TBB8_HUMAN
ID TBB8_HUMAN Reviewed; 444 AA.
AC Q3ZCM7; Q5SQX9; Q8WZ78;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Tubulin beta-8 chain {ECO:0000305};
DE AltName: Full=Tubulin beta 8 class VIII {ECO:0000312|HGNC:HGNC:20773};
GN Name=TUBB8 {ECO:0000312|HGNC:HGNC:20773};
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 [GENOMIC DNA].
RX PubMed=11731935; DOI=10.1086/338307;
RA van Geel M., Eichler E.E., Beck A.F., Shan Z., Haaf T.,
RA van der Maarel S.M., Frants R.R., de Jong P.J.;
RT "A cascade of complex subtelomeric duplications during the evolution of the
RT hominoid and Old World monkey genomes.";
RL Am. J. Hum. Genet. 70:269-278(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-444.
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 [6]
RP PHOSPHORYLATION AT SER-172.
RX PubMed=16371510; DOI=10.1091/mbc.e05-07-0621;
RA Fourest-Lieuvin A., Peris L., Gache V., Garcia-Saez I., Juillan-Binard C.,
RA Lantez V., Job D.;
RT "Microtubule regulation in mitosis: tubulin phosphorylation by the cyclin-
RT dependent kinase Cdk1.";
RL Mol. Biol. Cell 17:1041-1050(2006).
RN [7]
RP GLYCYLATION.
RX PubMed=19524510; DOI=10.1016/j.cell.2009.05.020;
RA Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N.,
RA Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.;
RT "Evolutionary divergence of enzymatic mechanisms for posttranslational
RT polyglycylation.";
RL Cell 137:1076-1087(2009).
RN [8]
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 [9]
RP GLUTAMYLATION.
RX PubMed=26875866; DOI=10.1016/j.cell.2016.01.019;
RA Valenstein M.L., Roll-Mecak A.;
RT "Graded control of microtubule severing by tubulin glutamylation.";
RL Cell 164:911-921(2016).
RN [10]
RP INVOLVEMENT IN OOMD2, VARIANTS OOMD2 27-GLU--ALA-33 DEL; LEU-176; VAL-210;
RP MET-238; MET-255; TRP-262; PRO-285 AND SER-348, AND CHARACTERIZATION OF
RP VARIANTS OOMD2 27-GLU--ALA-33 DEL; LEU-176; VAL-210; MET-238; MET-255;
RP TRP-262; PRO-285 AND SER-348.
RX PubMed=27273344; DOI=10.1136/jmedgenet-2016-103891;
RA Feng R., Yan Z., Li B., Yu M., Sang Q., Tian G., Xu Y., Chen B., Qu R.,
RA Sun Z., Sun X., Jin L., He L., Kuang Y., Cowan N.J., Wang L.;
RT "Mutations in TUBB8 cause a multiplicity of phenotypes in human oocytes and
RT early embryos.";
RL J. Med. Genet. 53:662-671(2016).
RN [11]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INVOLVEMENT IN OOMD2,
RP VARIANTS OOMD2 LYS-2; LEU-176; ALA-229; GLN-262; ILE-300; THR-363 AND
RP ASN-417, AND CHARACTERIZATION OF VARIANTS OOMD2 LYS-2; LEU-176; ALA-229;
RP GLN-262; ILE-300; THR-363 AND ASN-417.
RX PubMed=26789871; DOI=10.1056/nejmoa1510791;
RA Feng R., Sang Q., Kuang Y., Sun X., Yan Z., Zhang S., Shi J., Tian G.,
RA Luchniak A., Fukuda Y., Li B., Yu M., Chen J., Xu Y., Guo L., Qu R.,
RA Wang X., Sun Z., Liu M., Shi H., Wang H., Feng Y., Shao R., Chai R., Li Q.,
RA Xing Q., Zhang R., Nogales E., Jin L., He L., Gupta M.L. Jr., Cowan N.J.,
RA Wang L.;
RT "Mutations in TUBB8 and human oocyte meiotic arrest.";
RL N. Engl. J. Med. 374:223-232(2016).
CC -!- FUNCTION: Tubulin is the major constituent of microtubules. It binds
CC two moles of GTP, one at an exchangeable site on the beta chain and one
CC at a non-exchangeable site on the alpha chain (By similarity). TUBB8
CC has a key role in meiotic spindle assembly and oocyte maturation
CC (PubMed:26789871). {ECO:0000250, ECO:0000269|PubMed:26789871}.
