ID   ASPM_MOUSE              Reviewed;        3122 AA.
AC   Q8CJ27; A0A0G2JES1; B1ARM7; O88482; Q4G1G9; Q8BJI8; Q8BKT4;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Abnormal spindle-like microcephaly-associated protein homolog;
DE   AltName: Full=Calmodulin-binding protein Sha1;
DE            Short=Calmodulin-binding protein 1;
DE   AltName: Full=Spindle and hydroxyurea checkpoint abnormal protein;
GN   Name=Aspm; Synonyms=Calmbp1, Sha1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=Swiss Webster;
RX   PubMed=12355089; DOI=10.1038/ng995;
RA   Bond J., Roberts E., Mochida G.H., Hampshire D.J., Scott S., Askham J.M.,
RA   Springell K., Mahadevan M., Crow Y.J., Markham A.F., Walsh C.A.,
RA   Woods C.G.;
RT   "ASPM is a major determinant of cerebral cortical size.";
RL   Nat. Genet. 32:316-320(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RX   PubMed=15972725; DOI=10.1093/hmg/ddi220;
RA   Kouprina N., Pavlicek A., Collins N.K., Nakano M., Noskov V.N.,
RA   Ohzeki J.I., Mochida G.H., Risinger J.I., Goldsmith P., Gunsior M.,
RA   Solomon G., Gersch W., Kim J.H., Barrett J.C., Walsh C.A., Jurka J.,
RA   Masumoto H., Larionov V.;
RT   "The microcephaly ASPM gene is expressed in proliferating tissues and
RT   encodes for a mitotic spindle protein.";
RL   Hum. Mol. Genet. 14:2155-2165(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-612.
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2532-3122 (ISOFORM 1), FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=SWR/J;
RX   PubMed=9819352; DOI=10.1242/jcs.111.24.3609;
RA   Craig R., Norbury C.;
RT   "The novel murine calmodulin-binding protein Sha1 disrupts mitotic spindle
RT   and replication checkpoint functions in fission yeast.";
RL   J. Cell Sci. 111:3609-3619(1998).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=12351193; DOI=10.1016/s0925-4773(02)00253-8;
RA   Lueers G.H., Michels M., Schwaab U., Franz T.;
RT   "Murine calmodulin binding protein 1 (Calmbp1): tissue-specific expression
RT   during development and in adult tissues.";
RL   Mech. Dev. 118:229-232(2002).
RN   [7]
RP   FUNCTION, INTERACTION WITH KATNA1 AND KATNB1, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF PHE-302; PHE-352 AND PHE-377.
RX   PubMed=28436967; DOI=10.1038/ncb3511;
RA   Jiang K., Rezabkova L., Hua S., Liu Q., Capitani G., Maarten Altelaar A.F.,
RA   Heck A.J.R., Kammerer R.A., Steinmetz M.O., Akhmanova A.;
RT   "Microtubule minus-end regulation at spindle poles by an ASPM-katanin
RT   complex.";
RL   Nat. Cell Biol. 19:480-492(2017).
CC   -!- FUNCTION: Involved in mitotic spindle regulation and coordination of
CC       mitotic processes. The function in regulating microtubule dynamics at
CC       spindle poles including spindle orientation, astral microtubule density
CC       and poleward microtubule flux seem to depend on its association with
CC       the katanin complex formed by KATNA1 and KATNB1. Enhances the
CC       microtubule lattice severing activity of KATNA1 by recruiting the
CC       katanin complex to microtubules. Can block microtubule minus-end growth
CC       and reversely this function can be enhanced by the katanin complex
CC       (PubMed:28436967). May have a preferential role in regulating
CC       neurogenesis. {ECO:0000269|PubMed:12355089,
CC       ECO:0000269|PubMed:28436967, ECO:0000269|PubMed:9819352}.
CC   -!- SUBUNIT: Interacts with KATNA1 and KATNB1; katanin complex formation
CC       KATNA1:KATNB1 is required for the association.
CC       {ECO:0000269|PubMed:28436967}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9819352}.
