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Protein

Caspase recruitment domain-containing protein 8

Gene

CARD8

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

Functioni

Inhibits NF-kappa-B activation. May participate in a regulatory mechanism that coordinates cellular responses controlled by NF-kappa-B transcription factor. May be a component of the inflammasome, a protein complex which also includes PYCARD, NALP2 and CASP1 and whose function would be the activation of proinflammatory caspases.

GO - Molecular functioni

  1. cysteine-type endopeptidase activator activity involved in apoptotic process Source: HGNC
  2. NACHT domain binding Source: HGNC
  3. protein homodimerization activity Source: HGNC

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: GOC
  2. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: HGNC
  3. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: HGNC
  4. positive regulation of interleukin-1 beta secretion Source: HGNC
Complete GO annotation...

Keywords - Biological processi

Apoptosis

Protein family/group databases

MEROPSiS79.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Caspase recruitment domain-containing protein 8
Alternative name(s):
Apoptotic protein NDPP1
CARD-inhibitor of NF-kappa-B-activating ligand
Short name:
CARDINAL
DACAR
Tumor up-regulated CARD-containing antagonist of CASP9
Short name:
TUCAN
Gene namesi
Name:CARD8
Synonyms:KIAA0955, NDPP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:17057. CARD8.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HGNC
  2. NLRP3 inflammasome complex Source: UniProtKB
  3. nucleoplasm Source: HPA
  4. nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi366 – 3661L → R: Inhibits homodimer formation. 1 Publication

Organism-specific databases

PharmGKBiPA134916154.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 431431Caspase recruitment domain-containing protein 8PRO_0000144080Add
BLAST

Proteomic databases

MaxQBiQ9Y2G2.
PaxDbiQ9Y2G2.
PRIDEiQ9Y2G2.

Expressioni

Tissue specificityi

High expression in lung, ovary, testis and placenta. Lower expression in heart, kidney and liver. Also expressed in spleen, lymph node and bone marrow.

Gene expression databases

BgeeiQ9Y2G2.
CleanExiHS_CARD8.
ExpressionAtlasiQ9Y2G2. baseline and differential.
GenevestigatoriQ9Y2G2.

Organism-specific databases

HPAiHPA042071.
HPA043513.

Interactioni

Subunit structurei

May form homodimers. Interacts with NEMO and DRAL. Binds to caspase-1, CARD16/pseudo-ICE and CARD18/ICEBERG. Interacts with FNBP3 (By similarity). Interacts with NALP2 NACHT domain.By similarity2 Publications

Protein-protein interaction databases

BioGridi116564. 40 interactions.
IntActiQ9Y2G2. 3 interactions.
MINTiMINT-202188.
STRINGi9606.ENSP00000351901.

Structurei

Secondary structure

1
431
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi345 – 3506Combined sources
Helixi352 – 3587Combined sources
Helixi363 – 3719Combined sources
Helixi377 – 3859Combined sources
Beta strandi386 – 3883Combined sources
Helixi389 – 40113Combined sources
Helixi405 – 41814Combined sources
Helixi420 – 43112Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IKMX-ray2.46A345-431[»]
ProteinModelPortaliQ9Y2G2.
SMRiQ9Y2G2. Positions 345-431.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini340 – 43091CARDPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CARD domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG146295.
GeneTreeiENSGT00780000121905.
HOGENOMiHOG000082406.
HOVERGENiHBG050795.
InParanoidiQ9Y2G2.
KOiK12801.
OMAiHHEQWLV.
PhylomeDBiQ9Y2G2.
TreeFamiTF352798.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR025307. FIIND_dom.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
PF13553. FIIND. 1 hit.
[Graphical view]
SMARTiSM00114. CARD. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50209. CARD. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y2G2-1) [UniParc]FASTAAdd to basket

