CAR14_HUMAN
ID CAR14_HUMAN Reviewed; 1004 AA.
AC Q9BXL6; B8QQJ3; Q9BVB5;
DT 31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Caspase recruitment domain-containing protein 14;
DE AltName: Full=CARD-containing MAGUK protein 2;
DE Short=Carma 2;
GN Name=CARD14; Synonyms=CARMA2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND VARIANT TRP-820.
RX PubMed=11278692; DOI=10.1074/jbc.m010512200;
RA Bertin J., Wang L., Guo Y., Jacobson M.D., Poyet J.-L., Srinivasula S.M.,
RA Merriam S., DiStefano P.S., Alnemri E.S.;
RT "CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-
RT associated guanylate kinase (MAGUK) family members that interact with Bcl10
RT and activate NF-kappaB.";
RL J. Biol. Chem. 276:11877-11882(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT TRP-820.
RX PubMed=11356195; DOI=10.1016/s0014-5793(01)02414-0;
RA Gaide O., Martinon F., Micheau O., Bonnet D., Thome M., Tschopp J.;
RT "Carma1, a CARD-containing binding partner of Bcl10, induces Bcl10
RT phosphorylation and NF-kappaB activation.";
RL FEBS Lett. 496:121-127(2001).
RN [3]
RP ERRATUM OF PUBMED:11356195.
RA Gaide O., Martinon F., Micheau O., Bonnet D., Thome M., Tschopp J.;
RL FEBS Lett. 505:198-198(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, INTERACTION
RP WITH BCL10; TRAF2; TRAF3 AND TRAF6, SUBCELLULAR LOCATION, AND ALTERNATIVE
RP SPLICING.
RX PubMed=21302310; DOI=10.1002/jcp.22667;
RA Scudiero I., Zotti T., Ferravante A., Vessichelli M., Vito P., Stilo R.;
RT "Alternative splicing of CARMA2/CARD14 transcripts generates protein
RT variants with differential effect on NF-kappaB activation and endoplasmic
RT reticulum stress-induced cell death.";
RL J. Cell. Physiol. 226:3121-3131(2011).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Cervix, and Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP TISSUE SPECIFICITY, VARIANTS PSORS2 SER-117 AND ALA-138, AND
RP CHARACTERIZATION OF VARIANTS PSORS2 SER-117 AND ALA-138.
RX PubMed=22521418; DOI=10.1016/j.ajhg.2012.03.012;
RA Jordan C.T., Cao L., Roberson E.D., Pierson K.C., Yang C.F., Joyce C.E.,
RA Ryan C., Duan S., Helms C.A., Liu Y., Chen Y., McBride A.A., Hwu W.L.,
RA Wu J.Y., Chen Y.T., Menter A., Goldbach-Mansky R., Lowes M.A.,
RA Bowcock A.M.;
RT "PSORS2 is due to mutations in CARD14.";
RL Am. J. Hum. Genet. 90:784-795(2012).
RN [9]
RP FUNCTION, SUBUNIT, AND CHARACTERIZATION OF VARIANTS PSORS2 SER-117 AND
RP ALA-138.
RX PubMed=27071417; DOI=10.1042/bcj20160270;
RA Howes A., O'Sullivan P.A., Breyer F., Ghose A., Cao L., Krappmann D.,
RA Bowcock A.M., Ley S.C.;
RT "Psoriasis mutations disrupt CARD14 autoinhibition promoting BCL10-MALT1-
RT dependent NF-kappaB activation.";
RL Biochem. J. 473:1759-1768(2016).
RN [10]
RP SUBUNIT, FUNCTION, CHARACTERIZATION OF VARIANTS PSORS2 SER-117; ALA-138 AND
RP LYS-142, AND CHARACTERIZATION OF VARIANT ASN-171.
