LUZP1
entrez
7798
canonical
uniprot
Q86V48
canonical
ensembl
ENSG00000169641
resolver
ensp
ENSP00000303758
resolver
ensp
ENSP00000428061
resolver
ensp
ENSP00000516586
resolver
genesymbol
LUZP1
resolver
hgnc
HGNC:14985
resolver
uniprot
Q05DE3
resolver
uniprot
Q5TH93
resolver
uniprot
Q8N4X3
resolver
uniprot
Q8TEH1
resolver
uniprot_entry
LUZP1_HUMAN
resolver
uniprot_entry
Q05DE3_HUMAN
resolver
uniprot_sec
Q5TH93
resolver
uniprot_sec
Q8N4X3
resolver
uniprot_sec
Q8TEH1
resolver
amino_acid_sequence
MAEFTSYKETASSRHLRFKLQSLSRRLDELEEATKNLQKAEDELLDLQDKVIQAEGSNSSMLAEIEVLRQRVLRIEGKDEEIKRAEDLCRLMKEKLEEEENLTRELKSEIERLQKRMAELEKLEEAFSRSKNDCTQLCLSLNEERNLTKKISSELEMLRVKVKELESSEDRLDKTEQSLASELEKLKSLTLSFVSERKYLNEKEKENEKLIKELTQKLEQNKKMNRDYTRNASNLERNDLRIEDGISSTLPSKESRRKGGLDYLKQVENETRNKSENEKNRNQEDNKVKDLNQEIEKLKTQIKHFESLEEELKKMKSKNNDLQDNYLSEQNKNKLLASQLEEIKLQIKKQKELENGEVEGEDAFLSSKGRHERTKFRGHGSEASVSKHTARELSPQHKRERLRNREFALNNENYSLSNRQVSSPSFTNRRAAKASHMGVSTDSGTQETKKTEDRFVPGSSQSEGKKSREQPSVLSRYPPAAQEHSKAWKGTSKPGTESGLKGKVEKTTRTFSDTTHGSVPSDPLGRADKASDTSSETVFGKRGHVLGNGSQVTQAANSGCSKAIGALASSRRSSSEGLSKGKKAANGLEADNSCPNSKAPVLSKYPYSCRSQENILQGFSTSHKEGVNQPAAVVMEDSSPHEALRCRVIKSSGREKPDSDDDLDIASLVTAKLVNTTITPEPEPKPQPNSREKAKTRGAPRTSLFENDKDAGMENESVKSVRASTNTMELPDTNGAGVKSQRPFSPREALRSRAIIKPVIVDKDVKKIMGGSGTETTLEKQKPVSKPGPNKVTSSITIYPSDSSSPRAAPGEALRERHTSTSNIQVGLAELTSVSNHVSSPFELSIHKHDITLQLAEAERMADGPLKDRPETVVSRSSIIIKPSDPVERNSHAPPAETIRWKSHSAPSEVGFSDARHVTVRNAWKSRRDLKSLEDPPTRIGKNVESTNSNAYTQRSSTDFSELEQPRSCLFEQGTRRVGPSSGDAPEPSSRRTQSSLTVSEVLTRRNRVGDTITVAAWNHSASMEEEGEDCTLSVYRQLHNSLDPSELPGKQGLPESGRVRAEERLRPTRPCAEEN
uniprot
proteins
disease_involvement
DISEASE: Note=Interacts with a truncated form of SALL1 associated with Townes-Brocks syndrome 1 (TBS1) and may contribute to the cilium defects seen in TBS1 (PubMed:32553112). The truncated SALL1 form promotes proteasome-mediated degradation of LUZP1 (PubMed:32553112). {ECO:0000269|PubMed:32553112}.