CC       Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:28436967}. Nucleus
CC       {ECO:0000269|PubMed:9819352}. Note=Localizes to spindle poles during
CC       mitosis. Associates with microtubule minus ends (PubMed:28436967). The
CC       nuclear-cytoplasmic distribution could be regulated by the availability
CC       of calmodulin. {ECO:0000269|PubMed:28436967}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CJ27-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CJ27-2; Sequence=VSP_059014;
CC   -!- TISSUE SPECIFICITY: Expressed in fetal brain, peripheral nervous
CC       system, liver and spleen. In the adult, expressed exclusively in
CC       testis, ovary and spleen. {ECO:0000269|PubMed:12351193,
CC       ECO:0000269|PubMed:12355089}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during cerebral cortical neurogenesis,
CC       specifically in the cerebral cortical ventricular zone at 14.5 dpc and
CC       16.5 dpc. Expression is greatly reduced by the day of birth (P0), when
CC       neurogenesis in the cortical ventricular zone is completed and
CC       gliogenesis is increased. Expression is limited to rare scattered cells
CC       in the neocortex by postnatal day 9 (P9).
CC       {ECO:0000269|PubMed:12355089}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC79683.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF533752; AAN46088.1; -; mRNA.
DR   EMBL; AY971958; AAY46816.1; -; mRNA.
DR   EMBL; AC158946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL606536; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK050785; BAC34410.2; -; mRNA.
DR   EMBL; AK083710; BAC39000.1; -; mRNA.
DR   EMBL; AF062378; AAC79683.1; ALT_INIT; mRNA.
DR   CCDS; CCDS35729.1; -. [Q8CJ27-1]
DR   RefSeq; NP_033921.3; NM_009791.4. [Q8CJ27-1]
DR   PDB; 5LB7; X-ray; 1.50 A; C=347-355.
DR   PDBsum; 5LB7; -.
DR   SMR; Q8CJ27; -.
DR   BioGRID; 198457; 20.
DR   IntAct; Q8CJ27; 2.
DR   STRING; 10090.ENSMUSP00000059159; -.
DR   iPTMnet; Q8CJ27; -.
DR   PhosphoSitePlus; Q8CJ27; -.
DR   EPD; Q8CJ27; -.
DR   jPOST; Q8CJ27; -.
DR   MaxQB; Q8CJ27; -.
DR   PaxDb; 10090-ENSMUSP00000059159; -.
DR   PeptideAtlas; Q8CJ27; -.
DR   ProteomicsDB; 281852; -. [Q8CJ27-1]
DR   ProteomicsDB; 281853; -. [Q8CJ27-2]
DR   Pumba; Q8CJ27; -.
DR   Antibodypedia; 34476; 88 antibodies from 19 providers.
DR   DNASU; 12316; -.
DR   Ensembl; ENSMUST00000053364.12; ENSMUSP00000059159.9; ENSMUSG00000033952.15. [Q8CJ27-1]
DR   Ensembl; ENSMUST00000200083.5; ENSMUSP00000142880.2; ENSMUSG00000033952.15. [Q8CJ27-2]
DR   GeneID; 12316; -.
DR   KEGG; mmu:12316; -.
DR   UCSC; uc007cwh.1; mouse. [Q8CJ27-1]
DR   AGR; MGI:1334448; -.
DR   CTD; 259266; -.
DR   MGI; MGI:1334448; Aspm.
DR   VEuPathDB; HostDB:ENSMUSG00000033952; -.
DR   eggNOG; KOG0160; Eukaryota.
DR   eggNOG; KOG0165; Eukaryota.
DR   GeneTree; ENSGT00560000077332; -.
DR   InParanoid; Q8CJ27; -.
DR   OMA; CCCCYIF; -.
DR   OrthoDB; 53079at2759; -.
DR   PhylomeDB; Q8CJ27; -.
DR   TreeFam; TF351180; -.
DR   BioGRID-ORCS; 12316; 4 hits in 80 CRISPR screens.
DR   PRO; PR:Q8CJ27; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q8CJ27; Protein.
DR   Bgee; ENSMUSG00000033952; Expressed in primary oocyte and 196 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0072687; C:meiotic spindle; IDA:MGI.
DR   GO; GO:0005874; C:microtubule; IDA:MGI.
DR   GO; GO:0036449; C:microtubule minus-end; ISO:MGI.
DR   GO; GO:0030496; C:midbody; IDA:MGI.
DR   GO; GO:0097431; C:mitotic spindle pole; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0000922; C:spindle pole; IDA:MGI.
DR   GO; GO:0005516; F:calmodulin binding; IDA:MGI.
DR   GO; GO:0008356; P:asymmetric cell division; IMP:MGI.
DR   GO; GO:0007420; P:brain development; IMP:MGI.
DR   GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR   GO; GO:0048589; P:developmental growth; IMP:MGI.
DR   GO; GO:0021873; P:forebrain neuroblast division; IMP:MGI.
DR   GO; GO:0051661; P:maintenance of centrosome location; IMP:MGI.
DR   GO; GO:0008584; P:male gonad development; IMP:MGI.