Also known as: Long

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
MMRQRQSHYC SVLFLSVNYL GGTFPGDICS EENQIVSSYA SKVCFEIEED
60 70 80 90 100
YKNRQFLGPE GNVDVELIDK STNRYSVWFP TAGWYLWSAT GLGFLVRDEV
110 120 130 140 150
TVTIAFGSWS QHLALDLQHH EQWLVGGPLF DVTAEPEEAV AEIHLPHFIS
160 170 180 190 200
LQGEVDVSWF LVAHFKNEGM VLEHPARVEP FYAVLESPSF SLMGILLRIA
210 220 230 240 250
SGTRLSIPIT SNTLIYYHPH PEDIKFHLYL VPSDALLTKA IDDEEDRFHG
260 270 280 290 300
VRLQTSPPME PLNFGSSYIV SNSANLKVMP KELKLSYRSP GEIQHFSKFY
310 320 330 340 350
AGQMKEPIQL EITEKRHGTL VWDTEVKPVD LQLVAASAPP PFSGAAFVKE
360 370 380 390 400
NHRQLQARMG DLKGVLDDLQ DNEVLTENEK ELVEQEKTRQ SKNEALLSMV
410 420 430
EKKGDLALDV LFRSISERDP YLVSYLRQQN L
Length:431
Mass (Da):48,933
Last modified:November 1, 1999 - v1
Checksum:iCB54D130807732E6
GO
Isoform 2 (identifier: Q9Y2G2-2) [UniParc]FASTAAdd to basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     282-286: ELKLS → WISSL
     287-431: Missing.

Show »
Length:286
Mass (Da):32,369
Checksum:iE6344DB98904F814
GO
Isoform 3 (identifier: Q9Y2G2-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MMRQRQSHYCSVLFLSVNYLGGTFP → MEKKECPEKS...EQESSEGQDS
     152-152: Q → QA
     282-286: ELKLS → WISSL
     287-431: Missing.

Show »
Length:392
Mass (Da):44,088
Checksum:i69F2C3DF325C3043
GO
Isoform 4 (identifier: Q9Y2G2-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MMRQRQSHYCSVLFLSVNYLGGTFP → MEKKECPEKS...EQESSEGQDS
     152-152: Q → QA

Note: No experimental confirmation available.

Show »
Length:487
Mass (Da):55,109
Checksum:iBE398DFC6F431003
GO
Isoform 5 (identifier: Q9Y2G2-5) [UniParc]FASTAAdd to basket

Also known as: T60

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MMRQRQSHYCSVLFLSVNYLGGTFP → MEKKECPEKS...EQESSEGQDS
     152-152: Q → QA

Show »
Length:537
Mass (Da):60,652
Checksum:i55775D025C5461BE
GO

Sequence cautioni

The sequence BAA76799.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601E → G in AAL02427 (PubMed:11551959).Curated
Sequence conflicti148 – 1481F → S in AAH56891 (PubMed:15489334).Curated
Sequence conflicti219 – 2191P → R in BAH12488 (PubMed:14702039).Curated
Sequence conflicti326 – 3261V → M in AAL02427 (PubMed:11551959).Curated
Sequence conflicti417 – 4171E → G in ABW96891 (PubMed:18212821).Curated
Sequence conflicti422 – 4221L → P in AAL02427 (PubMed:11551959).Curated
Isoform 5 (identifier: Q9Y2G2-5)
Sequence conflicti84 – 841D → G in ABW96891 (PubMed:18212821).Curated
Sequence conflicti107 – 1071E → D in ABW96891 (PubMed:18212821).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti68 – 681I → V.1 Publication
Corresponds to variant rs11881179 [ dbSNP | Ensembl ].
VAR_048606
Natural varianti99 – 991E → A.1 Publication
Corresponds to variant rs59878320 [ dbSNP | Ensembl ].
VAR_061079

