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Caspase recruitment domain-containing protein 11 (CARD-containing MAGUK protein 1) (Carma 1)

 CAR11_HUMAN             Reviewed;        1154 AA.
Q9BXL7; A4D1Z7; Q2NKN7; Q548H3;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
26-FEB-2008, sequence version 3.
12-SEP-2018, entry version 161.
RecName: Full=Caspase recruitment domain-containing protein 11;
AltName: Full=CARD-containing MAGUK protein 1;
Short=Carma 1;
Name=CARD11; Synonyms=CARMA1 {ECO:0000303|PubMed:11356195};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH BCL10, AND
TISSUE SPECIFICITY.
PubMed=11278692; DOI=10.1074/jbc.M010512200;
Bertin J., Wang L., Guo Y., Jacobson M.D., Poyet J.-L.,
Srinivasula S.M., Merriam S., DiStefano P.S., Alnemri E.S.;
"CARD11 and CARD14 are novel caspase recruitment domain
(CARD)/membrane-associated guanylate kinase (MAGUK) family members
that interact with Bcl10 and activate NF-kappaB.";
J. Biol. Chem. 276:11877-11882(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 8-1154, FUNCTION, AND INTERACTION WITH
BCL10.
PubMed=11356195; DOI=10.1016/S0014-5793(01)02414-0;
Gaide O., Martinon F., Micheau O., Bonnet D., Thome M., Tschopp J.;
"Carma1, a CARD-containing binding partner of Bcl10, induces Bcl10
phosphorylation and NF-kappaB activation.";
FEBS Lett. 496:121-127(2001).
[6]
ERRATUM.
Gaide O., Martinon F., Micheau O., Bonnet D., Thome M., Tschopp J.;
FEBS Lett. 505:198-198(2001).
[7]
FUNCTION.
PubMed=12356734; DOI=10.1093/emboj/cdf505;
Pomerantz J.L., Denny E.M., Baltimore D.;
"CARD11 mediates factor-specific activation of NF-kappaB by the T cell
receptor complex.";
EMBO J. 21:5184-5194(2002).
[8]
IDENTIFICATION IN A MEMBRANE RAFT COMPLEX, INTERACTION WITH DPP4,
SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17287217; DOI=10.1074/jbc.M609157200;
Ohnuma K., Uchiyama M., Yamochi T., Nishibashi K., Hosono O.,
Takahashi N., Kina S., Tanaka H., Lin X., Dang N.H., Morimoto C.;
"Caveolin-1 triggers T-cell activation via CD26 in association with
CARMA1.";
J. Biol. Chem. 282:10117-10131(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; SER-593 AND
SER-925, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
INVOLVEMENT IN IMD11A.
PubMed=23374270; DOI=10.1016/j.jaci.2012.11.050;
Stepensky P., Keller B., Buchta M., Kienzler A.K., Elpeleg O.,
Somech R., Cohen S., Shachar I., Miosge L.A., Schlesier M., Fuchs I.,
Enders A., Eibel H., Grimbacher B., Warnatz K.;
"Deficiency of caspase recruitment domain family, member 11 (CARD11),
causes profound combined immunodeficiency in human subjects.";
J. Allergy Clin. Immunol. 131:477-485(2013).
[12]
INVOLVEMENT IN BENTA, VARIANTS BENTA SER-123 AND GLY-134, AND
CHARACTERIZATION OF VARIANTS BENTA SER-123 AND GLY-134.
PubMed=23129749; DOI=10.1084/jem.20120831;
Snow A.L., Xiao W., Stinson J.R., Lu W., Chaigne-Delalande B.,
Zheng L., Pittaluga S., Matthews H.F., Schmitz R., Jhavar S.,
Kuchen S., Kardava L., Wang W., Lamborn I.T., Jing H., Raffeld M.,
Moir S., Fleisher T.A., Staudt L.M., Su H.C., Lenardo M.J.;
"Congenital B cell lymphocytosis explained by novel germline CARD11
mutations.";
J. Exp. Med. 209:2247-2261(2012).
[13]
INVOLVEMENT IN IMD11A, VARIANT IMD11A 945-GLN--LEU-1154 DEL, AND
CHARACTERIZATION OF VARIANT IMD11A 945-GLN--LEU-1154 DEL.
