TTLL7
entrez
79739
canonical
uniprot
Q6ZT98
canonical
ensembl
ENSG00000137941
resolver
ensp
ENSP00000260505
resolver
ensp
ENSP00000435334
resolver
ensp
ENSP00000484660
resolver
ensp
ENSP00000535884
resolver
ensp
ENSP00000737423
resolver
genesymbol
TTLL7
resolver
hgnc
HGNC:26242
resolver
uniprot
Q5TAX8
resolver
uniprot
Q5TAX9
resolver
uniprot
Q6P990
resolver
uniprot
Q86YS1
resolver
uniprot
Q9H5U4
resolver
uniprot_entry
TTLL7_HUMAN
resolver
uniprot_sec
Q5TAX8
resolver
uniprot_sec
Q5TAX9
resolver
uniprot_sec
Q6P990
resolver
uniprot_sec
Q86YS1
resolver
uniprot_sec
Q9H5U4
resolver
amino_acid_sequence
MPSLPQEGVIQGPSPLDLNTELPYQSTMKRKVRKKKKKGTITANVAGTKFEIVRLVIDEMGFMKTPDEDETSNLIWCDSAVQQEKISELQNYQRINHFPGMGEICRKDFLARNMTKMIKSRPLDYTFVPRTWIFPAEYTQFQNYVKELKKKRKQKTFIVKPANGAMGHGISLIRNGDKLPSQDHLIVQEYIEKPFLMEGYKFDLRIYILVTSCDPLKIFLYHDGLVRMGTEKYIPPNESNLTQLYMHLTNYSVNKHNEHFERDETENKGSKRSIKWFTEFLQANQHDVAKFWSDISELVVKTLIVAEPHVLHAYRMCRPGQPPGSESVCFEVLGFDILLDRKLKPWLLEINRAPSFGTDQKIDYDVKRGVLLNALKLLNIRTSDKRRNLAKQKAEAQRRLYGQNSIKRLLPGSSDWEQQRHQLERRKEELKERLAQVRKQISREEHENRHMGNYRRIYPPEDKALLEKYENLLAVAFQTFLSGRAASFQRELNNPLKRMKEEDILDLLEQCEIDDEKLMGKTTKTRGPKPLCSMPESTEIMKRPKYCSSDSSYDSSSSSSESDENEKEEYQNKKREKQVTYNLKPSNHYKLIQQPSSIRRSVSCPRSISAQSPSSGDTRPFSAQQMISVSRPTSASRSHSLNRASSYMRHLPHSNDACSTNSQVSESLRQLKTKEQEDDLTSQTLFVLKDMKIRFPGKSDAESELLIEDIIDNWKYHKTKVASYWLIKLDSVKQRKVLDIVKTSIRTVLPRIWKVPDVEEVNLYRIFNRVFNRLLWSRGQGLWNCFCDSGSSWESIFNKSPEVVTPLQLQCCQRLVELCKQCLLVVYKYATDKRGSLSGIGPDWGNSRYLLPGSTQFFLRTPTYNLKYNSPGMTRSNVLFTSRYGHL
uniprot
proteins
ec_number
6.3.2.-
uniprot
proteins
function
FUNCTION: Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin (PubMed:16901895, PubMed:25959773). Mediates both ATP-dependent initiation and elongation steps of the polyglutamylation reaction (PubMed:16901895, PubMed:25959773). Preferentially modifies the beta-tubulin tail over an alpha-tail (PubMed:16901895, PubMed:25959773). Competes with monoglycylase TTLL3 for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions (By similarity). Required for neurite growth; responsible for the strong increase in tubulin polyglutamylation during postnatal neuronal maturation (By similarity). {ECO:0000250|UniProtKB:A4Q9F0, ECO:0000250|UniProtKB:F7E540, ECO:0000269|PubMed:16901895, ECO:0000269|PubMed:25959773}.
uniprot
proteins
mass_dalton
102999
uniprot
proteins
mutagenesis
MUTAGEN 106; /note="R->E: Nearly abolished polyglutamylase activity."; /evidence="ECO:0000269|PubMed:25959773"; MUTAGEN 143..146; /note="NYVK->EYVE: 70% decreased polyglutamylase activity."; /evidence="ECO:0000269|PubMed:25959773"; MUTAGEN 178; /note="K->E: Decreased polyglutamylase activity."; /evidence="ECO:0000269|PubMed:25959773"; MUTAGEN 205; /note="R->E: Nearly abolished polyglutamylase activity."; /evidence="ECO:0000269|PubMed:25959773"; MUTAGEN 227; /note="R->E: Nearly abolished polyglutamylase activity."; /evidence="ECO:0000269|PubMed:25959773"; MUTAGEN 271; /note="K->E: Nearly abolished polyglutamylase activity."; /evidence="ECO:0000269|PubMed:25959773"; MUTAGEN 349; /note="E->Q: Loss of polyglutamylase activity."; /evidence="ECO:0000269|PubMed:25959773"; MUTAGEN 352; /note="R->A,E: Nearly abolished polyglutamylase activity."; /evidence="ECO:0000269|PubMed:25959773"; MUTAGEN 385..393; /note="KRRNLAKQK->EEENLAEQE: 45% decreased binding to microtubules. Decreased polyglutamylase activity. 76% decreased binding to microtubules; when associated with 425-E--E-427."; /evidence="ECO:0000269|PubMed:25959773"; MUTAGEN 425..427; /note="RRK->EEE: 76% decreased binding to microtubules; when associated with 385-E--E-393."; /evidence="ECO:0000269|PubMed:25959773"; MUTAGEN 477..480; /note="FQTF->AQTA: 40% decreased polyglutamylase activity."; /evidence="ECO:0000269|PubMed:25959773"; MUTAGEN 490..500; /note="RELNNPLKRMK->DELNNPLDDMD: 69% decreased polyglutamylase activity."; /evidence="ECO:0000269|PubMed:25959773
uniprot
proteins
protein_family
Tubulin--tyrosine ligase family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
16901895
uniprot
proteins
pubmed
25959773
uniprot
proteins
sequence_length
887
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000250|UniProtKB:A4Q9F0}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:A4Q9F0}. Cell projection, dendrite {ECO:0000250|UniProtKB:A4Q9F0}. Perikaryon {ECO:0000250|UniProtKB:A4Q9F0}. Note=In cells with primary cilia, found in both cilia and basal bodies. In neuronal cells, found in dendrites and perikaryon. {ECO:0000250|UniProtKB:A4Q9F0}.
uniprot
proteins