ID TTLL1_HUMAN Reviewed; 423 AA. AC O95922; B2RDS7; Q9BR27; Q9NRS9; Q9UMU0; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1999, sequence version 1. DT 29-MAY-2024, entry version 181. DE RecName: Full=Polyglutamylase complex subunit TTLL1 {ECO:0000250|UniProtKB:Q91V51}; DE EC=6.3.2.- {ECO:0000250|UniProtKB:Q91V51}; DE AltName: Full=Tubulin polyglutamylase TTLL1; DE AltName: Full=Tubulin polyglutamylase complex subunit 3 {ECO:0000250|UniProtKB:Q91V51}; DE Short=PGs3 {ECO:0000250|UniProtKB:Q91V51}; DE AltName: Full=Tubulin--tyrosine ligase-like protein 1 {ECO:0000250|UniProtKB:Q91V51}; GN Name=TTLL1 {ECO:0000312|HGNC:HGNC:1312}; Synonyms=C22orf7; 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] (ISOFORMS A AND B), AND TISSUE SPECIFICITY. RX PubMed=11054573; DOI=10.1016/s0378-1119(00)00383-8; RA Trichet V., Ruault M., Roizes G., De Sario A.; RT "Characterization of the human tubulin tyrosine ligase-like 1 gene (TTLL1) RT mapping to 22q13.1."; RL Gene 257:109-117(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC TISSUE=Brain; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A; B AND 4). RX PubMed=12529303; DOI=10.1101/gr.695703; RA Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., RA Bye J.M., Beare D.M., Dunham I.; RT "Reevaluating human gene annotation: a second-generation analysis of RT chromosome 22."; RL Genome Res. 13:27-36(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:R84.1-R84.11(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC TISSUE=Testis; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C., RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., RA Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [7] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). RC TISSUE=Eye; 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 [9] RP INTERACTION WITH PCM1; CSTPP1 AND LRRC49, FUNCTION, AND MUTAGENESIS OF RP GLU-326. RX PubMed=34782749; DOI=10.1038/s41422-021-00584-9; RA Wang L., Paudyal S.C., Kang Y., Owa M., Liang F.X., Spektor A., Knaut H., RA Sanchez I., Dynlacht B.D.; RT "Regulators of tubulin polyglutamylation control nuclear shape and cilium RT disassembly by balancing microtubule and actin assembly."; RL Cell Res. 32:190-209(2022). CC -!- FUNCTION: Catalytic subunit of a polyglutamylase complex which modifies CC tubulin, generating side chains of glutamate on the gamma-carboxyl CC group of specific glutamate residues within the C-terminal tail of CC tubulin (PubMed:34782749). Probably involved in the side-chain CC elongation step of the polyglutamylation reaction rather than the CC initiation step. Modifies both alpha- and beta-tubulins with a CC preference for the alpha-tail. Unlike most polyglutamylases of the CC tubulin--tyrosine ligase family, only displays a catalytic activity CC when in complex with other proteins as it is most likely lacking CC domains important for autonomous activity. Part of the neuronal tubulin CC polyglutamylase complex. Mediates cilia and flagella polyglutamylation CC which is essential for their biogenesis and motility. Involved in CC respiratory motile cilia function through the regulation of beating CC asymmetry. Essential for sperm flagella biogenesis, motility and male CC fertility. Involved in KLF4 glutamylation which impedes its CC ubiquitination, thereby leading to somatic cell reprogramming, CC pluripotency maintenance and embryogenesis. CC {ECO:0000250|UniProtKB:Q91V51, ECO:0000269|PubMed:34782749}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + ATP + CC L-glutamate = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] CC + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60148, Rhea:RHEA-COMP:15519, CC Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:143623, CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:Q91V51}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60149; CC Evidence={ECO:0000250|UniProtKB:Q91V51}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:A4Q9E8}; CC -!