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2525MMRQR…GGTFP → MEKKECPEKSSSSEEELPRR DSGSSRNIDASKLIRLQGSR KLLVDNSIRELQYTKTGIFF QAEACVTNDTVYRELPCVSE TLCDISHFFQEDDETEAEPL LFRAVPECQLSGGDIPSVSE EQESSEGQDS in isoform 3 and isoform 5. 3 PublicationsVSP_012770Add
BLAST
Alternative sequencei1 – 2525MMRQR…GGTFP → MEKKECPEKSSSSEEELPRR VYRELPCVSETLCDISHFFQ EDDETEAEPLLFRAVPECQL SGGDIPSVSEEQESSEGQDS in isoform 4. 1 PublicationVSP_045253Add
BLAST
Alternative sequencei152 – 1521Q → QA in isoform 3, isoform 4 and isoform 5. 3 PublicationsVSP_012771
Alternative sequencei282 – 2865ELKLS → WISSL in isoform 2 and isoform 3. 3 PublicationsVSP_000782
Alternative sequencei287 – 431145Missing in isoform 2 and isoform 3. 3 PublicationsVSP_000783Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023172 mRNA. Translation: BAA76799.2. Different initiation.
AF322184 mRNA. Translation: AAG50014.1.
AF331519 mRNA. Translation: AAK01126.1.
AY026322 mRNA. Translation: AAK08982.1.
AF405558 mRNA. Translation: AAL02427.1.
EU118120 mRNA. Translation: ABW96891.1.
AF511652 mRNA. Translation: AAM46959.1.
AK297045 mRNA. Translation: BAH12482.1.
AK297069 mRNA. Translation: BAH12488.1.
AC008392 Genomic DNA. No translation available.
AC011466 Genomic DNA. No translation available.
CH471177 Genomic DNA. Translation: EAW52321.1.
CH471177 Genomic DNA. Translation: EAW52323.1.
BC056891 mRNA. Translation: AAH56891.1.
CCDSiCCDS12712.2. [Q9Y2G2-4]
CCDS54288.1. [Q9Y2G2-3]
CCDS54289.1. [Q9Y2G2-5]
RefSeqiNP_001171829.1. NM_001184900.1. [Q9Y2G2-5]
NP_001171830.1. NM_001184901.1. [Q9Y2G2-4]
NP_001171831.1. NM_001184902.1. [Q9Y2G2-3]
NP_001171832.1. NM_001184903.1. [Q9Y2G2-3]
NP_055774.2. NM_014959.3. [Q9Y2G2-4]
XP_006723154.1. XM_006723091.1. [Q9Y2G2-5]
XP_006723155.1. XM_006723092.1. [Q9Y2G2-5]
XP_006723156.1. XM_006723093.1. [Q9Y2G2-5]
XP_006723158.1. XM_006723095.1. [Q9Y2G2-4]
XP_006723159.1. XM_006723096.1. [Q9Y2G2-4]
XP_006723160.1. XM_006723097.1. [Q9Y2G2-4]
XP_006723167.1. XM_006723104.1. [Q9Y2G2-1]
XP_006723169.1. XM_006723106.1. [Q9Y2G2-3]
XP_006723172.1. XM_006723109.1. [Q9Y2G2-2]
UniGeneiHs.446146.
Hs.655940.

Genome annotation databases

EnsembliENST00000391898; ENSP00000375767; ENSG00000105483. [Q9Y2G2-5]
ENST00000447740; ENSP00000391248; ENSG00000105483. [Q9Y2G2-4]
ENST00000519940; ENSP00000428883; ENSG00000105483. [Q9Y2G2-5]
ENST00000520015; ENSP00000430747; ENSG00000105483. [Q9Y2G2-3]
ENST00000520153; ENSP00000428736; ENSG00000105483. [Q9Y2G2-4]
ENST00000520753; ENSP00000429839; ENSG00000105483. [Q9Y2G2-3]
ENST00000521613; ENSP00000427858; ENSG00000105483. [Q9Y2G2-4]
GeneIDi22900.
KEGGihsa:22900.
UCSCiuc002pie.4. human. [Q9Y2G2-1]
uc002pif.4. human. [Q9Y2G2-2]
uc002pih.4. human.
uc002pii.4. human. [Q9Y2G2-3]
uc010xzj.2. human.

