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Protein

Caspase recruitment domain-containing protein 11

Gene

CARD11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • CARD domain binding Source: UniProtKB
  • guanylate kinase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_118656. Activation of NF-kappaB in B cells.
REACT_12555. Downstream TCR signaling.
REACT_163994. FCERI mediated NF-kB activation.
REACT_188323. CLEC7A (Dectin-1) signaling.
SignaLinkiQ9BXL7.

Names & Taxonomyi

Protein namesi
Recommended name:
Caspase recruitment domain-containing protein 11
Alternative name(s):
CARD-containing MAGUK protein 1
Short name:
Carma 1
Gene namesi
Name:CARD11
Synonyms:CARMA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:16393. CARD11.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • immunological synapse Source: Ensembl
  • membrane raft Source: UniProtKB
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

Pathology & Biotechi

Involvement in diseasei

Persistent polyclonal B-cell lymphocytosis (PPBL)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:606445
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti123 – 1231G → S in PPBL; results in protein aggregation and constitutive NFKB activation. 1 Publication
VAR_069710
Natural varianti134 – 1341E → G in PPBL; results in protein aggregation and constitutive NFKB activation. 1 Publication
VAR_069711
Immunodeficiency 11 (IMD11)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:615206

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi606445. phenotype.
615206. phenotype.
Orphaneti300324. Persistent polyclonal B-cell lymphocytosis.
357237. Severe combined immunodeficiency due to CARD11 deficiency.
PharmGKBiPA26073.

Polymorphism and mutation databases

BioMutaiCARD11.
DMDMi172046231.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11541154Caspase recruitment domain-containing protein 11PRO_0000144086Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei466 – 4661Phosphoserine1 Publication
Modified residuei559 – 5591Phosphoserine; by PKC/PRKCB and PKC/PRKCQBy similarity
Modified residuei593 – 5931Phosphoserine1 Publication
Modified residuei644 – 6441Phosphoserine; by PKC/PRKCB and PKC/PRKCQBy similarity
Modified residuei652 – 6521Phosphoserine; by PKC/PRKCB and PKC/PRKCQBy similarity
Modified residuei925 – 9251Phosphoserine1 Publication

Post-translational modificationi

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.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BXL7.
PaxDbiQ9BXL7.
PRIDEiQ9BXL7.

PTM databases

PhosphoSiteiQ9BXL7.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ9BXL7.
CleanExiHS_CARD11.
ExpressionAtlasiQ9BXL7. baseline and differential.
GenevestigatoriQ9BXL7.

Organism-specific databases

HPAiHPA052984.

Interactioni

Subunit structurei

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).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
BCL10O959994EBI-7006141,EBI-958922

Protein-protein interaction databases

BioGridi124073. 21 interactions.
DIPiDIP-41797N.
IntActiQ9BXL7. 9 interactions.
MINTiMINT-193901.
STRINGi9606.ENSP00000380150.

