MDM1_HUMAN
ID MDM1_HUMAN Reviewed; 714 AA.
AC Q8TC05; B4DM65; E7EPQ3; O43406; Q8WTV9; Q9NR04;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Nuclear protein MDM1;
GN Name=MDM1;
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 2).
RA Yang Q.S., Ying K., Wu H., Xia F., Xie Y., Mao Y.M.;
RT "Cloning, mapping and characterization of a novel human MDM1 protein.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP ILE-103; HIS-489 AND LEU-552.
RC TISSUE=Prostate, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 462-714 (ISOFORM 1), AND VARIANT
RP HIS-489.
RC TISSUE=Brain;
RA Yu W., Sarginson J., Gibbs R.A.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242; SER-263; SER-584 AND
RP SER-648, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN [ST]-E-Y-X(3)-F MOTIF, AND
RP MUTAGENESIS OF 9-SER--PHE-15; 189-SER--PHE-195; 232-THR--PHE-238 AND
RP 306-SER--PHE-312.
RX PubMed=26337392; DOI=10.1091/mbc.e15-04-0235;
RA Van de Mark D., Kong D., Loncarek J., Stearns T.;
RT "MDM1 is a microtubule-binding protein that negatively regulates centriole
RT duplication.";
RL Mol. Biol. Cell 26:3788-3802(2015).
CC -!- FUNCTION: Microtubule-binding protein that negatively regulates
CC centriole duplication. Binds to and stabilizes microtubules
CC (PubMed:26337392). {ECO:0000269|PubMed:26337392}.
CC -!- INTERACTION:
CC Q8TC05; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-3951677, EBI-10961624;
CC Q8TC05; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-3951677, EBI-748420;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26337392}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:26337392}. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome, centriole
CC {ECO:0000269|PubMed:26337392}. Note=Localizes to the centriole lumen.
CC {ECO:0000269|PubMed:26337392}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8TC05-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TC05-2; Sequence=VSP_027546, VSP_027547;
CC Name=3;
CC IsoId=Q8TC05-3; Sequence=VSP_027544, VSP_027545;
CC Name=4;
CC IsoId=Q8TC05-4; Sequence=VSP_046400, VSP_046401;
CC -!- SIMILARITY: Belongs to the MDM1 family. {ECO:0000305}.
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DR EMBL; AF267851; AAF78952.1; -; mRNA.
DR EMBL; AK297311; BAG59777.1; -; mRNA.
DR EMBL; AC022511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022042; AAH22042.1; -; mRNA.
DR EMBL; BC028355; AAH28355.1; -; mRNA.
DR EMBL; AF007130; AAC19149.1; -; mRNA.
DR CCDS; CCDS44938.1; -. [Q8TC05-2]
DR CCDS; CCDS55841.1; -. [Q8TC05-4]
DR CCDS; CCDS55842.1; -. [Q8TC05-3]
DR CCDS; CCDS8983.1; -. [Q8TC05-1]
DR RefSeq; NP_001191957.1; NM_001205028.1. [Q8TC05-4]
DR RefSeq; NP_001191958.1; NM_001205029.1. [Q8TC05-3]
DR RefSeq; NP_059136.2; NM_017440.4. [Q8TC05-1]
DR RefSeq; NP_064513.1; NM_020128.2. [Q8TC05-2]
DR AlphaFoldDB; Q8TC05; -.
DR BioGRID; 121220; 9.
DR IntAct; Q8TC05; 7.
DR STRING; 9606.ENSP00000302537; -.
DR iPTMnet; Q8TC05; -.
DR PhosphoSitePlus; Q8TC05; -.
DR BioMuta; MDM1; -.
DR DMDM; 156632525; -.
DR EPD; Q8TC05; -.
DR jPOST; Q8TC05; -.
DR MassIVE; Q8TC05; -.
DR MaxQB; Q8TC05; -.
DR PaxDb; Q8TC05; -.
DR PeptideAtlas; Q8TC05; -.
DR PRIDE; Q8TC05; -.
DR ProteomicsDB; 17412; -.
DR ProteomicsDB; 74064; -. [Q8TC05-1]
DR ProteomicsDB; 74065; -. [Q8TC05-2]
DR ProteomicsDB; 74066; -. [Q8TC05-3]
DR Antibodypedia; 29303; 135 antibodies from 24 providers.