RX PubMed=27113748; DOI=10.15252/embr.201642109;
RA Afonina I.S., Van Nuffel E., Baudelet G., Driege Y., Kreike M., Staal J.,
RA Beyaert R.;
RT "The paracaspase MALT1 mediates CARD14-induced signaling in
RT keratinocytes.";
RL EMBO Rep. 17:914-927(2016).
RN [11]
RP VARIANTS PRP GLU-138 DEL AND PRO-156.
RX PubMed=22703878; DOI=10.1016/j.ajhg.2012.05.010;
RA Fuchs-Telem D., Sarig O., van Steensel M.A., Isakov O., Israeli S.,
RA Nousbeck J., Richard K., Winnepenninckx V., Vernooij M., Shomron N.,
RA Uitto J., Fleckman P., Richard G., Sprecher E.;
RT "Familial pityriasis rubra pilaris is caused by mutations in CARD14.";
RL Am. J. Hum. Genet. 91:163-170(2012).
RN [12]
RP VARIANTS CYS-38; GLN-62; ARG-150; ASN-171; HIS-176; HIS-179; LEU-191;
RP ASN-200; GLY-285; ASN-593; TRP-682; SER-714 AND GLU-973, VARIANTS PSORS2
RP SER-117; ALA-138; LYS-142 AND GLY-142, AND CHARACTERIZATION OF VARIANTS
RP PSORS2 LYS-142 AND GLY-142.
RX PubMed=22521419; DOI=10.1016/j.ajhg.2012.03.013;
RA Jordan C.T., Cao L., Roberson E.D., Duan S., Helms C.A., Nair R.P.,
RA Duffin K.C., Stuart P.E., Goldgar D., Hayashi G., Olfson E.H., Feng B.J.,
RA Pullinger C.R., Kane J.P., Wise C.A., Goldbach-Mansky R., Lowes M.A.,
RA Peddle L., Chandran V., Liao W., Rahman P., Krueger G.G., Gladman D.,
RA Elder J.T., Menter A., Bowcock A.M.;
RT "Rare and Common Variants in CARD14, Encoding an Epidermal Regulator of NF-
RT kappaB, in Psoriasis.";
RL Am. J. Hum. Genet. 90:796-808(2012).
RN [13]
RP VARIANTS PSORS2 TRP-69; SER-117 GLN-151; TRP-151; LYS-197; PRO-209;
RP THR-216; ALA-420; LEU-602 AND GLY-639, CHARACTERIZATION OF VARIANTS PSORS2
RP TRP-69; SER-117; ARG-150; GLN-151; TRP-151; LYS-197; PRO-209; THR-216;
RP ALA-420; LEU-602 AND GLY-639, VARIANTS GLN-62; ARG-150; ASN-200; THR-216;
RP CYS-218; VAL-338; PRO-350 AND PRO-357, AND CHARACTERIZATION OF VARIANTS
RP GLN-151; TRP-151; CYS-218; LEU-602; VAL-338; ALA-420; PRO-209 AND GLY-639.
RX PubMed=26358359; DOI=10.1111/bjd.14158;
RA Ammar M., Jordan C.T., Cao L., Lim E., Bouchlaka Souissi C., Jrad A.,
RA Omrane I., Kouidhi S., Zaraa I., Anbunathan H., Mokni M., Doss N.,
RA Guttman-Yassky E., El Gaaied A.B., Menter A., Bowcock A.M.;
RT "CARD14 alterations in Tunisian patients with psoriasis and further
RT characterization in European cohorts.";
RL Br. J. Dermatol. 174:330-337(2016).
RN [14]
RP VARIANTS PRP SER-117; SER-127 AND LEU-136, AND VARIANT HIS-176.
RX PubMed=27760266; DOI=10.1001/jamadermatol.2016.3601;
RA Takeichi T., Sugiura K., Nomura T., Sakamoto T., Ogawa Y., Oiso N.,
RA Futei Y., Fujisaki A., Koizumi A., Aoyama Y., Nakajima K., Hatano Y.,
RA Hayashi K., Ishida-Yamamoto A., Fujiwara S., Sano S., Iwatsuki K.,
RA Kawada A., Suga Y., Shimizu H., McGrath J.A., Akiyama M.;
RT "Pityriasis rubra pilaris type V as an autoinflammatory disease by CARD14
RT mutations.";
RL JAMA Dermatol. 153:66-70(2017).
