ASPM_HUMAN
ID ASPM_HUMAN Reviewed; 3477 AA.
AC Q8IZT6; Q4G1H1; Q5VYL3; Q86UX4; Q8IUL2; Q8IZJ7; Q8IZJ8; Q8IZJ9; Q8N4D1;
AC Q9NVS1; Q9NVT6;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Abnormal spindle-like microcephaly-associated protein;
DE AltName: Full=Abnormal spindle protein homolog;
DE Short=Asp homolog;
GN Name=ASPM; Synonyms=MCPH5;
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] (ISOFORM 1), FUNCTION, INVOLVEMENT IN MCPH5, AND
RP VARIANT HIS-2494.
RC TISSUE=Colon adenocarcinoma, and Fetal brain;
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 [MRNA] (ISOFORM 1), AND VARIANT HIS-2494.
RX PubMed=14704186; DOI=10.1093/genetics/165.4.2063;
RA Zhang J.;
RT "Evolution of the human ASPM gene, a major determinant of brain size.";
RL Genetics 165:2063-2070(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ALTERNATIVE SPLICING, AND
RP SUBCELLULAR LOCATION.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
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] OF 1-147 AND 709-3477 (ISOFORM 2),
RP AND VARIANT PHE-1090.
RC TISSUE=Kidney, and 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2740-3477 (ISOFORM 1).
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 [8]
RP INVOLVEMENT IN MCPH5, AND VARIANTS GLY-2562; ILE-2647 AND ARG-3132.
RX PubMed=14574646; DOI=10.1086/379085;
RA Bond J., Scott S., Hampshire D.J., Springell K., Corry P., Abramowicz M.J.,
RA Mochida G.H., Hennekam R.C.M., Maher E.R., Fryns J.-P., Alswaid A.,
RA Jafri H., Rashid Y., Mubaidin A., Walsh C.A., Roberts E., Woods C.G.;
RT "Protein-truncating mutations in ASPM cause variable reduction in brain
RT size.";
RL Am. J. Hum. Genet. 73:1170-1177(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-283; SER-425 AND
RP SER-1103, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367 AND SER-392, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-283 AND SER-392, 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 [14]
RP INVOLVEMENT IN MCPH5.
RX PubMed=22989186; DOI=10.1111/j.1399-0004.2012.01949.x;
RA Papari E., Bastami M., Farhadi A., Abedini S.S., Hosseini M., Bahman I.,
RA Mohseni M., Garshasbi M., Moheb L.A., Behjati F., Kahrizi K., Ropers H.H.,
RA Najmabadi H.;
RT "Investigation of primary microcephaly in Bushehr province of Iran: novel
RT STIL and ASPM mutations.";
RL Clin. Genet. 83:488-490(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367; SER-425; SER-605 AND
RP SER-1103, AND 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 [16]
RP FUNCTION, INTERACTION WITH KATNA1 AND KATNB1, AND SUBCELLULAR LOCATION.
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).
RN [17]
RP VARIANTS HIS-2494; ASP-2526; ILE-2647 AND PRO-3180.
RX PubMed=16673149; DOI=10.1007/s10048-006-0042-4;
RA Gul A., Hassan M.J., Mahmood S., Chen W., Rahmani S., Naseer M.I.,
RA Dellefave L., Muhammad N., Rafiq M.A., Ansar M., Chishti M.S., Ali G.,
RA Siddique T., Ahmad W.;
RT "Genetic studies of autosomal recessive primary microcephaly in 33
RT Pakistani families: Novel sequence variants in ASPM gene.";
RL Neurogenetics 7:105-110(2006).
RN [18]
RP VARIANT ILE-2647.
RX PubMed=18204051; DOI=10.1093/hmg/ddn021;
RA Wang J.-K., Li Y., Su B.;
RT "A common SNP of MCPH1 is associated with cranial volume variation in
RT Chinese population.";
RL Hum. Mol. Genet. 17:1329-1335(2008).
RN [19]
RP VARIANT PRO-3180.
