LITAF
entrez
9516
canonical
uniprot
Q99732
canonical
ensembl
ENSG00000189067
resolver
ensp
ENSP00000340118
resolver
ensp
ENSP00000397958
resolver
ensp
ENSP00000459138
resolver
ensp
ENSP00000483114
resolver
ensp
ENSP00000558177
resolver
ensp
ENSP00000598797
resolver
genesymbol
LITAF
resolver
genesymbol_syn
PIG7
resolver
genesymbol_syn
SIMPLE
resolver
hgnc
HGNC:16841
resolver
uniprot
D3DUG1
resolver
uniprot
G5E9K0
resolver
uniprot
Q05DW0
resolver
uniprot
Q9C0L6
resolver
uniprot_entry
LITAF_HUMAN
resolver
uniprot_sec
D3DUG1
resolver
uniprot_sec
G5E9K0
resolver
uniprot_sec
Q05DW0
resolver
uniprot_sec
Q9C0L6
resolver
amino_acid_sequence
MSVPGPYQAATGPSSAPSAPPSYEETVAVNSYYPTPPAPMPGPTTGLVTGPDGKGMNPPSYYTQPAPIPNNNPITVQTVYVQHPITFLDRPIQMCCPSCNKMIVSQLSYNAGALTWLSCGSLCLLGCIAGCCFIPFCVDALQDVDHYCPNCRALLGTYKRL
uniprot
proteins
disease_involvement
DISEASE: Charcot-Marie-Tooth disease, demyelinating, type 1C (CMT1C) [MIM:601098]: A dominant demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. {ECO:0000269|PubMed:12525712, ECO:0000269|PubMed:15776429, ECO:0000269|PubMed:15786462, ECO:0000269|PubMed:16118794, ECO:0000269|PubMed:21896645, ECO:0000269|PubMed:23166352, ECO:0000269|PubMed:24604904}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=Defects in LITAF may be involved in extramammary Paget disease (EMPD) carcinogenesis. EMPD is a cancerous disease representing about 8% of all malignant skin cancers; it usually appears in the anogenital area and can be fatal by metastasizing to internal organs when left untreated for a long time. The clinical features are usually those of eczematous eruptions with weeping and crust formation. {ECO:0000269|PubMed:15197774}.
uniprot
proteins
function
FUNCTION: Plays a role in endosomal protein trafficking and in targeting proteins for lysosomal degradation (PubMed:23166352). Plays a role in targeting endocytosed EGFR and ERGG3 for lysosomal degradation, and thereby helps down-regulate downstream signaling cascades (PubMed:23166352). Helps recruit the ESCRT complex components TSG101, HGS and STAM to cytoplasmic membranes (PubMed:23166352). Probably plays a role in regulating protein degradation via its interaction with NEDD4 (PubMed:15776429). May also contribute to the regulation of gene expression in the nucleus (PubMed:10200294, PubMed:15793005). Binds DNA (in vitro) and may play a synergistic role with STAT6 in the nucleus in regulating the expression of various cytokines (PubMed:15793005). May regulate the expression of numerous cytokines, such as TNF, CCL2, CCL5, CXCL1, IL1A and IL10 (PubMed:10200294, PubMed:15793005). {ECO:0000269|PubMed:15793005, ECO:0000269|PubMed:23166352, ECO:0000303|PubMed:15776429, ECO:0000305|PubMed:10200294}.
