site).
DR GlyGen; O00472; 1 site, 3 N-linked glycans (1 site).
DR iPTMnet; O00472; -.
DR PhosphoSitePlus; O00472; -.
DR BioMuta; ELL2; -.
DR EPD; O00472; -.
DR jPOST; O00472; -.
DR MassIVE; O00472; -.
DR MaxQB; O00472; -.
DR PaxDb; O00472; -.
DR PeptideAtlas; O00472; -.
DR PRIDE; O00472; -.
DR ProteomicsDB; 4705; -.
DR ProteomicsDB; 47920; -. [O00472-1]
DR Antibodypedia; 13079; 183 antibodies from 30 providers.
DR DNASU; 22936; -.
DR Ensembl; ENST00000237853.9; ENSP00000237853.4; ENSG00000118985.16. [O00472-1]
DR GeneID; 22936; -.
DR KEGG; hsa:22936; -.
DR MANE-Select; ENST00000237853.9; ENSP00000237853.4; NM_012081.6; NP_036213.2.
DR UCSC; uc003klr.4; human. [O00472-1]
DR CTD; 22936; -.
DR DisGeNET; 22936; -.
DR GeneCards; ELL2; -.
DR HGNC; HGNC:17064; ELL2.
DR HPA; ENSG00000118985; Low tissue specificity.
DR MIM; 601874; gene.
DR neXtProt; NX_O00472; -.
DR OpenTargets; ENSG00000118985; -.
DR PharmGKB; PA134935340; -.
DR VEuPathDB; HostDB:ENSG00000118985; -.
DR eggNOG; KOG4796; Eukaryota.
DR GeneTree; ENSGT00940000154828; -.
DR HOGENOM; CLU_021268_0_0_1; -.
DR InParanoid; O00472; -.
DR OMA; SCGRVTQ; -.
DR PhylomeDB; O00472; -.
DR TreeFam; TF326161; -.
DR PathwayCommons; O00472; -.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR SignaLink; O00472; -.
DR BioGRID-ORCS; 22936; 21 hits in 1080 CRISPR screens.
DR ChiTaRS; ELL2; human.
DR EvolutionaryTrace; O00472; -.
DR GenomeRNAi; 22936; -.
DR Pharos; O00472; Tbio.
DR PRO; PR:O00472; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O00472; protein.
DR Bgee; ENSG00000118985; Expressed in parotid gland and 188 other tissues.
DR ExpressionAtlas; O00472; baseline and differential.
DR Genevisible; O00472; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0042795; P:snRNA transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:ProtInc.
DR Gene3D; 1.10.10.2670; -; 1.
DR InterPro; IPR042065; E3_ELL-like.
DR InterPro; IPR031176; ELL/occludin.
DR InterPro; IPR031179; ELL2.
DR InterPro; IPR019464; ELL_N.
DR InterPro; IPR010844; Occludin_ELL.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR23288; PTHR23288; 2.
DR PANTHER; PTHR23288:SF36; PTHR23288:SF36; 2.
DR Pfam; PF10390; ELL; 1.
DR Pfam; PF07303; Occludin_ELL; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51980; OCEL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..640
FT /note="RNA polymerase II elongation factor ELL2"
FT /id="PRO_0000146735"
FT DOMAIN 526..636
FT /note="OCEL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01324"
FT REGION 172..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..384
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 140..389
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055476"
FT VARIANT 298
FT /note="A -> T (in dbSNP:rs3815768)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9108030"
FT /id="VAR_058406"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:7OKX"
FT HELIX 36..47
FT /evidence="ECO:0007829|PDB:7OKX"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:7OKX"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:7OKX"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:7OKX"
FT TURN 89..91
FT /evidence="ECO:0007829|PDB:7OKX"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:7OKX"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:7OKX"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:7OKX"
FT HELIX 128..145
FT /evidence="ECO:0007829|PDB:7OKX"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:2E5N"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:2E5N"
FT HELIX 235..248
FT /evidence="ECO:0007829|PDB:2E5N"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:2E5N"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:2E5N"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:2E5N"
FT HELIX 264..267
FT /evidence="ECO:0007829|PDB:2E5N"
FT HELIX 279..290
FT /evidence="ECO:0007829|PDB:2E5N"
FT HELIX 527..531
FT /evidence="ECO:0007829|PDB:5JW9"
FT HELIX 538..578
FT /evidence="ECO:0007829|PDB:5JW9"
FT HELIX 584..602
FT /evidence="ECO:0007829|PDB:5JW9"
FT HELIX 607..636
FT /evidence="ECO:0007829|PDB:5JW9"
SQ SEQUENCE 640 AA; 72324 MW; 96D6228AF868E6C9 CRC64;
MAAGGTGGLR EEQRYGLSCG RLGQDNITVL HVKLTETAIR ALETYQSHKN LIPFRPSIQF
QGLHGLVKIP KNDPLNEVHN FNFYLSNVGK DNPQGSFDCI QQTFSSSGAS QLNCLGFIQD
KITVCATNDS YQMTRERMTQ AEEESRNRST KVIKPGGPYV GKRVQIRKAP QAVSDTVPER
KRSTPMNPAN TIRKTHSSST ISQRPYRDRV IHLLALKAYK KPELLARLQK DGVNQKDKNS
LGAILQQVAN LNSKDLSYTL KDYVFKELQR DWPGYSEIDR RSLESVLSRK LNPSQNAAGT
SRSESPVCSS RDAVSSPQKR LLDSEFIDPL MNKKARISHL TNRVPPTLNG HLNPTSEKSA
AGLPLPPAAA AIPTPPPLPS TYLPISHPPQ IVNSNSNSPS TPEGRGTQDL PVDSFSQNDS
IYEDQQDKYT SRTSLETLPP GSVLLKCPKP MEENHSMSHK KSKKKSKKHK EKDQIKKHDI
ETIEEKEEDL KREEEIAKLN NSSPNSSGGV KEDCTASMEP SAIELPDYLI KYIAIVSYEQ
RQNYKDDFNA EYDEYRALHA RMETVARRFI KLDAQRKRLS PGSKEYQNVH EEVLQEYQKI
KQSSPNYHEE KYRCEYLHNK LAHIKRLIGE FDQQQAESWS
