ID EMAL3_HUMAN Reviewed; 896 AA. AC Q32P44; Q6ZQW7; Q8NA55; DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot. DT 06-DEC-2005, sequence version 1. DT 24-JAN-2024, entry version 154. DE RecName: Full=Echinoderm microtubule-associated protein-like 3; DE Short=EMAP-3; GN Name=EML3; 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 [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 8-896 (ISOFORM 2). RC TISSUE=Testis, and Uterus; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Uterus; 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 [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176 AND THR-881, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [4] RP FUNCTION, SUBCELLULAR LOCATION, AND MICROTUBULE-BINDING. RX PubMed=18445686; DOI=10.1242/jcs.019174; RA Tegha-Dunghu J., Neumann B., Reber S., Krause R., Erfle H., Walter T., RA Held M., Rogers P., Hupfeld K., Ruppert T., Ellenberg J., Gruss O.J.; RT "EML3 is a nuclear microtubule-binding protein required for the correct RT alignment of chromosomes in metaphase."; RL J. Cell Sci. 121:1718-1726(2008). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY RP 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY RP 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY RP 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 [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; SER-198; SER-204 AND RP SER-883, 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-883, 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 [14] RP INTERACTION WITH EML2. RX PubMed=25740311; DOI=10.1042/bj20150039; RA Richards M.W., O'Regan L., Roth D., Montgomery J.M., Straube A., Fry A.M., RA Bayliss R.; RT "Microtubule association of EML proteins and the EML4-ALK variant 3 RT oncoprotein require an N-terminal trimerization domain."; RL Biochem. J. 467:529-536(2015). RN [15] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TUBG1; HAUS1; HAUS2; RP HAUS3; HAUS4; HAUS5; HAUS6; HAUS7 AND HAUS8, PHOSPHORYLATION AT THR-881, RP AND MUTAGENESIS OF THR-881; SER-883 AND SER-889. RX PubMed=30723163; DOI=10.1074/jbc.ra118.007164; RA Luo J., Yang B., Xin G., Sun M., Zhang B., Guo X., Jiang Q., Zhang C.; RT "The microtubule-associated protein EML3 regulates mitotic spindle assembly RT by recruiting the Augmin complex to spindle microtubules."; RL J. Biol. Chem. 294:5643-5656(2019). CC -!- FUNCTION: Regulates mitotic spindle assembly, microtubule (MT)- CC kinetochore attachment and chromosome separation via recruitment of CC HAUS augmin-like complex and TUBG1 to the existing MTs and promoting CC MT-based MT nucleation (PubMed:30723163). Required for proper CC alignnment of chromosomes during metaphase (PubMed:18445686). CC {ECO:0000269|PubMed:18445686, ECO:0000269|PubMed:30723163}. CC -!- SUBUNIT: Homotrimer; self-association is mediated by the N-terminal CC coiled coil (By similarity). Interacts with EML2 but not with EML1 CC (PubMed:25740311). Interacts (phosphorylated at Thr-881) with TUBG1, CC HAUS1, HAUS2, HAUS3, HAUS4, HAUS5, HAUS6, HAUS7 and HAUS8. CC {ECO:0000250|UniProtKB:Q9HC35, ECO:0000269|PubMed:25740311, CC ECO:0000269|PubMed:30723163}. CC -!- INTERACTION: CC Q32P44; P54253: ATXN1; NbExp=3; IntAct=EBI-1046713, EBI-930964; CC Q32P44; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-1046713, EBI-742054; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:18445686, ECO:0000305}. Cytoplasm CC {ECO:0000269|PubMed:18445686}. Nucleus {ECO:0000269|PubMed:18445686}. CC Midbody {ECO:0000269|PubMed:18445686}. Cytoplasm, cytoskeleton, spindle CC {ECO:0000269|PubMed:18445686, ECO:0000269|PubMed:30723163}. CC Note=Localizes to microtubules throughout all mitotic stages and CC localizes to the midbody during cytokinesis. CC {ECO:0000269|PubMed:18445686}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q32P44-1; Sequence=Displayed; CC Name=2; CC IsoId=Q32P44-2; Sequence=VSP_024483; CC Name=3; CC IsoId=Q32P44-3; Sequence=VSP_039926, VSP_039927, VSP_039928; CC -!