DR   GO; GO:0090306; P:meiotic spindle assembly; IMP:MGI.
DR   GO; GO:0045769; P:negative regulation of asymmetric cell division; IMP:MGI.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI.
DR   GO; GO:0007405; P:neuroblast proliferation; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:MGI.
DR   GO; GO:0048477; P:oogenesis; IMP:MGI.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IGI:MGI.
DR   GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:MGI.
DR   GO; GO:0051445; P:regulation of meiotic cell cycle; IMP:CACAO.
DR   GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR   GO; GO:0051653; P:spindle localization; ISO:MGI.
DR   GO; GO:0007051; P:spindle organization; ISO:MGI.
DR   CDD; cd21223; CH_ASPM_rpt1; 1.
DR   CDD; cd21224; CH_ASPM_rpt2; 1.
DR   Gene3D; 1.20.5.190; -; 25.
DR   Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR031549; ASH.
DR   InterPro; IPR001715; CH_dom.
DR   InterPro; IPR036872; CH_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR22706:SF1; ABNORMAL SPINDLE-LIKE MICROCEPHALY-ASSOCIATED PROTEIN ISOFORM X1; 1.
DR   PANTHER; PTHR22706; UNCHARACTERIZED; 1.
DR   Pfam; PF15780; ASH; 1.
DR   Pfam; PF00307; CH; 1.
DR   Pfam; PF00612; IQ; 30.
DR   SMART; SM00033; CH; 2.
DR   SMART; SM00015; IQ; 55.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 16.
DR   PROSITE; PS50021; CH; 2.
DR   PROSITE; PS50096; IQ; 33.
DR   Genevisible; Q8CJ27; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calmodulin-binding; Cell cycle;
KW   Cell division; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule; Mitosis;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..3122
FT                   /note="Abnormal spindle-like microcephaly-associated
FT                   protein homolog"
FT                   /id="PRO_0000191336"
FT   DOMAIN          888..1024
FT                   /note="Calponin-homology (CH) 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          1078..1229
FT                   /note="Calponin-homology (CH) 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT   DOMAIN          1234..1263
FT                   /note="IQ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1315..1346
FT                   /note="IQ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1410..1439
FT                   /note="IQ 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1504..1535
FT                   /note="IQ 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1550..1579
FT                   /note="IQ 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1600..1629
FT                   /note="IQ 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1623..1652
FT                   /note="IQ 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1696..1725
FT                   /note="IQ 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1719..1750
FT                   /note="IQ 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1769..1798
FT                   /note="IQ 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1792..1821
FT                   /note="IQ 11"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1842..1871
FT                   /note="IQ 12"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1865..1896
FT                   /note="IQ 13"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1915..1946
FT                   /note="IQ 14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1938..1967
FT                   /note="IQ 15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          1988..2017
FT                   /note="IQ 16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          2011..2042
FT                   /note="IQ 17"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          2061..2092
FT                   /note="IQ 18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          2134..2165
FT                   /note="IQ 19"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          2157..2188
FT                   /note="IQ 20"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          2207..2238
FT                   /note="IQ 21"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          2230..2261
FT                   /note="IQ 22"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          2279..2310
FT                   /note="IQ 23"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          2302..2333
FT                   /note="IQ 24"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          2343..2374
FT                   /note="IQ 25"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          2366..2397
FT                   /note="IQ 26"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          2416..2447
FT                   /note="IQ 27"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          2491..2522
FT                   /note="IQ 28"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          2602..2633
FT                   /note="IQ 29"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          2674..2705
FT                   /note="IQ 30"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          2724..2755
FT                   /note="IQ 31"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   DOMAIN          2849..2880
FT                   /note="IQ 32"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          139..169
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..388
FT                   /note="Sufficient for interaction with KATNA1:KATNB1"
FT                   /evidence="ECO:0000269|PubMed:28436967"
FT   REGION          579..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1025..1045
FT                   /evidence="ECO:0000255"
FT   MOD_RES         348
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZT6"
FT   MOD_RES         373
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZT6"
FT   MOD_RES         573
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZT6"
FT   MOD_RES         1071
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IZT6"
FT   VAR_SEQ         1323..2587
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_059014"
FT   MUTAGEN         302
FT                   /note="F->A: Disrupts interaction with KATNA1:KATNB1; when
FT                   associated with A-377."
FT                   /evidence="ECO:0000269|PubMed:28436967"
FT   MUTAGEN         352
FT                   /note="F->A: Disrupts interaction with KATNA1:KATNB1."