DR DNASU; 56890; -.
DR Ensembl; ENST00000303145.11; ENSP00000302537.7; ENSG00000111554.15. [Q8TC05-1]
DR Ensembl; ENST00000393543.7; ENSP00000377175.3; ENSG00000111554.15. [Q8TC05-3]
DR Ensembl; ENST00000411698.6; ENSP00000391006.2; ENSG00000111554.15. [Q8TC05-4]
DR Ensembl; ENST00000430606.3; ENSP00000408694.2; ENSG00000111554.15. [Q8TC05-2]
DR GeneID; 56890; -.
DR KEGG; hsa:56890; -.
DR UCSC; uc001stz.3; human. [Q8TC05-1]
DR CTD; 56890; -.
DR DisGeNET; 56890; -.
DR GeneCards; MDM1; -.
DR HGNC; HGNC:29917; MDM1.
DR HPA; ENSG00000111554; Low tissue specificity.
DR MIM; 613813; gene.
DR neXtProt; NX_Q8TC05; -.
DR OpenTargets; ENSG00000111554; -.
DR PharmGKB; PA134879752; -.
DR VEuPathDB; HostDB:ENSG00000111554; -.
DR eggNOG; ENOG502QVRV; Eukaryota.
DR GeneTree; ENSGT00390000004106; -.
DR HOGENOM; CLU_023835_0_0_1; -.
DR InParanoid; Q8TC05; -.
DR OMA; KVNTEYR; -.
DR OrthoDB; 350018at2759; -.
DR PhylomeDB; Q8TC05; -.
DR TreeFam; TF331015; -.
DR PathwayCommons; Q8TC05; -.
DR SignaLink; Q8TC05; -.
DR BioGRID-ORCS; 56890; 14 hits in 1083 CRISPR screens.
DR ChiTaRS; MDM1; human.
DR GenomeRNAi; 56890; -.
DR Pharos; Q8TC05; Tbio.
DR PRO; PR:Q8TC05; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8TC05; protein.
DR Bgee; ENSG00000111554; Expressed in bronchial epithelial cell and 190 other tissues.
DR ExpressionAtlas; Q8TC05; baseline and differential.
DR Genevisible; Q8TC05; HS.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IMP:UniProtKB.
DR GO; GO:0046600; P:negative regulation of centriole replication; IMP:UniProtKB.
DR GO; GO:0060041; P:retina development in camera-type eye; IBA:GO_Central.
DR InterPro; IPR029136; MDM1.
DR PANTHER; PTHR32078; PTHR32078; 1.
DR Pfam; PF15501; MDM1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Cytoskeleton; Microtubule; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..714
FT /note="Nuclear protein MDM1"
FT /id="PRO_0000299059"
FT REGION 79..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 616..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 9..15
FT /note="ST]-E-Y-X(3)-F motif 1; required for efficient
FT microtubule binding and stabilization"
FT /evidence="ECO:0000269|PubMed:26337392"
FT MOTIF 189..195
FT /note="ST]-E-Y-X(3)-F motif 2; required for efficient
FT microtubule binding and stabilization"
FT /evidence="ECO:0000269|PubMed:26337392"
FT MOTIF 232..238
FT /note="ST]-E-Y-X(3)-F motif 3; required for efficient
FT microtubule binding and stabilization"
FT /evidence="ECO:0000269|PubMed:26337392"
FT MOTIF 306..312
FT /note="ST]-E-Y-X(3)-F motif 4; required for efficient
FT microtubule binding and stabilization"
FT /evidence="ECO:0000269|PubMed:26337392"
FT COMPBIAS 91..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..505
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 550..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..637
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D067"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D067"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D067"
FT MOD_RES 560
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D067"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 648
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 46..69
FT /note="ITKEPSFISKRRVPYHDPQISKSL -> NQGRCRTKIQHSDISSLLILVCST
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027544"
FT VAR_SEQ 70..714
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027545"
FT VAR_SEQ 167..222
FT /note="LDRLLRKKAGLTVVPSYNALRNSEYQRQFVWKTSKETAPAFAANQVFHNKSQ
FT FVPP -> VGIFTAFLFKSIEFFIGFIVISVILHFVFQNFPLLFSCLMSIRIVDNRLLT
FT LVIVN (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_027546"
FT VAR_SEQ 167..211
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046400"
FT VAR_SEQ 223..714
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_027547"
FT VAR_SEQ 335
FT /note="Q -> QGSLNAMWYAE (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046401"
FT VARIANT 103
FT /note="T -> I (in dbSNP:rs962976)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034782"
FT VARIANT 383
FT /note="V -> I (in dbSNP:rs17224810)"
FT /id="VAR_034783"
FT VARIANT 489
FT /note="R -> H (in dbSNP:rs2306393)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.5"
FT /id="VAR_034784"
FT VARIANT 552
FT /note="P -> L (in dbSNP:rs2306392)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_034785"
FT MUTAGEN 9..15
FT /note="SEYQRNF->AAAQRNA: Loss of microtubule binding, no
FT loss of centrosomal localization, little effect on
FT microtubule stability, loss of ability to block centriole
FT reduplication and defective blocking of normal centriole
FT duplication; when associated with 189-A--A-195; 232-A--A-
FT 238 and 306-A--A-312."
