ID BRWD3_HUMAN Reviewed; 1802 AA. AC Q6RI45; C9IZ39; C9J3F3; Q2T9J6; Q5JRN1; Q6RI37; Q6RI42; Q6RI44; Q8N916; DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 2. DT 24-JAN-2024, entry version 155. DE RecName: Full=Bromodomain and WD repeat-containing protein 3; GN Name=BRWD3; 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] (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY, RP CHROMOSOMAL TRANSLOCATION WITH ARHGAP20, AND VARIANT ARG-1288. RX PubMed=15543602; DOI=10.1002/gcc.20131; RA Kalla C., Nentwich H., Schlotter M., Mertens D., Wildenberger K., RA Doehner H., Stilgenbauer S., Lichter P.; RT "Translocation t(X;11)(q13;q23) in B-cell chronic lymphocytic leukemia RT disrupts two novel genes."; RL Genes Chromosomes Cancer 42:128-143(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-768 (ISOFORM 1). RC TISSUE=Lymph; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 623-1802 (ISOFORM 5), AND VARIANT RP ARG-1288. 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 [5] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703 AND SER-1577, AND RP IDENTIFICATION BY 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 [6] RP FUNCTION. RX PubMed=21834987; DOI=10.1186/1741-7007-9-54; RA Bai S.W., Herrera-Abreu M.T., Rohn J.L., Racine V., Tajadura V., RA Suryavanshi N., Bechtel S., Wiemann S., Baum B., Ridley A.J.; RT "Identification and characterization of a set of conserved and new RT regulators of cytoskeletal organisation, cell morphology and migration."; RL BMC Biol. 9:54-54(2011). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1579, 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-693 AND SER-1579, 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 [9] RP VARIANT XLID93 GLU-1596. RX PubMed=17668385; DOI=10.1086/520677; RA Field M., Tarpey P.S., Smith R., Edkins S., O'Meara S., Stevens C., RA Tofts C., Teague J., Butler A., Dicks E., Barthorpe S., Buck G., Cole J., RA Gray K., Halliday K., Hills K., Jenkinson A., Jones D., Menzies A., RA Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., RA Varian J., West S., Widaa S., Mallya U., Wooster R., Moon J., Luo Y., RA Hughes H., Shaw M., Friend K.L., Corbett M., Turner G., Partington M., RA Mulley J., Bobrow M., Schwartz C., Stevenson R., Gecz J., Stratton M.R., RA Futreal P.A., Raymond F.L.; RT "Mutations in the BRWD3 gene cause X-linked mental retardation associated RT with macrocephaly."; RL Am. J. Hum. Genet. 81:367-374(2007). CC -!- FUNCTION: Plays a role in the regulation of cell morphology and CC cytoskeletal organization. Required in the control of cell shape. CC {ECO:0000269|PubMed:21834987}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=BRWD3-A; CC IsoId=Q6RI45-1; Sequence=Displayed; CC Name=2; Synonyms=BRWD3-B; CC IsoId=Q6RI45-2; Sequence=VSP_024305; CC Name=3; Synonyms=BRWD3-C, BRWD3-D, BRWD3-E, BRWD3-F, BRWD3-G, BRWD3-L, CC BRWD3-M, BRWD3-N, BRWD3-O; CC IsoId=Q6RI45-3; Sequence=VSP_024303; CC Name=4; Synonyms=BRWD3-H, BRWD3-I, BRWD3-K, BRWD3-P; CC IsoId=Q6RI45-4; Sequence=VSP_024304; CC Name=5; CC IsoId=Q6RI45-5; Sequence=VSP_024306, VSP_024307; CC -!- TISSUE SPECIFICITY: Found in most adult tissues. Down-regulated in a CC majority of the B-CLL cases examined. {ECO:0000269|PubMed:15543602}. CC -!- DEVELOPMENTAL STAGE: Expressed in fetal liver. CC -!- DISEASE: Note=A chromosomal aberration involving BRWD3 can be found in CC patients with B-cell chronic lymphocytic leukemia (B-CLL). CC Translocation t(X;11)(q21;q23) with ARHGAP20 does not result in fusion CC transcripts but disrupts both genes. CC -!