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Caspase recruitment domain-containing protein 9 (hCARD9)

 CARD9_HUMAN             Reviewed;         536 AA.
Q9H257; Q5SXM5; Q5SXM6; Q9H854;
31-JAN-2002, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 2.
22-NOV-2017, entry version 148.
RecName: Full=Caspase recruitment domain-containing protein 9;
Short=hCARD9;
Name=CARD9;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASN-12, FUNCTION,
SUBCELLULAR LOCATION, AND INTERACTION WITH BCL10.
PubMed=11053425; DOI=10.1074/jbc.C000726200;
Bertin J., Guo Y., Wang L., Srinivasula S.M., Jacobson M.D.,
Poyet J.-L., Merriam S., Du M.-Q., Dyer M.J.S., Robison K.E.,
DiStefano P.S., Alnemri E.S.;
"CARD9 is a novel caspase recruitment domain-containing protein that
interacts with Bcl10/CLAP and activates NF-kappa B.";
J. Biol. Chem. 275:41082-41086(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
ASN-12.
TISSUE=Retinoblastoma, and Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Muscle;
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[7]
INVOLVEMENT IN CANDF2.
PubMed=19864672; DOI=10.1056/NEJMoa0810719;
Glocker E.-O., Hennigs A., Nabavi M., Schaeffer A.A., Woellner C.,
Salzer U., Pfeifer D., Veelken H., Warnatz K., Tahami F., Jamal S.,
Manguiat A., Rezaei N., Amirzargar A.A., Plebani A.,
Hannesschlaeger N., Gross O., Ruland J., Grimbacher B.;
"A homozygous CARD9 mutation in a family with susceptibility to fungal
infections.";
N. Engl. J. Med. 361:1727-1735(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277; SER-425; SER-483
AND SER-498, 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).
[9]
INTERACTION WITH NOD2.
PubMed=24960071; DOI=10.1016/j.febslet.2014.06.035;
Parkhouse R., Boyle J.P., Mayle S., Sawmynaden K., Rittinger K.,
Monie T.P.;
"Interaction between NOD2 and CARD9 involves the NOD2 NACHT and the
linker region between the NOD2 CARDs and NACHT domain.";
FEBS Lett. 588:2830-2836(2014).
[10]
VARIANTS CANDF2 SER-72 AND PRO-373.
PubMed=23335372; DOI=10.1182/blood-2012-08-450551;
Drewniak A., Gazendam R.P., Tool A.T., van Houdt M., Jansen M.H.,
van Hamme J.L., van Leeuwen E.M., Roos D., Scalais E., de Beaufort C.,
Janssen H., van den Berg T.K., Kuijpers T.W.;
"Invasive fungal infection and impaired neutrophil killing in human
CARD9 deficiency.";
Blood 121:2385-2392(2013).
[11]
VARIANT CANDF2 CYS-101.
PubMed=24131138; DOI=10.1056/NEJMoa1208487;
Lanternier F., Pathan S., Vincent Q.B., Liu L., Cypowyj S., Prando C.,
Migaud M., Taibi L., Ammar-Khodja A., Boudghene Stambouli O.,
Guellil B., Jacobs F., Goffard J.C., Schepers K., del Marmol V.,
Boussofara L., Denguezli M., Larif M., Bachelez H., Michel L.,
Lefranc G., Hay R., Jouvion G., Chretien F., Fraitag S.,
Bougnoux M.E., Boudia M., Abel L., Lortholary O., Casanova J.L.,
Picard C., Grimbacher B., Puel A.;
"Deep dermatophytosis and inherited CARD9 deficiency.";
N. Engl. J. Med. 369:1704-1714(2013).
-!- FUNCTION: Adapter protein that plays a key role in innate immune
response to a number of intracellular pathogens, such as
C.albicans and L.monocytogenes. Is at the crossroads of ITAM-
tyrosine kinase and the Toll-like receptors (TLR) and NOD2
signaling pathways. Probably controls various innate immune
response pathways depending on the intracellular pathogen. In
response to L.monocytogenes infection, acts by connecting NOD2
recognition of peptidoglycan to downstream activation of MAP
kinases (MAPK) without activating NF-kappa-B. Also involved in
activation of myeloid cells via classical ITAM-associated
receptors and TLR: required for TLR-mediated activation of MAPK,
while it is not required for TLR-induced activation of NF-kappa-B
(By similarity). Controls CLEC7A (dectin-1)-mediated myeloid cell
activation induced by the yeast cell wall component zymosan,
leading to cytokine production and innate anti-fungal immunity:
acts by regulating BCL10-MALT1-mediated NF-kappa-B activation
pathway. Activates NF-kappa-B via BCL10. In response to the hyphal
form of C.albicans, mediates CLEC6A (dectin-2)-induced I-kappa-B
kinase ubiquitination, leading to NF-kappa-B activation via
interaction with BCL10. In response to fungal infection, may be
required for the development and subsequent differentiation of
interleukin 17-producing T helper (TH-17) cells. {ECO:0000250,
ECO:0000269|PubMed:11053425}.