CC -!- FUNCTION: Acts as a scaffolding protein that can activate the
CC inflammatory transcription factor NF-kappa-B and p38/JNK MAP kinase
CC signaling pathways. Forms a signaling complex with BCL10 and MALT1, and
CC activates MALT1 proteolytic activity and inflammatory gene expression.
CC MALT1 is indispensable for CARD14-induced activation of NF-kappa-B and
CC p38/JNK MAP kinases (PubMed:11278692, PubMed:21302310, PubMed:27113748,
CC PubMed:27071417). May play a role in signaling mediated by TRAF2, TRAF3
CC and TRAF6 and protects cells against apoptosis.
CC {ECO:0000269|PubMed:11278692, ECO:0000269|PubMed:21302310,
CC ECO:0000269|PubMed:27071417, ECO:0000269|PubMed:27113748}.
CC -!- FUNCTION: [Isoform 3]: Not able to activate the inflammatory
CC transcription factor NF-kappa-B and may function as a dominant negative
CC regulator (PubMed:21302310, PubMed:26358359).
CC {ECO:0000269|PubMed:21302310, ECO:0000269|PubMed:26358359}.
CC -!- SUBUNIT: Interacts (via CARD domain) with BCL10 (via CARD domain)
CC (PubMed:21302310). Forms a complex with MALT1 and BCL10; resulting in
CC the formation of a CBM (CARD14-BLC10-MALT1) complex (PubMed:27113748,
CC PubMed:27071417). Interacts with TRAF2, TRAF3 and TRAF6
CC (PubMed:21302310). {ECO:0000269|PubMed:21302310,
CC ECO:0000269|PubMed:27071417, ECO:0000269|PubMed:27113748}.
CC -!- INTERACTION:
CC Q9BXL6-2; Q8WWY3: PRPF31; NbExp=4; IntAct=EBI-12114736, EBI-1567797;
CC Q9BXL6-2; Q5T619: ZNF648; NbExp=3; IntAct=EBI-12114736, EBI-11985915;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC {ECO:0000269|PubMed:21302310}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm
CC {ECO:0000269|PubMed:21302310}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm
CC {ECO:0000269|PubMed:21302310}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=CARD14fl {ECO:0000303|PubMed:27071417}, CARMA2fl
CC {ECO:0000303|PubMed:21302310};
CC IsoId=Q9BXL6-1; Sequence=Displayed;
CC Name=2; Synonyms=Short, CARD14sh {ECO:0000303|PubMed:27071417},
CC CARMA2sh {ECO:0000303|PubMed:21302310};
CC IsoId=Q9BXL6-2; Sequence=VSP_047403;
CC Name=3; Synonyms=Cardless, CARD14cardless, CARMA2cl
CC {ECO:0000303|PubMed:21302310};
CC IsoId=Q9BXL6-3; Sequence=VSP_047400, VSP_047401, VSP_047402;
CC -!- TISSUE SPECIFICITY: Isoform 1 is detected in placenta and epidermal
CC keratinocytes (PubMed:22521418). Isoform 2 is detected in leukocytes
CC and fetal brain (PubMed:22521418). {ECO:0000269|PubMed:22521418}.
CC -!- DOMAIN: A linker region between the coiled-coil and PDZ region holds
CC the protein in an inactive state (PubMed:27071417).
CC {ECO:0000269|PubMed:27071417}.
