TBB3_MOUSE
ID TBB3_MOUSE Reviewed; 450 AA.
AC Q9ERD7; Q3UF42; Q5I036;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Tubulin beta-3 chain;
GN Name=Tubb3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wu Y., Li C., Zhao S.;
RT "Cloning and sequencing of mouse tubulin beta-3 isotype.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, Spinal ganglion, and Sympathetic ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Olfactory epithelium, and Retina;
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 [4]
RP PROTEIN SEQUENCE OF 63-77; 104-121; 217-251; 253-276; 310-318; 337-350 AND
RP 381-390, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP GLUTAMYLATION.
RX PubMed=15890843; DOI=10.1126/science.1113010;
RA Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M.,
RA Temurak N., van Dijk J., Boucher D., van Dorsselaer A., Suryavanshi S.,
RA Gaertig J., Edde B.;
RT "Tubulin polyglutamylase enzymes are members of the TTL domain protein
RT family.";
RL Science 308:1758-1762(2005).
RN [6]
RP PHOSPHORYLATION AT SER-172 BY CDK1.
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 FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-262.
RX PubMed=20074521; DOI=10.1016/j.cell.2009.12.011;
RA Tischfield M.A., Baris H.N., Wu C., Rudolph G., Van Maldergem L., He W.,
RA Chan W.M., Andrews C., Demer J.L., Robertson R.L., Mackey D.A.,
RA Ruddle J.B., Bird T.D., Gottlob I., Pieh C., Traboulsi E.I., Pomeroy S.L.,
RA Hunter D.G., Soul J.S., Newlin A., Sabol L.J., Doherty E.J.,
RA de Uzcategui C.E., de Uzcategui N., Collins M.L., Sener E.C., Wabbels B.,
RA Hellebrand H., Meitinger T., de Berardinis T., Magli A., Schiavi C.,
RA Pastore-Trossello M., Koc F., Wong A.M., Levin A.V., Geraghty M.T.,
RA Descartes M., Flaherty M., Jamieson R.V., Moller H.U., Meuthen I.,
RA Callen D.F., Kerwin J., Lindsay S., Meindl A., Gupta M.L. Jr., Pellman D.,
RA Engle E.C.;
RT "Human TUBB3 mutations perturb microtubule dynamics, kinesin interactions,
RT and axon guidance.";
RL Cell 140:74-87(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP GLYCYLATION, AND GLUTAMYLATION.
RX PubMed=23897886; DOI=10.1083/jcb.201305041;
RA Bosch Grau M., Gonzalez Curto G., Rocha C., Magiera M.M., Marques Sousa P.,
RA Giordano T., Spassky N., Janke C.;
RT "Tubulin glycylases and glutamylases have distinct functions in
RT stabilization and motility of ependymal cilia.";
RL J. Cell Biol. 202:441-451(2013).
RN [11]
RP FUNCTION, INTERACTION WITH UNC5C, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=28483977; DOI=10.1523/jneurosci.2617-16.2017;
RA Shao Q., Yang T., Huang H., Alarmanazi F., Liu G.;
RT "Uncoupling of UNC5C with Polymerized TUBB3 in Microtubules Mediates
RT Netrin-1 Repulsion.";
RL J. Neurosci. 37:5620-5633(2017).
RN [12]
RP GLYCYLATION.
RX PubMed=33414192; DOI=10.1126/science.abd4914;
RA Gadadhar S., Alvarez Viar G., Hansen J.N., Gong A., Kostarev A.,
RA Ialy-Radio C., Leboucher S., Whitfield M., Ziyyat A., Toure A., Alvarez L.,
RA Pigino G., Janke C.;
RT "Tubulin glycylation controls axonemal dynein activity, flagellar beat, and
RT male fertility.";
RL Science 371:0-0(2021).
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. TUBB3 plays a critical
CC role in proper axon guidance and maintenance. Binding of NTN1/Netrin-1
CC to its receptor UNC5C might cause dissociation of UNC5C from
CC polymerized TUBB3 in microtubules and thereby lead to increased
CC microtubule dynamics and axon repulsion (PubMed:28483977). Plays a role
CC in dorsal root ganglion axon projection towards the spinal cord (By
CC similarity). {ECO:0000250|UniProtKB:Q13509,
CC ECO:0000269|PubMed:20074521, ECO:0000269|PubMed:28483977}.