Polymorphism databases

DMDMi14424229.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB023172 mRNA. Translation: BAA76799.2. Different initiation.
AF322184 mRNA. Translation: AAG50014.1.
AF331519 mRNA. Translation: AAK01126.1.
AY026322 mRNA. Translation: AAK08982.1.
AF405558 mRNA. Translation: AAL02427.1.
EU118120 mRNA. Translation: ABW96891.1.
AF511652 mRNA. Translation: AAM46959.1.
AK297045 mRNA. Translation: BAH12482.1.
AK297069 mRNA. Translation: BAH12488.1.
AC008392 Genomic DNA. No translation available.
AC011466 Genomic DNA. No translation available.
CH471177 Genomic DNA. Translation: EAW52321.1.
CH471177 Genomic DNA. Translation: EAW52323.1.
BC056891 mRNA. Translation: AAH56891.1.
CCDSiCCDS12712.2. [Q9Y2G2-4]
CCDS54288.1. [Q9Y2G2-3]
CCDS54289.1. [Q9Y2G2-5]
RefSeqiNP_001171829.1. NM_001184900.1. [Q9Y2G2-5]
NP_001171830.1. NM_001184901.1. [Q9Y2G2-4]
NP_001171831.1. NM_001184902.1. [Q9Y2G2-3]
NP_001171832.1. NM_001184903.1. [Q9Y2G2-3]
NP_055774.2. NM_014959.3. [Q9Y2G2-4]
XP_006723154.1. XM_006723091.1. [Q9Y2G2-5]
XP_006723155.1. XM_006723092.1. [Q9Y2G2-5]
XP_006723156.1. XM_006723093.1. [Q9Y2G2-5]
XP_006723158.1. XM_006723095.1. [Q9Y2G2-4]
XP_006723159.1. XM_006723096.1. [Q9Y2G2-4]
XP_006723160.1. XM_006723097.1. [Q9Y2G2-4]
XP_006723167.1. XM_006723104.1. [Q9Y2G2-1]
XP_006723169.1. XM_006723106.1. [Q9Y2G2-3]
XP_006723172.1. XM_006723109.1. [Q9Y2G2-2]
UniGeneiHs.446146.
Hs.655940.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IKMX-ray2.46A345-431[»]
ProteinModelPortaliQ9Y2G2.
SMRiQ9Y2G2. Positions 345-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116564. 40 interactions.
IntActiQ9Y2G2. 3 interactions.
MINTiMINT-202188.
STRINGi9606.ENSP00000351901.

Protein family/group databases

MEROPSiS79.001.

Polymorphism databases

DMDMi14424229.

Proteomic databases

MaxQBiQ9Y2G2.
PaxDbiQ9Y2G2.
PRIDEiQ9Y2G2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000391898; ENSP00000375767; ENSG00000105483. [Q9Y2G2-5]
ENST00000447740; ENSP00000391248; ENSG00000105483. [Q9Y2G2-4]
ENST00000519940; ENSP00000428883; ENSG00000105483. [Q9Y2G2-5]
ENST00000520015; ENSP00000430747; ENSG00000105483. [Q9Y2G2-3]
ENST00000520153; ENSP00000428736; ENSG00000105483. [Q9Y2G2-4]
ENST00000520753; ENSP00000429839; ENSG00000105483. [Q9Y2G2-3]
ENST00000521613; ENSP00000427858; ENSG00000105483. [Q9Y2G2-4]
GeneIDi22900.
KEGGihsa:22900.
UCSCiuc002pie.4. human. [Q9Y2G2-1]
uc002pif.4. human. [Q9Y2G2-2]
uc002pih.4. human.
uc002pii.4. human. [Q9Y2G2-3]
uc010xzj.2. human.