- DISEASE: Intellectual developmental disorder, X-linked 93 (XLID93) CC [MIM:300659]: A disorder characterized by significantly below average CC general intellectual functioning associated with impairments in CC adaptive behavior and manifested during the developmental period. CC Intellectual deficiency is the only primary symptom of non-syndromic X- CC linked forms, while syndromic forms present with associated physical, CC neurological and/or psychiatric manifestations. XLID93 is associated CC with macrocephaly. {ECO:0000269|PubMed:17668385}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- CAUTION: The translocation involving this gene was originally published CC as t(X;11)(q13;23), but BRWD3 is localized to Xq21 and not to Xq13. CC {ECO:0000305|PubMed:15543602}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC04641.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42978/BRWD3"; 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; AY497046; AAS45471.1; -; mRNA. DR EMBL; AY497047; AAS45472.1; -; mRNA. DR EMBL; AY497048; AAS45473.1; -; mRNA. DR EMBL; AY497049; AAS45474.1; -; mRNA. DR EMBL; AY497050; AAS45475.1; -; mRNA. DR EMBL; AY497051; AAS45476.1; -; mRNA. DR EMBL; AY497052; AAS45477.1; -; mRNA. DR EMBL; AY497053; AAS45478.1; -; mRNA. DR EMBL; AY497054; AAS45479.1; -; mRNA. DR EMBL; AY497055; AAS45480.1; -; mRNA. DR EMBL; AY497056; AAS45481.1; -; mRNA. DR EMBL; AY497057; AAS45482.1; -; mRNA. DR EMBL; AY497058; AAS45483.1; -; mRNA. DR EMBL; AY497059; AAS45484.1; -; mRNA. DR EMBL; AY497060; AAS45485.1; -; mRNA. DR EMBL; AL512504; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL590031; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL669934; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC111490; AAI11491.1; -; mRNA. DR EMBL; AK095887; BAC04641.1; ALT_INIT; mRNA. DR CCDS; CCDS14447.1; -. [Q6RI45-1] DR RefSeq; NP_694984.4; NM_153252.4. [Q6RI45-1] DR RefSeq; XP_016884873.1; XM_017029384.1. [Q6RI45-3] DR AlphaFoldDB; Q6RI45; -. DR SMR; Q6RI45; -. DR BioGRID; 129012; 45. DR IntAct; Q6RI45; 9. DR STRING; 9606.ENSP00000362372; -. DR ChEMBL; CHEMBL3769296; -. DR GlyGen; Q6RI45; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q6RI45; -. DR PhosphoSitePlus; Q6RI45; -. DR BioMuta; BRWD3; -. DR DMDM; 313104082; -. DR EPD; Q6RI45; -. DR jPOST; Q6RI45; -. DR MassIVE; Q6RI45; -. DR MaxQB; Q6RI45; -. DR PaxDb; 9606-ENSP00000362372; -. DR PeptideAtlas; Q6RI45; -. DR ProteomicsDB; 67319; -. [Q6RI45-1] DR ProteomicsDB; 67320; -. [Q6RI45-2] DR ProteomicsDB; 67321; -. [Q6RI45-3] DR ProteomicsDB; 67322; -. [Q6RI45-4] DR ProteomicsDB; 67323; -. [Q6RI45-5] DR Pumba; Q6RI45; -. DR Antibodypedia; 537; 54 antibodies from 16 providers. DR DNASU; 254065; -. DR Ensembl; ENST00000373275.5; ENSP00000362372.4; ENSG00000165288.11. [Q6RI45-1] DR GeneID; 254065; -. DR KEGG; hsa:254065; -. DR MANE-Select; ENST00000373275.5; ENSP00000362372.4; NM_153252.5; NP_694984.5. DR UCSC; uc004edt.4; human. [Q6RI45-1] DR AGR; HGNC:17342; -. DR CTD; 254065; -. DR DisGeNET; 254065; -. DR GeneCards; BRWD3; -. DR HGNC; HGNC:17342; BRWD3. DR HPA; ENSG00000165288; Low tissue specificity. DR MalaCards; BRWD3; -. DR MIM; 300553; gene. DR MIM; 300659; phenotype. DR neXtProt; NX_Q6RI45; -. DR OpenTargets; ENSG00000165288; -. DR Orphanet; 323; NON RARE IN EUROPE: FG syndrome phenotypic spectrum. DR