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 24-JAN-2024, entry version 185. 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 CYS-218 AND VAL-338. 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"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. DR RefSeq; XP_011523520.1; XM_011525218.2. [Q9BXL6-1] DR AlphaFoldDB; Q9BXL6; -. DR SMR; Q9BXL6; -. DR BioGRID; 122540; 14. DR IntAct; Q9BXL6; 7. DR STRING; 9606.ENSP00000498071; -. DR GlyGen; Q9BXL6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BXL6; -. DR PhosphoSitePlus; Q9BXL6; -. DR BioMuta; CARD14; -. DR DMDM; 296434421; -. DR jPOST; Q9BXL6; -. DR MassIVE; Q9BXL6; -. DR MaxQB; Q9BXL6; -. DR PaxDb; 9606-ENSP00000458715; -. DR PeptideAtlas; Q9BXL6; -. DR ProteomicsDB; 7285; -. DR ProteomicsDB; 79449; -. [Q9BXL6-1] DR Antibodypedia; 19763; 258 antibodies from 31 providers. DR DNASU; 79092; -. DR Ensembl; ENST00000344227.6; ENSP00000344549.2; ENSG00000141527.19. [Q9BXL6-1] DR Ensembl; ENST00000570421.5; ENSP00000461806.1; ENSG00000141527.19. [Q9BXL6-2] DR Ensembl; ENST00000571427.2; ENSP00000516501.1; ENSG00000141527.19. [Q9BXL6-1] DR Ensembl; ENST00000573882.5; ENSP00000458715.1; ENSG00000141527.19. [Q9BXL6-1] DR Ensembl; ENST00000648509.2; ENSP00000498071.1; ENSG00000141527.19. [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 AGR; HGNC:16446; -. 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; 4213113at2759; -. DR PhylomeDB; Q9BXL6; -. DR TreeFam; TF315606; -. DR PathwayCommons; Q9BXL6; -. DR SignaLink; Q9BXL6; -. DR BioGRID-ORCS; 79092; 31 hits in 1145 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 cell types or tissues. DR ExpressionAtlas; Q9BXL6; baseline and differential. 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 CDD; cd08806; CARD_CARD14_CARMA2; 1. DR CDD; cd00992; PDZ_signaling; 1. DR Gene3D; 2.30.42.10; -; 1. DR Gene3D; 1.10.533.10; Death Domain, Fas; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 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 PANTHER; PTHR14559; CASPASE RECRUITMENT DOMAIN FAMILY; 1. DR PANTHER; PTHR14559:SF1; CASPASE RECRUITMENT DOMAIN-CONTAINING PROTEIN 14; 1. DR Pfam; PF00619; CARD; 1. DR SUPFAM; SSF47986; DEATH domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50156; PDZ domain-like; 1. DR PROSITE; PS50209; CARD; 1. DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1. DR PROSITE; PS50106; PDZ; 1. DR Genevisible; Q9BXL6; HS. 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; uncertain significance; decreases FT NF-kappaB transcription factor activity; FT dbSNP:rs200731780)" FT /evidence="ECO:0000269|PubMed:26358359" FT /id="VAR_078586" FT VARIANT 151 FT /note="R -> W (in PSORS2; uncertain significance; decreases FT NF-kappaB transcription factor activity; FT 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 (probable risk factor for PSORS2; does not FT change MALT1 protease activity; 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; uncertain significance; no effect FT on NF-kappaB transcription factor activity)" FT /evidence="ECO:0000269|PubMed:26358359" FT /id="VAR_078589" FT VARIANT 216 FT /note="A -> T (in PSORS2; uncertain significance; decreases FT NF-kappaB transcription factor activity; FT dbSNP:rs574982768)" FT /evidence="ECO:0000269|PubMed:26358359" FT /id="VAR_078590" FT VARIANT 218 FT /note="R -> C (decreases NF-kappaB transcription factor FT activity; dbSNP:rs747854314)" FT /evidence="ECO:0000269|PubMed:26358359" FT /id="VAR_078591" FT VARIANT 285 FT /note="D -> G (risk factor for PSORS2; dbSNP:rs281875219)" FT /evidence="ECO:0000269|PubMed:22521419" FT /id="VAR_068234" FT VARIANT 338 FT /note="M -> V (does not change NF-kappaB transcription FT factor activity; 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; uncertain significance; decreases FT NF-kappaB transcription factor activity; FT 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; uncertain significance; does not FT change NF-kappaB transcription factor activity; FT dbSNP:rs201285077)" FT /evidence="ECO:0000269|PubMed:26358359" FT /id="VAR_078596" FT VARIANT 639 FT /note="A -> G (in PSORS2; uncertain significance; does not FT change NF-kappaB transcription 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 //