MEFV
entrez
4210
canonical
uniprot
O15553
canonical
ensembl
ENSG00000103313
resolver
ensp
ENSP00000219596
resolver
ensp
ENSP00000438711
resolver
genesymbol
MEFV
resolver
genesymbol_syn
MEF
resolver
genesymbol_syn
TRIM20
resolver
hgnc
HGNC:6998
resolver
uniprot
D2DTW2
resolver
uniprot
D3DUC0
resolver
uniprot
F5H0Q3
resolver
uniprot
Q3MJ84
resolver
uniprot
Q96PN4
resolver
uniprot
Q96PN5
resolver
uniprot_entry
D2DTW2_HUMAN
resolver
uniprot_entry
MEFV_HUMAN
resolver
uniprot_sec
D3DUC0
resolver
uniprot_sec
F5H0Q3
resolver
uniprot_sec
Q3MJ84
resolver
uniprot_sec
Q96PN4
resolver
uniprot_sec
Q96PN5
resolver
amino_acid_sequence
MAKTPSDHLLSTLEELVPYDFEKFKFKLQNTSVQKEHSRIPRSQIQRARPVKMATLLVTYYGEEYAVQLTLQVLRAINQRLLAEELHRAAIQEYSTQENGTDDSAASSSLGENKPRSLKTPDHPEGNEGNGPRPYGGGAASLRCSQPEAGRGLSRKPLSKRREKASEGLDAQGKPRTRSPALPGGRSPGPCRALEGGQAEVRLRRNASSAGRLQGLAGGAPGQKECRPFEVYLPSGKMRPRSLEVTISTGEKAPANPEILLTLEEKTAANLDSATEPRARPTPDGGASADLKEGPGNPEHSVTGRPPDTAASPRCHAQEGDPVDGTCVRDSCSFPEAVSGHPQASGSRSPGCPRCQDSHERKSPGSLSPQPLPQCKRHLKQVQLLFCEDHDEPICLICSLSQEHQGHRVRPIEEVALEHKKKIQKQLEHLKKLRKSGEEQRSYGEEKAVSFLKQTEALKQRVQRKLEQVYYFLEQQEHFFVASLEDVGQMVGQIRKAYDTRVSQDIALLDALIGELEAKECQSEWELLQDIGDILHRAKTVPVPEKWTTPQEIKQKIQLLHQKSEFVEKSTKYFSETLRSEMEMFNVPELIGAQAHAVNVILDAETAYPNLIFSDDLKSVRLGNKWERLPDGPQRFDSCIIVLGSPSFLSGRRYWEVEVGDKTAWILGACKTSISRKGNMTLSPENGYWVVIMMKENEYQASSVPPTRLLIKEPPKRVGIFVDYRVGSISFYNVTARSHIYTFASCSFSGPLQPIFSPGTRDGGKNTAPLTICPVGGQGPD
uniprot
proteins
disease_involvement
DISEASE: Familial Mediterranean fever, autosomal recessive (ARFMF) [MIM:249100]: A hereditary periodic fever syndrome characterized by recurrent episodic fever, serosal inflammation and pain in the abdomen, chest or joints. It is frequently complicated by reactive amyloidosis, which leads to renal failure and can be prophylactically treated with colchicine. {ECO:0000269|PubMed:10024914, ECO:0000269|PubMed:10090880, ECO:0000269|PubMed:10234504, ECO:0000269|PubMed:10364520, ECO:0000269|PubMed:10612841, ECO:0000269|PubMed:10842288, ECO:0000269|PubMed:10854105, ECO:0000269|PubMed:11464238, ECO:0000269|PubMed:11470495, ECO:0000269|PubMed:12124996, ECO:0000269|PubMed:15024744, ECO:0000269|PubMed:16378925, ECO:0000269|PubMed:16730661, ECO:0000269|PubMed:23031807, ECO:0000269|PubMed:24929125, ECO:0000269|PubMed:26347139, ECO:0000269|PubMed:27030597, ECO:0000269|PubMed:9288094, ECO:0000269|PubMed:9288758, ECO:0000269|PubMed:9668175}. Note=The disease is caused by variants affecting the gene represented in this entry. The disease-associated mutations in the B30.2/SPRY domain perturb ULK1 recruitment and autophagic degradation of inflammasome components, including NLRP3, and hence may contribute to the inflammatory phenotype associated with ARFMF. {ECO:0000269|PubMed:26347139}.; DISEASE: Familial Mediterranean fever, autosomal dominant (ADFMF) [MIM:134610]: A hereditary periodic fever syndrome characterized by periodic fever, serosal inflammation and pain in the abdomen, chest or joints as seen also in the autosomal recessive form of the disease. It is associated with reactive renal amyloidosis and characterized by colchicine unresponsiveness. {ECO:0000269|PubMed:10787449, ECO:0000269|PubMed:14679589}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Pyrin-associated autoinflammatory disease (PAAND) [MIM:608068]: An autosomal dominant autoinflammatory disorder characterized by childhood onset of recurrent episodes of fever, neutrophilic dermatosis, myalgia and arthralgia. The neutrophilic dermatosis comprises a spectrum of clinical manifestations, including severe acne, sterile skin abscesses, pyoderma gangrenosum, and neutrophilic small-vessel vasculitis. Pathological examination of affected