Orphanet; 528084; Non-specific syndromic intellectual disability. DR PharmGKB; PA134900775; -. DR VEuPathDB; HostDB:ENSG00000165288; -. DR eggNOG; KOG0644; Eukaryota. DR GeneTree; ENSGT00950000183107; -. DR HOGENOM; CLU_001108_0_0_1; -. DR InParanoid; Q6RI45; -. DR OMA; TVVTSWK; -. DR OrthoDB; 24713at2759; -. DR PhylomeDB; Q6RI45; -. DR TreeFam; TF324197; -. DR PathwayCommons; Q6RI45; -. DR SignaLink; Q6RI45; -. DR BioGRID-ORCS; 254065; 14 hits in 795 CRISPR screens. DR ChiTaRS; BRWD3; human. DR GeneWiki; BRWD3; -. DR GenomeRNAi; 254065; -. DR Pharos; Q6RI45; Tbio. DR PRO; PR:Q6RI45; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q6RI45; Protein. DR Bgee; ENSG00000165288; Expressed in tendon of biceps brachii and 171 other cell types or tissues. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0007010; P:cytoskeleton organization; IMP:UniProtKB. DR GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd05529; Bromo_WDR9_I_like; 1. DR CDD; cd00200; WD40; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 2. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR019775; WD40_repeat_CS. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR16266:SF25; BROMODOMAIN AND WD REPEAT-CONTAINING PROTEIN 3; 1. DR PANTHER; PTHR16266; WD REPEAT DOMAIN 9; 1. DR Pfam; PF00439; Bromodomain; 2. DR Pfam; PF00400; WD40; 7. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00297; BROMO; 2. DR SMART; SM00320; WD40; 8. DR SUPFAM; SSF47370; Bromodomain; 2. DR SUPFAM; SSF50978; WD40 repeat-like; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 2. DR PROSITE; PS00678; WD_REPEATS_1; 2. DR PROSITE; PS50082; WD_REPEATS_2; 5. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; Q6RI45; HS. PE 1: Evidence at protein level; KW Alternative splicing; Bromodomain; Chromosomal rearrangement; KW Disease variant; Intellectual disability; Phosphoprotein; KW Reference proteome; Repeat; WD repeat. FT CHAIN 1..1802 FT /note="Bromodomain and WD repeat-containing protein 3" FT /id="PRO_0000283089" FT REPEAT 170..209 FT /note="WD 1" FT REPEAT 213..251 FT /note="WD 2" FT REPEAT 255..297 FT /note="WD 3" FT REPEAT 307..347 FT /note="WD 4" FT REPEAT 353..393 FT /note="WD 5" FT REPEAT 400..452 FT /note="WD 6" FT REPEAT 456..495 FT /note="WD 7" FT REPEAT 502..542 FT /note="WD 8" FT DOMAIN 1158..1228 FT /note="Bromo 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT DOMAIN 1317..1412 FT /note="Bromo 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT REGION 768..910 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1262..1292 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1326..1361 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1438..1500 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1520..1725 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 800..819 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 842..881 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 882..900 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1338..1361 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1453..1468 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1476..1500 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1521..1535 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1536..1550 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1566..1603 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1604..1626 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1627..1648 