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. Interacts with UNC5C (via cytoplasmic domain); this
CC interaction is decreased by NTN1/Netrin-1 (PubMed:28483977). Interacts
CC with NLRP5/MATER at cytoskeleton microtubules (By similarity).
CC Interacts with DPYSL5 (By similarity). {ECO:0000250|UniProtKB:Q13509,
CC ECO:0000269|PubMed:28483977}.
CC -!- INTERACTION:
CC Q9ERD7; P47757: Capzb; NbExp=2; IntAct=EBI-2255594, EBI-299194;
CC Q9ERD7; O08747: Unc5c; NbExp=3; IntAct=EBI-2255594, EBI-21004500;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:20074521}. Cell projection, growth cone
CC {ECO:0000269|PubMed:28483977}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:28483977}. Cell projection, filopodium
CC {ECO:0000269|PubMed:28483977}.
CC -!- TISSUE SPECIFICITY: Expressed in the external granular layer cells of
CC the cerebellar cortex (at protein level).
CC {ECO:0000269|PubMed:28483977}.
CC -!- DEVELOPMENTAL STAGE: Detected at postnatal day 2 and 4.
CC {ECO:0000269|PubMed:28483977}.
CC -!- DOMAIN: The highly acidic C-terminal region may bind cations such as
CC calcium.
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 polyglycylated,
CC resulting in polyglycine chains on the gamma-carboxyl group.
CC Glycylation is mainly limited to tubulin incorporated into axonemes
CC (cilia and flagella) whereas glutamylation is prevalent in neuronal
CC cells, centrioles, axonemes, and the mitotic spindle. Both
CC modifications can coexist on the same protein on adjacent residues, and
CC lowering polyglycylation levels increases polyglutamylation, and
CC reciprocally. Cilia and flagella glycylation is required for their
CC stability and maintenance. Flagella glycylation controls sperm motility
CC (PubMed:33414192). {ECO:0000269|PubMed:19524510,
CC ECO:0000269|PubMed:23897886, ECO:0000269|PubMed:33414192}.
CC -!- PTM: Some glutamate residues at the C-terminus are polyglutamylated,
CC resulting in polyglutamate chains on the gamma-carboxyl group
CC (PubMed:15890843). 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 (By similarity). Glutamylation is also involved in cilia
CC motility (PubMed:23897886). {ECO:0000250|UniProtKB:Q71U36,
CC ECO:0000269|PubMed:15890843, ECO:0000269|PubMed:23897886}.
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 -!- SIMILARITY: Belongs to the tubulin family. {ECO:0000305}.
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DR EMBL; AF312873; AAG26010.1; -; mRNA.
DR EMBL; AK012528; BAB28299.1; -; mRNA.
DR EMBL; AK051298; BAC34596.1; -; mRNA.
DR EMBL; AK149014; BAE28719.1; -; mRNA.
DR EMBL; BC031357; AAH31357.1; -; mRNA.
DR EMBL; BC088749; AAH88749.1; -; mRNA.
DR CCDS; CCDS22757.1; -.
DR RefSeq; NP_075768.1; NM_023279.2.
DR AlphaFoldDB; Q9ERD7; -.
DR SMR; Q9ERD7; -.
DR BioGRID; 204379; 19.
DR DIP; DIP-48419N; -.
DR IntAct; Q9ERD7; 16.
DR MINT; Q9ERD7; -.
DR STRING; 10090.ENSMUSP00000071134; -.
DR CarbonylDB; Q9ERD7; -.
DR iPTMnet; Q9ERD7; -.
DR PhosphoSitePlus; Q9ERD7; -.
DR SwissPalm; Q9ERD7; -.
DR REPRODUCTION-2DPAGE; IPI00112251; -.
DR REPRODUCTION-2DPAGE; Q9ERD7; -.
DR UCD-2DPAGE; Q9ERD7; -.
DR EPD; Q9ERD7; -.
DR jPOST; Q9ERD7; -.
DR MaxQB; Q9ERD7; -.
DR PaxDb; Q9ERD7; -.
DR PeptideAtlas; Q9ERD7; -.
DR PRIDE; Q9ERD7; -.