- SUBUNIT: Part of the neuronal tubulin polyglutamylase complex which CC contains TPGS1, TPGS2, TTLL1, LRRC49 and NICN1. Interacts with PCM1, CC CSTPP1 and LRRC49 (PubMed:34782749). {ECO:0000250|UniProtKB:Q91V51, CC ECO:0000269|PubMed:34782749}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000250|UniProtKB:Q91V51}. Cytoplasm, cytoskeleton, cilium basal CC body {ECO:0000250|UniProtKB:Q91V51}. Cytoplasm, cytoskeleton, cilium CC axoneme {ECO:0000250|UniProtKB:Q91V51}. Cell projection, cilium, CC flagellum {ECO:0000250|UniProtKB:Q91V51}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist.; CC Name=A; Synonyms=TTLL1a; CC IsoId=O95922-1; Sequence=Displayed; CC Name=B; Synonyms=TTLL1b, Truncated; CC IsoId=O95922-2; Sequence=VSP_006671, VSP_006672; CC Name=4; CC IsoId=O95922-4; Sequence=VSP_011825; CC -!- TISSUE SPECIFICITY: Expressed in a wide range of tissues. Has a CC stronger expression in heart, brain and testis. CC {ECO:0000269|PubMed:11054573}. CC -!- DOMAIN: Gln-144 is the main determinant for regioselectivity, which CC segregates between initiases and elongases in all tubulin--tyrosine CC ligase family. A glutamine residue at this position is found in CC elongases TTLL6, TTLL9, TTLL11, TTLL13, TTLL10 and favors glutamate- CC chain elongation, whereas an arginine residue is found in initiases CC TTLL2, TTLL4, TTLL5, TTLL3, TTLL8 and favors initiation. CC {ECO:0000250|UniProtKB:A4Q9E8}. CC -!- SIMILARITY: Belongs to the tubulin polyglutamylase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAB51423.1; 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; AF104927; AAG29879.1; -; mRNA. DR EMBL; AF173935; AAF91088.1; -; mRNA. DR EMBL; AL136687; CAB66622.1; -; mRNA. DR EMBL; AL096883; CAB51423.1; ALT_SEQ; mRNA. DR EMBL; AL096886; CAB51469.1; -; mRNA. DR EMBL; AL589867; CAC34478.1; -; mRNA. DR EMBL; CR456599; CAG30485.1; -; mRNA. DR EMBL; AK315658; BAG38024.1; -; mRNA. DR EMBL; AL022476; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471138; EAW73279.1; -; Genomic_DNA. DR EMBL; BC014968; AAH14968.1; -; mRNA. DR CCDS; CCDS14043.1; -. [O95922-1] DR RefSeq; NP_036395.1; NM_012263.4. [O95922-1] DR RefSeq; XP_011528410.1; XM_011530108.2. DR RefSeq; XP_016884240.1; XM_017028751.1. DR RefSeq; XP_016884241.1; XM_017028752.1. DR RefSeq; XP_016884242.1; XM_017028753.1. DR AlphaFoldDB; O95922; -. DR SMR; O95922; -. DR BioGRID; 117340; 25. DR ComplexPortal; CPX-2572; Tubulin polyglutamylase complex. DR IntAct; O95922; 20. DR STRING; 9606.ENSP00000266254; -. DR GlyGen; O95922; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O95922; -. DR PhosphoSitePlus; O95922; -. DR BioMuta; TTLL1; -. DR EPD; O95922; -. DR jPOST; O95922; -. DR MassIVE; O95922; -. DR PaxDb; 9606-ENSP00000266254; -. DR PeptideAtlas; O95922; -. DR ProteomicsDB; 51124; -. [O95922-1] DR ProteomicsDB; 51126; -. [O95922-4] DR Antibodypedia; 27458; 52 antibodies from 19 providers. DR DNASU; 25809; -. DR Ensembl; ENST00000266254.12; ENSP00000266254.7; ENSG00000100271.17. [O95922-1] DR Ensembl; ENST00000331018.8; ENSP00000333734.7; ENSG00000100271.17. [O95922-4] DR Ensembl; ENST00000439248.5; ENSP00000401518.1; ENSG00000100271.17. [O95922-2] DR Ensembl; ENST00000440761.1; ENSP00000403332.1; ENSG00000100271.17. [O95922-2] DR GeneID; 25809; -. DR KEGG; hsa:25809; -. DR MANE-Select; ENST00000266254.12; ENSP00000266254.7; NM_012263.5; NP_036395.1. DR UCSC; uc003bdi.5; human. [O95922-1] DR AGR; HGNC:1312; -. DR CTD; 25809; -. DR DisGeNET; 25809; -. DR GeneCards; TTLL1; -. DR HGNC; HGNC:1312; TTLL1. DR HPA; ENSG00000100271; Low tissue specificity. DR MIM; 608955; gene. DR neXtProt; NX_O95922; -. DR OpenTargets; ENSG00000100271; -. DR PharmGKB; PA35030; -. DR VEuPathDB; HostDB:ENSG00000100271; -. DR eggNOG; KOG2157; Eukaryota. DR GeneTree; ENSGT00940000156720; -. DR HOGENOM; CLU_2960116_0_0_1; -. DR InParanoid; O95922; -. DR OMA; DWNFYWS; -. DR OrthoDB; 7265at2759; -. DR PhylomeDB; O95922; -. DR TreeFam; TF313087; -. DR PathwayCommons; O95922; -. DR Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin. DR SignaLink; O95922; -. DR BioGRID-ORCS; 25809; 12 hits in 1145 CRISPR screens. DR ChiTaRS; TTLL1; human. DR GeneWiki; TTLL1; -. DR GenomeRNAi; 25809; -. DR Pharos; O95922; Tdark. DR PRO; PR:O95922; -. DR Proteomes; UP000005640; Chromosome 22. DR RNAct; O95922; Protein. DR Bgee; ENSG00000100271; Expressed in cortical plate and 151 other cell types or tissues. DR ExpressionAtlas; O95922; baseline and differential. DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl. DR