-!- SUBUNIT: Interacts with NOD2 (via NACHT domain) (PubMed:24960071).
Interacts with RIPK2 (By similarity). Interacts with VHL; without
leading to protein degradation (By similarity). Self-associates.
Interacts (via CARD domain) with BCL10 (via CARD domain)
(PubMed:11053425). {ECO:0000250|UniProtKB:A2AIV8,
ECO:0000250|UniProtKB:Q9EPY0, ECO:0000269|PubMed:11053425,
ECO:0000269|PubMed:24960071}.
-!- INTERACTION:
A8K932:-; NbExp=3; IntAct=EBI-751319, EBI-10174671;
O14639:ABLIM1; NbExp=3; IntAct=EBI-751319, EBI-487024;
Q08117:AES; NbExp=3; IntAct=EBI-751319, EBI-717810;
Q9Y2J4-4:AMOTL2; NbExp=5; IntAct=EBI-751319, EBI-10187270;
O95999:BCL10; NbExp=6; IntAct=EBI-751319, EBI-958922;
Q9H2G9:BLZF1; NbExp=3; IntAct=EBI-751319, EBI-2548012;
Q6P1W5:C1orf94; NbExp=3; IntAct=EBI-751319, EBI-946029;
Q53TS8:C2CD6; NbExp=3; IntAct=EBI-751319, EBI-739879;
Q9BWT7:CARD10; NbExp=4; IntAct=EBI-11530605, EBI-3866279;
Q8IYA8:CCDC36; NbExp=3; IntAct=EBI-751319, EBI-8638439;
A6NC98:CCDC88B; NbExp=4; IntAct=EBI-11530605, EBI-347573;
Q8TD31-3:CCHCR1; NbExp=3; IntAct=EBI-751319, EBI-10175300;
Q96GN5:CDCA7L; NbExp=3; IntAct=EBI-751319, EBI-5278764;
Q8IYX8-2:CEP57L1; NbExp=3; IntAct=EBI-751319, EBI-10181988;
Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-751319, EBI-739624;
Q2TBE0:CWF19L2; NbExp=3; IntAct=EBI-751319, EBI-5453285;
Q9UER7:DAXX; NbExp=3; IntAct=EBI-751319, EBI-77321;
Q9UII6:DUSP13; NbExp=4; IntAct=EBI-11530605, EBI-749800;
O60573:EIF4E2; NbExp=3; IntAct=EBI-751319, EBI-398610;
Q9H5Z6:FAM124B; NbExp=3; IntAct=EBI-751319, EBI-741626;
Q3B820:FAM161A; NbExp=4; IntAct=EBI-11530605, EBI-719941;
Q5VWN6:FAM208B; NbExp=4; IntAct=EBI-11530605, EBI-745958;
Q5VWN6-2:FAM208B; NbExp=3; IntAct=EBI-751319, EBI-10172380;
Q9Y247:FAM50B; NbExp=3; IntAct=EBI-751319, EBI-742802;
Q6NT76:HMBOX1; NbExp=3; IntAct=EBI-751319, EBI-2549423;
Q7L273:KCTD9; NbExp=3; IntAct=EBI-751319, EBI-4397613;
Q9BVG8-5:KIFC3; NbExp=4; IntAct=EBI-11530605, EBI-14069005;
P08727:KRT19; NbExp=3; IntAct=EBI-751319, EBI-742756;
Q15323:KRT31; NbExp=3; IntAct=EBI-751319, EBI-948001;
Q6A162:KRT40; NbExp=3; IntAct=EBI-751319, EBI-10171697;
P60370:KRTAP10-5; NbExp=3; IntAct=EBI-751319, EBI-10172150;
Q96BZ8:LENG1; NbExp=3; IntAct=EBI-751319, EBI-726510;
P25800:LMO1; NbExp=3; IntAct=EBI-751319, EBI-8639312;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-751319, EBI-741037;
P50222:MEOX2; NbExp=3; IntAct=EBI-751319, EBI-748397;
P55081:MFAP1; NbExp=3; IntAct=EBI-751319, EBI-1048159;
Q9UJV3-2:MID2; NbExp=4; IntAct=EBI-11530605, EBI-10172526;