skin shows a dense, predominantly neutrophilic, vascular, perivascular, and interstitial infiltrate. PAAND has incomplete penetrance and variable expressivity. {ECO:0000269|PubMed:27030597, ECO:0000269|PubMed:28835462}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma (PubMed:10807793, PubMed:11468188, PubMed:16037825, PubMed:16785446, PubMed:17431422, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923, PubMed:26347139, PubMed:27030597, PubMed:28835462). Organizes autophagic machinery by serving as a platform for the assembly of ULK1, Beclin 1/BECN1, ATG16L1, and ATG8 family members and recognizes specific autophagy targets, thus coordinating target recognition with assembly of the autophagic apparatus and initiation of autophagy (PubMed:16785446, PubMed:17431422, PubMed:26347139). Acts as an autophagy receptor for the degradation of several inflammasome components, including CASP1, NLRP1 and NLRP3, hence preventing excessive IL1B- and IL18-mediated inflammation (PubMed:16785446, PubMed:17431422, PubMed:26347139). However, it can also have a positive effect in the inflammatory pathway, acting as an innate immune sensor that triggers PYCARD/ASC specks formation, caspase-1 activation, and IL1B and IL18 production (PubMed:16037825, PubMed:27030597, PubMed:28835462). Together with AIM2, also acts as a mediator of pyroptosis, necroptosis and apoptosis (PANoptosis), an integral part of host defense against pathogens, in response to bacterial infection (By similarity). It is required for PSTPIP1-induced PYCARD/ASC oligomerization and inflammasome formation (PubMed:10807793, PubMed:11468188, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923). Recruits PSTPIP1 to inflammasomes, and is required for PSTPIP1 oligomerization (PubMed:10807793, PubMed:11468188, PubMed:17964261, PubMed:18577712, PubMed:19109554, PubMed:19584923). {ECO:0000250|UniProtKB:Q9JJ26, ECO:0000269|PubMed:10807793, ECO:0000269|PubMed:11468188, ECO:0000269|PubMed:16037825, ECO:0000269|PubMed:16785446, ECO:0000269|PubMed:17431422, ECO:0000269|PubMed:17964261, ECO:0000269|PubMed:18577712, ECO:0000269|PubMed:19109554, ECO:0000269|PubMed:19584923, ECO:0000269|PubMed:26347139, ECO:0000269|PubMed:27030597, ECO:0000269|PubMed:28835462}.
uniprot
proteins
mass_dalton
86444
uniprot
proteins
mutagenesis
MUTAGEN 16; /note="L->P: Does not form MEFV- and PSTPIP1-containing perinuclear specks."; /evidence="ECO:0000269|PubMed:16037825"; MUTAGEN 24; /note="F->S: Does not form MEFV- and PSTPIP1-containing perinuclear specks."; /evidence="ECO:0000269|PubMed:16037825"; MUTAGEN 208; /note="S->A: Loss of interaction with 14-3-3 proteins."; /evidence="ECO:0000269|PubMed:28835462"; MUTAGEN 244; /note="E->D: No effect on PYCARD/ASC specks formation. No effect on interaction with 14-3-3 proteins."; /evidence="ECO:0000269|PubMed:28835462"; MUTAGEN 244; /note="E->P: No effect on PYCARD/ASC specks formation. Increased interaction with 14-3-3 proteins."; /evidence="ECO:0000269|PubMed:28835462"; MUTAGEN 244; /note="E->R: Increased PYCARD/ASC specks formation. Decreased interaction with 14-3-3 proteins."; /evidence="ECO:0000269|PubMed:28835462"; MUTAGEN 330; /note="D->A: Loss of cleavage by CASP1."; /evidence="ECO:0000269|PubMed:18577712"; MUTAGEN 397..404; /note="Missing: No effect on GABARAP-binding. Loss of GABARAP-binding; when associated with 470-Y--G-488 and 523-S--D-530."; MUTAGEN 470..488; /note="Missing: No effect on GABARAP-binding. Loss of GABARAP-binding; when associated with 397-I--H-404 and 523-S--D-530."; MUTAGEN 523..530; /note="Missing: No effect on GABARAP-binding. Loss of GABARAP-binding; when associated with 397-I--H-404 and 470-Y--G-488.