PubMed=23561803; DOI=10.1016/j.jaci.2013.02.012;
Greil J., Rausch T., Giese T., Bandapalli O.R., Daniel V.,
Bekeredjian-Ding I., Stuetz A.M., Drees C., Roth S., Ruland J.,
Korbel J.O., Kulozik A.E.;
"Whole-exome sequencing links caspase recruitment domain 11 (CARD11)
inactivation to severe combined immunodeficiency.";
J. Allergy Clin. Immunol. 131:1376-1383(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448; SER-512; SER-535;
SER-593; SER-886 AND SER-925, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
INVOLVEMENT IN IMD11B, VARIANTS IMD11B ASP-57; PRO-194 AND TRP-975,
CHARACTERIZATION OF VARIANTS IMD11B ASP-57; PRO-194 AND TRP-975,
CHARACTERIZATION OF VARIANT BENTA GLY-134, FUNCTION, AND INTERACTION
WITH BCL10.
PubMed=28628108; DOI=10.1038/ng.3898;
Ma C.A., Stinson J.R., Zhang Y., Abbott J.K., Weinreich M.A.,
Hauk P.J., Reynolds P.R., Lyons J.J., Nelson C.G., Ruffo E.,
Dorjbal B., Glauzy S., Yamakawa N., Arjunaraja S., Voss K.,
Stoddard J., Niemela J., Zhang Y., Rosenzweig S.D., McElwee J.J.,
DiMaggio T., Matthews H.F., Jones N., Stone K.D., Palma A.,
Oleastro M., Prieto E., Bernasconi A.R., Dubra G., Danielian S.,
Zaiat J., Marti M.A., Kim B., Cooper M.A., Romberg N., Meffre E.,
Gelfand E.W., Snow A.L., Milner J.D.;
"Germline hypomorphic CARD11 mutations in severe atopic disease.";
Nat. Genet. 49:1192-1201(2017).
-!- FUNCTION: Involved in the costimulatory signal essential for T-
cell receptor (TCR)-mediated T-cell activation. Its binding to
DPP4 induces T-cell proliferation and NF-kappa-B activation in a
T-cell receptor/CD3-dependent manner. Activates NF-kappa-B via
BCL10 and IKK. Stimulates the phosphorylation of BCL10. Also
activates the TORC1 signaling pathway.
{ECO:0000269|PubMed:11278692, ECO:0000269|PubMed:11356195,
ECO:0000269|PubMed:12356734, ECO:0000269|PubMed:28628108}.
-!- SUBUNIT: Found in a membrane raft complex, at least composed of
BCL10, CARD11, DPP4 and IKBKB. CARD11 and BCL10 bind to each other
by CARD-CARD interaction. Interacts (via PDZ domain) with DPP4
(via cytoplasmic tail). Interacts with BCL10; as part of a CBM
(CARD11-BCL10-MALT1) complex involved in NF-kappa-B activation
(PubMed:28628108). {ECO:0000269|PubMed:11278692,
ECO:0000269|PubMed:11356195, ECO:0000269|PubMed:17287217,
ECO:0000269|PubMed:28628108}.
-!- INTERACTION:
O95999:BCL10; NbExp=7; IntAct=EBI-7006141, EBI-958922;
Q13191-1:CBLB; NbExp=4; IntAct=EBI-7006141, EBI-15555129;
P48729:CSNK1A1; NbExp=5; IntAct=EBI-7006141, EBI-1383726;
P48729-1:CSNK1A1; NbExp=5; IntAct=EBI-7006141, EBI-10106282;
Q9UDY8:MALT1; NbExp=2; IntAct=EBI-7006141, EBI-1047372;
P70218:Map4k1 (xeno); NbExp=2; IntAct=EBI-7006141, EBI-2906801;
Q05655:PRKCD; NbExp=7; IntAct=EBI-7006141, EBI-704279;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17287217}.
Membrane raft {ECO:0000269|PubMed:17287217}. Note=Colocalized with
DPP4 in membrane rafts. {ECO:0000269|PubMed:17287217}.
-!- TISSUE SPECIFICITY: Detected in adult peripheral blood leukocytes,
thymus, spleen and liver. Also found in promyelocytic leukemia HL-
60 cells, chronic myelogenous leukemia K-562 cells, Burkitt's
lymphoma Raji cells and colorectal adenocarcinoma SW480 cells. Not
detected in HeLaS3, MOLT-4, A-549 and G431 cells.
{ECO:0000269|PubMed:11278692}.
