Mphosph9
entrez
269702
canonical
uniprot
A6H5Y1
canonical
ensembl
ENSMUSG00000038126
resolver
ensp
ENSMUSP00000031344
resolver
ensp
ENSMUSP00000138982
resolver
enst
ENSMUST00000031344
resolver
enst
ENSMUST00000184951
resolver
genesymbol
Mphosph9
resolver
uniprot
A0A8Q0L6P9
resolver
uniprot
A0A8Q0P9S6
resolver
uniprot
E9QPF8
resolver
uniprot
Q8BUK7
resolver
uniprot
Q8BV15
resolver
uniprot
V9GX48
resolver
uniprot_entry
A0A8Q0L6P9_MOUSE
resolver
uniprot_entry
MPP9_MOUSE
resolver
uniprot_sec
A0A8Q0P9S6
resolver
uniprot_sec
E9QPF8
resolver
uniprot_sec
Q8BUK7
resolver
uniprot_sec
Q8BV15
resolver
uniprot_sec
V9GX48
resolver
amino_acid_sequence
MEDFDLVENLQKTSPSVESDIKSAPQSLGLSLHANRSSPHLSTNGVSSFSGKTGPPVIQGTVEVLTALRQDLQNSGRTDSELWKSCERIQEEIRKLVKLQLSHASRPSCSSSSVSEQVSAETQMGFFSENSERNESVVSSPASKEPETQPASSTSYPDCHVDSSSVSSGYGTFCILDMNTHKAKEPTEPLEPGAASQGQHPASVVQAHGPAGGAAAINFFTQTPEELCASLKEDGSTFPGEFDRNFLGENKISEVYSGKANSGKSVTSWAQRLKQNQSKQAHTEDDCSGPKPGSELNWKPPADTFDLAADAARPCAFYINKPAESPSSWLSDSGTGLTYWKLEEKDMYHSLPETLEKTFAPSPAERPLSQVLTLDPGAIRMKPKEHVAGIQAHGFLHALDDRISFSPDSVLEPSLSRHSDTDSSSQASHNPSQVSGFSKYPSTTRASPVDTWKNHAFQRESRTSSTIPSRYTITSNDISVKTVDEENTVTVASVSQSQLPGTANSVPECISLASLEDPVMLSKIRQNLKEKHARHVADLRAYYESEISSLKQKLEAKDISAVEEWKKKNEILADRCGQLDSALNEATSRVRTLEKNNNLLEIEVSDLRERFNAASSASKVLQERIEEMRTSNKEKDNTITRLKCRLQDLEEAFENAYKLSDDKEARLRQENKMFQDLLGEYESLGKEHGRVKDTLNTTENKLLDAHTQISDLKRTISKLEAQVKQAEHESMLSLRNGAKVPERPSRSNSVATSDVSRRKWLIPGAEYSIFTGQPLDPRDRKLDKQLEEALVPGYHSPPEKDSSLGSSPASLLVKKKRDTPDTPPIIKALKELDEERVFKSWGTQTEKEDSSSKLVNSRQTEPSVNTGRSPEKCAQQRPKRQTSASQRSSSLPPSSRKANTPTKREIMLTPVTVAYSPKRSPKENLSPGFSHLLSKNESSPVRFDILLDDLDTVPVSTLQQTTAKKQLQFLLDDSEEKKYSEKNSDDPVNPSSCPEHSPNGLKKVSTRQAWEKSKSVSLEQCQPGSAAPQDNGFEYTAKIRTLAETERFFDELTKEKDQIEAALSRMPSPGGRITLQTRLNQEALEDRLEKINRELGSVRMTLKKFHVLRSSANL
uniprot
proteins
function
FUNCTION: Negatively regulates cilia formation by recruiting the CP110-CEP97 complex (a negative regulator of ciliogenesis) at the distal end of the mother centriole in ciliary cells (PubMed:30375385). At the beginning of cilia formation, MPHOSPH9 undergoes TTBK2-mediated phosphorylation and degradation via the ubiquitin-proteasome system and removes itself and the CP110-CEP97 complex from the distal end of the mother centriole, which subsequently promotes cilia formation (By similarity). {ECO:0000250|UniProtKB:Q99550, ECO:0000269|PubMed:30375385}.
uniprot
proteins
mass_dalton
123259
uniprot
proteins
post_translational_modification
PTM: TTBK2-mediated phosphorylation at Ser-710 and Ser-717, promotes its ubiquitination at Lys-713 leading to proteasomal degradation, loss of MPHOSPH9 facilitates the removal of the CP110-CEP97 complex from the mother centrioles, promoting the initiation of ciliogenesis (By similarity). Phosphorylated in M (mitotic) phase (By similarity). {ECO:0000250|UniProtKB:Q99550}.; PTM: Ubiquitinated at Lys-713, leading to proteasomal degradation. {ECO:0000250|UniProtKB:Q99550}.
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
30375385
uniprot
proteins
sequence_length
1114
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250|UniProtKB:Q99550}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q99550}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q99550}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:30375385}. Note=Localizes to the distal and proximal end of centriole pairs in duplicated centrosomes. In ciliated cells, localizes to the distal and proximal end of daughter centriole and proximal of the mother centriole but not in the distal end of the mother centriole (By similarity). Recruited by KIF24 to the distal end of mother centriole where it forms a ring-like structure (By similarity). {ECO:0000250|UniProtKB:Q99550}.
uniprot
proteins