CC -!- DISEASE: Psoriasis 2 (PSORS2) [MIM:602723]: A common, chronic
CC inflammatory disease of the skin with multifactorial etiology. It is
CC characterized by red, scaly plaques usually found on the scalp, elbows
CC and knees. These lesions are caused by abnormal keratinocyte
CC proliferation and infiltration of inflammatory cells into the dermis
CC and epidermis. {ECO:0000269|PubMed:22521418,
CC ECO:0000269|PubMed:22521419, ECO:0000269|PubMed:26358359,
CC ECO:0000269|PubMed:27071417, ECO:0000269|PubMed:27113748}. Note=Disease
CC susceptibility is associated with variants affecting the gene
CC represented in this entry.
CC -!- DISEASE: Pityriasis rubra pilaris (PRP) [MIM:173200]: A rare,
CC papulosquamous skin disease characterized by the appearance of
CC keratotic follicular papules, well-demarcated salmon-colored
CC erythematous plaques covered with fine powdery scales interspersed with
CC distinct islands of uninvolved skin, and palmoplantar keratoderma. Most
CC cases are sporadic. The rare familial cases show autosomal dominant
CC inheritance with incomplete penetrance and variable expression.
CC Familial PRP usually presents at birth or appears during the first
CC years of life and runs a chronic course. It is characterized by
CC prominent follicular hyperkeratosis, diffuse palmoplantar keratoderma,
CC and erythema. {ECO:0000269|PubMed:22703878,
CC ECO:0000269|PubMed:27760266}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- CAUTION: Supposed to contain a SH3 domain which is not detected by
CC PROSITE, Pfam or SMART. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Caspase recruitment domain family, member 14
CC (CARD14); Note=Leiden Open Variation Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/CARD14";
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DR EMBL; AF322642; AAG53403.1; -; mRNA.
DR EMBL; AY032927; AAK54453.1; -; mRNA.
DR EMBL; EU652409; ACF49506.1; -; mRNA.
DR EMBL; AC087741; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018142; AAH18142.1; -; mRNA.
DR EMBL; BC001326; AAH01326.1; -; mRNA.
DR CCDS; CCDS11768.1; -. [Q9BXL6-1]
DR CCDS; CCDS58605.1; -. [Q9BXL6-2]
DR RefSeq; NP_001244899.1; NM_001257970.1. [Q9BXL6-2]
DR RefSeq; NP_077015.2; NM_024110.4. [Q9BXL6-1]
DR RefSeq; NP_438170.1; NM_052819.2. [Q9BXL6-3]
DR RefSeq; XP_011523514.1; XM_011525212.1.
DR RefSeq; XP_011523515.1; XM_011525213.1. [Q9BXL6-1]
DR RefSeq; XP_011523517.1; XM_011525215.1.
DR RefSeq; XP_011523518.1; XM_011525216.1. [Q9BXL6-1]
DR RefSeq; XP_011523519.1; XM_011525217.1. [Q9BXL6-1]
DR RefSeq; XP_011523520.1; XM_011525218.2. [Q9BXL6-1]
DR AlphaFoldDB; Q9BXL6; -.
DR SMR; Q9BXL6; -.
DR BioGRID; 122540; 15.
DR IntAct; Q9BXL6; 7.
DR STRING; 9606.ENSP00000458715; -.
DR iPTMnet; Q9BXL6; -.
DR PhosphoSitePlus; Q9BXL6; -.
DR BioMuta; CARD14; -.
DR DMDM; 296434421; -.
DR jPOST; Q9BXL6; -.
DR MassIVE; Q9BXL6; -.
DR MaxQB; Q9BXL6; -.
DR PaxDb; Q9BXL6; -.
DR PeptideAtlas; Q9BXL6; -.
DR PRIDE; Q9BXL6; -.
DR ProteomicsDB; 7285; -.
DR ProteomicsDB; 79449; -. [Q9BXL6-1]
DR Antibodypedia; 19763; 211 antibodies from 31 providers.
DR DNASU; 79092; -.