Structurei

Secondary structure

1
1154
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 274Combined sources
Helixi30 – 367Combined sources
Helixi39 – 4810Combined sources
Helixi54 – 618Combined sources
Turni70 – 734Combined sources
Helixi74 – 807Combined sources
Helixi84 – 9815Combined sources
Helixi100 – 1078Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JUPX-ray3.20A/B21-116[»]
4LWDX-ray1.79A18-110[»]
ProteinModelPortaliQ9BXL7.
SMRiQ9BXL7. Positions 21-110.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 11093CARDPROSITE-ProRule annotationAdd
BLAST
Domaini667 – 75589PDZAdd
BLAST
Domaini973 – 1140168Guanylate kinase-likeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili130 – 449320Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 CARD domain.PROSITE-ProRule annotation
Contains 1 guanylate kinase-like domain.Curated
Contains 1 PDZ (DHR) domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG47732.
GeneTreeiENSGT00530000063108.
HOVERGENiHBG099790.
InParanoidiQ9BXL7.
KOiK07367.
OMAiAKNKHCL.
OrthoDBiEOG747PH5.
PhylomeDBiQ9BXL7.
TreeFamiTF351139.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
2.30.42.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50209. CARD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BXL7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGGGPEMDD YMETLKDEED ALWENVECNR HMLSRYINPA KLTPYLRQCK
60 70 80 90 100
VIDEQDEDEV LNAPMLPSKI NRAGRLLDIL HTKGQRGYVV FLESLEFYYP
110 120 130 140 150
ELYKLVTGKE PTRRFSTIVV EEGHEGLTHF LMNEVIKLQQ QMKAKDLQRC
160 170 180 190 200
ELLARLRQLE DEKKQMTLTR VELLTFQERY YKMKEERDSY NDELVKVKDD
210 220 230 240 250
NYNLAMRYAQ LSEEKNMAVM RSRDLQLEID QLKHRLNKME EECKLERNQS
260 270 280 290 300
LKLKNDIENR PKKEQVLELE RENEMLKTKN QELQSIIQAG KRSLPDSDKA
310 320 330 340 350
ILDILEHDRK EALEDRQELV NRIYNLQEEA RQAEELRDKY LEEKEDLELK
360 370 380 390 400
CSTLGKDCEM YKHRMNTVML QLEEVERERD QAFHSRDEAQ TQYSQCLIEK
410 420 430 440 450
DKYRKQIREL EEKNDEMRIE MVRREACIVN LESKLRRLSK DSNNLDQSLP
460 470 480 490 500
RNLPVTIISQ DFGDASPRTN GQEADDSSTS EESPEDSKYF LPYHPPQRRM
510 520 530 540 550
NLKGIQLQRA KSPISLKRTS DFQAKGHEEE GTDASPSSCG SLPITNSFTK
560 570 580 590 600
MQPPRSRSSI MSITAEPPGN DSIVRRYKED APHRSTVEED NDSGGFDALD
610 620 630 640 650
LDDDSHERYS FGPSSIHSSS SSHQSEGLDA YDLEQVNLMF RKFSLERPFR
660 670 680 690 700
PSVTSVGHVR GPGPSVQHTT LNGDSLTSQL TLLGGNARGS FVHSVKPGSL
710 720 730 740 750
AEKAGLREGH QLLLLEGCIR GERQSVPLDT CTKEEAHWTI QRCSGPVTLH
760 770 780 790 800
YKVNHEGYRK LVKDMEDGLI TSGDSFYIRL NLNISSQLDA CTMSLKCDDV
810 820 830 840 850
VHVRDTMYQD RHEWLCARVD PFTDHDLDMG TIPSYSRAQQ LLLVKLQRLM
860 870 880 890 900
HRGSREEVDG THHTLRALRN TLQPEEALST SDPRVSPRLS RASFLFGQLL
910 920 930 940 950
QFVSRSENKY KRMNSNERVR IISGSPLGSL ARSSLDATKL LTEKQEELDP
960 970 980 990 1000
ESELGKNLSL IPYSLVRAFY CERRRPVLFT PTVLAKTLVQ RLLNSGGAME
1010 1020 1030 1040 1050
FTICKSDIVT RDEFLRRQKT ETIIYSREKN PNAFECIAPA NIEAVAAKNK
1060 1070 1080 1090 1100
HCLLEAGIGC TRDLIKSNIY PIVLFIRVCE KNIKRFRKLL PRPETEEEFL
1110 1120 1130 1140 1150
RVCRLKEKEL EALPCLYATV EPDMWGSVEE LLRVVKDKIG EEQRKTIWVD

EDQL
Length:1,154
Mass (Da):133,284
Last modified:February 26, 2008 - v3
Checksum:i2F3512D903795D18
GO

Sequence cautioni

The sequence AAG53402.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAI11720.2 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAQ96893.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAL23962.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti815 – 8151L → P in AAG53402 (PubMed:11278692).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti123 – 1231G → S in PPBL; results in protein aggregation and constitutive NFKB activation. 1 Publication
VAR_069710
Natural varianti134 – 1341E → G in PPBL; results in protein aggregation and constitutive NFKB activation. 1 Publication
VAR_069711
Natural varianti670 – 6701T → M.
Corresponds to variant rs3735134 [ dbSNP | Ensembl ].
VAR_028117
Natural varianti694 – 6941S → L.
Corresponds to variant rs3735133 [ dbSNP | Ensembl ].
VAR_028118

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF322641 mRNA. Translation: AAG53402.1. Different initiation.
AC004906 Genomic DNA. Translation: AAQ96893.1. Sequence problems.
CH236953 Genomic DNA. Translation: EAL23962.1. Sequence problems.
BC111719 mRNA. Translation: AAI11720.2. Different initiation.
AF352576 mRNA. Translation: AAL34460.1.
CCDSiCCDS5336.2.
RefSeqiNP_115791.3. NM_032415.5.
UniGeneiHs.648101.

