DZIP1
entrez
22873
canonical
uniprot
Q86YF9
canonical
ensembl
ENSG00000134874
resolver
ensp
ENSP00000355175
resolver
ensp
ENSP00000366025
resolver
ensp
ENSP00000567762
resolver
ensp
ENSP00000567764
resolver
ensp
ENSP00000567769
resolver
ensp
ENSP00000567770
resolver
ensp
ENSP00000617350
resolver
genesymbol
DZIP1
resolver
genesymbol_syn
DZIP
resolver
genesymbol_syn
DZIP2
resolver
genesymbol_syn
KIAA0996
resolver
hgnc
HGNC:20908
resolver
uniprot
B3KSP1
resolver
uniprot
Q5W078
resolver
uniprot
Q5W079
resolver
uniprot
Q8WY45
resolver
uniprot
Q8WY46
resolver
uniprot
Q9UGA5
resolver
uniprot
Q9Y2K0
resolver
uniprot_entry
B3KSP1_HUMAN
resolver
uniprot_entry
DZIP1_HUMAN
resolver
uniprot_sec
Q5W078
resolver
uniprot_sec
Q5W079
resolver
uniprot_sec
Q8WY45
resolver
uniprot_sec
Q8WY46
resolver
uniprot_sec
Q9UGA5
resolver
uniprot_sec
Q9Y2K0
resolver
amino_acid_sequence
MQAEAADWFSSMPFQKHVYYPLASGPEGPDVAVAAAAAGAASMACAPPSAASGPLPFFQFRPRLESVDWRRLSAIDVDKVAGAVDVLTLQENIMNITFCKLEDEKCPHCQSGVDPVLLKLIRLAQFTIEYLLHSQEFLTSQLHTLEERLRLSHCDGEQSKKLLTKQAGEIKTLKEECKRRKKMISTQQLMIEAKANYYQCHFCDKAFMNQAFLQSHIQRRHTEENSHFEYQKNAQIEKLRSEIVVLKEELQLTRSELEAAHHASAVRFSKEYEMQKTKEEDFLKLFDRWKEEEKEKLVDEMEKVKEMFMKEFKELTSKNSALEYQLSEIQKSNMQIKSNIGTLKDAHEFKEDRSPYPQDFHNVMQLLDSQESKWTARVQAIHQEHKKEKGRLLSHIEKLRTSMIDDLNASNVFYKKRIEELGQRLQEQNELIITQRQQIKDFTCNPLNSISEPKGNPLAWQAFESQPAAPAVPMNAPALHTLETKSSLPMVHEQAFSSHILEPIEELSEEEKGRENEQKLNNNKMHLRKALKSNSSLTKGLRTMVEQNLMEKLETLGINADIRGISSDQLHRVLKSVESERHKQEREIPNFHQIREFLEHQVSCKIEEKALLSSDQCSVSQMDTLSTGEVPKMIQLPSKNRQLIRQKAVSTDRTSVPKIKKNVMEDPFPRKSSTITTPPFSSEEEQEDDDLIRAYASPGPLPVPPPQNKGSFGKNTVKSDADGTEGSEIEDTDDSPKPAGVAVKTPTEKVEKMFPHRKNVNKPVGGTNVPEMFIKKEELQELKCADVEDEDWDISSLEEEISLGKKSGKEQKEPPPAKNEPHFAHVLNAWGAFNPKGPKGEGLQENESSTLKSSLVTVTDWSDTSDV
uniprot
proteins
disease_involvement
DISEASE: Mitral valve prolapse 3 (MVP3) [MIM:610840]: An autosomal dominant form of mitral valve prolapse, a valvular heart disease characterized by abnormally elongated and thickened mitral valve leaflets, that typically show myxomatous degeneration with increased leaflet compliance. It is associated with mitral regurgitation. Myxomatous mitral valves have an abnormal layered architecture characterized by loose collagen in fibrosa, expanded spongiosa strongly positive for proteoglycans, and disrupted elastin in atrialis. In classic mitral valve prolapse, leaflets are at least 5 mm thick, whereas in the non-classic form, they are less than 5 mm thick. Severe classic mitral valve prolapse is strongly associated with arrhythmias, endocarditis, heart failure, and need for valve surgery. {ECO:0000269|PubMed:31118289}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spermatogenic failure 47 (SPGF47) [MIM:619102]: An autosomal recessive infertility disorder caused by spermatogenesis defects resulting in asthenoteratozoospermia. SPGF47 is characterized by reduced sperm concentrations and immotile spermatozoa, with short or absent flagella as well as centriolar abnormalities. {ECO:0000269|PubMed:32051257}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Molecular adapter that recruits protein complexes required for cilium assembly and function to the cilium basal body (PubMed:19852954, PubMed:23955340, PubMed:27979967, PubMed:32051257). At the exit of mitosis, localizes to the basal body and ciliary base of the forming primary cilium where it recruits and activates RAB8A to direct vesicle-mediated transport of proteins to the cilium (By similarity). Also recruits the BBSome, a complex involved in cilium biogenesis, by bridging it to PCM1 at the centriolar satellites of the cilium (PubMed:27979967). It is also required for the recruitment to the cilium basal body of the intraflagellar transport (IFT) machinery as well as the ciliary appendage proteins CEP164 and NINEIN (By similarity). Functions as a regulator of Hedgehog signaling both through its role in cilium assembly but also probably through its ability to retain GLI3 within the cytoplasm (By similarity). It is involved in spermatogenesis through its role in organization of the basal body and assembly of the sperm flagellum (PubMed:32051257). Also indirectly involved in heart development through its function in ciliogenesis (PubMed:31118289). {ECO:0000250|UniProtKB:Q8BMD2, ECO:0000269|PubMed:19852954, ECO:0000269|PubMed:23955340, ECO:0000269|PubMed:27979967, ECO:0000269|PubMed:31118289, ECO:0000269|PubMed:32051257}.
uniprot
proteins
mass_dalton
98664
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-226 by PLK1 before mitosis prevents interaction with PCM1 and localization to centriolar satellites. Thereby, it negatively regulates the localization of the BBSome to centriolar satellites. {ECO:0000250|UniProtKB:Q8BMD2}.
uniprot
proteins
protein_family
DZIP C2H2-type zinc-finger protein family
uniprot
proteins
pubmed
10231032
uniprot
proteins
pubmed
12511597
uniprot
proteins
pubmed
15057823
uniprot
proteins
pubmed
15081113
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
19852954
uniprot
proteins
pubmed
23955340
uniprot
proteins
pubmed
25860027
uniprot
proteins
pubmed
27979967
uniprot
proteins
pubmed
31118289
uniprot
proteins
pubmed
32051257
uniprot
proteins
sequence_length
867
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:19852954}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000269|PubMed:27979967}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:19852954}. Nucleus {ECO:0000269|PubMed:15081113}. Nucleus speckle {ECO:0000250|UniProtKB:Q8BMD2}. Cytoplasm {ECO:0000269|PubMed:15081113}. Note=Localizes to the centriole in cells lacking cilia and to the cilium basal body in ciliated cells (PubMed:19852954). At the exit of mitosis, when the primary cilium is reassembled in daughter cells, localizes at the mother centriole that acts as the basal body of the assembling primary cilium and also accumulates at the ciliary base that constitutes a diffusion barrier for ciliary proteins (By similarity). {ECO:0000250|UniProtKB:Q8BMD2, ECO:0000269|PubMed:19852954}.
uniprot
proteins