CC -!- SUBUNIT: Dimer of alpha and beta chains. A typical microtubule is a
CC hollow water-filled tube with an outer diameter of 25 nm and an inner
CC diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to
CC form protofilaments running lengthwise along the microtubule wall with
CC the beta-tubulin subunit facing the microtubule plus end conferring a
CC structural polarity. Microtubules usually have 13 protofilaments but
CC different protofilament numbers can be found in some organisms and
CC specialized cells.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:26789871}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:26789871}.
CC -!- TISSUE SPECIFICITY: Expressed at a high level in oocytes, at different
CC stages of development. {ECO:0000269|PubMed:26789871}.
CC -!- DOMAIN: The MREI motif is common among all beta-tubulin isoforms and
CC may be critical for tubulin autoregulation.
CC {ECO:0000250|UniProtKB:P07437}.
CC -!- PTM: Some glutamate residues at the C-terminus are polyglutamylated,
CC resulting in polyglutamate chains on the gamma-carboxyl group
CC (PubMed:26875866). Polyglutamylation plays a key role in microtubule
CC severing by spastin (SPAST). SPAST preferentially recognizes and acts
CC on microtubules decorated with short polyglutamate tails: severing
CC activity by SPAST increases as the number of glutamates per tubulin
CC rises from one to eight, but decreases beyond this glutamylation
CC threshold (PubMed:26875866). Glutamylation is also involved in cilia
CC motility (By similarity). {ECO:0000250|UniProtKB:P99024,
CC ECO:0000269|PubMed:26875866}.
CC -!- PTM: Some glutamate residues at the C-terminus are monoglycylated but
CC not polyglycylated due to the absence of functional TTLL10 in human.
CC Monoglycylation is mainly limited to tubulin incorporated into cilia
CC and flagella axonemes, which is required for their stability and
CC maintenance. Flagella glycylation controls sperm motility. Both
CC polyglutamylation and monoglycylation can coexist on the same protein
CC on adjacent residues, and lowering glycylation levels increases
CC polyglutamylation, and reciprocally. {ECO:0000250|UniProtKB:P07437,
CC ECO:0000305|PubMed:19524510}.
CC -!- PTM: Phosphorylated on Ser-172 by CDK1 during the cell cycle, from
CC metaphase to telophase, but not in interphase. This phosphorylation
CC inhibits tubulin incorporation into microtubules.
CC {ECO:0000269|PubMed:16371510}.
CC -!- DISEASE: Oocyte maturation defect 2 (OOMD2) [MIM:616780]: An autosomal
CC dominant infertility disorder caused by defective oocyte maturation.
CC Oocytes are arrested at metaphase I, and have an abnormal or no
CC detectable spindle on polarization microscopy.
CC {ECO:0000269|PubMed:26789871, ECO:0000269|PubMed:27273344}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; AF355127; AAL32434.1; -; Genomic_DNA.
DR EMBL; CR590375; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL713922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW86545.1; -; Genomic_DNA.
DR EMBL; BC101270; AAI01271.1; -; mRNA.
DR EMBL; BC101271; AAI01272.1; -; mRNA.
DR CCDS; CCDS7051.1; -.
DR RefSeq; NP_817124.1; NM_177987.2.
DR AlphaFoldDB; Q3ZCM7; -.
DR SMR; Q3ZCM7; -.
DR BioGRID; 131462; 562.
DR IntAct; Q3ZCM7; 90.
DR MINT; Q3ZCM7; -.
DR STRING; 9606.ENSP00000456206; -.
DR ChEMBL; CHEMBL2095182; -.
DR DrugCentral; Q3ZCM7; -.
DR iPTMnet; Q3ZCM7; -.
DR MetOSite; Q3ZCM7; -.
DR PhosphoSitePlus; Q3ZCM7; -.
DR SwissPalm; Q3ZCM7; -.
DR BioMuta; TUBB8; -.
DR DMDM; 182705285; -.
DR EPD; Q3ZCM7; -.
DR jPOST; Q3ZCM7; -.
DR MassIVE; Q3ZCM7; -.
DR MaxQB; Q3ZCM7; -.
DR PaxDb; Q3ZCM7; -.
DR PeptideAtlas; Q3ZCM7; -.
DR PRIDE; Q3ZCM7; -.
DR ProteomicsDB; 61904; -.
DR Antibodypedia; 59334; 104 antibodies from 22 providers.
DR DNASU; 347688; -.
DR Ensembl; ENST00000568584.6; ENSP00000456206.2; ENSG00000261456.6.
DR GeneID; 347688; -.
DR KEGG; hsa:347688; -.
DR MANE-Select; ENST00000568584.6; ENSP00000456206.2; NM_177987.3; NP_817124.1.
DR UCSC; uc001ifi.3; human.
DR CTD; 347688; -.
DR DisGeNET; 347688; -.
DR GeneCards; TUBB8; -.
DR HGNC; HGNC:20773; TUBB8.
DR HPA; ENSG00000261456; Tissue enhanced (testis).
DR MalaCards; TUBB8; -.
DR MIM; 616768; gene.
DR MIM; 616780; phenotype.
DR neXtProt; NX_Q3ZCM7; -.
DR OpenTargets; ENSG00000261456; -.
DR Orphanet; 488191; Female infertility due to oocyte meiotic arrest.
DR VEuPathDB; HostDB:ENSG00000261456; -.
DR eggNOG; KOG1375; Eukaryota.
DR GeneTree; ENSGT00940000161436; -.
DR InParanoid; Q3ZCM7; -.
DR OMA; NARNMMA; -.
DR OrthoDB; 962471at2759; -.
DR PhylomeDB; Q3ZCM7; -.
DR TreeFam; TF300298; -.
DR PathwayCommons; Q3ZCM7; -.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
DR Reactome; R-HSA-190861; Gap junction assembly.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-437239; Recycling pathway of L1.
DR Reactome; R-HSA-5617833; Cilium Assembly.
DR Reactome; R-HSA-5626467; RHO GTPases activate IQGAPs.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9609736; Assembly and cell surface presentation of NMDA receptors.
DR Reactome; R-HSA-9619483; Activation of AMPK downstream of NMDARs.
DR Reactome; R-HSA-9646399; Aggrephagy.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-HSA-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q3ZCM7; -.
DR BioGRID-ORCS; 347688; 372 hits in 992 CRISPR screens.
DR GenomeRNAi; 347688; -.
DR Pharos; Q3ZCM7; Tclin.
DR PRO; PR:Q3ZCM7; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q3ZCM7; protein.
DR Bgee; ENSG00000261456; Expressed in cortical plate and 83 other tissues.
DR ExpressionAtlas; Q3ZCM7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; IDA:HPA.
DR GO; GO:0072687; C:meiotic spindle; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0072686; C:mitotic spindle; IDA:HPA.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
DR GO; GO:0001556; P:oocyte maturation; IMP:UniProtKB.
DR GO; GO:0007056; P:spindle assembly involved in female meiosis; IMP:UniProtKB.
DR Gene3D; 1.10.287.600; -; 1.
DR Gene3D; 3.30.1330.20; -; 1.
DR Gene3D; 3.40.50.1440; -; 1.
DR InterPro; IPR013838; Beta-tubulin_BS.
DR InterPro; IPR002453; Beta_tubulin.
DR InterPro; IPR008280; Tub_FtsZ_C.
DR InterPro; IPR000217; Tubulin.
DR InterPro; IPR037103; Tubulin/FtsZ-like_C.
DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom.
DR InterPro; IPR036525; Tubulin/FtsZ_GTPase_sf.
DR InterPro; IPR023123; Tubulin_C.
DR InterPro; IPR017975; Tubulin_CS.
DR InterPro; IPR003008; Tubulin_FtsZ_GTPase.
DR PANTHER; PTHR11588; PTHR11588; 1.
DR Pfam; PF00091; Tubulin; 1.
DR Pfam; PF03953; Tubulin_C; 1.
DR PRINTS; PR01163; BETATUBULIN.
DR PRINTS; PR01161; TUBULIN.
DR SMART; SM00864; Tubulin; 1.
DR SMART; SM00865; Tubulin_C; 1.
DR SUPFAM; SSF52490; SSF52490; 1.
DR SUPFAM; SSF55307; SSF55307; 1.
DR PROSITE; PS00227; TUBULIN; 1.