DR Ensembl; ENST00000344227.6; ENSP00000344549.2; ENSG00000141527.18. [Q9BXL6-1]
DR Ensembl; ENST00000570421.5; ENSP00000461806.1; ENSG00000141527.18. [Q9BXL6-2]
DR Ensembl; ENST00000573882.5; ENSP00000458715.1; ENSG00000141527.18. [Q9BXL6-1]
DR Ensembl; ENST00000648509.2; ENSP00000498071.1; ENSG00000141527.18. [Q9BXL6-1]
DR GeneID; 79092; -.
DR KEGG; hsa:79092; -.
DR MANE-Select; ENST00000648509.2; ENSP00000498071.1; NM_001366385.1; NP_001353314.1.
DR UCSC; uc002jxw.3; human. [Q9BXL6-1]
DR CTD; 79092; -.
DR DisGeNET; 79092; -.
DR GeneCards; CARD14; -.
DR HGNC; HGNC:16446; CARD14.
DR HPA; ENSG00000141527; Tissue enhanced (esophagus, skin, vagina).
DR MalaCards; CARD14; -.
DR MIM; 173200; phenotype.
DR MIM; 602723; phenotype.
DR MIM; 607211; gene.
DR neXtProt; NX_Q9BXL6; -.
DR OpenTargets; ENSG00000141527; -.
DR Orphanet; 2897; Pityriasis rubra pilaris.
DR PharmGKB; PA134959119; -.
DR VEuPathDB; HostDB:ENSG00000141527; -.
DR eggNOG; KOG0708; Eukaryota.
DR GeneTree; ENSGT00940000160777; -.
DR HOGENOM; CLU_009760_0_0_1; -.
DR InParanoid; Q9BXL6; -.
DR OMA; VVWTEQN; -.
DR OrthoDB; 115953at2759; -.
DR PhylomeDB; Q9BXL6; -.
DR TreeFam; TF315606; -.
DR PathwayCommons; Q9BXL6; -.
DR SignaLink; Q9BXL6; -.
DR BioGRID-ORCS; 79092; 31 hits in 1067 CRISPR screens.
DR ChiTaRS; CARD14; human.
DR GeneWiki; CARD14; -.
DR GenomeRNAi; 79092; -.
DR Pharos; Q9BXL6; Tbio.
DR PRO; PR:Q9BXL6; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9BXL6; protein.
DR Bgee; ENSG00000141527; Expressed in lower esophagus mucosa and 133 other tissues.
DR ExpressionAtlas; Q9BXL6; baseline and differential.
DR Genevisible; Q9BXL6; HS.
DR GO; GO:0016235; C:aggresome; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; NAS:UniProtKB.
DR GO; GO:0050700; F:CARD domain binding; IPI:UniProtKB.
DR GO; GO:0007250; P:activation of NF-kappaB-inducing kinase activity; NAS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IMP:UniProtKB.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR001315; CARD.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00619; CARD; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50209; CARD; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Coiled coil; Cytoplasm; Disease variant;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1004
FT /note="Caspase recruitment domain-containing protein 14"
FT /id="PRO_0000144088"
FT DOMAIN 15..107
FT /note="CARD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00046"
FT DOMAIN 568..658
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 807..990
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00100"
FT REGION 409..568
FT /note="Maintains the protein in an inactive state"
FT /evidence="ECO:0000269|PubMed:27071417"
FT COILED 128..409
FT /evidence="ECO:0000255"
FT MOD_RES 544