GO; GO:0005929; C:cilium; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005576; C:extracellular region; IEA:GOC. DR GO; GO:0005874; C:microtubule; IDA:UniProt. DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015631; F:tubulin binding; IBA:GO_Central. DR GO; GO:0070740; F:tubulin-glutamic acid ligase activity; IDA:UniProt. DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IEA:Ensembl. DR GO; GO:0002395; P:immune response in nasopharyngeal-associated lymphoid tissue; IEA:Ensembl. DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:UniProt. DR GO; GO:0120197; P:mucociliary clearance; IEA:Ensembl. DR GO; GO:0018095; P:protein polyglutamylation; TAS:UniProtKB. DR GO; GO:0120222; P:regulation of blastocyst development; IEA:Ensembl. DR GO; GO:0007288; P:sperm axoneme assembly; IEA:Ensembl. DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1. DR InterPro; IPR004344; TTL/TTLL_fam. DR PANTHER; PTHR12241:SF31; POLYGLUTAMYLASE COMPLEX SUBUNIT TTLL1; 1. DR PANTHER; PTHR12241; TUBULIN POLYGLUTAMYLASE; 1. DR Pfam; PF03133; TTL; 1. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR PROSITE; PS51221; TTL; 1. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cell projection; Cilium; Cytoplasm; KW Cytoskeleton; Flagellum; Ligase; Magnesium; Metal-binding; Microtubule; KW Nucleotide-binding; Reference proteome. FT CHAIN 1..423 FT /note="Polyglutamylase complex subunit TTLL1" FT /id="PRO_0000212438" FT DOMAIN 1..367 FT /note="TTL" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568" FT REGION 391..423 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 138 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:A4Q9E8" FT BINDING 144..145 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:A4Q9E8" FT BINDING 144 FT /ligand="a protein" FT /ligand_id="ChEBI:CHEBI:16541" FT /ligand_part="L-glutamate residue" FT /ligand_part_id="ChEBI:CHEBI:29973" FT /ligand_part_note="L-glutamate acceptor residue in protein FT target" FT /evidence="ECO:0000250|UniProtKB:A4Q9E8" FT BINDING 181..184 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:A4Q9E8" FT BINDING 194..196 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:A4Q9E8" FT BINDING 220 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:A4Q9E8" FT BINDING 241..242 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000250|UniProtKB:A4Q9E8" FT BINDING 259 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:A4Q9E8" FT BINDING 313 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:A4Q9E8" FT BINDING 326 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:A4Q9E8" FT BINDING 326 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:A4Q9E8" FT BINDING 328 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:A4Q9E8" FT BINDING 344 FT /ligand="L-glutamate" FT /ligand_id="ChEBI:CHEBI:29985" FT /evidence="ECO:0000250|UniProtKB:A4Q9E8" FT SITE 144 FT /note="Essential for specifying alpha-elongation versus FT initiation step of the polyglutamylase activity" FT /evidence="ECO:0000250|UniProtKB:A4Q9E8" FT VAR_SEQ 39..59 FT /note="MSVQTIRNVFSVEAGYRLSDD -> LLDLPEFRYRSCLNEFPDFRV (in FT isoform B)" FT /evidence="ECO:0000303|PubMed:11054573, FT ECO:0000303|PubMed:12529303" FT /id="VSP_006671" FT VAR_SEQ 60..423 FT /note="Missing (in isoform B)" FT /evidence="ECO:0000303|PubMed:11054573, FT ECO:0000303|PubMed:12529303" FT /id="VSP_006672" FT VAR_SEQ 298..326 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:12529303" FT /id="VSP_011825" FT VARIANT 168 FT /note="S -> L (in dbSNP:rs6003030)" FT /id="VAR_052409" FT MUTAGEN 326 FT /note="E->G: Abolishes microtubule polyglutamylation. FT Decreases MAP4 recruitment to microtubules." FT /evidence="ECO:0000269|PubMed:34782749" SQ SEQUENCE 423 AA; 48988 MW; AFFDEEE008D2E655 CRC64; MAGKVKWVTD IEKSVLINNF EKRGWVQVTE NEDWNFYWMS VQTIRNVFSV EAGYRLSDDQ IVNHFPNHYE LTRKDLMVKN IKRYRKELEK EGSPLAEKDE NGKYLYLDFV PVTYMLPADY NLFVEEFRKS PSSTWIMKPC GKAQGKGIFL INKLSQIKKW SRDSKTSSFV SQSNKEAYVI SLYINNPLLI GGRKFDLRLY VLVSTYRPLR CYMYKLGFCR FCTVKYTPST SELDNMFVHL TNVAIQKHGE DYNHIHGGKW TVSNLRLYLE STRGKEVTSK LFDEIHWIIV QSLKAVAPVM NNDKHCFECY GYDIIIDDKL KPWLIEVNAS PSLTSSTAND RILKYNLIND TLNIAVPNGE IPDCKWNKSP PKEVLGNYEI LYDEELAQGD GADRELRSRQ GQSLGPRAGR SRDSGRAVLT TWK //