Genome annotation databases

EnsembliENST00000396946; ENSP00000380150; ENSG00000198286.
GeneIDi84433.
KEGGihsa:84433.
UCSCiuc003smv.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF322641 mRNA. Translation: AAG53402.1. Different initiation.
AC004906 Genomic DNA. Translation: AAQ96893.1. Sequence problems.
CH236953 Genomic DNA. Translation: EAL23962.1. Sequence problems.
BC111719 mRNA. Translation: AAI11720.2. Different initiation.
AF352576 mRNA. Translation: AAL34460.1.
CCDSiCCDS5336.2.
RefSeqiNP_115791.3. NM_032415.5.
UniGeneiHs.648101.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JUPX-ray3.20A/B21-116[»]
4LWDX-ray1.79A18-110[»]
ProteinModelPortaliQ9BXL7.
SMRiQ9BXL7. Positions 21-110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124073. 21 interactions.
DIPiDIP-41797N.
IntActiQ9BXL7. 9 interactions.
MINTiMINT-193901.
STRINGi9606.ENSP00000380150.

PTM databases

PhosphoSiteiQ9BXL7.

Polymorphism and mutation databases

BioMutaiCARD11.
DMDMi172046231.

Proteomic databases

MaxQBiQ9BXL7.
PaxDbiQ9BXL7.
PRIDEiQ9BXL7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000396946; ENSP00000380150; ENSG00000198286.
GeneIDi84433.
KEGGihsa:84433.
UCSCiuc003smv.3. human.

Organism-specific databases

CTDi84433.
GeneCardsiGC07M002912.
H-InvDBHIX0033921.
HGNCiHGNC:16393. CARD11.
HPAiHPA052984.
MIMi606445. phenotype.
607210. gene.
615206. phenotype.
neXtProtiNX_Q9BXL7.
Orphaneti300324. Persistent polyclonal B-cell lymphocytosis.
357237. Severe combined immunodeficiency due to CARD11 deficiency.
PharmGKBiPA26073.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG47732.
GeneTreeiENSGT00530000063108.
HOVERGENiHBG099790.
InParanoidiQ9BXL7.
KOiK07367.
OMAiAKNKHCL.
OrthoDBiEOG747PH5.
PhylomeDBiQ9BXL7.
TreeFamiTF351139.

Enzyme and pathway databases

ReactomeiREACT_118656. Activation of NF-kappaB in B cells.
REACT_12555. Downstream TCR signaling.
REACT_163994. FCERI mediated NF-kB activation.
REACT_188323. CLEC7A (Dectin-1) signaling.
SignaLinkiQ9BXL7.

Miscellaneous databases

ChiTaRSiCARD11. human.
GeneWikiiCARD11.
GenomeRNAii84433.
NextBioi74170.
PROiQ9BXL7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BXL7.
CleanExiHS_CARD11.
ExpressionAtlasiQ9BXL7. baseline and differential.
GenevestigatoriQ9BXL7.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
2.30.42.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR027417. P-loop_NTPase.
IPR001478. PDZ.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF50156. SSF50156. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS50209. CARD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CARD11 and CARD14 are novel caspase recruitment domain (CARD)/membrane-associated guanylate kinase (MAGUK) family members that interact with Bcl10 and activate NF-kappaB."
    Bertin J., Wang L., Guo Y., Jacobson M.D., Poyet J.-L., Srinivasula S.M., Merriam S., DiStefano P.S., Alnemri E.S.
    J. Biol. Chem. 276:11877-11882(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "The DNA sequence of human chromosome 7."
    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.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Human chromosome 7: DNA sequence and biology."
    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.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Carma1, a CARD-containing binding partner of Bcl10, induces Bcl10 phosphorylation and NF-kappaB activation."
    Gaide O., Martinon F., Micheau O., Bonnet D., Thome M., Tschopp J.
    FEBS Lett. 496:121-127(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-1154.
  6. Erratum
    Gaide O., Martinon F., Micheau O., Bonnet D., Thome M., Tschopp J.
    FEBS Lett. 505:198-198(2001)
  7. Cited for: IDENTIFICATION IN A MEMBRANE RAFT COMPLEX, INTERACTION WITH DPP4, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; SER-593 AND SER-925, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Deficiency of caspase recruitment domain family, member 11 (CARD11), causes profound combined immunodeficiency in human subjects."
    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.
    J. Allergy Clin. Immunol. 131:477-485(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN IMD11.
  11. Cited for: VARIANTS PPBL SER-123 AND GLY-134, CHARACTERIZATION OF VARIANTS PPBL SER-123 AND GLY-134.

Entry informationi

Entry nameiCAR11_HUMAN
AccessioniPrimary (citable) accession number: Q9BXL7
Secondary accession number(s): A4D1Z7, Q2NKN7, Q548H3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: February 26, 2008
Last modified: May 27, 2015
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Supposed to contain a SH3 domain which is not detected by PROSITE, Pfam or SMART.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.