DR ProteomicsDB; 254859; -.
DR TopDownProteomics; Q9ERD7; -.
DR DNASU; 22152; -.
DR Ensembl; ENSMUST00000071134; ENSMUSP00000071134; ENSMUSG00000062380.
DR GeneID; 22152; -.
DR KEGG; mmu:22152; -.
DR UCSC; uc009nvt.1; mouse.
DR CTD; 10381; -.
DR MGI; MGI:107813; Tubb3.
DR VEuPathDB; HostDB:ENSMUSG00000062380; -.
DR eggNOG; KOG1375; Eukaryota.
DR GeneTree; ENSGT00940000159115; -.
DR HOGENOM; CLU_015718_1_1_1; -.
DR InParanoid; Q9ERD7; -.
DR OMA; EMEGECV; -.
DR OrthoDB; 962471at2759; -.
DR PhylomeDB; Q9ERD7; -.
DR TreeFam; TF300298; -.
DR Reactome; R-MMU-190840; Microtubule-dependent trafficking of connexons from Golgi to the plasma membrane.
DR Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-MMU-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-MMU-437239; Recycling pathway of L1.
DR Reactome; R-MMU-5610787; Hedgehog 'off' state.
DR Reactome; R-MMU-5617833; Cilium Assembly.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-MMU-8955332; Carboxyterminal post-translational modifications of tubulin.
DR Reactome; R-MMU-9646399; Aggrephagy.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-MMU-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR Reactome; R-MMU-983189; Kinesins.
DR BioGRID-ORCS; 22152; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Tubb3; mouse.
DR PRO; PR:Q9ERD7; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9ERD7; protein.
DR Bgee; ENSMUSG00000062380; Expressed in cortical plate and 202 other tissues.
DR ExpressionAtlas; Q9ERD7; baseline and differential.
DR Genevisible; Q9ERD7; MM.
DR GO; GO:0030424; C:axon; IDA:ARUK-UCL.
DR GO; GO:0071944; C:cell periphery; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0030425; C:dendrite; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IDA:UniProtKB.
DR GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0072686; C:mitotic spindle; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005525; F:GTP binding; IBA:GO_Central.
DR GO; GO:1990890; F:netrin receptor binding; IPI:UniProtKB.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IBA:GO_Central.
DR GO; GO:0007411; P:axon guidance; IMP:UniProtKB.
DR GO; GO:1990791; P:dorsal root ganglion development; ISS:UniProtKB.
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; ISO:MGI.
DR GO; GO:0038007; P:netrin-activated signaling pathway; IMP:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; ISO:MGI.
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 Cell projection; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW GTP-binding; Isopeptide bond; Microtubule; Nucleotide-binding;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..450
FT /note="Tubulin beta-3 chain"
FT /id="PRO_0000048251"
FT REGION 422..450
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 431..450
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 438
FT /note="5-glutamyl polyglutamate"
FT /evidence="ECO:0000250|UniProtKB:Q2T9S0"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q2T9S0"
FT MUTAGEN 262
FT /note="R->C: Brain from homozygous mice shows defects in
FT the guidance of commissural axons and nerves, without
FT evidence of cortical cells migration defects."
FT /evidence="ECO:0000269|PubMed:20074521"
FT CONFLICT 206
FT /note="A -> S (in Ref. 2; BAE28719)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 450 AA; 50419 MW; 4B9D9B7DBA102949 CRC64;
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPSGNYVGDS DLQLERISVY YNEASSHKYV
PRAILVDLEP GTMDSVRSGA FGHLFRPDNF IFGQSGAGNN WAKGHYTEGA ELVDSVLDVV
RKECENCDCL QGFQLTHSLG GGTGSGMGTL LISKVREEYP DRIMNTFSVV PSPKVSDTVV
EPYNATLSIH QLVENTDETY CIDNEALYDI CFRTLKLATP TYGDLNHLVS ATMSGVTTSL
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTARGSQQ YRALTVPELT QQMFDAKNMM
AACDPRHGRY LTVATVFRGR MSMKEVDEQM LAIQSKNSSY FVEWIPNNVK VAVCDIPPRG
LKMSSTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS
EYQQYQDATA EEEGEMYEDD DEESEAQGPK
