EMAL3_HUMAN
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 03-AUG-2022, entry version 147.
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};
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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; 62.
DR IntAct; Q32P44; 18.
DR MINT; Q32P44; -.
DR STRING; 9606.ENSP00000378254; -.
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; Q32P44; -.
DR PeptideAtlas; Q32P44; -.
DR PRIDE; Q32P44; -.
DR ProteomicsDB; 61624; -. [Q32P44-1]
DR ProteomicsDB; 61625; -. [Q32P44-2]
DR ProteomicsDB; 61626; -. [Q32P44-3]
DR Antibodypedia; 28533; 54 antibodies from 13 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 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; 271572at2759; -.
DR PhylomeDB; Q32P44; -.
DR TreeFam; TF317832; -.
DR PathwayCommons; Q32P44; -.
DR SignaLink; Q32P44; -.
DR BioGRID-ORCS; 256364; 16 hits in 1075 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 168 other tissues.
DR ExpressionAtlas; Q32P44; baseline and differential.
DR Genevisible; Q32P44; HS.
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 plate congression; IMP:UniProtKB.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 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_repeat.
DR Pfam; PF03451; HELP; 1.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF50998; SSF50998; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
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