-!- PTM: Phosphorylation at Ser-559, Ser-644 and Ser-652 by PRKCB and
PRKCQ leads to a shift from an inactive to an active form that
activates the NF-kappa-B signaling.
{ECO:0000250|UniProtKB:Q8CIS0}.
-!- DISEASE: B-cell expansion with NFKB and T-cell anergy (BENTA)
[MIM:616452]: An autosomal dominant condition characterized by
onset in infancy of splenomegaly and polyclonal expansion of B
cells, resulting in peripheral lymphocytosis. Affected individuals
also show mild immune dysfunction, including some defective
antibody responses and T-cell anergy. There may be a
predisposition to the development of B-cell malignancy.
{ECO:0000269|PubMed:23129749, ECO:0000269|PubMed:28628108}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Immunodeficiency 11 A (IMD11A) [MIM:615206]: An autosomal
recessive primary immunodeficiency characterized by normal numbers
of T and B-lymphocytes, but defective intracellular signaling.
There is a block in B-cell differentiation with increased numbers
of transitional B-cells and hypogammaglobulinemia, as well as
decreased numbers of regulatory T-cells and defects in T-cell
function. {ECO:0000269|PubMed:23374270,
ECO:0000269|PubMed:23561803}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Immunodeficiency 11B with atopic dermatitis (IMD11B)
[MIM:617638]: An autosomal dominant disorder of immune dysfunction
characterized by onset of moderate to severe atopic dermatitis in
early childhood. Some patients may have recurrent infections and
other variable immune abnormalities. Laboratory studies show
defects in T-cell activation, increased IgE, and eosinophilia.
{ECO:0000269|PubMed:28628108}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- CAUTION: Supposed to contain a SH3 domain which is not detected by
PROSITE, Pfam or SMART. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAG53402.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAI11720.2; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAQ96893.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=EAL23962.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF322641; AAG53402.1; ALT_INIT; mRNA.
EMBL; AC004906; AAQ96893.1; ALT_SEQ; Genomic_DNA.
EMBL; CH236953; EAL23962.1; ALT_SEQ; Genomic_DNA.
EMBL; BC111719; AAI11720.2; ALT_INIT; mRNA.
EMBL; AF352576; AAL34460.1; -; mRNA.
CCDS; CCDS5336.2; -.
RefSeq; NP_001311210.1; NM_001324281.1.
RefSeq; NP_115791.3; NM_032415.5.
RefSeq; XP_011513888.1; XM_011515586.2.
UniGene; Hs.648101; -.
PDB; 4JUP; X-ray; 3.20 A; A/B=21-116.
PDB; 4LWD; X-ray; 1.79 A; A=18-110.
PDBsum; 4JUP; -.
PDBsum; 4LWD; -.
ProteinModelPortal; Q9BXL7; -.
SMR; Q9BXL7; -.
BioGrid; 124073; 30.
CORUM; Q9BXL7; -.
DIP; DIP-41797N; -.
IntAct; Q9BXL7; 16.
MINT; Q9BXL7; -.
STRING; 9606.ENSP00000380150; -.
iPTMnet; Q9BXL7; -.
PhosphoSitePlus; Q9BXL7; -.
BioMuta; CARD11; -.
DMDM; 172046231; -.
EPD; Q9BXL7; -.
MaxQB; Q9BXL7; -.
PaxDb; Q9BXL7; -.
PeptideAtlas; Q9BXL7; -.
PRIDE; Q9BXL7; -.
ProteomicsDB; 79450; -.
Ensembl; ENST00000396946; ENSP00000380150; ENSG00000198286.
GeneID; 84433; -.
KEGG; hsa:84433; -.
UCSC; uc003smv.5; human.
CTD; 84433; -.
DisGeNET; 84433; -.
EuPathDB; HostDB:ENSG00000198286.9; -.
GeneCards; CARD11; -.
H-InvDB; HIX0033921; -.
HGNC; HGNC:16393; CARD11.
HPA; HPA052984; -.
MalaCards; CARD11; -.
MIM; 607210; gene.
MIM; 615206; phenotype.
MIM; 616452; phenotype.
MIM; 617638; phenotype.
neXtProt; NX_Q9BXL7; -.
OpenTargets; ENSG00000198286; -.
Orphanet; 300324; Persistent polyclonal B-cell lymphocytosis.
Orphanet; 357237; Severe combined immunodeficiency due to CARD11 deficiency.