uniprot
proteins
function
FUNCTION: F-actin cross-linking protein (PubMed:30990684). Stabilizes actin and acts as a negative regulator of primary cilium formation (PubMed:32496561). Positively regulates the phosphorylation of both myosin II and protein phosphatase 1 regulatory subunit PPP1R12A/MYPT1 and promotes the assembly of myosin II stacks within actin stress fibers (PubMed:38832964). Inhibits the phosphorylation of myosin light chain MYL9 by DAPK3 and suppresses the constriction velocity of the contractile ring during cytokinesis (PubMed:38009294). Binds to microtubules and promotes epithelial cell apical constriction by up-regulating levels of diphosphorylated myosin light chain (MLC) through microtubule-dependent inhibition of MLC dephosphorylation by myosin phosphatase (By similarity). Involved in regulation of cell migration, nuclear size and centriole number, probably through regulation of the actin cytoskeleton (By similarity). Component of the CERF-1 and CERF-5 chromatin remodeling complexes in embryonic stem cells where it acts to stabilize the complexes (By similarity). Plays a role in embryonic brain and cardiovascular development (By similarity). {ECO:0000250|UniProtKB:Q8R4U7, ECO:0000269|PubMed:30990684, ECO:0000269|PubMed:32496561, ECO:0000269|PubMed:38009294, ECO:0000269|PubMed:38832964}.
uniprot
proteins
mass_dalton
120275
uniprot
proteins
mutagenesis
MUTAGEN 573; /note="S->A: Does not affect localization to the centrosome or midbody during mitosis."; /evidence="ECO:0000269|PubMed:38009294"; MUTAGEN 574; /note="S->A: Does not affect localization to the centrosome or midbody during mitosis."; /evidence="ECO:0000269|PubMed:38009294"; MUTAGEN 679; /note="T->A: Does not affect localization to the centrosome or midbody during mitosis."; /evidence="ECO:0000269|PubMed:38009294"; MUTAGEN 838..840; /note="VSS->ASA: Abolishes binding to FLNA; when associated with 873-A--A-875."; /evidence="ECO:0000269|PubMed:30990684"; MUTAGEN 840; /note="S->A: Does not affect localization to the centrosome or midbody during mitosis."; /evidence="ECO:0000269|PubMed:38009294"; MUTAGEN 873..875; /note="VVS->AVA: Abolishes binding to FLNA; when associated with 838-A--A-840."; /evidence="ECO:0000269|PubMed:30990684"; MUTAGEN 878; /note="S->A: Does not affect localization to the centrosome or midbody during mitosis."; /evidence="ECO:0000269|PubMed:38009294"; MUTAGEN 891; /note="S->A: Does not affect localization to the centrosome or midbody during mitosis."; /evidence="ECO:0000269|PubMed:38009294"; MUTAGEN 926; /note="S->A: Does not affect localization to the centrosome or midbody during mitosis."; /evidence="ECO:0000269|PubMed:38009294
uniprot
proteins
pubmed
12693554
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26638075
uniprot
proteins
pubmed
30990684
uniprot
proteins
pubmed
32496561
uniprot
proteins
pubmed
32553112
uniprot
proteins
pubmed
38009294
uniprot
proteins
pubmed
38832964
uniprot
proteins
sequence_length
1076
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:26638075, ECO:0000269|PubMed:32496561, ECO:0000269|PubMed:32553112}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:32496561}. Midbody {ECO:0000269|PubMed:32496561, ECO:0000269|PubMed:32553112}. Chromosome, centromere {ECO:0000269|PubMed:38009294}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:38009294}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:30990684, ECO:0000269|PubMed:32553112, ECO:0000269|PubMed:38832964}. Nucleus {ECO:0000250|UniProtKB:Q9ESV1}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9ESV1}. Perikaryon {ECO:0000250|UniProtKB:Q9ESV1}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q8R4U7}. Note=Localizes to the proximal end of basal bodies (PubMed:32496561). During mitosis, localizes at the inner centromere in metaphase, at the central spindle in anaphase, and at the midbody in telophase (PubMed:38009294). Central spindle localization requires KIF20A while centromere localization requires the kinase activity of the chromosomal passenger complex (PubMed:38009294). {ECO:0000269|PubMed:32496561, ECO:0000269|PubMed:38009294}.
uniprot
proteins