FT                   /evidence="ECO:0000269|PubMed:28436967"
FT   MUTAGEN         377
FT                   /note="F->A: Disrupts interaction with KATNA1:KATNB1; when
FT                   associated with A-302."
FT                   /evidence="ECO:0000269|PubMed:28436967"
FT   CONFLICT        433
FT                   /note="T -> K (in Ref. 1; AAN46088 and 2; AAY46816)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        443..444
FT                   /note="IS -> TC (in Ref. 1; AAN46088 and 2; AAY46816)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        498
FT                   /note="E -> Q (in Ref. 1; AAN46088 and 2; AAY46816)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        513
FT                   /note="S -> P (in Ref. 1; AAN46088 and 2; AAY46816)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        591
FT                   /note="H -> L (in Ref. 1; AAN46088 and 2; AAY46816)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1111
FT                   /note="I -> V (in Ref. 1; AAN46088 and 2; AAY46816)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1378
FT                   /note="R -> G (in Ref. 1; AAN46088)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2836..2866
FT                   /note="AVRRFLLCRRQEKITSCATRIQALWRGYSWR -> RYAAFSSAEDRKRSLAA
FT                   PLEFRHYGEAILE (in Ref. 5; AAC79683)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2938
FT                   /note="S -> R (in Ref. 5; AAC79683)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   3122 AA;  364218 MW;  EB559BA254EE8270 CRC64;
     MATMQAASCP EERGRRARPD PEAGDPSPPV LLLSHFCGVP FLCFGDVRVG TSRTRSLVLH
     NPHEEPLQVE LSLLRAAGQG FSVAPNRCEL KPKEKLTISV TWTPLREGGV REIVTFLVND
     FLKHQAILLG NAEEPKKKKR SLWNTSKKIP ASSKHTKRTS KNQHFNESFT ISQKDRIRSP
     LQPCENLAMS ECSSPTENKV PTPSISPIRE CQSETCLPLF LRESTAYSSL HESENTQNLK
     VQDASISQTF DFNEEVANET FINPISVCHQ SEGDRKLTLA PNCSSPLNST QTQIHFLSPD
     SFVNNRYTSD NDLKSMKNVL SDTFRKDPAE SVCLESQTVH EVCQTILSPD SFLNDNYGLK
     KGLNFKSVNP VLSPTQFVKD SMGHVGQQTG KSNEASQDWR INEGLAYTPE CQHAQTPSSR
     SEKQNPVEVK PHTYDFTKQK PKISEFQDAF CHQSKQPHKR RPILSATVTK RKPTNAREKL
     PEINKPDAKR CLEGLVGERG KEVGSLREKG FHSSLPVVEP GVSKALSYRD EVTPATVVVA
     RKRKSHGTVG DANGKVAAEE WMDMCEVKRI HFSPLESTPS TVARTTKKEG HTSKRISSLE
     RSGLKKKMDS SILKTPLSKT KKKRRSIVAV AQSHLTFIKP LKAAIPRHPM PFAAKNMFYD
     ERWKEKQEQG FTWWLNYILT PDDFTVKTNV SKVNAASLVL GAESQHKISV PKAPTKEEVS
     LRAYTASCRL NRLRRTACSL FTSEKMVKAI KKVEIEIEVG RLLVRKDRHL WKDIGQRQKV
     LNWLLSYNPL WLRIGLETVF GELIPLADNS DVTGLAMFIL NRLLWNPDIA AEYRHPTVPL
     LFRDGHEAAL SKFTLKKLLL LICFLDHAKI SRLIDHDPCL FCKDAEFKAS KELLLAFSRD
