RAVR1_HUMAN
ID RAVR1_HUMAN Reviewed; 606 AA.
AC Q8IY67; A6NMU4; Q8IY60; Q8TF24;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Ribonucleoprotein PTB-binding 1;
DE AltName: Full=Protein raver-1;
GN Name=RAVER1; Synonyms=KIAA1978;
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=11853319; DOI=10.1093/dnares/8.6.319;
RA Nagase T., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XXII. The
RT complete sequences of 50 new cDNA clones which code for large proteins.";
RL DNA Res. 8:319-327(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 182-606 (ISOFORM 2).
RC TISSUE=Cervix, 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [5]
RP IDENTIFICATION BY 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-463, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-463, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-567 (ISOFORM 2), AND IDENTIFICATION BY MASS
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-488 AND SER-567 (ISOFORM 2),
RP AND 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 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=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-14, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-463, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-14; THR-463 AND SER-474, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT THR-488 AND SER-567 (ISOFORM 2), CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-14 AND THR-463, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-567 (ISOFORM 2), CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-14 AND THR-463, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-463, AND IDENTIFICATION BY
RP 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: Cooperates with PTBP1 to modulate regulated alternative
CC splicing events. Promotes exon skipping. Cooperates with PTBP1 to
CC modulate switching between mutually exclusive exons during maturation
CC of the TPM1 pre-mRNA (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PTBP1, RAVER2, VCL and ACTN1. Part of a complex
CC containing RAVER1, VCL and ACTN1 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8IY67; O75791: GRAP2; NbExp=3; IntAct=EBI-2105155, EBI-740418;
CC Q8IY67-1; P18206-2: VCL; NbExp=3; IntAct=EBI-15788272, EBI-11027067;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Nuclear, in perinucleolar structures. Shuttles between nucleus and
CC cytoplasm. Cytoplasm, at focal contacts and cell-cell contacts.
CC Associated with myotubes during muscle differentiation (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IY67-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IY67-2; Sequence=VSP_017035, VSP_017036;
CC Name=3;
CC IsoId=Q8IY67-3; Sequence=VSP_040968, VSP_040969;
CC -!- MISCELLANEOUS: [Isoform 3]: 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 -!- SEQUENCE CAUTION:
CC Sequence=AAH37565.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=BAB85564.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AB075858; BAB85564.1; ALT_SEQ; mRNA.
DR EMBL; AC011511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037428; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC037565; AAH37565.1; ALT_SEQ; mRNA.
DR CCDS; CCDS45960.1; -. [Q8IY67-2]
DR RefSeq; NP_597709.2; NM_133452.2.
DR PDB; 3H2U; X-ray; 2.75 A; B/D=39-321.
DR PDB; 3H2V; X-ray; 2.90 A; E/F/G/H=59-130.
DR PDB; 3SMZ; X-ray; 1.99 A; A=39-320.
DR PDB; 3VF0; X-ray; 2.54 A; B=39-321.
DR PDBsum; 3H2U; -.
DR PDBsum; 3H2V; -.
DR PDBsum; 3SMZ; -.
DR PDBsum; 3VF0; -.
DR AlphaFoldDB; Q8IY67; -.
DR SMR; Q8IY67; -.
DR BioGRID; 125936; 151.
DR DIP; DIP-46973N; -.
DR IntAct; Q8IY67; 18.
DR MINT; Q8IY67; -.
DR GlyGen; Q8IY67; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IY67; -.
DR PhosphoSitePlus; Q8IY67; -.
DR BioMuta; RAVER1; -.
DR DMDM; 74759693; -.
DR CPTAC; CPTAC-997; -.
DR EPD; Q8IY67; -.
DR jPOST; Q8IY67; -.
DR MassIVE; Q8IY67; -.
DR MaxQB; Q8IY67; -.
DR PaxDb; Q8IY67; -.
DR PeptideAtlas; Q8IY67; -.
DR PRIDE; Q8IY67; -.
DR ProteomicsDB; 71118; -. [Q8IY67-1]
DR ProteomicsDB; 71119; -. [Q8IY67-2]
DR ProteomicsDB; 71120; -. [Q8IY67-3]
DR Antibodypedia; 6733; 114 antibodies from 18 providers.
DR DNASU; 125950; -.
DR Ensembl; ENST00000615032.4; ENSP00000479520.1; ENSG00000161847.14. [Q8IY67-1]
DR GeneID; 125950; -.
DR KEGG; hsa:125950; -.
DR UCSC; uc060tgw.1; human. [Q8IY67-1]
DR CTD; 125950; -.
DR DisGeNET; 125950; -.
DR GeneCards; RAVER1; -.
DR HGNC; HGNC:30296; RAVER1.
DR HPA; ENSG00000161847; Low tissue specificity.
DR MIM; 609950; gene.
DR neXtProt; NX_Q8IY67; -.
DR OpenTargets; ENSG00000161847; -.
DR PharmGKB; PA144596390; -.
DR VEuPathDB; HostDB:ENSG00000161847; -.
DR eggNOG; KOG0148; Eukaryota.
DR GeneTree; ENSGT00940000160550; -.
DR InParanoid; Q8IY67; -.
DR OrthoDB; 249777at2759; -.
DR PhylomeDB; Q8IY67; -.
DR PathwayCommons; Q8IY67; -.
DR SignaLink; Q8IY67; -.
DR BioGRID-ORCS; 125950; 21 hits in 1073 CRISPR screens.
