ID   TTL_HUMAN               Reviewed;         377 AA.
AC   Q8NG68; Q7Z302; Q8N426;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=Tubulin--tyrosine ligase;
DE            Short=TTL;
DE            EC=6.3.2.25;
GN   Name=TTL;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Miyazaki K., Okamoto Y., Kato C., Sakamoto M., Ohira M., Morohashi A.,
RA   Nakagawara A.;
RT   "Homo sapiens tubulin tyrosine ligase mRNA, complete cds.";
RL   Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 205-377.
RC   TISSUE=Uterus;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K.,
RA   Ottenwalder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [4]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the post-translational addition of a tyrosine
CC       to the C-terminal end of detyrosinated alpha-tubulin (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + detyrosinated alpha-tubulin + L-tyrosine
CC       = alpha-tubulin + ADP + phosphate.
CC   -!- COFACTOR: Magnesium (By similarity).
CC   -!- COFACTOR: Potassium (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
CC   -!- SIMILARITY: Contains 1 TTL domain.
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DR   EMBL; AB071393; BAC06832.2; -; mRNA.
DR   EMBL; BC036819; AAH36819.1; -; mRNA.
DR   EMBL; BX538316; CAD98091.1; -; mRNA.
DR   IPI; IPI00166611; -.
DR   RefSeq; NP_714923.1; -.
DR   UniGene; Hs.358997; -.
DR   PhosphoSite; Q8NG68; -.
DR   PeptideAtlas; Q8NG68; -.
DR   PRIDE; Q8NG68; -.
DR   Ensembl; ENSG00000114999; Homo sapiens.
DR   GeneID; 150465; -.
DR   KEGG; hsa:150465; -.
DR   GeneCards; GC02P112956; -.
DR   HGNC; HGNC:21586; TTL.
DR   MIM; 608291; gene.
DR   PharmGKB; PA134934330; -.
DR   HOGENOM; Q8NG68; -.
DR   HOVERGEN; Q8NG68; -.
DR   OMA; Q8NG68; CIEPAIS.
DR   BRENDA; 6.3.2.25; 247.
DR   NextBio; 86445; -.
DR   ArrayExpress; Q8NG68; -.
DR   Bgee; Q8NG68; -.
DR   CleanEx; HS_TTL; -.
DR   GermOnline; ENSG00000114999; Homo sapiens.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004835; F:tubulin-tyrosine ligase activity; IEA:EC.
DR   GO; GO:0006464; P:protein modification process; IEA:InterPro.
DR   InterPro; IPR004344; Tub_tyr_ligase.
DR   PANTHER; PTHR12241; Tub_tyr_ligase; 1.
DR   Pfam; PF03133; TTL; 1.
DR   PROSITE; PS51221; TTL; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Ligase; Magnesium; Nucleotide-binding; Potassium.
FT   CHAIN         1    377       Tubulin--tyrosine ligase.
FT                                /FTId=PRO_0000212434.
FT   DOMAIN        3    370       TTL.
FT   CONFLICT    245    245       I -> V (in Ref. 3; CAD98091).
SQ   SEQUENCE   377 AA;  43212 MW;  7A13E2C28E1AD6EA CRC64;
     MYTFVVRDEN SSVYAEVSRL LLATGHWKRL RRDNPRFNLM LGERNRLPFG RLGHEPGLVQ
     LVNYYRGADK LCRKASLVKL IKTSPELAES CTWFPESYVI YPTNLKTPVA PAQNGIQPPI
     SNSRTDEREF FLASYNRKKE DGEGNVWIAK SSAGAKGEGI LISSEASELL DFIDNQGQVH
     VIQKYLEHPL LLEPGHRKFD IRSWVLVDHQ YNIYLYREGV LRTASEPYHV DNFQDKTCHL
     TNHCIQKEYS KNYGKYEEGN EMFFKEFNQY LTSALNITLE SSILLQIKHI IRNCLLSVEP
     AISTKHLPYQ SFQLFGFDFM VDEELKVWLI EVNGAPACAQ KLYAELCQGI VDIAISSVFP
     PPDVEQPQTQ PAAFIKL
//