TTLL3
entrez
26140
canonical
uniprot
Q9Y4R7
canonical
ensembl
ENSG00000214021
resolver
ensp
ENSP00000312148
resolver
ensp
ENSP00000392549
resolver
ensp
ENSP00000403874
resolver
ensp
ENSP00000510679
resolver
ensp
ENSP00000515513
resolver
ensp
ENSP00000520491
resolver
ensp
ENSP00000657865
resolver
ensp
ENSP00000657866
resolver
ensp
ENSP00000722604
resolver
enst
ENST00000426895
resolver
enst
ENST00000685419
resolver
genesymbol
TTLL3
resolver
hgnc
HGNC:24483
resolver
uniprot
A0A8I5KXU2
resolver
uniprot
J3KQB2
resolver
uniprot
Q4KMS8
resolver
uniprot
Q6AWA3
resolver
uniprot
Q6ZU95
resolver
uniprot
Q8NDN8
resolver
uniprot
Q96GG8
resolver
uniprot
Q9H876
resolver
uniprot
Q9UI99
resolver
uniprot_entry
A0A8I5KXU2_HUMAN
resolver
uniprot_entry
J3KQB2_HUMAN
resolver
uniprot_entry
TTLL3_HUMAN
resolver
uniprot_sec
Q4KMS8
resolver
uniprot_sec
Q6AWA3
resolver
uniprot_sec
Q6ZU95
resolver
uniprot_sec
Q8NDN8
resolver
uniprot_sec
Q96GG8
resolver
uniprot_sec
Q9H876
resolver
uniprot_sec
Q9UI99
resolver
amino_acid_sequence
MNRLRNAKIYVERAVKQKKIFTIQGCYPVIRCLLRRRGWVEKKMVHRSGPTLLPPQKDLDSSAMGDSDTTEDEDEDEDEEFQPSQLFDFDDLLKFDDLDGTHALMVGLCLNLRNLPWFDEVDANSFFPRCYCLGAEDDKKAFIEDFWLTAARNVLKLVVKSEWKSYPIQAVEEEASGDKQPKKQEKNPVLVSPEFVDEALCACEEYLSNLAHMDIDKDLEAPLYLTPEGWSLFLQRYYQVVHEGAELRHLDTQVQRCEDILQQLQAVVPQIDMEGDRNIWIVKPGAKSRGRGIMCMDHLEEMLKLVNGNPVVMKDGKWVVQKYIERPLLIFGTKFDLRQWFLVTDWNPLTVWFYRDSYIRFSTQPFSLKNLDNSVHLCNNSIQKHLENSCHRHPLLPPDNMWSSQRFQAHLQEMGAPNAWSTIIVPGMKDAVIHALQTSQDTVQCRKASFELYGADFVFGEDFQPWLIEINASPTMAPSTAVTARLCAGVQADTLRVVIDRMLDRNCDTGAFELIYKQPAVEVPQYVGIRLLVEGFTIKKPMAMCHRRMGVRPAVPLLTQRGSGEARHHFPSLHTKAQLPSPHVLRHQGQVLRRQHSKLVGTKALSTTGKALRTLPTAKVFISLPPNLDFKVAPSILKPRKAPALLCLRGPQLEVPCCLCPLKSEQFLAPVGRSRPKANSRPDCDKPRAEACPMKRLSPLKPLPLVGTFQRRRGLGDMKLGKPLLRFPTALVLDPTPNKKKQVKYLGLDSIAVGGSRVDGARPCTPGSTARA
uniprot
proteins
ec_number
6.3.2.-
uniprot
proteins
function
FUNCTION: Monoglycylase which modifies alpha- and beta-tubulin, adding a single glycine on the gamma-carboxyl groups of specific glutamate residues to generate monoglycine side chains within the C-terminal tail of tubulin. Not involved in elongation step of the polyglycylation reaction (By similarity). Preferentially glycylates a beta-tail peptide over the alpha-tail, although shifts its preference toward alpha-tail as beta-tail glutamylation increases (By similarity). Competes with polyglutamylases for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions (By similarity). Together with TTLL8, mediates microtubule glycylation of primary and motile cilia, which is essential for their stability and maintenance (By similarity). Involved in microtubule glycylation of primary cilia in colon which controls cell proliferation of epithelial cells and plays an essential role in colon cancer development (PubMed:25180231). Together with TTLL8, glycylates sperm flagella which regulates axonemal dynein motor activity, thereby controlling flagellar beat, directional sperm swimming and male fertility (By similarity). {ECO:0000250|UniProtKB:A4Q9E5, ECO:0000250|UniProtKB:B2GUB3, ECO:0000269|PubMed:25180231}.
uniprot
proteins
mass_dalton
87414
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
25180231
uniprot
proteins
sequence_length
772
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:25180231}. Cell projection, cilium {ECO:0000250|UniProtKB:A4Q9E5}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:A4Q9E5}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A4Q9E5}.
uniprot
proteins