PharmGKB; PA26073; -.
eggNOG; ENOG410ISRJ; Eukaryota.
eggNOG; ENOG41126VR; LUCA.
GeneTree; ENSGT00530000063108; -.
HOVERGEN; HBG099790; -.
InParanoid; Q9BXL7; -.
KO; K07367; -.
OMA; EACIVNL; -.
OrthoDB; EOG091G0T58; -.
PhylomeDB; Q9BXL7; -.
TreeFam; TF351139; -.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
SignaLink; Q9BXL7; -.
SIGNOR; Q9BXL7; -.
ChiTaRS; CARD11; human.
GeneWiki; CARD11; -.
GenomeRNAi; 84433; -.
PRO; PR:Q9BXL7; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000198286; Expressed in 159 organ(s), highest expression level in leukocyte.
CleanEx; HS_CARD11; -.
ExpressionAtlas; Q9BXL7; baseline and differential.
Genevisible; Q9BXL7; HS.
GO; GO:0032449; C:CBM complex; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0050700; F:CARD domain binding; IPI:UniProtKB.
GO; GO:0004385; F:guanylate kinase activity; NAS:UniProtKB.
GO; GO:0030183; P:B cell differentiation; IEA:Ensembl.
GO; GO:0042100; P:B cell proliferation; IEA:Ensembl.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0002377; P:immunoglobulin production; IEA:Ensembl.
GO; GO:0070970; P:interleukin-2 secretion; IEA:Ensembl.
GO; GO:0030890; P:positive regulation of B cell proliferation; IEA:Ensembl.
GO; GO:0001819; P:positive regulation of cytokine production; IMP:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0045086; P:positive regulation of interleukin-2 biosynthetic process; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
GO; GO:0045577; P:regulation of B cell differentiation; IEA:Ensembl.
GO; GO:0045580; P:regulation of T cell differentiation; IEA:Ensembl.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0031295; P:T cell costimulation; IDA:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0045061; P:thymic T cell selection; IEA:Ensembl.
GO; GO:0038202; P:TORC1 signaling; IMP:UniProtKB.
InterPro; IPR001315; CARD.
InterPro; IPR033538; CARD11.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR036034; PDZ_sf.
PANTHER; PTHR14559:SF4; PTHR14559:SF4; 1.
Pfam; PF00619; CARD; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF50156; SSF50156; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50209; CARD; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Complete proteome; Cytoplasm;
Disease mutation; Membrane; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 1154 Caspase recruitment domain-containing
protein 11.
/FTId=PRO_0000144086.
DOMAIN 18 110 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
DOMAIN 667 755 PDZ.
DOMAIN 973 1140 Guanylate kinase-like.
COILED 130 449 {ECO:0000255}.
MOD_RES 448 448 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 466 466 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 512 512 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 535 535 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 559 559 Phosphoserine; by PKC/PRKCB and
PKC/PRKCQ.
{ECO:0000250|UniProtKB:Q8CIS0}.
MOD_RES 593 593 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 644 644 Phosphoserine; by PKC/PRKCB and
PKC/PRKCQ.
{ECO:0000250|UniProtKB:Q8CIS0}.
MOD_RES 652 652 Phosphoserine; by PKC/PRKCB and
PKC/PRKCQ.
{ECO:0000250|UniProtKB:Q8CIS0}.
MOD_RES 886 886 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 925 925 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
VARIANT 57 57 E -> D (in IMD11B; no effect on protein
abundance; decreased interaction with
BCL10; dominant negative effect on NF-
kappaB signaling; dominant negative
effect on TORC1 signaling).
{ECO:0000269|PubMed:28628108}.
/FTId=VAR_079284.
VARIANT 123 123 G -> S (in BENTA; results in protein
aggregation; constitutive activation of
NF-kappaB signaling; dbSNP:rs387907352).
{ECO:0000269|PubMed:23129749}.
/FTId=VAR_069710.
VARIANT 134 134 E -> G (in BENTA; results in protein
aggregation; constitutive activation of
NF-kappaB signaling; dbSNP:rs387907351).
{ECO:0000269|PubMed:23129749,
ECO:0000269|PubMed:28628108}.
/FTId=VAR_069711.
VARIANT 194 194 L -> P (in IMD11B; no effect on protein
abundance; decreased interaction with
BCL10; dominant negative effect on NF-
kappaB signaling; dominant negative
effect on TORC1 signaling).