RX PubMed=27535533; DOI=10.1038/nature19057;
RG Exome Aggregation Consortium;
RA Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E., Fennell T.,
RA O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B., Tukiainen T.,
RA Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K., Zhao F., Zou J.,
RA Pierce-Hoffman E., Berghout J., Cooper D.N., Deflaux N., DePristo M.,
RA Do R., Flannick J., Fromer M., Gauthier L., Goldstein J., Gupta N.,
RA Howrigan D., Kiezun A., Kurki M.I., Moonshine A.L., Natarajan P.,
RA Orozco L., Peloso G.M., Poplin R., Rivas M.A., Ruano-Rubio V., Rose S.A.,
RA Ruderfer D.M., Shakir K., Stenson P.D., Stevens C., Thomas B.P., Tiao G.,
RA Tusie-Luna M.T., Weisburd B., Won H.H., Yu D., Altshuler D.M.,
RA Ardissino D., Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
RA Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S., Laakso M.,
RA McCarroll S., McCarthy M.I., McGovern D., McPherson R., Neale B.M.,
RA Palotie A., Purcell S.M., Saleheen D., Scharf J.M., Sklar P.,
RA Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C., Wilson J.G.,
RA Daly M.J., MacArthur D.G.;
RT "Analysis of protein-coding genetic variation in 60,706 humans.";
RL Nature 536:285-291(2016).
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 seems to depend on the 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:15972725, ECO:0000269|PubMed:28436967}.
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:0000250}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000269|PubMed:15972725}. Nucleus {ECO:0000250}. Note=The
CC nuclear-cytoplasmic distribution could be regulated by the availability
CC of calmodulin (By similarity). Localizes to spindle poles during
CC mitosis (PubMed:19690332). Associates with microtubule minus ends (By
CC similarity). {ECO:0000250|UniProtKB:Q8CJ27}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8IZT6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IZT6-2; Sequence=VSP_010680;
CC -!- DISEASE: Microcephaly 5, primary, autosomal recessive (MCPH5)
CC [MIM:608716]: A disease defined as a head circumference more than 3
CC standard deviations below the age-related mean. Brain weight is
CC markedly reduced and the cerebral cortex is disproportionately small.
CC Despite this marked reduction in size, the gyral pattern is relatively
CC well preserved, with no major abnormality in cortical architecture.
CC Affected individuals are mentally retarded. Primary microcephaly is
CC further defined by the absence of other syndromic features or
CC significant neurological deficits due to degenerative brain disorder.
CC {ECO:0000269|PubMed:12355089, ECO:0000269|PubMed:14574646,
CC ECO:0000269|PubMed:22989186}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH34607.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA91676.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ASPMID44463ch1q31.html";
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DR EMBL; AF509326; AAN40011.1; -; mRNA.
DR EMBL; AY099890; AAM44119.1; -; mRNA.
DR EMBL; AY099891; AAM44120.1; -; mRNA.
DR EMBL; AY099892; AAM44121.1; -; mRNA.
DR EMBL; AY099893; AAM44122.1; -; mRNA.
DR EMBL; AY101201; AAM48745.1; -; mRNA.
DR EMBL; AY367065; AAR12641.1; -; mRNA.
DR EMBL; AY971956; AAY46814.1; -; mRNA.
DR EMBL; AL353809; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91274.1; -; Genomic_DNA.
DR EMBL; BC015396; AAH15396.1; -; mRNA.
DR EMBL; BC034607; AAH34607.1; ALT_INIT; mRNA.
DR EMBL; AK001411; BAA91676.1; ALT_INIT; mRNA.
DR CCDS; CCDS1389.1; -. [Q8IZT6-1]
DR CCDS; CCDS55672.1; -. [Q8IZT6-2]
DR RefSeq; NP_001193775.1; NM_001206846.1. [Q8IZT6-2]
DR RefSeq; NP_060606.3; NM_018136.4. [Q8IZT6-1]
DR SMR; Q8IZT6; -.
DR BioGRID; 129236; 130.
DR IntAct; Q8IZT6; 89.
DR STRING; 9606.ENSP00000356379; -.
DR CarbonylDB; Q8IZT6; -.
DR iPTMnet; Q8IZT6; -.
DR PhosphoSitePlus; Q8IZT6; -.
DR BioMuta; ASPM; -.
DR DMDM; 215273935; -.
DR EPD; Q8IZT6; -.
DR jPOST; Q8IZT6; -.
DR MassIVE; Q8IZT6; -.
DR MaxQB; Q8IZT6; -.
DR PaxDb; Q8IZT6; -.
DR PeptideAtlas; Q8IZT6; -.
DR PRIDE; Q8IZT6; -.