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336"
FT VAR_SEQ 1..237
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:21302310"
FT /id="VSP_047400"
FT VAR_SEQ 619..671
FT /note="DYEASEPLFKAVLEDTTLEEAVGLLRRVDGFCCLSVKVNTDGYKRLLQDLEA
FT K -> SRARPLLSPGLLMGTVAAGGVTQADFTSPRRCRSTLGWASALSWADVKRSAHL
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:21302310"
FT /id="VSP_047401"
FT VAR_SEQ 672..1004
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:21302310"
FT /id="VSP_047402"
FT VAR_SEQ 741..1004
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:21302310"
FT /id="VSP_047403"
FT VARIANT 38
FT /note="R -> C (in dbSNP:rs281875217)"
FT /evidence="ECO:0000269|PubMed:22521419"
FT /id="VAR_068222"
FT VARIANT 62
FT /note="R -> Q (in dbSNP:rs115582620)"
FT /evidence="ECO:0000269|PubMed:22521419,
FT ECO:0000269|PubMed:26358359"
FT /id="VAR_068223"
FT VARIANT 69
FT /note="R -> W (in PSORS2; reduces NF-kappa-B activation;
FT dbSNP:rs375624435)"
FT /evidence="ECO:0000269|PubMed:26358359"
FT /id="VAR_078583"
FT VARIANT 117
FT /note="G -> S (in PSORS2 and PRP; may result in altered
FT splicing of exon 3; increases NF-kappaB transcription
FT factor activity; enhances CBCL10-MALT1-CARD14 complex
FT formation; enhances MALT1 protease activity;
FT dbSNP:rs281875215)"
FT /evidence="ECO:0000269|PubMed:22521418,
FT ECO:0000269|PubMed:22521419, ECO:0000269|PubMed:26358359,
FT ECO:0000269|PubMed:27071417, ECO:0000269|PubMed:27113748,
FT ECO:0000269|PubMed:27760266"
FT /id="VAR_068224"
FT VARIANT 127
FT /note="C -> S (in PRP)"
FT /evidence="ECO:0000269|PubMed:27760266"
FT /id="VAR_078584"
FT VARIANT 136
FT /note="Q -> L (in PRP)"
FT /evidence="ECO:0000269|PubMed:27760266"
FT /id="VAR_078585"
FT VARIANT 138
FT /note="E -> A (in PSORS2; increases NF-kappaB transcription
FT factor activity; enhances CBCL10-MALT1-CARD14 complex
FT formation; enhances MALT1 protease activity;
FT dbSNP:rs281875214)"
FT /evidence="ECO:0000269|PubMed:22521418,
FT ECO:0000269|PubMed:22521419, ECO:0000269|PubMed:27071417,
FT ECO:0000269|PubMed:27113748"
FT /id="VAR_068225"
FT VARIANT 138
FT /note="Missing (in PRP)"
FT /evidence="ECO:0000269|PubMed:22703878"
FT /id="VAR_068819"
FT VARIANT 142
FT /note="E -> G (in PSORS2; increases NF-kappaB transcription
FT factor activity; dbSNP:rs281875213)"
FT /evidence="ECO:0000269|PubMed:22521419"
FT /id="VAR_068226"
FT VARIANT 142
FT /note="E -> K (in PSORS2; increases NF-kappaB transcription
FT factor activity; enhances MALT1 protease activity;
FT dbSNP:rs281875212)"
FT /evidence="ECO:0000269|PubMed:22521419,
FT ECO:0000269|PubMed:27113748"
FT /id="VAR_068227"
FT VARIANT 150
FT /note="L -> R (in PSORS2; increases NF-kappaB transcription
FT factor activity; dbSNP:rs146214639)"
FT /evidence="ECO:0000269|PubMed:22521419,
