TTL10_HUMAN
ID TTL10_HUMAN Reviewed; 673 AA.
AC Q6ZVT0; B1AMF6; Q5T2W4; Q5T2W5; Q8N9X2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Inactive polyglycylase TTLL10 {ECO:0000303|PubMed:19524510};
DE AltName: Full=Tubulin--tyrosine ligase-like protein 10;
GN Name=TTLL10 {ECO:0000312|HGNC:HGNC:26693};
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] (ISOFORMS 1 AND 3).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [5]
RP FUNCTION, AND MUTAGENESIS OF SER-448 AND LYS-467.
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 [6]
RP VARIANT [LARGE SCALE ANALYSIS] THR-130.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Inactive polyglycylase. {ECO:0000269|PubMed:19524510}.
CC -!- INTERACTION:
CC Q6ZVT0; A2RRN7: CADPS; NbExp=3; IntAct=EBI-7844656, EBI-10179719;
CC Q6ZVT0; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-7844656, EBI-739624;
CC Q6ZVT0; Q13643: FHL3; NbExp=3; IntAct=EBI-7844656, EBI-741101;
CC Q6ZVT0; Q6A162: KRT40; NbExp=3; IntAct=EBI-7844656, EBI-10171697;
CC Q6ZVT0; Q99750: MDFI; NbExp=3; IntAct=EBI-7844656, EBI-724076;
CC Q6ZVT0; P55209: NAP1L1; NbExp=5; IntAct=EBI-7844656, EBI-356392;
CC Q6ZVT0; Q9UL42: PNMA2; NbExp=3; IntAct=EBI-7844656, EBI-302355;
CC Q6ZVT0; Q93062: RBPMS; NbExp=3; IntAct=EBI-7844656, EBI-740322;
CC Q6ZVT0; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-7844656, EBI-741515;
CC Q6ZVT0; P14373: TRIM27; NbExp=3; IntAct=EBI-7844656, EBI-719493;
CC Q6ZVT0; Q15654: TRIP6; NbExp=3; IntAct=EBI-7844656, EBI-742327;
CC Q6ZVT0-3; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-11979997, EBI-739624;
CC Q6ZVT0-3; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-11979997, EBI-742887;
CC Q6ZVT0-3; Q13643: FHL3; NbExp=3; IntAct=EBI-11979997, EBI-741101;
CC Q6ZVT0-3; O76013-2: KRT36; NbExp=3; IntAct=EBI-11979997, EBI-11958506;
CC Q6ZVT0-3; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-11979997, EBI-741037;
CC Q6ZVT0-3; Q99750: MDFI; NbExp=3; IntAct=EBI-11979997, EBI-724076;
CC Q6ZVT0-3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11979997, EBI-16439278;
CC Q6ZVT0-3; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-11979997, EBI-11522433;
CC Q6ZVT0-3; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-11979997, EBI-739895;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6ZVT0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZVT0-2; Sequence=VSP_032262;
CC Name=3;
CC IsoId=Q6ZVT0-3; Sequence=VSP_032262, VSP_032263, VSP_032264;
CC -!- CAUTION: Two inactivating mutations in human TTLL10 (Ser-448 and Lys-
CC 467) are proposed to explain the lack of polyglycylation.
CC {ECO:0000305|PubMed:19524510}.
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DR EMBL; AK093438; BAC04164.1; -; mRNA.
DR EMBL; AK124125; BAC85781.1; -; mRNA.
DR EMBL; AL162741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390719; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471183; EAW56285.1; -; Genomic_DNA.
DR EMBL; BC126152; AAI26153.1; -; mRNA.
DR EMBL; BC126154; AAI26155.1; -; mRNA.
DR CCDS; CCDS44036.1; -. [Q6ZVT0-1]
DR CCDS; CCDS8.1; -. [Q6ZVT0-3]
DR RefSeq; NP_001123517.1; NM_001130045.1. [Q6ZVT0-1]
DR RefSeq; NP_694986.2; NM_153254.2. [Q6ZVT0-3]
DR RefSeq; XP_005244795.1; XM_005244738.1. [Q6ZVT0-2]
DR RefSeq; XP_011539479.1; XM_011541177.2. [Q6ZVT0-1]
DR RefSeq; XP_016856401.1; XM_017000912.1. [Q6ZVT0-1]
DR AlphaFoldDB; Q6ZVT0; -.
DR SMR; Q6ZVT0; -.
DR BioGRID; 129020; 16.
DR IntAct; Q6ZVT0; 17.
DR MINT; Q6ZVT0; -.
DR STRING; 9606.ENSP00000368592; -.
DR iPTMnet; Q6ZVT0; -.
DR PhosphoSitePlus; Q6ZVT0; -.
DR BioMuta; TTLL10; -.
DR DMDM; 172046174; -.
DR MassIVE; Q6ZVT0; -.
DR PaxDb; Q6ZVT0; -.
DR PeptideAtlas; Q6ZVT0; -.
DR PRIDE; Q6ZVT0; -.
DR ProteomicsDB; 68439; -. [Q6ZVT0-1]
DR ProteomicsDB; 68440; -. [Q6ZVT0-2]
DR ProteomicsDB; 68441; -. [Q6ZVT0-3]
DR Antibodypedia; 51322; 44 antibodies from 15 providers.
DR DNASU; 254173; -.