{ECO:0000269|PubMed:28628108}.
/FTId=VAR_079285.
VARIANT 670 670 T -> M (in dbSNP:rs3735134).
/FTId=VAR_028117.
VARIANT 694 694 S -> L (in dbSNP:rs3735133).
/FTId=VAR_028118.
VARIANT 945 1154 Missing (in IMD11A; results in defective
NF-kappa-B activation).
{ECO:0000269|PubMed:23561803}.
/FTId=VAR_079158.
VARIANT 975 975 R -> W (in IMD11B; no effect on protein
abundance; dominant negative effect on
NF-kappaB signaling; dominant negative
effect on TORC1 signaling;
dbSNP:rs1064795307).
{ECO:0000269|PubMed:28628108}.
/FTId=VAR_079286.
CONFLICT 815 815 L -> P (in Ref. 1; AAG53402).
{ECO:0000305}.
HELIX 24 27 {ECO:0000244|PDB:4LWD}.
HELIX 30 36 {ECO:0000244|PDB:4LWD}.
HELIX 39 48 {ECO:0000244|PDB:4LWD}.
HELIX 54 61 {ECO:0000244|PDB:4LWD}.
TURN 70 73 {ECO:0000244|PDB:4LWD}.
HELIX 74 80 {ECO:0000244|PDB:4LWD}.
HELIX 84 98 {ECO:0000244|PDB:4LWD}.
HELIX 100 107 {ECO:0000244|PDB:4LWD}.
SEQUENCE 1154 AA; 133284 MW; 2F3512D903795D18 CRC64;
MPGGGPEMDD YMETLKDEED ALWENVECNR HMLSRYINPA KLTPYLRQCK VIDEQDEDEV
LNAPMLPSKI NRAGRLLDIL HTKGQRGYVV FLESLEFYYP ELYKLVTGKE PTRRFSTIVV
EEGHEGLTHF LMNEVIKLQQ QMKAKDLQRC ELLARLRQLE DEKKQMTLTR VELLTFQERY
YKMKEERDSY NDELVKVKDD NYNLAMRYAQ LSEEKNMAVM RSRDLQLEID QLKHRLNKME
EECKLERNQS LKLKNDIENR PKKEQVLELE RENEMLKTKN QELQSIIQAG KRSLPDSDKA
ILDILEHDRK EALEDRQELV NRIYNLQEEA RQAEELRDKY LEEKEDLELK CSTLGKDCEM
YKHRMNTVML QLEEVERERD QAFHSRDEAQ TQYSQCLIEK DKYRKQIREL EEKNDEMRIE
MVRREACIVN LESKLRRLSK DSNNLDQSLP RNLPVTIISQ DFGDASPRTN GQEADDSSTS
EESPEDSKYF LPYHPPQRRM NLKGIQLQRA KSPISLKRTS DFQAKGHEEE GTDASPSSCG
SLPITNSFTK MQPPRSRSSI MSITAEPPGN DSIVRRYKED APHRSTVEED NDSGGFDALD
LDDDSHERYS FGPSSIHSSS SSHQSEGLDA YDLEQVNLMF RKFSLERPFR PSVTSVGHVR
GPGPSVQHTT LNGDSLTSQL TLLGGNARGS FVHSVKPGSL AEKAGLREGH QLLLLEGCIR
GERQSVPLDT CTKEEAHWTI QRCSGPVTLH YKVNHEGYRK LVKDMEDGLI TSGDSFYIRL
NLNISSQLDA CTMSLKCDDV VHVRDTMYQD RHEWLCARVD PFTDHDLDMG TIPSYSRAQQ
LLLVKLQRLM HRGSREEVDG THHTLRALRN TLQPEEALST SDPRVSPRLS RASFLFGQLL
QFVSRSENKY KRMNSNERVR IISGSPLGSL ARSSLDATKL LTEKQEELDP ESELGKNLSL
IPYSLVRAFY CERRRPVLFT PTVLAKTLVQ RLLNSGGAME FTICKSDIVT RDEFLRRQKT
ETIIYSREKN PNAFECIAPA NIEAVAAKNK HCLLEAGIGC TRDLIKSNIY PIVLFIRVCE
KNIKRFRKLL PRPETEEEFL RVCRLKEKEL EALPCLYATV EPDMWGSVEE LLRVVKDKIG
EEQRKTIWVD EDQL


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