ID KTNB1_HUMAN Reviewed; 655 AA.
AC Q9BVA0; A6NCG6; O60620;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 187.
DE RecName: Full=Katanin p80 WD40 repeat-containing subunit B1 {ECO:0000255|HAMAP-Rule:MF_03022};
DE Short=Katanin p80 subunit B1 {ECO:0000255|HAMAP-Rule:MF_03022};
DE AltName: Full=p80 katanin {ECO:0000255|HAMAP-Rule:MF_03022};
GN Name=KATNB1 {ECO:0000255|HAMAP-Rule:MF_03022};
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], AND SUBCELLULAR LOCATION.
RX PubMed=9568719; DOI=10.1016/s0092-8674(00)81578-0;
RA Hartman J.J., Mahr J., McNally K., Okawa K., Iwamatsu A., Thomas S.,
RA Cheesman S., Heuser J., Vale R.D., McNally F.J.;
RT "Katanin, a microtubule-severing protein, is a novel AAA ATPase that
RT targets to the centrosome using a WD40-containing subunit.";
RL Cell 93:277-287(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=9658175; DOI=10.1091/mbc.9.7.1847;
RA McNally F.J., Thomas S.;
RT "Katanin is responsible for the M-phase microtubule-severing activity in
RT Xenopus eggs.";
RL Mol. Biol. Cell 9:1847-1861(1998).
RN [8]
RP FUNCTION, AND INTERACTION WITH KATNA1.
RX PubMed=10751153; DOI=10.1242/jcs.113.9.1623;
RA McNally K.P., Bazirgan O.A., McNally F.J.;
RT "Two domains of p80 katanin regulate microtubule severing and spindle pole
RT targeting by p60 katanin.";
RL J. Cell Sci. 113:1623-1633(2000).
RN [9]
RP INTERACTION WITH NDEL1, AND SUBCELLULAR LOCATION.
RX PubMed=16203747; DOI=10.1093/hmg/ddi339;
RA Toyo-Oka K., Sasaki S., Yano Y., Mori D., Kobayashi T., Toyoshima Y.Y.,
RA Tokuoka S.M., Ishii S., Shimizu T., Muramatsu M., Hiraiwa N., Yoshiki A.,
RA Wynshaw-Boris A., Hirotsune S.;
RT "Recruitment of katanin p60 by phosphorylated NDEL1, an LIS1 interacting
RT protein, is essential for mitotic cell division and neuronal migration.";
RL Hum. Mol. Genet. 14:3113-3128(2005).
RN [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-395, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [12]
RP INTERACTION WITH CAMSAP2 AND CAMSAP3.
RX PubMed=24486153; DOI=10.1016/j.devcel.2014.01.001;
RA Jiang K., Hua S., Mohan R., Grigoriev I., Yau K.W., Liu Q., Katrukha E.A.,
RA Altelaar A.F., Heck A.J., Hoogenraad C.C., Akhmanova A.;
RT "Microtubule minus-end stabilization by polymerization-driven CAMSAP
RT deposition.";
RL Dev. Cell 28:295-309(2014).
RN [13]
RP INVOLVEMENT IN LIS6, VARIANTS LIS6 LEU-535 AND ARG-540, AND
RP CHARACTERIZATION OF VARIANT LIS6 LEU-535.
RX PubMed=25521378; DOI=10.1016/j.neuron.2014.12.014;
RA Mishra-Gorur K., Caglayan A.O., Schaffer A.E., Chabu C., Henegariu O.,
RA Vonhoff F., Akguemues G.T., Nishimura S., Han W., Tu S., Baran B.,
RA Guemues H., Dilber C., Zaki M.S., Hossni H.A., Riviere J.B., Kayserili H.,
RA Spencer E.G., Rosti R.O., Schroth J., Per H., Caglar C., Caglar C.,
RA Doelen D., Baranoski J.F., Kumandas S., Minja F.J., Erson-Omay E.Z.,
RA Mane S.M., Lifton R.P., Xu T., Keshishian H., Dobyns W.B., Chi N.C.,
RA Sestan N., Louvi A., Bilguevar K., Yasuno K., Gleeson J.G., Guenel M.;
RT "Mutations in KATNB1 cause complex cerebral malformations by disrupting
RT asymmetrically dividing neural progenitors.";
RL Neuron 84:1226-1239(2014).
RN [14]
RP INTERACTION WITH KATNA1 AND KATNAL1, AND SUBCELLULAR LOCATION.