FT ECO:0000269|PubMed:26358359"
FT /id="VAR_068228"
FT VARIANT 151
FT /note="R -> Q (in PSORS2; unknown pathological
FT significance; decreases NF-kappaB transcription factor
FT activity; dbSNP:rs200731780)"
FT /evidence="ECO:0000269|PubMed:26358359"
FT /id="VAR_078586"
FT VARIANT 151
FT /note="R -> W (in PSORS2; unknown pathological
FT significance; decreases NF-kappaB transcription factor
FT activity; dbSNP:rs777305616)"
FT /evidence="ECO:0000269|PubMed:26358359"
FT /id="VAR_078587"
FT VARIANT 156
FT /note="L -> P (in PRP; dbSNP:rs387907240)"
FT /evidence="ECO:0000269|PubMed:22703878"
FT /id="VAR_068820"
FT VARIANT 171
FT /note="H -> N (may be associated with susceptibility to
FT psoriasis; does not change MALT1 protease activity;
FT dbSNP:rs281875216)"
FT /evidence="ECO:0000269|PubMed:22521419,
FT ECO:0000269|PubMed:27113748"
FT /id="VAR_068229"
FT VARIANT 176
FT /note="D -> H (in dbSNP:rs144475004)"
FT /evidence="ECO:0000269|PubMed:22521419,
FT ECO:0000269|PubMed:27760266"
FT /id="VAR_068230"
FT VARIANT 179
FT /note="R -> H (in dbSNP:rs199517469)"
FT /evidence="ECO:0000269|PubMed:22521419"
FT /id="VAR_068231"
FT VARIANT 191
FT /note="V -> L (in dbSNP:rs281875218)"
FT /evidence="ECO:0000269|PubMed:22521419"
FT /id="VAR_068232"
FT VARIANT 197
FT /note="E -> K (in PSORS2; increases NF-kappaB transcription
FT factor activity; dbSNP:rs200790561)"
FT /evidence="ECO:0000269|PubMed:26358359"
FT /id="VAR_078588"
FT VARIANT 200
FT /note="S -> N (in dbSNP:rs114688446)"
FT /evidence="ECO:0000269|PubMed:22521419,
FT ECO:0000269|PubMed:26358359"
FT /id="VAR_068233"
FT VARIANT 209
FT /note="L -> P (in PSORS2; unknown pathological
FT significance; no effect on NF-kappaB transcription factor
FT activity)"
FT /evidence="ECO:0000269|PubMed:26358359"
FT /id="VAR_078589"
FT VARIANT 216
FT /note="A -> T (in PSORS2; unknown pathological
FT significance; decreases NF-kappaB transcription factor
FT activity; dbSNP:rs574982768)"
FT /evidence="ECO:0000269|PubMed:26358359"
FT /id="VAR_078590"
FT VARIANT 218
FT /note="R -> C (unknown pathological significance; decreases
FT NF-kappaB transcription factor activity;
FT dbSNP:rs747854314)"
FT /evidence="ECO:0000269|PubMed:26358359"
FT /id="VAR_078591"
FT VARIANT 285
FT /note="D -> G (may be associated with susceptibility to
FT psoriasis; dbSNP:rs281875219)"
FT /evidence="ECO:0000269|PubMed:22521419"
FT /id="VAR_068234"
FT VARIANT 338
FT /note="M -> V (unknown pathological significance; does not
FT change NF-kappaB transcription factor activity;
FT dbSNP:rs200132496)"
FT /evidence="ECO:0000269|PubMed:26358359"
FT /id="VAR_078592"
FT VARIANT 350
FT /note="L -> P (in dbSNP:rs1412261979)"
FT /evidence="ECO:0000269|PubMed:26358359"
FT /id="VAR_078593"
FT VARIANT 357
FT /note="L -> P"
FT /evidence="ECO:0000269|PubMed:26358359"