DR ProteomicsDB; 71424; -. [Q8IZT6-1]
DR ProteomicsDB; 71425; -. [Q8IZT6-2]
DR Antibodypedia; 34476; 84 antibodies from 19 providers.
DR DNASU; 259266; -.
DR Ensembl; ENST00000294732.11; ENSP00000294732.7; ENSG00000066279.19. [Q8IZT6-2]
DR Ensembl; ENST00000367409.9; ENSP00000356379.4; ENSG00000066279.19. [Q8IZT6-1]
DR GeneID; 259266; -.
DR KEGG; hsa:259266; -.
DR MANE-Select; ENST00000367409.9; ENSP00000356379.4; NM_018136.5; NP_060606.3.
DR UCSC; uc001gtu.4; human. [Q8IZT6-1]
DR CTD; 259266; -.
DR DisGeNET; 259266; -.
DR GeneCards; ASPM; -.
DR GeneReviews; ASPM; -.
DR HGNC; HGNC:19048; ASPM.
DR HPA; ENSG00000066279; Group enriched (bone marrow, lymphoid tissue).
DR MalaCards; ASPM; -.
DR MIM; 605481; gene.
DR MIM; 608716; phenotype.
DR neXtProt; NX_Q8IZT6; -.
DR OpenTargets; ENSG00000066279; -.
DR Orphanet; 2512; Autosomal recessive primary microcephaly.
DR PharmGKB; PA38782; -.
DR VEuPathDB; HostDB:ENSG00000066279; -.
DR eggNOG; KOG0160; Eukaryota.
DR eggNOG; KOG0165; Eukaryota.
DR GeneTree; ENSGT00560000077332; -.
DR HOGENOM; CLU_000237_0_0_1; -.
DR InParanoid; Q8IZT6; -.
DR OMA; CCCCYIF; -.
DR OrthoDB; 1249457at2759; -.
DR PhylomeDB; Q8IZT6; -.
DR TreeFam; TF351180; -.
DR PathwayCommons; Q8IZT6; -.
DR SignaLink; Q8IZT6; -.
DR SIGNOR; Q8IZT6; -.
DR BioGRID-ORCS; 259266; 113 hits in 1100 CRISPR screens.
DR ChiTaRS; ASPM; human.
DR GeneWiki; ASPM_(gene); -.
DR GenomeRNAi; 259266; -.
DR Pharos; Q8IZT6; Tbio.
DR PRO; PR:Q8IZT6; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8IZT6; protein.
DR Bgee; ENSG00000066279; Expressed in oocyte and 114 other tissues.
DR Genevisible; Q8IZT6; HS.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0072687; C:meiotic spindle; IEA:Ensembl.
DR GO; GO:0036449; C:microtubule minus-end; IDA:HGNC.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:HGNC.
DR GO; GO:0005634; C:nucleus; IDA:HGNC.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0008356; P:asymmetric cell division; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0048589; P:developmental growth; IEA:Ensembl.
DR GO; GO:0021873; P:forebrain neuroblast division; IEA:Ensembl.
DR GO; GO:0051661; P:maintenance of centrosome location; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0090306; P:meiotic spindle assembly; IEA:Ensembl.
DR GO; GO:0045769; P:negative regulation of asymmetric cell division; IEA:Ensembl.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0048477; P:oogenesis; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IEA:Ensembl.
DR GO; GO:0051445; P:regulation of meiotic cell cycle; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0051653; P:spindle localization; IMP:HGNC.
DR GO; GO:0007051; P:spindle organization; IMP:HGNC.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR011989; ARM-like.
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; 6.
DR Pfam; PF15780; ASH; 1.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00612; IQ; 39.
DR SMART; SM00033; CH; 2.
DR SMART; SM00015; IQ; 63.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF52540; SSF52540; 18.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50096; IQ; 39.
PE 1: Evidence at protein level;
KW Alternative splicing; Calmodulin-binding; Cell cycle; Cell division;
KW Coiled coil; Cytoplasm; Cytoskeleton; Disease variant;
KW Intellectual disability; Mitosis; Nucleus; Phosphoprotein;
KW Primary microcephaly; Reference proteome; Repeat.