RX PubMed=26929214; DOI=10.1074/mcp.m115.056465;
RA Cheung K., Senese S., Kuang J., Bui N., Ongpipattanakul C., Gholkar A.,
RA Cohn W., Capri J., Whitelegge J.P., Torres J.Z.;
RT "Proteomic analysis of the mammalian Katanin family of microtubule-severing
RT enzymes defines Katanin p80 subunit B-like 1 (KATNBL1) as a regulator of
RT mammalian Katanin microtubule-severing.";
RL Mol. Cell. Proteomics 15:1658-1669(2016).
RN [15]
RP VARIANT LIS6 TRP-33.
RX PubMed=25521379; DOI=10.1016/j.neuron.2014.12.017;
RA Hu W.F., Pomp O., Ben-Omran T., Kodani A., Henke K., Mochida G.H., Yu T.W.,
RA Woodworth M.B., Bonnard C., Raj G.S., Tan T.T., Hamamy H., Masri A.,
RA Shboul M., Al Saffar M., Partlow J.N., Al-Dosari M., Alazami A.,
RA Alowain M., Alkuraya F.S., Reiter J.F., Harris M.P., Reversade B.,
RA Walsh C.A.;
RT "Katanin p80 regulates human cortical development by limiting centriole and
RT cilia number.";
RL Neuron 84:1240-1257(2014).
CC -!- FUNCTION: Participates in a complex which severs microtubules in an
CC ATP-dependent manner. May act to target the enzymatic subunit of this
CC complex to sites of action such as the centrosome. Microtubule severing
CC may promote rapid reorganization of cellular microtubule arrays and the
CC release of microtubules from the centrosome following nucleation.
CC Microtubule release from the mitotic spindle poles may allow
CC depolymerization of the microtubule end proximal to the spindle pole,
CC leading to poleward microtubule flux and poleward motion of chromosome.
CC Microtubule release within the cell body of neurons may be required for
CC their transport into neuronal processes by microtubule-dependent motor
CC proteins. This transport is required for axonal growth.
CC {ECO:0000255|HAMAP-Rule:MF_03022, ECO:0000269|PubMed:10751153}.
CC -!- SUBUNIT: Interacts with PAFAH1B1 (By similarity). Interacts with KATNA1
CC (PubMed:10751153, PubMed:26929214). This interaction enhances the
CC microtubule binding and severing activity of KATNA1 and also targets
CC this activity to the centrosome (PubMed:10751153). This interaction is
CC weakly competed by KATNBL1 which has a lower affinity for it
CC (PubMed:26929214). Interacts with ASPM; the katanin complex formation
CC KATNA1:KATNB1 is required for the association of ASPM (By similarity).
CC Interacts with dynein, microtubules and NDEL1 (PubMed:16203747).
CC Interacts with KATNAL1; this interaction is weakly competed by KATNBL1
CC which has a lower affinity for it (PubMed:26929214). Interacts with
CC CAMSAP2 and CAMSAP3; leading to regulate the length of CAMSAP-decorated
CC microtubule stretches (PubMed:24486153). {ECO:0000250|UniProtKB:Q8BG40,
CC ECO:0000269|PubMed:10751153, ECO:0000269|PubMed:16203747,
CC ECO:0000269|PubMed:24486153, ECO:0000269|PubMed:26929214}.
CC -!- INTERACTION:
CC Q9BVA0; O75449: KATNA1; NbExp=10; IntAct=EBI-11147603, EBI-1048692;
CC Q9BVA0; Q9BW62: KATNAL1; NbExp=8; IntAct=EBI-11147603, EBI-743591;
CC Q9BVA0; P40337-2: VHL; NbExp=3; IntAct=EBI-11147603, EBI-12157263;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26929214,
CC ECO:0000269|PubMed:9658175}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:16203747,
CC ECO:0000269|PubMed:9568719}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000269|PubMed:16203747, ECO:0000269|PubMed:26929214,
CC ECO:0000269|PubMed:9658175}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9568719, ECO:0000269|PubMed:9658175}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:26929214}. Note=Predominantly
CC cytoplasmic. Localized to the interphase centrosome and mitotic spindle
CC poles (PubMed:9658175). Localizes within the cytoplasm, partially
CC overlapping with microtubules, in interphase and to the mitotic spindle
CC and spindle poles during mitosis (PubMed:26929214).
CC {ECO:0000269|PubMed:26929214, ECO:0000269|PubMed:9658175}.
CC -!- DISEASE: Lissencephaly 6, with microcephaly (LIS6) [MIM:616212]: A form
CC of lissencephaly, a disorder of cortical development characterized by
CC agyria or pachygyria and disorganization of the clear neuronal
CC lamination of normal six-layered cortex. LIS6 features include
CC hypoplasia of the corpus callosum, severe microcephaly and
CC developmental delay. {ECO:0000269|PubMed:25521378,
CC ECO:0000269|PubMed:25521379}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the WD repeat KATNB1 family. {ECO:0000255|HAMAP-
CC Rule:MF_03022}.