Q7Z6G3-2:NECAB2; NbExp=3; IntAct=EBI-751319, EBI-10172876;
Q9P286:PAK5; NbExp=3; IntAct=EBI-751319, EBI-741896;
P40425:PBX2; NbExp=3; IntAct=EBI-751319, EBI-348489;
Q8IXK0:PHC2; NbExp=3; IntAct=EBI-751319, EBI-713786;
Q9NRD5:PICK1; NbExp=4; IntAct=EBI-11530605, EBI-79165;
Q96PV4:PNMA5; NbExp=3; IntAct=EBI-751319, EBI-10171633;
Q6NYC8:PPP1R18; NbExp=3; IntAct=EBI-751319, EBI-2557469;
Q14D33:RTP5; NbExp=3; IntAct=EBI-751319, EBI-10217913;
Q9BWG6:SCNM1; NbExp=4; IntAct=EBI-11530605, EBI-748391;
Q9Y2D8:SSX2IP; NbExp=3; IntAct=EBI-751319, EBI-2212028;
Q9NZ72:STMN3; NbExp=4; IntAct=EBI-11530605, EBI-725557;
O75558:STX11; NbExp=3; IntAct=EBI-751319, EBI-714135;
P63165:SUMO1; NbExp=3; IntAct=EBI-751319, EBI-80140;
Q8N8B7:TCEANC; NbExp=3; IntAct=EBI-751319, EBI-954696;
P56279:TCL1A; NbExp=3; IntAct=EBI-751319, EBI-749995;
Q9UBB9:TFIP11; NbExp=3; IntAct=EBI-751319, EBI-1105213;
Q13829:TNFAIP1; NbExp=3; IntAct=EBI-751319, EBI-2505861;
P36406:TRIM23; NbExp=3; IntAct=EBI-751319, EBI-740098;
Q14134:TRIM29; NbExp=3; IntAct=EBI-751319, EBI-702370;
Q8IWZ5:TRIM42; NbExp=3; IntAct=EBI-751319, EBI-5235829;
Q9BYV2:TRIM54; NbExp=3; IntAct=EBI-751319, EBI-2130429;
Q3SY00:TSGA10IP; NbExp=4; IntAct=EBI-11530605, EBI-10241197;
Q99598:TSNAX; NbExp=5; IntAct=EBI-751319, EBI-742638;
Q9Y4E8:USP15; NbExp=3; IntAct=EBI-751319, EBI-1043104;
Q548N1:VPS28; NbExp=3; IntAct=EBI-751319, EBI-10243107;
Q8N3Z6:ZCCHC7; NbExp=3; IntAct=EBI-751319, EBI-7265024;
P15622-3:ZNF250; NbExp=3; IntAct=EBI-751319, EBI-10177272;
Q8TAU3:ZNF417; NbExp=3; IntAct=EBI-751319, EBI-740727;
Q7Z3I7:ZNF572; NbExp=6; IntAct=EBI-751319, EBI-10172590;
Q96SQ5:ZNF587; NbExp=3; IntAct=EBI-751319, EBI-6427977;
Q8N720:ZNF655; NbExp=3; IntAct=EBI-751319, EBI-625509;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11053425}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9H257-1; Sequence=Displayed;
Name=2;
IsoId=Q9H257-2; Sequence=VSP_024392, VSP_024393;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9H257-3; Sequence=VSP_024390, VSP_024391;
Note=No experimental confirmation available. May be produced at
very low levels due to a premature stop codon in the mRNA,
leading to nonsense-mediated mRNA decay.;
-!- TISSUE SPECIFICITY: Highly expressed in spleen. Also detected in
liver, placenta, lung, peripheral blood leukocytes and in brain.
-!- PTM: Phosphorylated at Thr-531 and Thr-533 by CK2 following
interaction with VHL, leading to inhibit the ability to activate
NF-kappa-B. {ECO:0000250}.