FT CHAIN 1..3477
FT /note="Abnormal spindle-like microcephaly-associated
FT protein"
FT /id="PRO_0000191332"
FT DOMAIN 920..1056
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1110..1261
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1347..1378
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1393..1422
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1582..1613
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1632..1661
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1655..1684
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1728..1757
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1751..1782
FT /note="IQ 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1801..1830
FT /note="IQ 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1824..1853
FT /note="IQ 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1874..1903
FT /note="IQ 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1897..1928
FT /note="IQ 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1947..1978
FT /note="IQ 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1970..2001
FT /note="IQ 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2020..2049
FT /note="IQ 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2043..2074
FT /note="IQ 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2093..2124
FT /note="IQ 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2116..2147
FT /note="IQ 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2166..2197
FT /note="IQ 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2189..2218
FT /note="IQ 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2239..2270
FT /note="IQ 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2262..2293
FT /note="IQ 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2311..2342
FT /note="IQ 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2334..2365
FT /note="IQ 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2384..2415
FT /note="IQ 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2407..2438
FT /note="IQ 25"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2457..2488
FT /note="IQ 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2530..2561
FT /note="IQ 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2624..2653
FT /note="IQ 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2665..2696
FT /note="IQ 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2688..2719
FT /note="IQ 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2738..2767
FT /note="IQ 31"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2859..2890
FT /note="IQ 32"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2909..2938
FT /note="IQ 33"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2932..2963
FT /note="IQ 34"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 2954..2985
FT /note="IQ 35"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 3029..3060
FT /note="IQ 36"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 3079..3110
FT /note="IQ 37"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 3181..3210