Organism-specific databases

CTDi22900.
GeneCardsiGC19M048711.
H-InvDBHIX0020041.
HGNCiHGNC:17057. CARD8.
HPAiHPA042071.
HPA043513.
MIMi609051. gene.
neXtProtiNX_Q9Y2G2.
PharmGKBiPA134916154.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG146295.
GeneTreeiENSGT00780000121905.
HOGENOMiHOG000082406.
HOVERGENiHBG050795.
InParanoidiQ9Y2G2.
KOiK12801.
OMAiHHEQWLV.
PhylomeDBiQ9Y2G2.
TreeFamiTF352798.

Miscellaneous databases

ChiTaRSiCARD8. human.
GeneWikiiCARD8.
GenomeRNAii22900.
NextBioi43531.
PROiQ9Y2G2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y2G2.
CleanExiHS_CARD8.
ExpressionAtlasiQ9Y2G2. baseline and differential.
GenevestigatoriQ9Y2G2.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR001315. CARD.
IPR011029. DEATH-like_dom.
IPR025307. FIIND_dom.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
PF13553. FIIND. 1 hit.
[Graphical view]
SMARTiSM00114. CARD. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50209. CARD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:63-70(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "CARD-8 protein, a new CARD family member that regulates caspase-1 activation and apoptosis."
    Razmara M., Srinivasula S.M., Wang L., Poyet J.-L., Geddes B.J., DiStefano P.S., Bertin J., Alnemri E.S.
    J. Biol. Chem. 277:13952-13958(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CARD16 AND CARD18.
  3. "NDPP1 is a novel CARD domain containing protein which can inhibit apoptosis and suppress NF-kappaB activation."
    Zhang H., Fu W.
    Int. J. Oncol. 20:1035-1040(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "DACAR, a novel CARD-containing protein."
    Guiet C., Vito P.
    Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  5. "CARDINAL, a novel caspase recruitment domain protein, is an inhibitor of multiple NF-kappa B activation pathways."
    Bouchier-Hayes L., Conroy H., Egan H., Adrain C., Creagh E.M., MacFarlane M., Martin S.J.
    J. Biol. Chem. 276:44069-44077(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  6. "Novel isoforms of the CARD8 (TUCAN) gene evade a nonsense mutation."
    Bagnall R.D., Roberts R.G., Mirza M.M., Torigoe T., Prescott N.J., Mathew C.G.
    Eur. J. Hum. Genet. 16:619-625(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), ALTERNATIVE SPLICING.
  7. Guo J.H., Yu L.
    Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Kidney.
  8. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), VARIANTS VAL-68 AND ALA-99.
    Tissue: Umbilical cord blood.
  9. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Eye.
  12. "TUCAN, an antiapoptotic caspase-associated recruitment domain family protein overexpressed in cancer."
    Pathan N., Marusawa H., Krajewska M., Matsuzawa S., Kim H., Okada K., Torii S., Kitada S., Krajewski S., Welsh K., Pio F., Godzik A., Reed J.C.
    J. Biol. Chem. 276:32220-32229(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  13. "TUCAN/CARDINAL and DRAL participate in a common pathway for modulation of NF-kappaB activation."
    Stilo R., Leonardi A., Formisano L., Di Jeso B., Vito P., Liguoro D.
    FEBS Lett. 521:165-169(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS OF LEU-366.
  14. "NALP3 forms an IL-1beta-processing inflammasome with increased activity in Muckle-Wells autoinflammatory disorder."
    Agostini L., Martinon F., Burns K., McDermott M.F., Hawkins P.N., Tschopp J.
    Immunity 20:319-325(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NALP2, SUBCELLULAR LOCATION.
  15. "The structure of the CARD8 caspase-recruitment domain suggests its association with the FIIND domain and procaspases through adjacent surfaces."
    Jin T., Huang M., Smith P., Jiang J., Xiao T.S.
    Acta Crystallogr. F 69:482-487(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS) OF 345-431.

Entry informationi

Entry nameiCARD8_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2G2
Secondary accession number(s): B5KVR6
, B7Z496, B7Z4A2, E9PEM7, G3XAM9, Q6PGP8, Q96P82
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: November 1, 1999
Last modified: April 1, 2015
This is version 132 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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.