- PTM: Phosphorylation at Thr-881 during mitosis is required for CC interaction with TUBG1, HAUS1, HAUS2, HAUS3, HAUS4, HAUS5, HAUS6, HAUS7 CC and HAUS8 and their recruitment to spindle microtubules. CC {ECO:0000269|PubMed:30723163}. CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA CC decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the WD repeat EMAP family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC04073.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAC87566.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK093146; BAC04073.1; ALT_INIT; mRNA. DR EMBL; AK128679; BAC87566.1; ALT_SEQ; mRNA. DR EMBL; BC108280; AAI08281.1; -; mRNA. DR CCDS; CCDS76415.1; -. [Q32P44-2] DR CCDS; CCDS8023.2; -. [Q32P44-1] DR RefSeq; NP_001287722.1; NM_001300793.1. DR RefSeq; NP_694997.2; NM_153265.2. [Q32P44-1] DR AlphaFoldDB; Q32P44; -. DR SMR; Q32P44; -. DR BioGRID; 129161; 67. DR IntAct; Q32P44; 19. DR MINT; Q32P44; -. DR STRING; 9606.ENSP00000434513; -. DR GlyCosmos; Q32P44; 4 sites, 1 glycan. DR GlyGen; Q32P44; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q32P44; -. DR PhosphoSitePlus; Q32P44; -. DR BioMuta; EML3; -. DR DMDM; 121945710; -. DR EPD; Q32P44; -. DR jPOST; Q32P44; -. DR MassIVE; Q32P44; -. DR MaxQB; Q32P44; -. DR PaxDb; 9606-ENSP00000378254; -. DR PeptideAtlas; Q32P44; -. DR ProteomicsDB; 61624; -. [Q32P44-1] DR ProteomicsDB; 61625; -. [Q32P44-2] DR ProteomicsDB; 61626; -. [Q32P44-3] DR Antibodypedia; 28533; 71 antibodies from 14 providers. DR DNASU; 256364; -. DR Ensembl; ENST00000394773.7; ENSP00000378254.2; ENSG00000149499.12. [Q32P44-1] DR Ensembl; ENST00000494448.5; ENSP00000431752.1; ENSG00000149499.12. [Q32P44-3] DR Ensembl; ENST00000529309.5; ENSP00000434513.1; ENSG00000149499.12. [Q32P44-2] DR GeneID; 256364; -. DR KEGG; hsa:256364; -. DR MANE-Select; ENST00000394773.7; ENSP00000378254.2; NM_153265.3; NP_694997.2. DR UCSC; uc001ntu.2; human. [Q32P44-1] DR AGR; HGNC:26666; -. DR CTD; 256364; -. DR DisGeNET; 256364; -. DR GeneCards; EML3; -. DR HGNC; HGNC:26666; EML3. DR HPA; ENSG00000149499; Low tissue specificity. DR MIM; 618118; gene. DR neXtProt; NX_Q32P44; -. DR OpenTargets; ENSG00000149499; -. DR PharmGKB; PA142671910; -. DR VEuPathDB; HostDB:ENSG00000149499; -. DR eggNOG; KOG2106; Eukaryota. DR GeneTree; ENSGT00940000159589; -. DR HOGENOM; CLU_1402011_0_0_1; -. DR InParanoid; Q32P44; -. DR OrthoDB; 2959353at2759; -. DR PhylomeDB; Q32P44; -. DR TreeFam; TF317832; -. DR PathwayCommons; Q32P44; -. DR SignaLink; Q32P44; -. DR BioGRID-ORCS; 256364; 16 hits in 1154 CRISPR screens. DR ChiTaRS; EML3; human. DR GenomeRNAi; 256364; -. DR Pharos; Q32P44; Tdark. DR PRO; PR:Q32P44; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q32P44; Protein. DR Bgee; ENSG00000149499; Expressed in lower esophagus mucosa and 170 other cell types or tissues. DR ExpressionAtlas; Q32P44; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:1990498; C:mitotic spindle microtubule; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005819; C:spindle; IDA:UniProtKB. DR GO; GO:0005876; C:spindle microtubule; IDA:UniProtKB. DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central. DR GO; GO:0043621; F:protein self-association; IPI:UniProtKB. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central. DR GO; GO:0007080; P:mitotic metaphase chromosome alignment; IMP:UniProtKB. DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2. DR InterPro; IPR005108; HELP. DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR13720:SF15; ECHINODERM MICROTUBULE-ASSOCIATED PROTEIN-LIKE 3; 1. DR PANTHER; PTHR13720; WD-40 REPEAT PROTEIN; 1. DR Pfam; PF03451; HELP; 1. DR Pfam; PF00400; WD40; 5. DR SMART; SM00320; WD40; 8. DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 2. DR PROSITE; PS50082; WD_REPEATS_2; 3. DR PROSITE; PS50294; WD_REPEATS_REGION; 1. DR Genevisible; Q32P44; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cell cycle; Cell division; Coiled