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DR EMBL; AF052432; AAC09328.1; -; mRNA.
DR EMBL; BT007022; AAP35668.1; -; mRNA.
DR EMBL; CR456762; CAG33043.1; -; mRNA.
DR EMBL; AC092118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471092; EAW82951.1; -; Genomic_DNA.
DR EMBL; BC001353; AAH01353.1; -; mRNA.
DR CCDS; CCDS10788.1; -.
DR RefSeq; NP_005877.2; NM_005886.2.
DR RefSeq; XP_016878352.1; XM_017022863.1.
DR RefSeq; XP_016878353.1; XM_017022864.1.
DR AlphaFoldDB; Q9BVA0; -.
DR SMR; Q9BVA0; -.
DR BioGRID; 115588; 66.
DR ComplexPortal; CPX-6365; Katanin complex, KATNA1-KATNB1 variant.
DR ComplexPortal; CPX-6367; Katanin complex, KATNAL2-KATNB1 variant.
DR ComplexPortal; CPX-6382; Katanin complex, KATNAL1-KATNB1 variant.
DR CORUM; Q9BVA0; -.
DR IntAct; Q9BVA0; 44.
DR MINT; Q9BVA0; -.
DR STRING; 9606.ENSP00000368982; -.
DR ChEMBL; CHEMBL3879844; -.
DR GlyCosmos; Q9BVA0; 1 site, 1 glycan.
DR GlyGen; Q9BVA0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BVA0; -.
DR PhosphoSitePlus; Q9BVA0; -.
DR BioMuta; KATNB1; -.
DR DMDM; 60390213; -.
DR EPD; Q9BVA0; -.
DR jPOST; Q9BVA0; -.
DR MassIVE; Q9BVA0; -.
DR MaxQB; Q9BVA0; -.
DR PaxDb; 9606-ENSP00000368982; -.
DR PeptideAtlas; Q9BVA0; -.
DR ProteomicsDB; 79189; -.
DR Pumba; Q9BVA0; -.
DR Antibodypedia; 28973; 362 antibodies from 25 providers.
DR DNASU; 10300; -.
DR Ensembl; ENST00000379661.8; ENSP00000368982.3; ENSG00000140854.13.
DR GeneID; 10300; -.
DR KEGG; hsa:10300; -.
DR MANE-Select; ENST00000379661.8; ENSP00000368982.3; NM_005886.3; NP_005877.2.
DR UCSC; uc002eml.2; human.
DR AGR; HGNC:6217; -.
DR CTD; 10300; -.
DR DisGeNET; 10300; -.
DR GeneCards; KATNB1; -.
DR HGNC; HGNC:6217; KATNB1.
DR HPA; ENSG00000140854; Low tissue specificity.
DR MalaCards; KATNB1; -.
DR MIM; 602703; gene.
DR MIM; 616212; phenotype.
DR neXtProt; NX_Q9BVA0; -.
DR OpenTargets; ENSG00000140854; -.
DR Orphanet; 89844; Lissencephaly syndrome, Norman-Roberts type.
DR PharmGKB; PA30018; -.
DR VEuPathDB; HostDB:ENSG00000140854; -.
DR eggNOG; KOG0267; Eukaryota.
DR GeneTree; ENSGT00940000157918; -.
DR HOGENOM; CLU_007811_0_0_1; -.
DR InParanoid; Q9BVA0; -.
DR OMA; TYADIPN; -.
DR OrthoDB; 1330549at2759; -.
DR PhylomeDB; Q9BVA0; -.
DR TreeFam; TF332359; -.
DR PathwayCommons; Q9BVA0; -.
DR SignaLink; Q9BVA0; -.
DR SIGNOR; Q9BVA0; -.
DR BioGRID-ORCS; 10300; 350 hits in 1164 CRISPR screens.
DR ChiTaRS; KATNB1; human.
DR GeneWiki; KATNB1; -.
DR GenomeRNAi; 10300; -.
DR Pharos; Q9BVA0; Tbio.
DR PRO; PR:Q9BVA0; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9BVA0; Protein.
DR Bgee; ENSG00000140854; Expressed in middle temporal gyrus and 193 other cell types or tissues.
DR ExpressionAtlas; Q9BVA0; baseline and differential.
DR Genevisible; Q9BVA0; HS.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0008352; C:katanin complex; IDA:MGI.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0060590; F:ATPase regulator activity; IDA:GO_Central.