DR PROSITE; PS00228; TUBULIN_B_AUTOREG; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Disease variant; GTP-binding; Isopeptide bond;
KW Microtubule; Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..444
FT /note="Tubulin beta-8 chain"
FT /id="PRO_0000320631"
FT REGION 423..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1..4
FT /note="MREI motif"
FT /evidence="ECO:0000250|UniProtKB:P07437"
FT COMPBIAS 427..444
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 140..146
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255"
FT MOD_RES 172
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000269|PubMed:16371510"
FT MOD_RES 436
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000250|UniProtKB:Q2T9S0"
FT VARIANT 2
FT /note="R -> K (in OOMD2; loss of function in oocyte
FT maturation; decreased alpha/beta-tubulin heterodimer
FT assembly; dbSNP:rs869025273)"
FT /evidence="ECO:0000269|PubMed:26789871"
FT /id="VAR_076898"
FT VARIANT 27..33
FT /note="Missing (in OOMD2; loss of alpha/beta-tubulin
FT heterodimer assembly; loss of function in meiotic spindle
FT assembly)"
FT /evidence="ECO:0000269|PubMed:27273344"
FT /id="VAR_076899"
FT VARIANT 176
FT /note="S -> L (in OOMD2; loss of function in oocyte
FT maturation; loss of function in meiotic spindle assembly;
FT decreased alpha/beta-tubulin heterodimer assembly;
FT dbSNP:rs869025609)"
FT /evidence="ECO:0000269|PubMed:26789871,
FT ECO:0000269|PubMed:27273344"
FT /id="VAR_076900"
FT VARIANT 210
FT /note="I -> V (in OOMD2; decreased alpha/beta-tubulin
FT heterodimer assembly; loss of function in meiotic spindle
FT assembly; dbSNP:rs781853492)"
FT /evidence="ECO:0000269|PubMed:27273344"
FT /id="VAR_076901"
FT VARIANT 229
FT /note="V -> A (in OOMD2; loss of function in oocyte
FT maturation; decreased alpha/beta-tubulin heterodimer
FT assembly; dbSNP:rs869025271)"
FT /evidence="ECO:0000269|PubMed:26789871"
FT /id="VAR_076902"
FT VARIANT 238
FT /note="T -> M (in OOMD2; decreased alpha/beta-tubulin
FT heterodimer assembly; loss of function in meiotic spindle
FT assembly; dbSNP:rs1057520306)"
FT /evidence="ECO:0000269|PubMed:27273344"
FT /id="VAR_076903"
FT VARIANT 255
FT /note="V -> M (in OOMD2; loss of function in meiotic
FT spindle assembly; dbSNP:rs782269374)"
FT /evidence="ECO:0000269|PubMed:27273344"
FT /id="VAR_076904"
FT VARIANT 262
FT /note="R -> Q (in OOMD2; loss of function in oocyte
FT maturation; decreased alpha/beta-tubulin heterodimer
FT assembly; dbSNP:rs869025610)"
FT /evidence="ECO:0000269|PubMed:26789871"
FT /id="VAR_076905"
FT VARIANT 262
FT /note="R -> W (in OOMD2; decreased alpha/beta-tubulin
FT heterodimer assembly; does not affect function in meiotic
FT spindle assembly; dbSNP:rs782486119)"
FT /evidence="ECO:0000269|PubMed:27273344"
FT /id="VAR_076906"
FT VARIANT 285
FT /note="T -> P (in OOMD2; loss of function in meiotic
FT spindle assembly)"
FT /evidence="ECO:0000269|PubMed:27273344"
FT /id="VAR_076907"
FT VARIANT 300
FT /note="M -> I (in OOMD2; loss of function in oocyte
FT maturation; decreased alpha/beta-tubulin heterodimer
FT assembly; dbSNP:rs869025612)"
FT /evidence="ECO:0000269|PubMed:26789871"
FT /id="VAR_076908"
FT VARIANT 345
FT /note="L -> F (in dbSNP:rs4880608)"
FT /id="VAR_039240"
FT VARIANT 348
FT /note="N -> S (in OOMD2; loss of function in meiotic
FT spindle assembly; dbSNP:rs1270068662)"
FT /evidence="ECO:0000269|PubMed:27273344"
FT /id="VAR_076909"
FT VARIANT 363
FT /note="M -> T (in OOMD2; loss of function in oocyte
FT maturation; decreased alpha/beta-tubulin heterodimer
FT assembly; dbSNP:rs869025611)"
FT /evidence="ECO:0000269|PubMed:26789871"
FT /id="VAR_076910"
FT VARIANT 417
FT /note="D -> N (in OOMD2; loss of function in oocyte
FT maturation; loss of function in meiotic spindle assembly;
FT decreased alpha/beta-tubulin heterodimer assembly;
FT dbSNP:rs869025272)"
FT /evidence="ECO:0000269|PubMed:26789871"
FT /id="VAR_076911"
SQ SEQUENCE 444 AA; 49776 MW; 3EC4AC10946BF590 CRC64;
MREIVLTQIG QCGNQIGAKF WEVISDEHAI DSAGTYHGDS HLQLERINVY YNEASGGRYV
PRAVLVDLEP GTMDSVRSGP FGQVFRPDNF IFGQCGAGNN WAKGHYTEGA ELMESVMDVV
RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LLSKIREEYP DRIINTFSIL PSPKVSDTVV
EPYNATLSVH QLIENADETF CIDNEALYDI CSKTLKLPTP TYGDLNHLVS ATMSGVTTCL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVAELT QQMFDAKNMM
AACDPRHGRY LTAAAIFRGR MPMREVDEQM FNIQDKNSSY FADWLPNNVK TAVCDIPPRG
LKMSATFIGN NTAIQELFKR VSEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA EEEEDEEYAE EEVA
