TTC3
entrez
7267
canonical
uniprot
P53804
canonical
ensembl
ENSG00000182670
resolver
ensp
ENSP00000381981
resolver
ensp
ENSP00000387880
resolver
ensp
ENSP00000403943
resolver
ensp
ENSP00000408456
resolver
ensp
ENSP00000512889
resolver
ensp
ENSP00000512893
resolver
enst
ENST00000411496
resolver
genesymbol
TTC3
resolver
genesymbol_syn
DCRR1
resolver
genesymbol_syn
RNF105
resolver
genesymbol_syn
TPRD
resolver
hgnc
HGNC:12393
resolver
uniprot
A8K7H7
resolver
uniprot
B2RPA7
resolver
uniprot
D3DSG9
resolver
uniprot
D3DSH2
resolver
uniprot
D3DSH3
resolver
uniprot
H7BZ57
resolver
uniprot
O60767
resolver
uniprot
P78476
resolver
uniprot
P78477
resolver
uniprot
Q569I2
resolver
uniprot
Q6P578
resolver
uniprot
Q9UEK4
resolver
uniprot_entry
H7BZ57_HUMAN
resolver
uniprot_entry
TTC3_HUMAN
resolver
uniprot_sec
A8K7H7
resolver
uniprot_sec
B2RPA7
resolver
uniprot_sec
D3DSG9
resolver
uniprot_sec
D3DSH2
resolver
uniprot_sec
D3DSH3
resolver
uniprot_sec
O60767
resolver
uniprot_sec
P78476
resolver
uniprot_sec
P78477
resolver
uniprot_sec
Q569I2
resolver
uniprot_sec
Q6P578
resolver
uniprot_sec
Q9UEK4
resolver
amino_acid_sequence
MDNFAEGDFTVADYALLEDCPHVDDCVFAAEFMSNDYVRVTQLYCDGVGVQYKDYIQSERNLEFDICSIWCSKPISVLQDYCDAIKINIFWPLLFQHQNSSVISRLHPCVDANNSRASEINLKKLQHLELMEDIVDLAKKVANDSFLIGGLLRIGCKIENKILAMEEALNWIKYAGDVTILTKLGSIDNCWPMLSIFFTEYKYHITKIVMEDCNLLEELKTQSCMDCIEEGELMKMKGNEEFSKERFDIAIIYYTRAIEYRPENYLLYGNRALCFLRTGQFRNALGDGKRATILKNTWPKGHYRYCDALSMLGEYDWALQANIKAQKLCKNDPEGIKDLIQQHVKLQKQIEDLQGRTANKDPIKAFYENRAYTPRSLSAPIFTTSLNFVEKERDFRKINHEMANGGNQNLKVADEALKVDDCDCHPEFSPPSSQPPKHKGKQKSRNNESEKFSSSSPLTLPADLKNILEKQFSKSSRAAHQDFANIMKMLRSLIQDGYMALLEQRCRSAAQAFTELLNGLDPQKIKQLNLAMINYVLVVYGLAISLLGIGQPEELSEAENQFKRIIEHYPSEGLDCLAYCGIGKVYLKKNRFLEALNHFEKARTLIYRLPGVLTWPTSNVIIEESQPQKIKMLLEKFVEECKFPPVPDAICCYQKCHGYSKIQIYITDPDFKGFIRISCCQYCKIEFHMNCWKKLKTTTFNDKIDKDFLQGICLTPDCEGVISKIIIFSSGGEVKCEFEHKVIKEKVPPRPILKQKCSSLEKLRLKEDKKLKRKIQKKEAKKLAQERMEEDLRESNPPKNEEQKETVDNVQRCQFLDDRILQCIKQYADKIKSGIQNTAMLLKELLSWKVLSTEDYTTCFSSRNFLNEAVDYVIRHLIQENNRVKTRIFLHVLSELKEVEPKLAAWIQKLNSFGLDATGTFFSRYGASLKLLDFSIMTFLWNEKYGHKLDSIEGKQLDYFSEPASLKEARCLIWLLEEHRDKFPALHSALDEFFDIMDSRCTVLRKQDSGEAPFSSTKVKNKSKKKKPKDSKPMLVGSGTTSVTSNNEIITSSEDHSNRNSDSAGPFAVPDHLRQDVEEFEALYDQHSNEYVVRNKKLWDMNPKQKCSTLYDYFSQFLEEHGPLDMSNKMFSAEYEFFPEETRQILEKAGGLKPFLLGCPRFVVIDNCIALKKVASRLKKKRKKKNIKTKVEEISKAGEYVRVKLQLNPAAREFKPDVKSKPVSDSSSAPAFENVKPKPVSANSPKPACEDVKAKPVSDNSSRQVSEDGQPKGVSSNSPKPGSEDANYKRVSCNSPKPVLEDVKPTYWAQSHLVTGYCTYLPFQRFDITQTPPAYINVLPGLPQYTSIYTPLASLSPEYQLPRSVPVVPSFVANDRADKNAAAYFEGHHLNAENVAGHQIASETQILEGSLGISVKSHCSTGDAHTVLSESNRNDEHCGNSNNKCEVIPESTSAVTNIPHVQMVAIQVSWNIIHQEVNTEPYNPFEERQGEISRIEKEHQVLQDQLQEVYENYEQIKLKGLEETRDLEEKLKRHLEENKISKTELDWFLQDLEREIKKWQQEKKEIQERLKSLKKKIKKVSNASEMYTQKNDGKEKEHELHLDQSLEISNTLTNEKMKIEEYIKKGKEDYEESHQRAVAAEVSVLENWKESEVYKLQIMESQAEAFLKKLGLISRDPAAYPDMESDIRSWELFLSNVTKEIEKAKSQFEEQIKAIKNGSRLSELSKVQISELSFPACNTVHPELLPESSGDDGQGLVTSASDVTGNHAALHRDPSVFSAGDSPGEAPSALLPGPPPGQPEATQLTGPKRAGQAALSERSPVADRKQPVPPGRAARSSQSPKKPFNSIIEHLSVVFPCYNSTELAGFIKKVRSKNKNSLSGLSIDEIVQRVTEHILDEQKKKKPNPGKDKRTYEPSSATPVTRSSQGSPSVVVAPSPKTKGQKAEDVPVRIALGASSCEICHEVFKSKNVRVLKCGHKYHKGCFKQWLKGQSACPACQGRDLLTEESPSGRGWPSQNQELPSCSSR