uniprot
proteins
post_translational_modification
PTM: Cleaved by CASP1 (Probable). The N-terminal cleavage product localizes to the nucleus as a filamentous network and to the cytoplasm, interacts more strongly with RELA and NFKBIA than the full-length protein, enhances the nuclear localization of RELA and induces NFKBIA proteolysis. The C-terminal cleavage product localizes to the cytoplasm (Probable). {ECO:0000305|PubMed:18577712}.; PTM: Phosphorylation at Ser-242 is required for the interaction with 14-3-3 proteins and down-regulation of pyrin pro-inflammatory activity. {ECO:0000269|PubMed:27030597}.; PTM: Degraded along with the delivery of its substrates to autolysosomal compartments (at protein level). {ECO:0000269|PubMed:26347139}.
uniprot
proteins
pubmed
10024914
uniprot
proteins
pubmed
10090880
uniprot
proteins
pubmed
10234504
uniprot
proteins
pubmed
10364520
uniprot
proteins
pubmed
10612841
uniprot
proteins
pubmed
10666224
uniprot
proteins
pubmed
10737995
uniprot
proteins
pubmed
10787449
uniprot
proteins
pubmed
10807793
uniprot
proteins
pubmed
10842288
uniprot
proteins
pubmed
10854105
uniprot
proteins
pubmed
11115844
uniprot
proteins
pubmed
11464238
uniprot
proteins
pubmed
11468188
uniprot
proteins
pubmed
11470495
uniprot
proteins
pubmed
11498534
uniprot
proteins
pubmed
12124996
uniprot
proteins
pubmed
12384939
uniprot
proteins
pubmed
14595024
uniprot
proteins
pubmed
14679589
uniprot
proteins
pubmed
15024744
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16037825
uniprot
proteins
pubmed
16378925
uniprot
proteins
pubmed
16730661
uniprot
proteins
pubmed
16785446
uniprot
proteins
pubmed
17431422
uniprot
proteins
pubmed
17964261
uniprot
proteins
pubmed
18577712
uniprot
proteins
pubmed
19109554
uniprot
proteins
pubmed
19584923
uniprot
proteins
pubmed
19729025
uniprot
proteins
pubmed
23031807
uniprot
proteins
pubmed
23505238
uniprot
proteins
pubmed
24929125
uniprot
proteins
pubmed
26347139
uniprot
proteins
pubmed
27030597
uniprot
proteins
pubmed
28835462
uniprot
proteins
pubmed
9288094
uniprot
proteins
pubmed
9288758
uniprot
proteins
pubmed
9668175
uniprot
proteins
sequence_length
781
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11468188, ECO:0000269|PubMed:19109554}. Cell projection, ruffle {ECO:0000269|PubMed:11468188}. Cell projection, lamellipodium {ECO:0000269|PubMed:11468188}. Nucleus {ECO:0000269|PubMed:11115844}. Cytoplasm {ECO:0000269|PubMed:10666224, ECO:0000269|PubMed:11498534, ECO:0000269|PubMed:18577712, ECO:0000269|PubMed:19584923, ECO:0000269|PubMed:26347139}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:26347139}. Note=Associated with microtubules and with the filamentous actin of perinuclear filaments and peripheral lamellar ruffles (PubMed:11468188). In pre-apoptotic cells, colocalizes with PYCARD/ASC in large specks (inflammasomes) (PubMed:11468188). In migrating monocytes, strongly polarized at the leading edge of the cell where it colocalizes with polymerizing actin and PYCARD/ASC (PubMed:11468188). {ECO:0000269|PubMed:11468188}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:11115844}.
uniprot
proteins