DR Ensembl; ENST00000379288.3; ENSP00000368590.3; ENSG00000162571.14. [Q6ZVT0-3]
DR Ensembl; ENST00000379289.6; ENSP00000368591.1; ENSG00000162571.14. [Q6ZVT0-1]
DR Ensembl; ENST00000379290.6; ENSP00000368592.1; ENSG00000162571.14. [Q6ZVT0-1]
DR GeneID; 254173; -.
DR KEGG; hsa:254173; -.
DR MANE-Select; ENST00000379289.6; ENSP00000368591.1; NM_001130045.2; NP_001123517.1.
DR UCSC; uc001acy.2; human. [Q6ZVT0-1]
DR CTD; 254173; -.
DR DisGeNET; 254173; -.
DR GeneCards; TTLL10; -.
DR HGNC; HGNC:26693; TTLL10.
DR HPA; ENSG00000162571; Group enriched (choroid plexus, fallopian tube, testis).
DR neXtProt; NX_Q6ZVT0; -.
DR OpenTargets; ENSG00000162571; -.
DR PharmGKB; PA142670679; -.
DR VEuPathDB; HostDB:ENSG00000162571; -.
DR eggNOG; KOG2157; Eukaryota.
DR GeneTree; ENSGT00940000160919; -.
DR HOGENOM; CLU_022993_1_0_1; -.
DR InParanoid; Q6ZVT0; -.
DR OMA; NRHINDT; -.
DR OrthoDB; 626048at2759; -.
DR PhylomeDB; Q6ZVT0; -.
DR TreeFam; TF329363; -.
DR PathwayCommons; Q6ZVT0; -.
DR Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR SignaLink; Q6ZVT0; -.
DR BioGRID-ORCS; 254173; 12 hits in 1071 CRISPR screens.
DR GenomeRNAi; 254173; -.
DR Pharos; Q6ZVT0; Tdark.
DR PRO; PR:Q6ZVT0; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q6ZVT0; protein.
DR Bgee; ENSG00000162571; Expressed in right uterine tube and 102 other tissues.
DR ExpressionAtlas; Q6ZVT0; baseline and differential.
DR Genevisible; Q6ZVT0; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070735; F:protein-glycine ligase activity; TAS:Reactome.
DR GO; GO:0018094; P:protein polyglycylation; TAS:Reactome.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR InterPro; IPR027752; TTLL10.
DR PANTHER; PTHR46810; PTHR46810; 1.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..673
FT /note="Inactive polyglycylase TTLL10"
FT /id="PRO_0000324520"
FT DOMAIN 155..552
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 1..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 569..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..33
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..66
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..626
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 362..365
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 375
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT BINDING 377
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q6ZT98"
FT VAR_SEQ 1..73
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_032262"
FT VAR_SEQ 468..477
FT /note="KRMQQIMAHC -> VRPLCPPVWE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_032263"
FT VAR_SEQ 478..673
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_032264"
FT VARIANT 130
FT /note="A -> T (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs139755178)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_039806"
FT VARIANT 249
FT /note="V -> A (in dbSNP:rs13374146)"
FT /id="VAR_039807"
FT VARIANT 448
FT /note="S -> N (in dbSNP:rs1320571)"
FT /id="VAR_039808"
FT VARIANT 578
FT /note="G -> D (in dbSNP:rs2274791)"
FT /id="VAR_058480"
FT MUTAGEN 448
FT /note="S->N: Recovers polyglycylase activity; when
FT associated with T-467."
FT /evidence="ECO:0000269|PubMed:19524510"
FT MUTAGEN 467
FT /note="K->T: Recovers polyglycylase activity; when
FT associated with N-448."
FT /evidence="ECO:0000269|PubMed:19524510"
FT CONFLICT 214
FT /note="Y -> D (in Ref. 1; BAC85781)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="K -> R (in Ref. 1; BAC04164)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 673 AA; 75042 MW; AF81F9215D73A446 CRC64;
MDHSCTRFIH RRGPPTRTRA GFKRGKRPRI QQRPRARVSG TIPASRLHPA PASQPGPCPA
PGHCPVGPAH ERPMGSSQEE GLRCQPSQPD HDADGHCGPD LEGAERASAT PGPPGLLNSH
RPADSDDTNA AGPSAALLEG LLLGGGKPSP HSTRPGPFFY IGGSNGATII SSYCKSKGWQ
RIHDSRRDDY TLKWCEVKSR DSYGSFREGE QLLYQLPNNK LLTTKIGLLS TLRGRARAMS
KASKVPGGVQ ARLEKDAAAP ALEDLPWTSP GYLRPQRVLR MEEFFPETYR LDLKHEREAF
FTLFDETQIW ICKPTASNQG KGIFLLRNQE EVAALQAKTR SMEDDPIHHK TPFRGPQARV
VQRYIQNPLL VDGRKFDVRS YLLIACTTPY MIFFGHGYAR LTLSLYDPHS SDLGGHLTNQ
FMQKKSPLYM LLKEHTVWSM EHLNRYISDT FWKARGLAKD WVFTTLKKRM QQIMAHCFLA
AKPKLDCKLG YFDLIGCDFL IDDNFKVWLL EMNSNPALHT NCEVLKEVIP GVVIETLDLV
LETFRKSLRG QKMLPLLSQR RFVLLHNGEA DPRPHLGGSC SLRRWPPLPT RQAKSSGPPM
PHAPDQPGAR RPAPPPLVPQ RPRPPGPDLD SAHDGEPQAP GTEQSGTGNR HPAQEPSPGT
AKEEREEPEN ARP
