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";
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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 Genevisible; Q6RI45; HS.
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.
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
//