     FLSGEGDLSR HLSFLGLPVS HVQTPLDEFD FAVTNLAVDL QCGVRLVRTV ELLTQNWNLS
     DKLRIPAISR VQKMHNVDLV LQVLKSRGVP LTDEHGSAIS SKDVVDRHRE KTLGLLWKIA
     LAFQVDISLN LDQLKEEIDF LKHTHSIKRA MSALTCPSQA ITNKQRDKRI SGNFERYGDS
     VQLLMDWVNA VCAFYNKKVE NFTVSFSDGR ILCYLIHHYH PCYVPFDAIC QRTSQSVACA
     QTGSVVLNSS SESEGGCLDL SLEALDHEST PEMYKELLEN EKKNFHLVRS AARDLGGIPA
     MIHHSDMSNT IPDEKVVITY LSFLCARLLD LRKEIRAARL IQTTWRKYKL KRDLKHHQER
     DKAARVIQSV VLNFLSRRRL QKNVSAALVI QKCWRRVSAQ RKLRMLKNEK LAKLQNKSAV
     LIQAYWRRYS TRKRFLRLKH YSVILQSRIR MKIALTSYKR YLWATVTIQR HWRAYLSRKR
     DQQIFRKLKS SSLVIQFMFR RWKRRKLQLQ TKAAVTLQRA FREWHLRKQI RERSAVVIQS
     WYRMHRELQK YIYIRSCVIV IQRRVRCFQA QKLYKRRKDA ILTLQKHYRA RQKGKLAHAD
     YLQKRAATIR LQAAFRGMKA RHSYRLQIGA ACVLQSYWRM RQERVRFLNL KKMVIKLQAH
     IRKYQQLQKY KKIKKAAITI QTHFRASISA RRVLASYQKT RSSVIVLQSA CRGMQARKAF
     RHALASVIKI QSYYRAYICR KTFQNFKNAT IKLQSIVKMK QSRKQYLQIR AAALFIQRWY
     RSQKLASQKR KEYIQVRESC IKLQSHFRGC LVRKQLRLQC KAAISLQSYF RMRTARQRYL
     KMCKAALVIQ SFYCAYRAQI SQRKNFLQVK RAAICLQAAY RGCKVRRQIK QQSTAAVTIQ
     RVFRGHSQRM KYQTMLQSAV KIQRWYRAQK VAYDMRIQFL KTREAVVCLQ SAYRGWQVRQ
     QLRRQHEAAV KIQSTFRMAV AQQQYKLLRA AAAVIQQHVR ARAAGKRQHL AYIQLRHAAL
     VFQAAWKGKM LRRQIARQHQ CAALIQSYYR MHIQRRKWSI MKTAALQIQL CYRAYKVGKE
     QRHLYLKTKA AVVTLQSAYR GMKVRKRVAE CHKAAVTIQS KFRAYRTQKK YTTYRTSAIV
     IQRWYRNIKI TTQQHQEYLN LRRAAVQVQA AYRGIRVRRR IQHMHMAATL IEAMFKMRQS
     RVRYLKMRTA ALIIQVRYRA YYLGKIQHEK YLRTLKAIKT LQAGVRGARV RRTVRKMHFA
     ATLIQSHFRG HRQQTYFHRL RKAATMVQQR YRAVKEGSAE FQRYSRLRRS VLLIQAAFRG
     LRTRRHLKAM HLAATLIQRR FRTFAMRRKF LSLRKTAIWI QRQYRARLYA KYSRQQLLLE
     KAVIKIQSSY RGWVVRKRVQ KMHRAATVIQ ATFRMHGAYM RYQHLKRASV VIQVHTAAEL
     QRQKHAAVIL QAAVRGMKTR SHLKTMHSSA TLIQSQFRAF IVRRRFIALR KAAIFVQRKF
     RATLYAKHKL HQFLQLRKAA ITIQSSYRRL MVQKKLQEMH RAAALIQATF RMHRTYVAFH
     IWKCASIRIQ QCYRTYRTIK LQKEKLIREE QHSAAVLIQS TYRMYRQRCF YQQRRWAAKV
     IQKTYRANKR RQDLLYVCKE ETPLLQMHFQ GLNTAKQGRQ QHGAAMITQK HFRAFKARRL
     MEAERGFQAG CRKYKAKKYL SKVEAACRIQ AWYRRWRAHK KYLTLLKAVN IIEGYLSAQL
     ARRRFLKMRA AAIIIQRKWR ATLSVRGARE NLKRHRAACV IQAHFRGYQA RQSFLQQRSA
     VLIIQRHVRA MVAAKQERIK YIKLKKSTVV VQALVRGWLV RKRVSEQKAK TRLFHFTAAA
     YCHMCALKIQ RAYRLHVTLR NAKKHMDSVI FIQRWFRKRL QRKRFIEQYH KILSTRREAH
     ACWLQQDRAA SVIQKAVRRF LLCRRQEKIT SCATRIQALW RGYSWRKKND HTEIKAIRRS
     LRAVSTTVEE ENKLYRRTER ALHHLLTYKH LSAILDALKH LEVVTRLSPL CCENMAESGA
     VSTIFVVIRS CNRSVPCMEV VGYAVQVLLN VAKYDKTIAA VYEAENCVDT LLELLQVYRE
     KPGDRVAEKS ASIFTRTCCL LAVLLKTEQC AFDAQSRSKV TDRIYRLYKF TVPKHKVNTQ
     GLFDKQKQNS CVGFPCIPER TMKTRLVSRL KPQWVLRRDN VEEITNSLQA IQLVMDTLGI
     SY
//