coil; KW Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Nucleus; Phosphoprotein; KW Reference proteome; Repeat; WD repeat. FT CHAIN 1..896 FT /note="Echinoderm microtubule-associated protein-like 3" FT /id="PRO_0000284390" FT REPEAT 234..286 FT /note="WD 1" FT REPEAT 295..344 FT /note="WD 2" FT REPEAT 350..392 FT /note="WD 3" FT REPEAT 398..434 FT /note="WD 4" FT REPEAT 448..487 FT /note="WD 5" FT REPEAT 504..543 FT /note="WD 6" FT REPEAT 549..584 FT /note="WD 7" FT REPEAT 589..626 FT /note="WD 8" FT REPEAT 629..667 FT /note="WD 9" FT REPEAT 674..709 FT /note="WD 10" FT REPEAT 716..755 FT /note="WD 11" FT REPEAT 765..823 FT /note="WD 12" FT REPEAT 830..869 FT /note="WD 13" FT REGION 50..209 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 876..896 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 16..43 FT /evidence="ECO:0000255" FT COMPBIAS 78..93 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 113..133 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 149..165 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 172..193 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 176 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 198 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 204 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 881 FT /note="Phosphothreonine; by CDK1" FT /evidence="ECO:0000269|PubMed:30723163, FT ECO:0007744|PubMed:16964243" FT MOD_RES 883 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..29 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_039926" FT VAR_SEQ 152..223 FT /note="PRRNSSSSSSPSERPRQKLSRKAISSANLLVRSGSTESRGGKDPLSSPGGPG FT SRRSNYNLEGISVKMFLRGR -> AASAEALQEGNLLRQPVSAVREHREPWGKRPPLQP FT WGPWISEEQLQFGRHLSEDVPSRAPHYHVHPVWHPQP (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_039927" FT VAR_SEQ 224..896 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_039928" FT VAR_SEQ 786..896 FT /note="GVWPDGSDGTDINSLCRSHNERVVAVADDFCKVHLFQYPCARAKAPSRMYGG FT HGSHVTSVRFTHDDSHLVSLGGKDASIFQWRVLGAGGAGPAPATPSRTPSLSPASSLDV FT -> VPVRSCQGAEPHVRGPRQPRDQRPIHARRLAPRLAGRQGRQHLPVASAGRWGRGAG FT ARHALSNPLPVPRLLPRRLIAAWRDRLARRRGPAPPCPSLAQSPTTRGRLFPGLTSRHS FT RSRIFLEGANGAPAHTV (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_024483" FT VARIANT 620 FT /note="Q -> K (in dbSNP:rs34098002)" FT /id="VAR_031725" FT MUTAGEN 881 FT /note="T->A: Loss of phosphorylation and impaired FT interaction with TUBG1, HAUS2, HAUS3, HAUS4, HAUS5, HAUS6, FT HAUS7 and HAUS8." FT /evidence="ECO:0000269|PubMed:30723163" FT MUTAGEN 883 FT /note="S->A: No loss of phosphorylation." FT /evidence="ECO:0000269|PubMed:30723163" FT MUTAGEN 889 FT /note="S->A: No loss of phosphorylation." FT /evidence="ECO:0000269|PubMed:30723163" FT CONFLICT 65 FT /note="S -> SS (in Ref. 1; BAC04073)" FT /evidence="ECO:0000305" FT CONFLICT 381 FT /note="D -> N (in Ref. 1; BAC04073)" FT /evidence="ECO:0000305" FT VARIANT Q32P44-2:788 FT /note="V -> M (in dbSNP:rs34709729)" FT /evidence="ECO:0000305" FT /id="VAR_082934" SQ SEQUENCE 896 AA; 95197 MW; 21D2EBD29B969D34 CRC64; MDGAAGPGDG PAREALQSLS QRLRVQEQEM ELVKAALAEA LRLLRLQVPP SSLQGSGTPA PPGDSLAAPP GLPPTCTPSL VSRGTQTETE VELKSSPGPP GLSNGPPAPQ GASEEPSGTQ SEGGGSSSSG AGSPGPPGIL RPLQPPQRAD TPRRNSSSSS SPSERPRQKL SRKAISSANL LVRSGSTESR GGKDPLSSPG GPGSRRSNYN LEGISVKMFL RGRPITMYIP SGIRSLEELP SGPPPETLSL DWVYGYRGRD SRSNLFVLRS GEVVYFIACV VVLYRPGGGP GGPGGGGQRH YRGHTDCVRC LAVHPDGVRV ASGQTAGVDK DGKPLQPVVH IWDSETLLKL QEIGLGAFER GVGALAFSAA DQGAFLCVVD DSNEHMLSVW DCSRGMKLAE IKSTNDSVLA VGFNPRDSSC IVTSGKSHVH FWNWSGGVGV PGNGTLTRKQ GVFGKYKKPK FIPCFVFLPD GDILTGDSEG NILTWGRSPS DSKTPGRGGA KETYGIVAQA HAHEGSIFAL CLRRDGTVLS GGGRDRRLVQ WGPGLVALQE AEIPEHFGAV RAIAEGLGSE LLVGTTKNAL LRGDLAQGFS PVIQGHTDEL WGLCTHPSQN RFLTCGHDRQ LCLWDGESHA LAWSIDLKET GLCADFHPSG AVVAVGLNTG RWLVLDTETR EIVSDVIDGN EQLSVVRYSP DGLYLAIGSH DNVIYIYSVS SDGAKSSRFG RCMGHSSFIT HLDWSKDGNF IMSNSGDYEI LYWDVAGGCK QLKNRYESRD REWATYTCVL GFHVYGVWPD GSDGTDINSL CRSHNERVVA VADDFCKVHL FQYPCARAKA PSRMYGGHGS HVTSVRFTHD DSHLVSLGGK DASIFQWRVL GAGGAGPAPA TPSRTPSLSP ASSLDV //