FT /note="IQ 38"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 3204..3235
FT /note="IQ 39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..409
FT /note="Sufficient for interaction with KATNA1:KATNB1"
FT /evidence="ECO:0000250|UniProtKB:Q8CJ27"
FT REGION 415..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1057..1078
FT /evidence="ECO:0000255"
FT COMPBIAS 559..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1103
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1356..2940
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15972725"
FT /id="VSP_010680"
FT VARIANT 313
FT /note="I -> V (in dbSNP:rs12025066)"
FT /id="VAR_047263"
FT VARIANT 430
FT /note="R -> G (in dbSNP:rs6428388)"
FT /id="VAR_024369"
FT VARIANT 869
FT /note="T -> S (in dbSNP:rs7551108)"
FT /id="VAR_046758"
FT VARIANT 1090
FT /note="S -> F (in dbSNP:rs16841081)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_046759"
FT VARIANT 2494
FT /note="Y -> H (in dbSNP:rs964201)"
FT /evidence="ECO:0000269|PubMed:12355089,
FT ECO:0000269|PubMed:14704186, ECO:0000269|PubMed:16673149"
FT /id="VAR_046760"
FT VARIANT 2526
FT /note="N -> D (in dbSNP:rs587783267)"
FT /evidence="ECO:0000269|PubMed:16673149"
FT /id="VAR_071930"
FT VARIANT 2562
FT /note="S -> G (in dbSNP:rs41310927)"
FT /evidence="ECO:0000269|PubMed:14574646"
FT /id="VAR_019084"
FT VARIANT 2620
FT /note="Q -> H (in dbSNP:rs12138336)"
FT /id="VAR_046761"
FT VARIANT 2647
FT /note="L -> I (in dbSNP:rs3762271)"
FT /evidence="ECO:0000269|PubMed:14574646,
FT ECO:0000269|PubMed:16673149, ECO:0000269|PubMed:18204051"
FT /id="VAR_019085"
FT VARIANT 3132
FT /note="L -> R (in dbSNP:rs36004306)"
FT /evidence="ECO:0000269|PubMed:14574646"
FT /id="VAR_019086"
FT VARIANT 3180
FT /note="Q -> P (in dbSNP:rs193251130)"
FT /evidence="ECO:0000269|PubMed:16673149,
FT ECO:0000269|PubMed:27535533"
FT /id="VAR_071931"
FT VARIANT 3258
FT /note="H -> R (in dbSNP:rs7528827)"
FT /id="VAR_046762"
FT CONFLICT 2355
FT /note="Q -> R (in Ref. 1; AAN40011 and 2; AAR12641)"
FT /evidence="ECO:0000305"
FT CONFLICT 2977
FT /note="I -> V (in Ref. 7; BAA91676)"
FT /evidence="ECO:0000305"
FT CONFLICT 3049
FT /note="F -> S (in Ref. 7; BAA91676)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3477 AA; 409800 MW; EB6EDAD3FF186108 CRC64;
MANRRVGRGC WEVSPTERRP PAGLRGPAAE EEASSPPVLS LSHFCRSPFL CFGDVLLGAS
RTLSLALDNP NEEVAEVKIS HFPAADLGFS VSQRCFVLQP KEKIVISVNW TPLKEGRVRE
IMTFLVNDVL KHQAILLGNA EEQKKKKRSL WDTIKKKKIS ASTSHNRRVS NIQNVNKTFS
VSQKVDRVRS PLQACENLAM NEGGPPTENN SLILEENKIP ISPISPAFNE CHGATCLPLS
VRRSTTYSSL HASENRELLN VHSANVSKVS FNEKAVTETS FNSVNVNGQR GENSKLSLTP
NCSSTLNITQ SQIHFLSPDS FVNNSHGANN ELELVTCLSS DMFMKDNSQP VHLESTIAHE
IYQKILSPDS FIKDNYGLNQ DLESESVNPI LSPNQFLKDN MAYMCTSQQT CKVPLSNENS
QVPQSPEDWR KSEVSPRIPE CQGSKSPKAI FEELVEMKSN YYSFIKQNNP KFSAVQDISS
HSHNKQPKRR PILSATVTKR KATCTRENQT EINKPKAKRC LNSAVGEHEK VINNQKEKED
FHSYLPIIDP ILSKSKSYKN EVTPSSTTAS VARKRKSDGS MEDANVRVAI TEHTEVREIK
RIHFSPSEPK TSAVKKTKNV TTPISKRISN REKLNLKKKT DLSIFRTPIS KTNKRTKPII
AVAQSSLTFI KPLKTDIPRH PMPFAAKNMF YDERWKEKQE QGFTWWLNFI LTPDDFTVKT