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1649..1663 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1680..1694 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 693 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 703 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 885 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2AHJ4" FT MOD_RES 886 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2AHJ4" FT MOD_RES 1577 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 1579 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1763 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:A2AHJ4" FT VAR_SEQ 1..404 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15543602" FT /id="VSP_024303" FT VAR_SEQ 1..330 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15543602" FT /id="VSP_024304" FT VAR_SEQ 1..171 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15543602" FT /id="VSP_024305" FT VAR_SEQ 1385..1386 FT /note="GS -> DL (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_024306" FT VAR_SEQ 1387..1802 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_024307" FT VARIANT 1288 FT /note="K -> R (in dbSNP:rs3122407)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15543602" FT /id="VAR_031491" FT VARIANT 1596 FT /note="K -> E (in XLID93; uncertain significance; FT dbSNP:rs137853272)" FT /evidence="ECO:0000269|PubMed:17668385" FT /id="VAR_036940" SQ SEQUENCE 1802 AA; 203598 MW; 8AA086ABFDCBA2C9 CRC64; MAAAPTQIEA ELYYLIARFL QSGPCNKSAQ VLVQELEEHQ LIPRRLDWEG KEHRRSFEDL VAANAHIPPD YLLKICERIG PLLDKEIPQS VPGVQTLLGV GRQSLLRDAK DCKSTLWNGS AFAALHRGRP PELPVNYVKP PNVVNITSAR QLTGCSRFGH IFPSSAYQHI KMHKRILGHL SSVYCVAFDR SGRRIFTGSD DCLVKIWATD DGRLLATLRG HSAEISDMAV NYENTLIAAG SCDKVVRVWC LRTCAPVAVL QGHSASITSI QFCPSTKGTN RYLTSTGADG TICFWQWHVK TMKFRDRPVK FTERSRPGVQ ISCSSFSSGG MFITTGSTDH VIRIYYLGSE VPEKIAELES HTDKVVAVQF CNNGDSLRFV SGSRDGTARI WQYQQQEWKS IVLDMATKMT GNNLPSGEDK ITKLKVTMVA WDRYDTTVIT AVNNFLLKVW NSITGQLLHT LSGHDDEVFV LEAHPFDQRI ILSAGHDGNI FIWDLDRGTK IRNYFNMIEG QGHGAVFDCK FSPDGNHFAC TDSHGHLLLF GFGCSKYYEK IPDQMFFHTD YRPLIRDANN YVLDEQTQQA PHLMPPPFLV DVDGNPHPTK FQRLVPGREN CKDEQLIPQL GYVANGDGEV VEQVIGQQTN DQDESILDGI IRELQREQDL RLINEGDVPH LPVNRAYSVN GALRSPNMDI SSSPNIRLRR HSSQIEGVRQ MHNNAPRSQM ATERDLMAWS RRVVVNELNN GVSRVQEECR TAKGDIEISL YTVEKKKKPS YTTQRNDYEP SCGRSLRRTQ RKRQHTYQTR SNIEHNSQAS CQNSGVQEDS DSSSEEDETV GTSDASVEDP VVEWQSESSS SDSSSEYSDW TADAGINLQP PKRQTRQTTR KICSSSDEEN LKSLEERQKK PKQTRKKKGG LVSIAGEPNE EWFAPQWILD TIPRRSPFVP QMGDELIYFR QGHEAYVRAV RKSKIYSVNL QKQPWNKMDL REQEFVKIVG IKYEVGPPTL CCLKLAFLDP ISGKMTGESF SIKYHDMPDV IDFLVLHQFY NEAKERNWQI GDRFRSIIDD AWWFGTVESQ QPFQPEYPDS SFQCYSVHWD NNEREKMSPW DMEPIPEGTA FPDEVGAGVP VSQEELTALL YKPQEGEWGA HSRDEECERV IQGINHLLSL DFASPFAVPV DLSAYPLYCT VVAYPTDLNT IRRRLENRFY RRISALMWEV RYIEHNARTF NEPDSPIVKA AKIVTDVLLR FIGDQSCTDI LDTYNKIKAE ERNSTDAEED TEIVDLDSDG PGTSSGRKVK CRGRRQSLKC NPDAWKKQCK ELLSLIYERE DSEPFRQPAD LLSYPGHQEQ EGESSESVVP ERQQDSSLSE DYQDVIDTPV DFSTVKETLE AGNYGSPLEF YKDVRQIFNN SKAYTSNKKS RIYSMMLRLS ALFESHIKNI ISEYKSAIQS QKRRRPRYRK RLRSSSSSLS SSGAPSPKGK QKQMKLQPKN DQNTSVSHAR TSSPFSSPVS DAAEGLSLYL LDDEPDGPFS SSSFGGYSRS GNSHDPGKAK SFRNRVLPVK QDHSLDGPLT NGDGREPRTG IKRKLLSASE EDENMGGEDK EKKETKEKSH LSTSESGELG SSLSSESTCG SDSDSESTSR TDQDYVDGDH DYSKFIQTRP KRKLRKQHGN GKRNWKTRGT GGRGRWGRWG RWSRGGRGRG GRGRGSRGRG GGGTRGRGRG RGGRGASRGA TRAKRARIAD DEFDTMFSGR FSRLPRIKTR NQGRRTVLYN DDSDNDNFVS TEDPLNLGTS RSGRVRKMTE KARVSHLMGW NY //