FT MUTAGEN 189..195
FT /note="SEYQRQF->AAAQRQA: Loss of microtubule binding, no
FT loss of centrosomal localization, little effect on
FT microtubule stability, loss of ability to block centriole
FT reduplication and defective blocking of normal centriole
FT duplication; when associated with 9-A--A-15; 232-A--A-238
FT and 306-A--A-312."
FT MUTAGEN 232..238
FT /note="TEYKRNF->AAAKRNA: Loss of microtubule binding, no
FT loss of centrosomal localization, little effect on
FT microtubule stability, loss of ability to block centriole
FT reduplication and defective blocking of normal centriole
FT duplication; when associated with 9-A--A-15; 189-A--A-195
FT and 306-A--A-312."
FT MUTAGEN 306..312
FT /note="SEYRAKF->AAARAKA: Loss of microtubule binding, no
FT loss of centrosomal localization, little effect on
FT microtubule stability, loss of ability to block centriole
FT reduplication and defective blocking of normal centriole
FT duplication; when associated with 9-A--A-15; 189-A--A-195
FT and 232-A--A-238."
FT CONFLICT 42
FT /note="D -> Y (in Ref. 2; BAG59777)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="G -> E (in Ref. 2; BAG59777)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 714 AA; 80735 MW; 301E3A89A5BFF13B CRC64;
MPVRFKGLSE YQRNFLWKKS YLSESCNSSV GRKYPWAGLR SDQLGITKEP SFISKRRVPY
HDPQISKSLE WNGAISESNV VASPEPEAPE TPKSQEAEQK DVTQERVHSL EASRVPKRTR
SHSADSRAEG ASDVENNEGV TNHTPVNENV ELEHSTKVLS ENVDNGLDRL LRKKAGLTVV
PSYNALRNSE YQRQFVWKTS KETAPAFAAN QVFHNKSQFV PPFKGNSVIH ETEYKRNFKG
LSPVKEPKLR NDLRENRNLE TVSPERKSNK IDDRLKLEAE MELKDLHQPK RKLTPWKHQR
LGKVNSEYRA KFLSPAQYLY KAGAWTHVKG NMPNQVKELR EKAEFYRKRV QGTHFSRDHL
NQILSDSNCC WDVSSTTSSE GTVSSNIRAL DLAGDPTSHK TLQKCPSTEP EEKGNIVEEQ
PQKNTTEKLG VSAPTIPVRR RLAWDTENTS EDVQKQPGEK EEEDDNEEEG DRKTGKQAFM
GEQEKLDVRE KSKADKMKEG SDSSVSSEKG GRLPTPKLRE LGGIQRTHHD LTTPAVGGAV
LVSPSKMKPP APEQRKRMTS QDCLETSKND FTKKESRAVS LLTSPAAGIK TVDPLPLRED
SEDNIHKFAE ATLPVSKIPK YPTNPPGQLP SPPHVPSYWH PSRRIQGSLR DPEFQHNVGK
ARMNNLQLPQ HEAFNDEDED RLSEISARSA ASSLRAFQTL ARAKKRKENF WGKT