NISEVNAATL LLGIENQHKI SVPRAPTKEE MSLRAYTARC RLNRLRRAAC RLFTSEKMVK
AIKKLEIEIE ARRLIVRKDR HLWKDVGERQ KVLNWLLSYN PLWLRIGLET TYGELISLED
NSDVTGLAMF ILNRLLWNPD IAAEYRHPTV PHLYRDGHEE ALSKFTLKKL LLLVCFLDYA
KISRLIDHDP CLFCKDAEFK ASKEILLAFS RDFLSGEGDL SRHLGLLGLP VNHVQTPFDE
FDFAVTNLAV DLQCGVRLVR TMELLTQNWD LSKKLRIPAI SRLQKMHNVD IVLQVLKSRG
IELSDEHGNT ILSKDIVDRH REKTLRLLWK IAFAFQVDIS LNLDQLKEEI AFLKHTKSIK
KTISLLSCHS DDLINKKKGK RDSGSFEQYS ENIKLLMDWV NAVCAFYNKK VENFTVSFSD
GRVLCYLIHH YHPCYVPFDA ICQRTTQTVE CTQTGSVVLN SSSESDDSSL DMSLKAFDHE
NTSELYKELL ENEKKNFHLV RSAVRDLGGI PAMINHSDMS NTIPDEKVVI TYLSFLCARL
LDLRKEIRAA RLIQTTWRKY KLKTDLKRHQ EREKAARIIQ LAVINFLAKQ RLRKRVNAAL
VIQKYWRRVL AQRKLLMLKK EKLEKVQNKA ASLIQGYWRR YSTRQRFLKL KYYSIILQSR
IRMIIAVTSY KRYLWATVTI QRHWRAYLRR KQDQQRYEML KSSTLIIQSM FRKWKQRKMQ
SQVKATVILQ RAFREWHLRK QAKEENSAII IQSWYRMHKE LRKYIYIRSC VVIIQKRFRC
FQAQKLYKRR KESILTIQKY YKAYLKGKIE RTNYLQKRAA AIQLQAAFRR LKAHNLCRQI
RAACVIQSYW RMRQDRVRFL NLKKTIIKFQ AHVRKHQQRQ KYKKMKKAAV IIQTHFRAYI
FAMKVLASYQ KTRSAVIVLQ SAYRGMQARK MYIHILTSVI KIQSYYRAYV SKKEFLSLKN
ATIKLQSTVK MKQTRKQYLH LRAAALFIQQ CYRSKKIAAQ KREEYMQMRE SCIKLQAFVR
GYLVRKQMRL QRKAVISLQS YFRMRKARQY YLKMYKAIIV IQNYYHAYKA QVNQRKNFLQ
VKKAATCLQA AYRGYKVRQL IKQQSIAALK IQSAFRGYNK RVKYQSVLQS IIKIQRWYRA
YKTLHDTRTH FLKTKAAVIS LQSAYRGWKV RKQIRREHQA ALKIQSAFRM AKAQKQFRLF
KTAALVIQQN FRAWTAGRKQ CMEYIELRHA VLVLQSMWKG KTLRRQLQRQ HKCAIIIQSY
YRMHVQQKKW KIMKKAALLI QKYYRAYSIG REQNHLYLKT KAAVVTLQSA YRGMKVRKRI
KDCNKAAVTI QSKYRAYKTK KKYATYRASA IIIQRWYRGI KITNHQHKEY LNLKKTAIKI
QSVYRGIRVR RHIQHMHRAA TFIKAMFKMH QSRISYHTMR KAAIVIQVRC RAYYQGKMQR
EKYLTILKAV KVLQASFRGV RVRRTLRKMQ TAATLIQSNY RRYRQQTYFN KLKKITKTVQ
QRYWAMKERN IQFQRYNKLR HSVIYIQAIF RGKKARRHLK MMHIAATLIQ RRFRTLMMRR
RFLSLKKTAI LIQRKYRAHL CTKHHLQFLQ VQNAVIKIQS SYRRWMIRKR MREMHRAATF
IQSTFRMHRL HMRYQALKQA SVVIQQQYQA NRAAKLQRQH YLRQRHSAVI LQAAFRGMKT
RRHLKSMHSS ATLIQSRFRS LLVRRRFISL KKATIFVQRK YRATICAKHK LYQFLHLRKA
AITIQSSYRR LMVKKKLQEM QRAAVLIQAT FRMYRTYITF QTWKHASILI QQHYRTYRAA
KLQRENYIRQ WHSAVVIQAA YKGMKARQLL REKHKASIVI QSTYRMYRQY CFYQKLQWAT
KIIQEKYRAN KKKQKVFQHN ELKKETCVQA GFQDMNIKKQ IQEQHQAAII IQKHCKAFKI
RKHYLHLRAT VVSIQRRYRK LTAVRTQAVI CIQSYYRGFK VRKDIQNMHR AATLIQSFYR
MHRAKVDYET KKTAIVVIQN YYRLYVRVKT ERKNFLAVQK SVRTIQAAFR GMKVRQKLKN
VSEEKMAAIV NQSALCCYRS KTQYEAVQSE GVMIQEWYKA SGLACSQEAE YHSQSRAAVT
IQKAFCRMVT RKLETQKCAA LRIQFFLQMA VYRRRFVQQK RAAITLQHYF RTWQTRKQFL
LYRKAAVVLQ NHYRAFLSAK HQRQVYLQIR SSVIIIQARS KGFIQKRKFQ EIKNSTIKIQ
AMWRRYRAKK YLCKVKAACK IQAWYRCWRA HKEYLAILKA VKIIQGCFYT KLERTRFLNV
RASAIIIQRK WRAILPAKIA HEHFLMIKRH RAACLIQAHY RGYKGRQVFL RQKSAALIIQ
KYIRAREAGK HERIKYIEFK KSTVILQALV RGWLVRKRFL EQRAKIRLLH FTAAAYYHLN
AVRIQRAYKL YLAVKNANKQ VNSVICIQRW FRARLQEKRF IQKYHSIKKI EHEGQECLSQ
RNRAASVIQK AVRHFLLRKK QEKFTSGIIK IQALWRGYSW RKKNDCTKIK AIRLSLQVVN
REIREENKLY KRTALALHYL LTYKHLSAIL EALKHLEVVT RLSPLCCENM AQSGAISKIF
VLIRSCNRSI PCMEVIRYAV QVLLNVSKYE KTTSAVYDVE NCIDILLELL QIYREKPGNK
VADKGGSIFT KTCCLLAILL KTTNRASDVR SRSKVVDRIY SLYKLTAHKH KMNTERILYK
QKKNSSISIP FIPETPVRTR IVSRLKPDWV LRRDNMEEIT NPLQAIQMVM DTLGIPY