FT /id="VAR_078594"
FT VARIANT 420
FT /note="T -> A (in PSORS2; unknown pathological
FT significance; decreases NF-kappaB transcription factor
FT activity; dbSNP:rs762364495)"
FT /evidence="ECO:0000269|PubMed:26358359"
FT /id="VAR_078595"
FT VARIANT 547
FT /note="R -> S (in dbSNP:rs2066964)"
FT /id="VAR_024401"
FT VARIANT 585
FT /note="V -> I (in dbSNP:rs34367357)"
FT /id="VAR_048608"
FT VARIANT 593
FT /note="I -> N (in dbSNP:rs281875220)"
FT /evidence="ECO:0000269|PubMed:22521419"
FT /id="VAR_068235"
FT VARIANT 602
FT /note="S -> L (in PSORS2; unknown pathological
FT significance; does not change NF-kappaB transcription
FT factor activity; dbSNP:rs201285077)"
FT /evidence="ECO:0000269|PubMed:26358359"
FT /id="VAR_078596"
FT VARIANT 639
FT /note="A -> G (in PSORS2; unknown pathological
FT significance; does not change NF-kappaB transcription
FT factor activity)"
FT /evidence="ECO:0000269|PubMed:26358359"
FT /id="VAR_078597"
FT VARIANT 682
FT /note="R -> W (in dbSNP:rs117918077)"
FT /evidence="ECO:0000269|PubMed:22521419"
FT /id="VAR_068236"
FT VARIANT 714
FT /note="G -> S (in dbSNP:rs151150961)"
FT /evidence="ECO:0000269|PubMed:22521419"
FT /id="VAR_068237"
FT VARIANT 820
FT /note="R -> W (in dbSNP:rs11652075)"
FT /evidence="ECO:0000269|PubMed:11278692,
FT ECO:0000269|PubMed:11356195"
FT /id="VAR_059196"
FT VARIANT 883
FT /note="R -> H (in dbSNP:rs2289541)"
FT /id="VAR_022043"
FT VARIANT 962
FT /note="R -> Q (in dbSNP:rs34850974)"
FT /id="VAR_061080"
FT VARIANT 973
FT /note="D -> E (in dbSNP:rs144285237)"
FT /evidence="ECO:0000269|PubMed:22521419"
FT /id="VAR_068238"
SQ SEQUENCE 1004 AA; 113270 MW; 761CBAC219956076 CRC64;
MGELCRRDSA LTALDEETLW EMMESHRHRI VRCICPSRLT PYLRQAKVLC QLDEEEVLHS
PRLTNSAMRA GHLLDLLKTR GKNGAIAFLE SLKFHNPDVY TLVTGLQPDV DFSNFSGLME
TSKLTECLAG AIGSLQEELN QEKGQKEVLL RRCQQLQEHL GLAETRAEGL HQLEADHSRM
KREVSAHFHE VLRLKDEMLS LSLHYSNALQ EKELAASRCR SLQEELYLLK QELQRANMVS
SCELELQEQS LRTASDQESG DEELNRLKEE NEKLRSLTFS LAEKDILEQS LDEARGSRQE
LVERIHSLRE RAVAAERQRE QYWEEKEQTL LQFQKSKMAC QLYREKVNAL QAQVCELQKE
RDQAYSARDS AQREISQSLV EKDSLRRQVF ELTDQVCELR TQLRQLQAEP PGVLKQEART
REPCPREKQR LVRMHAICPR DDSDCSLVSS TESQLLSDLS ATSSRELVDS FRSSSPAPPS
QQSLYKRVAE DFGEEPWSFS SCLEIPEGDP GALPGAKAGD PHLDYELLDT ADLPQLESSL
QPVSPGRLDV SESGVLMRRR PARRILSQVT MLAFQGDALL EQISVIGGNL TGIFIHRVTP
GSAADQMALR PGTQIVMVDY EASEPLFKAV LEDTTLEEAV GLLRRVDGFC CLSVKVNTDG
YKRLLQDLEA KVATSGDSFY IRVNLAMEGR AKGELQVHCN EVLHVTDTMF QGCGCWHAHR
VNSYTMKDTA AHGTIPNYSR AQQQLIALIQ DMTQQCTVTR KPSSGGPQKL VRIVSMDKAK
ASPLRLSFDR GQLDPSRMEG SSTCFWAESC LTLVPYTLVR PHRPARPRPV LLVPRAVGKI
LSEKLCLLQG FKKCLAEYLS QEEYEAWSQR GDIIQEGEVS GGRCWVTRHA VESLMEKNTH
ALLDVQLDSV CTLHRMDIFP IVIHVSVNEK MAKKLKKGLQ RLGTSEEQLL EAARQEEGDL
DRAPCLYSSL APDGWSDLDG LLSCVRQAIA DEQKKVVWTE QSPR
