[1]	NUCLEOTIDE SEQUENCE [MRNA]. Miyazaki K., Okamoto Y., Kato C., Sakamoto M., Ohira M., Morohashi A., Nakagawara A.; "Homo sapiens tubulin tyrosine ligase mRNA, complete cds."; Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 205-377. TISSUE=Uterus; The German cDNA consortium; Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.

Comments

FUNCTION: Catalyzes the post-translational addition of a tyrosine to the C-terminal end of detyrosinated alpha-tubulin (By similarity).
CATALYTIC ACTIVITY: ATP + detyrosinated alpha-tubulin + L-tyrosine = alpha-tubulin + ADP + phosphate.
COFACTOR: Magnesium (By similarity).
COFACTOR: Potassium (By similarity).
SUBUNIT: Monomer (By similarity).
SIMILARITY: Belongs to the tubulin--tyrosine ligase family.
SIMILARITY: Contains 1 TTL domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AB071393; BAC06832.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC036819; AAH36819.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX538316; CAD98091.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_714923.1; -.

UniGene

Hs.358997

3D structure databases

ModBase

Q8NG68.

PTM databases

PhosphoSite

Q8NG68; -.

Organism-specific databases

GC02P112956; -.

HGNC:21586; TTL.

TTL.

608291; gene. [NCBI / EBI]

PharmGKB

PA134934330; -.

GeneCards

Q8NG68.

Gene expression databases

ArrayExpress

Q8NG68; -.

CleanEx

HS_TTL; -.

GermOnline

ENSG00000114999; Homo sapiens.

Ontologies

GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030955;	Molecular function: potassium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004835;	Molecular function: tubulin-tyrosine ligase activity (inferred from electronic annotation from InterPro).
GO:0006464;	Biological process: protein modification process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR004344; Tub_tyr_ligase.
Graphical view of domain structure.

PANTHER

PTHR12241; Tub_tyr_ligase; 1.

Pfam

PF03133; TTL; 1.
Pfam graphical view of domain structure.

PROSITE

PS51221; TTL; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PeptideAtlas

Q8NG68; -.

Proteomics databases

PRIDE

Q8NG68; -.

Genome annotation databases

Ensembl

ENSG00000114999; Homo sapiens. [Contig view]

GeneID

150465; -.

KEGG

hsa:150465; -.

Phylogenomic databases

HOGENOM

Q8NG68; -.

HOVERGEN

Q8NG68; -.

Other

Q8NG68; -.

86445; -.

TTL; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Ligase; Magnesium; Potassium.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 377`	`377`	`Tubulin--tyrosine ligase.`	`PRO_0000212434`
`DOMAIN`	`3 370`	`368`	`TTL.`
`CONFLICT`	`245 245`		`I -> V (in Ref. 3; CAD98091).`

Sequence information

Length: 377 AA [This is the length of the unprocessed precursor]

Molecular weight: 43212 Da [This is the MW of the unprocessed precursor]

CRC64: 7A13E2C28E1AD6EA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MYTFVVRDEN SSVYAEVSRL LLATGHWKRL RRDNPRFNLM LGERNRLPFG RLGHEPGLVQ 

        70         80         90        100        110        120 
LVNYYRGADK LCRKASLVKL IKTSPELAES CTWFPESYVI YPTNLKTPVA PAQNGIQPPI 

       130        140        150        160        170        180 
SNSRTDEREF FLASYNRKKE DGEGNVWIAK SSAGAKGEGI LISSEASELL DFIDNQGQVH 

       190        200        210        220        230        240 
VIQKYLEHPL LLEPGHRKFD IRSWVLVDHQ YNIYLYREGV LRTASEPYHV DNFQDKTCHL 

       250        260        270        280        290        300 
TNHCIQKEYS KNYGKYEEGN EMFFKEFNQY LTSALNITLE SSILLQIKHI IRNCLLSVEP 

       310        320        330        340        350        360 
AISTKHLPYQ SFQLFGFDFM VDEELKVWLI EVNGAPACAQ KLYAELCQGI VDIAISSVFP 

       370 
PPDVEQPQTQ PAAFIKL

Q8NG68 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools