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Protein

Caspase recruitment domain-containing protein 9

Gene

CARD9

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

Functioni

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.By similarity1 Publication

GO - Molecular functioni

  1. CARD domain binding Source: UniProtKB
  2. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. defense response to Gram-positive bacterium Source: Ensembl
  2. defense response to virus Source: Ensembl
  3. innate immune response Source: Reactome
  4. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
  5. nucleotide-binding oligomerization domain containing signaling pathway Source: Reactome
  6. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  7. positive regulation of interleukin-6 production Source: Ensembl
  8. positive regulation of JNK cascade Source: MGI
  9. positive regulation of stress-activated MAPK cascade Source: MGI
  10. positive regulation of tumor necrosis factor production Source: Ensembl
  11. regulation of apoptotic process Source: InterPro
  12. regulation of interleukin-2 biosynthetic process Source: Ensembl
  13. regulation of interleukin-6 biosynthetic process Source: Ensembl
  14. regulation of tumor necrosis factor biosynthetic process Source: Ensembl
  15. response to drug Source: Ensembl
  16. response to exogenous dsRNA Source: Ensembl
  17. response to fungus Source: Ensembl
  18. response to muramyl dipeptide Source: Ensembl
  19. response to peptidoglycan Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_75776. NOD1/2 Signaling Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Caspase recruitment domain-containing protein 9
Short name:
hCARD9
Gene namesi
Name:CARD9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:16391. CARD9.

Subcellular locationi

  1. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Candidiasis, familial, 2 (CANDF2)3 Publications

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).

Disease descriptionA 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.

See also OMIM:212050
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti72 – 721G → S in CANDF2; loss of protein expression. 1 Publication
VAR_070828
Natural varianti101 – 1011R → C in CANDF2. 1 Publication
VAR_070829
Natural varianti373 – 3731R → P in CANDF2; loss of protein expression. 1 Publication
VAR_070830

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi212050. phenotype.
Orphaneti1334. Chronic mucocutaneous candidosis.
397587. Deep dermatophytosis.
PharmGKBiPA26077.

Polymorphism and mutation databases

BioMutaiCARD9.
DMDMi143811370.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 536536Caspase recruitment domain-containing protein 9PRO_0000144082Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei460 – 4601Phosphoserine1 Publication
Modified residuei531 – 5311Phosphothreonine; by CK2By similarity
Modified residuei533 – 5331Phosphothreonine; by CK2By similarity

Post-translational modificationi

Phosphorylated at Thr-531 and Thr-533 by CK2 following interaction with VHL, leading to inhibit the ability to activate NF-kappa-B.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H257.
PaxDbiQ9H257.
PRIDEiQ9H257.

PTM databases

PhosphoSiteiQ9H257.

Expressioni

Tissue specificityi

Highly expressed in spleen. Also detected in liver, placenta, lung, peripheral blood leukocytes and in brain.

Gene expression databases

BgeeiQ9H257.
CleanExiHS_CARD9.
ExpressionAtlasiQ9H257. baseline and differential.
GenevestigatoriQ9H257.

Organism-specific databases

HPAiHPA059502.

Interactioni

Subunit structurei

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).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
A8K9323EBI-751319,EBI-10174671
A8KAD63EBI-751319,EBI-10174974
ABLIM1O146393EBI-751319,EBI-487024
AESQ081173EBI-751319,EBI-717810
ALS2CR11Q53TS83EBI-751319,EBI-739879
AMOTL2Q9Y2J4-45EBI-751319,EBI-10187270
BCL10O959996EBI-751319,EBI-958922
BLZF1Q9H2G93EBI-751319,EBI-2548012
C1orf94Q6P1W53EBI-751319,EBI-946029
CCDC36Q8IYA83EBI-751319,EBI-8638439
CCHCR1Q8TD31-33EBI-751319,EBI-10175300
CDCA7LQ96GN53EBI-751319,EBI-5278764
CEP57L1Q8IYX8-23EBI-751319,EBI-10181988
CEP70Q8NHQ13EBI-751319,EBI-739624
DAXXQ9UER73EBI-751319,EBI-77321
DUSP13Q9UII63EBI-751319,EBI-749800
EIF4E2O605733EBI-751319,EBI-398610
FAM124BQ9H5Z63EBI-751319,EBI-741626
FAM161AQ3B8203EBI-751319,EBI-719941
FAM208BQ5VWN6-23EBI-751319,EBI-10172380
FAM50BQ9Y2473EBI-751319,EBI-742802
HMBOX1Q6NT763EBI-751319,EBI-2549423
KCTD9Q7L2733EBI-751319,EBI-4397613
KRT19P087273EBI-751319,EBI-742756
KRT31Q153233EBI-751319,EBI-948001
KRT40Q6A1623EBI-751319,EBI-10171697
KRTAP10-5P603703EBI-751319,EBI-10172150
LENG1Q96BZ83EBI-751319,EBI-726510
LMO1P258003EBI-751319,EBI-8639312
LZTS2Q9BRK43EBI-751319,EBI-741037
MEOX2A4D1273EBI-751319,EBI-10172134
MFAP1P550813EBI-751319,EBI-1048159
NECAB2H3BTW23EBI-751319,EBI-10172876
PAK7Q8TB933EBI-751319,EBI-741896
PBX2P404253EBI-751319,EBI-348489
PHC2Q8IXK03EBI-751319,EBI-713786
PNMA5Q96PV43EBI-751319,EBI-10171633
PPP1R18Q6NYC83EBI-751319,EBI-2557469
RTP5Q14D333EBI-751319,EBI-10217913
SSX2IPQ9Y2D83EBI-751319,EBI-2212028
STX11O755583EBI-751319,EBI-714135
SUMO1P631653EBI-751319,EBI-80140
TCEANCQ8N8B73EBI-751319,EBI-954696
TCL1AP562793EBI-751319,EBI-749995
TFIP11Q9UBB93EBI-751319,EBI-1105213
TNFAIP1Q138293EBI-751319,EBI-2505861
TRIM23P364063EBI-751319,EBI-740098
TRIM29Q141343EBI-751319,EBI-702370
TRIM42A1L4B63EBI-751319,EBI-10172216
TRIM54Q9BYV23EBI-751319,EBI-2130429
TSNAXQ995985EBI-751319,EBI-742638
USP15Q9Y4E83EBI-751319,EBI-1043104
VPS28Q548N13EBI-751319,EBI-10243107
ZCCHC7Q8N3Z63EBI-751319,EBI-7265024
ZNF250P15622-33EBI-751319,EBI-10177272
ZNF417Q8TAU33EBI-751319,EBI-740727
ZNF572A1L4E93EBI-751319,EBI-10172590
ZNF572Q7Z3I73EBI-751319,EBI-10257016
ZNF587Q96SQ53EBI-751319,EBI-6427977
ZNF655Q8N7203EBI-751319,EBI-625509

Protein-protein interaction databases

BioGridi122094. 75 interactions.
IntActiQ9H257. 65 interactions.
STRINGi9606.ENSP00000360797.

Structurei

3D structure databases

ProteinModelPortaliQ9H257.
SMRiQ9H257. Positions 11-98.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 9893CARDPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili117 – 277161Sequence AnalysisAdd
BLAST
Coiled coili332 – 41988Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 CARD domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG243105.
GeneTreeiENSGT00530000063108.
HOGENOMiHOG000231538.
HOVERGENiHBG058091.
InParanoidiQ9H257.
KOiK12794.
OMAiQLLMSEV.
OrthoDBiEOG747PH5.
PhylomeDBiQ9H257.
TreeFamiTF351139.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR001315. CARD.
IPR011029. DEATH-like_dom.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50209. CARD. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H257-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSDYENDDEC WSVLEGFRVT LTSVIDPSRI TPYLRQCKVL NPDDEEQVLS
60 70 80 90 100
DPNLVIRKRK VGVLLDILQR TGHKGYVAFL ESLELYYPQL YKKVTGKEPA
110 120 130 140 150
RVFSMIIDAS GESGLTQLLM TEVMKLQKKV QDLTALLSSK DDFIKELRVK
160 170 180 190 200
DSLLRKHQER VQRLKEECEA GSRELKRCKE ENYDLAMRLA HQSEEKGAAL
210 220 230 240 250
MRNRDLQLEI DQLKHSLMKA EDDCKVERKH TLKLRHAMEQ RPSQELLWEL
260 270 280 290 300
QQEKALLQAR VQELEASVQE GKLDRSSPYI QVLEEDWRQA LRDHQEQANT
310 320 330 340 350
IFSLRKDLRQ GEARRLRCME EKEMFELQCL ALRKDSKMYK DRIEAILLQM
360 370 380 390 400
EEVAIERDQA IATREELHAQ HARGLQEKDA LRKQVRELGE KADELQLQVF
410 420 430 440 450
QCEAQLLAVE GRLRRQQLET LVLSSDLEDG SPRRSQELSL PQDLEDTQLS
460 470 480 490 500
DKGCLAGGGS PKQPFAALHQ EQVLRNPHDA GLSSGEPPEK ERRRLKESFE
510 520 530
NYRRKRALRK MQKGWRQGEE DRENTTGSDN TDTEGS
Length:536
Mass (Da):62,241
Last modified:April 3, 2007 - v2
Checksum:i6EB18353112F2BAC
GO
Isoform 2 (identifier: Q9H257-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     482-492: LSSGEPPEKER → PAGLPGIGAVC
     493-536: Missing.

Note: No experimental confirmation available.

Show »
Length:492
Mass (Da):56,667
Checksum:iAADBCF6A5E81125F
GO
Isoform 3 (identifier: Q9H257-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     360-366: AIATREE → STQMEGL
     367-536: Missing.

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.

Show »
Length:366
Mass (Da):42,953
Checksum:iEC1CB0ABCF6C7CF4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121S → N.2 Publications
Corresponds to variant rs4077515 [ dbSNP | Ensembl ].
VAR_048607
Natural varianti72 – 721G → S in CANDF2; loss of protein expression. 1 Publication
VAR_070828
Natural varianti101 – 1011R → C in CANDF2. 1 Publication
VAR_070829
Natural varianti373 – 3731R → P in CANDF2; loss of protein expression. 1 Publication
VAR_070830

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei360 – 3667AIATREE → STQMEGL in isoform 3. 1 PublicationVSP_024390
Alternative sequencei367 – 536170Missing in isoform 3. 1 PublicationVSP_024391Add
BLAST
Alternative sequencei482 – 49211LSSGEPPEKER → PAGLPGIGAVC in isoform 2. 1 PublicationVSP_024392Add
BLAST
Alternative sequencei493 – 53644Missing in isoform 2. 1 PublicationVSP_024393Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF311287 mRNA. Translation: AAG28790.1.
AK024001 mRNA. Translation: BAB14766.1.
AK292081 mRNA. Translation: BAF84770.1.
AL592301 Genomic DNA. Translation: CAI13931.1.
AL592301 Genomic DNA. Translation: CAI13932.1.
CH471090 Genomic DNA. Translation: EAW88220.1.
BC008877 mRNA. Translation: AAH08877.1.
CCDSiCCDS48057.1. [Q9H257-2]
CCDS6997.1. [Q9H257-1]
RefSeqiNP_434700.2. NM_052813.4. [Q9H257-1]
NP_434701.1. NM_052814.3. [Q9H257-2]
UniGeneiHs.694071.

Genome annotation databases

EnsembliENST00000371732; ENSP00000360797; ENSG00000187796. [Q9H257-1]
ENST00000371734; ENSP00000360799; ENSG00000187796. [Q9H257-2]
ENST00000489932; ENSP00000451368; ENSG00000187796. [Q9H257-3]
GeneIDi64170.
KEGGihsa:64170.
UCSCiuc004chg.3. human. [Q9H257-1]
uc010nbj.2. human. [Q9H257-3]
uc022bpo.1. human. [Q9H257-2]

Polymorphism and mutation databases

BioMutaiCARD9.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF311287 mRNA. Translation: AAG28790.1.
AK024001 mRNA. Translation: BAB14766.1.
AK292081 mRNA. Translation: BAF84770.1.
AL592301 Genomic DNA. Translation: CAI13931.1.
AL592301 Genomic DNA. Translation: CAI13932.1.
CH471090 Genomic DNA. Translation: EAW88220.1.
BC008877 mRNA. Translation: AAH08877.1.
CCDSiCCDS48057.1. [Q9H257-2]
CCDS6997.1. [Q9H257-1]
RefSeqiNP_434700.2. NM_052813.4. [Q9H257-1]
NP_434701.1. NM_052814.3. [Q9H257-2]
UniGeneiHs.694071.

3D structure databases

ProteinModelPortaliQ9H257.
SMRiQ9H257. Positions 11-98.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122094. 75 interactions.
IntActiQ9H257. 65 interactions.
STRINGi9606.ENSP00000360797.

PTM databases

PhosphoSiteiQ9H257.

Polymorphism and mutation databases

BioMutaiCARD9.
DMDMi143811370.

Proteomic databases

MaxQBiQ9H257.
PaxDbiQ9H257.
PRIDEiQ9H257.

Protocols and materials databases

DNASUi64170.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371732; ENSP00000360797; ENSG00000187796. [Q9H257-1]
ENST00000371734; ENSP00000360799; ENSG00000187796. [Q9H257-2]
ENST00000489932; ENSP00000451368; ENSG00000187796. [Q9H257-3]
GeneIDi64170.
KEGGihsa:64170.
UCSCiuc004chg.3. human. [Q9H257-1]
uc010nbj.2. human. [Q9H257-3]
uc022bpo.1. human. [Q9H257-2]

Organism-specific databases

CTDi64170.
GeneCardsiGC09M139259.
HGNCiHGNC:16391. CARD9.
HPAiHPA059502.
MIMi212050. phenotype.
607212. gene.
neXtProtiNX_Q9H257.
Orphaneti1334. Chronic mucocutaneous candidosis.
397587. Deep dermatophytosis.
PharmGKBiPA26077.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG243105.
GeneTreeiENSGT00530000063108.
HOGENOMiHOG000231538.
HOVERGENiHBG058091.
InParanoidiQ9H257.
KOiK12794.
OMAiQLLMSEV.
OrthoDBiEOG747PH5.
PhylomeDBiQ9H257.
TreeFamiTF351139.

Enzyme and pathway databases

ReactomeiREACT_75776. NOD1/2 Signaling Pathway.

Miscellaneous databases

GeneWikiiCARD9.
GenomeRNAii64170.
NextBioi66079.
PROiQ9H257.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H257.
CleanExiHS_CARD9.
ExpressionAtlasiQ9H257. baseline and differential.
GenevestigatoriQ9H257.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR001315. CARD.
IPR011029. DEATH-like_dom.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50209. CARD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CARD9 is a novel caspase recruitment domain-containing protein that interacts with Bcl10/CLAP and activates NF-kappa B."
    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.
    J. Biol. Chem. 275:41082-41086(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASN-12, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BCL10.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), VARIANT ASN-12.
    Tissue: Retinoblastoma and Synovium.
  3. "DNA sequence and analysis of human chromosome 9."
    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.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 2).
    Tissue: Muscle.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  7. Cited for: INVOLVEMENT IN CANDF2.
  8. "Interaction between NOD2 and CARD9 involves the NOD2 NACHT and the linker region between the NOD2 CARDs and NACHT domain."
    Parkhouse R., Boyle J.P., Mayle S., Sawmynaden K., Rittinger K., Monie T.P.
    FEBS Lett. 588:2830-2836(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOD2.
  9. Cited for: VARIANTS CANDF2 SER-72 AND PRO-373.
  10. Cited for: VARIANT CANDF2 CYS-101.

Entry informationi

Entry nameiCARD9_HUMAN
AccessioniPrimary (citable) accession number: Q9H257
Secondary accession number(s): Q5SXM5, Q5SXM6, Q9H854
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: April 3, 2007
Last modified: April 29, 2015
This is version 123 of the entry and version 2 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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. 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.