DR ChiTaRS; RAVER1; human.
DR EvolutionaryTrace; Q8IY67; -.
DR GeneWiki; RAVER1; -.
DR GenomeRNAi; 125950; -.
DR Pharos; Q8IY67; Tbio.
DR PRO; PR:Q8IY67; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8IY67; protein.
DR Bgee; ENSG00000161847; Expressed in granulocyte and 99 other tissues.
DR ExpressionAtlas; Q8IY67; baseline and differential.
DR Genevisible; Q8IY67; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR CDD; cd12663; RRM1_RAVER1; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034635; RAVER1.
DR InterPro; IPR034633; RAVER1_RRM1.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR23189:SF46; PTHR23189:SF46; 2.
DR Pfam; PF00076; RRM_1; 3.
DR SMART; SM00360; RRM; 3.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT CHAIN 2..606
FT /note="Ribonucleoprotein PTB-binding 1"
FT /id="PRO_0000081487"
FT DOMAIN 59..130
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 132..210
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 221..299
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..395
FT /note="Interaction with PTBP1"
FT /evidence="ECO:0000250"
FT REGION 391..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 45..60
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 22..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..442
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 463
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 474
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CW46"
FT VAR_SEQ 74..75
FT /note="EV -> PS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11853319"
FT /id="VSP_040968"
FT VAR_SEQ 76..606
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11853319"
FT /id="VSP_040969"
FT VAR_SEQ 477
FT /note="R -> RGLQKDSGPLPTPPGVSLLGEPPKDYRIPLNPYLNLHSLLPASNLAG
FT KEARGWGGAGRSRRPAEGPLTNPPAPGGGSSSSKAFQLKSRLLSPLSSARLPPEPGLSD
FT SYSFDYPSDMGPRRLFSHPREPALGPHGPSRHKMSPPPSGFGERSSGGSGG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017035"
FT VAR_SEQ 536..606
FT /note="VRAGGGDMQGWEAPAPQRPLTRPALPSVSRPHWAARNAALPTCCPRPSPAQK
FT AAMWASTPRASAATTRTPT -> TPLGGQKRSFAHLLPSPEPSPEGSYVGQHSQGLGGH
FT YADSYLKRKRIF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017036"
FT HELIX 41..56
FT /evidence="ECO:0007829|PDB:3SMZ"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:3SMZ"
FT HELIX 72..78
FT /evidence="ECO:0007829|PDB:3SMZ"
FT TURN 79..81
FT /evidence="ECO:0007829|PDB:3SMZ"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:3SMZ"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:3SMZ"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:3SMZ"
FT HELIX 103..113
FT /evidence="ECO:0007829|PDB:3SMZ"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:3SMZ"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:3SMZ"
FT HELIX 145..152
FT /evidence="ECO:0007829|PDB:3SMZ"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:3SMZ"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:3SMZ"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:3SMZ"
FT STRAND 172..182
FT /evidence="ECO:0007829|PDB:3SMZ"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:3SMZ"
FT STRAND 204..207
FT /evidence="ECO:0007829|PDB:3SMZ"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:3SMZ"
FT TURN 215..218
FT /evidence="ECO:0007829|PDB:3SMZ"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:3SMZ"
FT HELIX 235..241
FT /evidence="ECO:0007829|PDB:3SMZ"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:3SMZ"
FT STRAND 249..255
FT /evidence="ECO:0007829|PDB:3SMZ"
FT STRAND 261..268
FT /evidence="ECO:0007829|PDB:3SMZ"
FT HELIX 272..282
FT /evidence="ECO:0007829|PDB:3SMZ"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:3SMZ"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:3SMZ"
FT HELIX 303..313
FT /evidence="ECO:0007829|PDB:3SMZ"
FT MOD_RES Q8IY67-2:488
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES Q8IY67-2:567
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
SQ SEQUENCE 606 AA; 63877 MW; 09FA9935A6281B42 CRC64;
MAADVSVTHR PPLSPKSGAE VEAGDAAERR APEEELPPLD PEEIRKRLEH TERQFRNRRK
ILIRGLPGDV TNQEVHDLLS DYELKYCFVD KYKGTAFVTL LNGEQAEAAI NAFHQSRLRE
RELSVQLQPT DALLCVANLP PSLTQQQFEE LVRPFGSLER CFLVYSERTG QSKGYGFAEY
MKKDSAARAK SDLLGKPLGP RTLYVHWTDA GQLTPALLHS RCLCVDRLPP GFNDVDALCR
ALSAVHSPTF CQLACGQDGQ LKGFAVLEYE TAEMAEEAQQ QADGLSLGGS HLRVSFCAPG
PPGRSMLAAL IAAQATALNR GKGLLPEPNI LQLLNNLGPS ASLQLLLNPL LHGSAGGKQG
LLGAPPAMPL LNGPALSTAL LQLALQTQGQ KKPGILGDSP LGALQPGAQP ANPLLGELPA
GGGLPPELPP RRGKPPPLLP SVLGPAGGDR EALGLGPPAA QLTPPPAPVG LRGSGLRGPL
SHFYSGSPTS YFTSGLQAGL KQSHLSKAIG SSPLGSGEGL LGLSPGPNGH SHLLKVRAGG
GDMQGWEAPA PQRPLTRPAL PSVSRPHWAA RNAALPTCCP RPSPAQKAAM WASTPRASAA
TTRTPT