DR GO; GO:0070840; F:dynein complex binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; NAS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; NAS:ComplexPortal.
DR GO; GO:0007019; P:microtubule depolymerization; IBA:GO_Central.
DR GO; GO:0051013; P:microtubule severing; IEA:UniProtKB-UniRule.
DR GO; GO:0007079; P:mitotic chromosome movement towards spindle pole; IEA:UniProtKB-UniRule.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0031117; P:positive regulation of microtubule depolymerization; IMP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0006605; P:protein targeting; NAS:UniProtKB.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR HAMAP; MF_03022; Katanin_p80_B1; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR028021; Katanin_C-terminal.
DR InterPro; IPR026962; KTNB1.
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; PTHR19845; KATANIN P80 SUBUNIT; 1.
DR PANTHER; PTHR19845:SF0; KATANIN P80 WD40 REPEAT-CONTAINING SUBUNIT B1; 1.
DR Pfam; PF13925; Katanin_con80; 1.
DR Pfam; PF00400; WD40; 6.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 5.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Disease variant;
KW Lissencephaly; Microtubule; Mitosis; Phosphoprotein; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..655
FT /note="Katanin p80 WD40 repeat-containing subunit B1"
FT /id="PRO_0000051049"
FT REPEAT 18..58
FT /note="WD 1"
FT REPEAT 61..100
FT /note="WD 2"
FT REPEAT 103..142
FT /note="WD 3"
FT REPEAT 145..184
FT /note="WD 4"
FT REPEAT 187..226
FT /note="WD 5"
FT REPEAT 229..269
FT /note="WD 6"
FT REGION 1..300
FT /note="Interaction with centrosomes"
FT REGION 1..284
FT /note="Interaction with dynein"
FT /evidence="ECO:0000250"
FT REGION 285..434
FT /note="Interaction with PAFAH1B1"
FT /evidence="ECO:0000250"
FT REGION 311..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..655
FT /note="Interaction with KATNA1 and NDEL1"
FT /evidence="ECO:0000250"
FT COMPBIAS 351..378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 395
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 33
FT /note="G -> W (in LIS6; dbSNP:rs730880259)"
FT /evidence="ECO:0000269|PubMed:25521379"
FT /id="VAR_073319"
FT VARIANT 181
FT /note="M -> V (in dbSNP:rs60158050)"
FT /id="VAR_062099"
FT VARIANT 535
FT /note="S -> L (in LIS6; causes reduced interaction with
FT KATNA1 and NDEL1; dbSNP:rs730880257)"
FT /evidence="ECO:0000269|PubMed:25521378"
FT /id="VAR_073320"
FT VARIANT 540
FT /note="L -> R (in LIS6; dbSNP:rs730880258)"
FT /evidence="ECO:0000269|PubMed:25521378"
FT /id="VAR_073321"
FT CONFLICT 104
FT /note="H -> L (in Ref. 1; AAC09328)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="R -> G (in Ref. 1; AAC09328)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="C -> R (in Ref. 1; AAC09328)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 655 AA; 72334 MW; 411903E306B6EC16 CRC64;
MATPVVTKTA WKLQEIVAHA SNVSSLVLGK ASGRLLATGG DDCRVNLWSI NKPNCIMSLT
GHTSPVESVR LNTPEELIVA GSQSGSIRVW DLEAAKILRT LMGHKANICS LDFHPYGEFV
ASGSQDTNIK LWDIRRKGCV FRYRGHSQAV RCLRFSPDGK WLASAADDHT VKLWDLTAGK
MMSEFPGHTG PVNVVEFHPN EYLLASGSSD RTIRFWDLEK FQVVSCIEGE PGPVRSVLFN
PDGCCLYSGC QDSLRVYGWE PERCFDVVLV NWGKVADLAI CNDQLIGVAF SQSNVSSYVV
DLTRVTRTGT VARDPVQDHR PLAQPLPNPS APLRRIYERP STTCSKPQRV KQNSESERRS
PSSEDDRDER ESRAEIQNAE DYNEIFQPKN SISRTPPRRS EPFPAPPEDD AATAKEAAKP
SPAMDVQFPV PNLEVLPRPP VVASTPAPKA EPAIIPATRN EPIGLKASDF LPAVKIPQQA
ELVDEDAMSQ IRKGHDTMCV VLTSRHKNLD TVRAVWTMGD IKTSVDSAVA INDLSVVVDL
LNIVNQKASL WKLDLCTTVL PQIEKLLQSK YESYVQTGCT SLKLILQRFL PLITDMLAAP
PSVGVDISRE ERLHKCRLCY KQLKSISGLV KSKSGLSGRH GSTFRELHLL MASLD
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