-!- DISEASE: Candidiasis, familial, 2 (CANDF2) [MIM:212050]: A primary
immunodeficiency disorder with altered immune responses and
impaired clearance of fungal infections, selective against
Candida. It is characterized by persistent and/or recurrent
infections of the skin, nails and mucous membranes caused by
organisms of the genus Candida, mainly Candida albicans.
{ECO:0000269|PubMed:19864672, ECO:0000269|PubMed:23335372,
ECO:0000269|PubMed:24131138}. Note=The disease is caused by
mutations affecting the gene represented in this entry. Defects
induce reduced numbers of CD4(+) Th17 lymphocytes as well as a
lack of monocyte-derived cytokines in response to Candida strains.
Neutrophils show a selective Candida albicans killing defect with
abnormal ultrastructural phagolysosomes and outgrowth of hyphae
(PubMed:23335372). {ECO:0000269|PubMed:23335372}.
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EMBL; AF311287; AAG28790.1; -; mRNA.
EMBL; AK024001; BAB14766.1; -; mRNA.
EMBL; AK292081; BAF84770.1; -; mRNA.
EMBL; AL592301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471090; EAW88220.1; -; Genomic_DNA.
EMBL; BC008877; AAH08877.1; -; mRNA.
CCDS; CCDS48057.1; -. [Q9H257-2]
CCDS; CCDS6997.1; -. [Q9H257-1]
RefSeq; NP_434700.2; NM_052813.4. [Q9H257-1]
RefSeq; NP_434701.1; NM_052814.3. [Q9H257-2]
UniGene; Hs.694071; -.
ProteinModelPortal; Q9H257; -.
SMR; Q9H257; -.
BioGrid; 122094; 76.
IntAct; Q9H257; 126.
STRING; 9606.ENSP00000360797; -.
iPTMnet; Q9H257; -.
PhosphoSitePlus; Q9H257; -.
BioMuta; CARD9; -.
DMDM; 143811370; -.
EPD; Q9H257; -.
MaxQB; Q9H257; -.
PaxDb; Q9H257; -.
PeptideAtlas; Q9H257; -.
PRIDE; Q9H257; -.
DNASU; 64170; -.
Ensembl; ENST00000371732; ENSP00000360797; ENSG00000187796. [Q9H257-1]
Ensembl; ENST00000371734; ENSP00000360799; ENSG00000187796. [Q9H257-2]
Ensembl; ENST00000489932; ENSP00000451368; ENSG00000187796. [Q9H257-3]
GeneID; 64170; -.
KEGG; hsa:64170; -.
UCSC; uc004chg.4; human. [Q9H257-1]
CTD; 64170; -.
DisGeNET; 64170; -.
EuPathDB; HostDB:ENSG00000187796.13; -.
GeneCards; CARD9; -.
HGNC; HGNC:16391; CARD9.
HPA; HPA059502; -.
MalaCards; CARD9; -.
MIM; 212050; phenotype.
MIM; 607212; gene.
neXtProt; NX_Q9H257; -.
OpenTargets; ENSG00000187796; -.
Orphanet; 1334; Chronic mucocutaneous candidosis.
Orphanet; 397587; Deep dermatophytosis.
PharmGKB; PA26077; -.
eggNOG; ENOG410IE3N; Eukaryota.
eggNOG; ENOG410Y2EE; LUCA.
GeneTree; ENSGT00530000063108; -.
HOGENOM; HOG000231538; -.
HOVERGEN; HBG058091; -.
InParanoid; Q9H257; -.
KO; K12794; -.
OMA; PQLYKKV; -.
OrthoDB; EOG091G0T58; -.
PhylomeDB; Q9H257; -.
TreeFam; TF351139; -.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
SIGNOR; Q9H257; -.
GeneWiki; CARD9; -.
GenomeRNAi; 64170; -.
PRO; PR:Q9H257; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000187796; -.
CleanEx; HS_CARD9; -.
ExpressionAtlas; Q9H257; baseline and differential.
Genevisible; Q9H257; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0050700; F:CARD domain binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEP:UniProtKB.
GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0046330; P:positive regulation of JNK cascade; IDA:MGI.
GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; IDA:MGI.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
GO; GO:0045076; P:regulation of interleukin-2 biosynthetic process; IEA:Ensembl.
GO; GO:0045408; P:regulation of interleukin-6 biosynthetic process; IEA:Ensembl.
