ASPM_MOUSE
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 03-AUG-2022, entry version 146.
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; 19.
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; Q8CJ27; -.
DR PeptideAtlas; Q8CJ27; -.
DR PRIDE; Q8CJ27; -.
DR ProteomicsDB; 281852; -. [Q8CJ27-1]
DR ProteomicsDB; 281853; -. [Q8CJ27-2]
DR Antibodypedia; 34476; 84 antibodies from 19 providers.
DR DNASU; 12316; -.
DR Ensembl; ENSMUST00000053364; ENSMUSP00000059159; ENSMUSG00000033952. [Q8CJ27-1]
DR Ensembl; ENSMUST00000200083; ENSMUSP00000142880; ENSMUSG00000033952. [Q8CJ27-2]
DR GeneID; 12316; -.
DR KEGG; mmu:12316; -.
DR UCSC; uc007cwh.1; mouse. [Q8CJ27-1]
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; 482623at2759; -.
DR PhylomeDB; Q8CJ27; -.
DR TreeFam; TF351180; -.
DR BioGRID-ORCS; 12316; 4 hits in 75 CRISPR screens.
DR PRO; PR:Q8CJ27; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8CJ27; protein.
DR Bgee; ENSMUSG00000033952; Expressed in primary oocyte and 192 other tissues.
DR Genevisible; Q8CJ27; MM.
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 Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR031549; ASH.
DR InterPro; IPR029955; ASPM.
DR InterPro; IPR001715; CH-domain.
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; PTHR22590:SF4; PTHR22590:SF4; 4.
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; SSF47576; SSF47576; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF52540; SSF52540; 16.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50096; IQ; 33.
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
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