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: E3 ubiquitin-protein ligase which catalyzes the formation of 'Lys-48'-polyubiquitin chains (PubMed:20059950, PubMed:30696809). Mediates the ubiquitination and subsequent degradation of phosphorylated Akt (AKT1, AKT2 and AKT3) in the nucleus (PubMed:20059950). Acts as a terminal regulator of Akt signaling after activation; its phosphorylation by Akt, which is a prerequisite for ubiquitin ligase activity, suggests the existence of a regulation mechanism required to control Akt levels after activation (PubMed:20059950). Positively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation by mediating the ubiquitination and subsequent degradation of SMURF2 (PubMed:30696809). Regulates neuronal differentiation by regulating actin remodeling and Golgi organization via a signaling cascade involving RHOA, CIT and ROCK (PubMed:17488780, PubMed:24695496). Inhibits cell proliferation (PubMed:30203323). {ECO:0000269|PubMed:17488780, ECO:0000269|PubMed:20059950, ECO:0000269|PubMed:24695496, ECO:0000269|PubMed:30203323, ECO:0000269|PubMed:30696809}.
uniprot
proteins
mass_dalton
229869
uniprot
proteins
mutagenesis
MUTAGEN 378; /note="S->A: Abolishes phosphorylation by Akt and impairs ubiquitin ligase activity on Akt."; /evidence="ECO:0000269|PubMed:20059950
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:20059950, ECO:0000269|PubMed:30696809}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylation on Ser-378 by Akt is required for ubiquitin ligase activity. {ECO:0000269|PubMed:20059950}.; PTM: Proteolytically cleaved into differently sized N- and C-terminal fragments. {ECO:0000269|PubMed:30203323}.
uniprot
proteins
pubmed
10830953
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17488780
uniprot
proteins
pubmed
20059950
uniprot
proteins
pubmed
24695496
uniprot
proteins
pubmed
27066578
uniprot
proteins
pubmed
29290964
uniprot
proteins
pubmed
30203323
uniprot
proteins
pubmed
30696809
uniprot
proteins
pubmed
8724848
uniprot
proteins
pubmed
8947847
uniprot
proteins
pubmed
9254009
uniprot
proteins
pubmed
9503011
uniprot
proteins
sequence_length
2025
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20059950, ECO:0000269|PubMed:30203323}. Cytoplasm {ECO:0000269|PubMed:30203323}. Golgi apparatus {ECO:0000250|UniProtKB:D3ZSP7}. Note=Nuclear localization may be dependent on the proteolytic cleavage of full length protein in the cytoplasm (PubMed:30203323). This cleavage may reveal an N-terminal nuclear localization signal, allowing N-terminal fragments to enter the nucleus (PubMed:30203323). {ECO:0000269|PubMed:30203323}.
uniprot
proteins