GO; GO:0042534; P:regulation of tumor necrosis factor biosynthetic process; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0043330; P:response to exogenous dsRNA; IEA:Ensembl.
GO; GO:0009620; P:response to fungus; IEA:Ensembl.
GO; GO:0032495; P:response to muramyl dipeptide; IEA:Ensembl.
GO; GO:0032494; P:response to peptidoglycan; IEA:Ensembl.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
InterPro; IPR001315; CARD.
InterPro; IPR011029; DEATH-like_dom_sf.
Pfam; PF00619; CARD; 1.
SUPFAM; SSF47986; SSF47986; 1.
PROSITE; PS50209; CARD; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
Disease mutation; Immunity; Innate immunity; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 536 Caspase recruitment domain-containing
protein 9.
/FTId=PRO_0000144082.
DOMAIN 6 98 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
COILED 117 277 {ECO:0000255}.
COILED 332 419 {ECO:0000255}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000250|UniProtKB:Q9EPY0}.
MOD_RES 277 277 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 424 424 Phosphoserine.
{ECO:0000250|UniProtKB:Q9EPY0}.
MOD_RES 425 425 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 431 431 Phosphoserine.
{ECO:0000250|UniProtKB:A2AIV8}.
MOD_RES 450 450 Phosphoserine.
{ECO:0000250|UniProtKB:Q9EPY0}.
MOD_RES 460 460 Phosphoserine.
{ECO:0000244|PubMed:18088087}.
MOD_RES 483 483 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 498 498 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 531 531 Phosphothreonine; by CK2.
{ECO:0000250|UniProtKB:Q9EPY0}.
MOD_RES 533 533 Phosphothreonine; by CK2.
{ECO:0000250|UniProtKB:Q9EPY0}.
VAR_SEQ 360 366 AIATREE -> STQMEGL (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_024390.
VAR_SEQ 367 536 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_024391.
VAR_SEQ 482 492 LSSGEPPEKER -> PAGLPGIGAVC (in isoform
2). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_024392.
VAR_SEQ 493 536 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_024393.
VARIANT 12 12 S -> N (in dbSNP:rs4077515).
{ECO:0000269|PubMed:11053425,
ECO:0000269|PubMed:14702039}.
/FTId=VAR_048607.
VARIANT 72 72 G -> S (in CANDF2; found in a compound
heterozygote also carrying P-373; patient
neutrophils do not express CARD9;
dbSNP:rs398122362).
{ECO:0000269|PubMed:23335372}.
/FTId=VAR_070828.
VARIANT 101 101 R -> C (in CANDF2; dbSNP:rs398122364).
{ECO:0000269|PubMed:24131138}.
/FTId=VAR_070829.
VARIANT 373 373 R -> P (in CANDF2; found in a compound
heterozygote also carrying S-72; patient
neutrophils do not express CARD9;
dbSNP:rs149712114).
{ECO:0000269|PubMed:23335372}.
/FTId=VAR_070830.
SEQUENCE 536 AA; 62241 MW; 6EB18353112F2BAC CRC64;
MSDYENDDEC WSVLEGFRVT LTSVIDPSRI TPYLRQCKVL NPDDEEQVLS DPNLVIRKRK
VGVLLDILQR TGHKGYVAFL ESLELYYPQL YKKVTGKEPA RVFSMIIDAS GESGLTQLLM
TEVMKLQKKV QDLTALLSSK DDFIKELRVK DSLLRKHQER VQRLKEECEA GSRELKRCKE
ENYDLAMRLA HQSEEKGAAL MRNRDLQLEI DQLKHSLMKA EDDCKVERKH TLKLRHAMEQ
RPSQELLWEL QQEKALLQAR VQELEASVQE GKLDRSSPYI QVLEEDWRQA LRDHQEQANT
IFSLRKDLRQ GEARRLRCME EKEMFELQCL ALRKDSKMYK DRIEAILLQM EEVAIERDQA
IATREELHAQ HARGLQEKDA LRKQVRELGE KADELQLQVF QCEAQLLAVE GRLRRQQLET
LVLSSDLEDG SPRRSQELSL PQDLEDTQLS DKGCLAGGGS PKQPFAALHQ EQVLRNPHDA
GLSSGEPPEK ERRRLKESFE NYRRKRALRK MQKGWRQGEE DRENTTGSDN TDTEGS


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