uniprot
proteins
mass_dalton
17107
uniprot
proteins
mutagenesis
MUTAGEN 17..20; /note="PSAP->ASAA: Impaired function in targeting endocytosed proteins for lysosomal degradation."; /evidence="ECO:0000269|PubMed:23166352"; MUTAGEN 17..19; /note="PSA->AGG: Abolishes interaction with TSG101."; /evidence="ECO:0000269|PubMed:16118794"; MUTAGEN 23; /note="Y->A: Abolishes interaction with NEDD4."; /evidence="ECO:0000269|PubMed:16118794"; MUTAGEN 23; /note="Y->A: Abolishes interaction with WWOX. Abolishes interaction with NEDD4. Abolishes interaction with NEDD4 and impairs location at endosomes; when associated with A-61."; /evidence="ECO:0000269|PubMed:15064722, ECO:0000269|PubMed:27927196"; MUTAGEN 61; /note="Y->A: No effect on interaction with WWOX. No effect on interaction with NEDD4. Abolishes interaction with NEDD4 and impairs location at endosomes; when associated with A-23."; /evidence="ECO:0000269|PubMed:15064722, ECO:0000269|PubMed:27927196"; MUTAGEN 96; /note="C->A: Abolishes association with cytoplasmic vesicle membranes."; /evidence="ECO:0000269|PubMed:27582497"; MUTAGEN 135; /note="P->T: Decreases protein stability and association with early endosome membranes. Impaired function in targeting endocytosed proteins for lysosomal degradation."; /evidence="ECO:0000269|PubMed:21896645, ECO:0000269|PubMed:23166352"; MUTAGEN 144; /note="V->M: No effect on location at endosomes, but impairs protein stability."; /evidence="ECO:0000269|PubMed:27927196"; MUTAGEN 148; /note="C->A: Abolishes association with cytoplasmic vesicle membranes."; /evidence="ECO:0000269|PubMed:27582497
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residues in response to EGF. {ECO:0000269|PubMed:23166352}.
uniprot
proteins
protein_family
CDIP1/LITAF family
uniprot
proteins
pubmed
10200294
uniprot
proteins
pubmed
11274176
uniprot
proteins
pubmed
12525712
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15064722
uniprot
proteins
pubmed
15197774
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
15776429
uniprot
proteins
pubmed
15786462
uniprot
proteins
pubmed
15793005
uniprot
proteins
pubmed
16118794
uniprot
proteins
pubmed
16954198
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
21896645
uniprot
proteins
pubmed
23166352
uniprot
proteins
pubmed
24604904
uniprot
proteins
pubmed
27582497
uniprot
proteins
pubmed
27927196
uniprot
proteins
pubmed
9305847
uniprot
proteins
sequence_length
161
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15793005}. Nucleus {ECO:0000269|PubMed:15793005, ECO:0000269|PubMed:16954198}. Lysosome membrane {ECO:0000269|PubMed:11274176, ECO:0000269|PubMed:27582497}; Peripheral membrane protein {ECO:0000269|PubMed:11274176}; Cytoplasmic side {ECO:0000269|PubMed:11274176}. Early endosome membrane {ECO:0000269|PubMed:21896645, ECO:0000269|PubMed:23166352, ECO:0000269|PubMed:27582497}. Late endosome membrane {ECO:0000269|PubMed:27582497}. Endosome membrane {ECO:0000269|PubMed:27927196}; Peripheral membrane protein {ECO:0000269|PubMed:27927196}; Cytoplasmic side {ECO:0000269|PubMed:27927196}. Cell membrane {ECO:0000269|PubMed:16118794, ECO:0000269|PubMed:27582497}; Peripheral membrane protein {ECO:0000269|PubMed:27582497}; Cytoplasmic side {ECO:0000269|PubMed:27582497}. Golgi apparatus membrane {ECO:0000269|PubMed:16118794}. Note=Associated with membranes of lysosomes, early and late endosomes (PubMed:11274176, PubMed:27582497, PubMed:27927196). Can translocate from the cytoplasm into the nucleus (PubMed:15793005). Detected at Schmidt-Lanterman incisures and in nodal regions of myelinating Schwann cells (By similarity). {ECO:0000250|UniProtKB:Q9JLJ0, ECO:0000269|PubMed:11274176, ECO:0000269|PubMed:15793005, ECO:0000269|PubMed:27582497, ECO:0000269|PubMed:27927196}.
uniprot
proteins