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Protein

Apoptosis-associated speck-like protein containing a CARD

Gene

Pycard

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as key mediator in apoptosis and inflammation. Promotes caspase-mediated apoptosis involving predominantly caspase-8 and also caspase-9 in a probable cell type-specific manner. Involved in activation of the mitochondrial apoptotic pathway, promotes caspase-8-dependent proteolytic maturation of BID independently of FADD in certain cell types and also mediates mitochondrial translocation of BAX and activates BAX-dependent apoptosis coupled to activation of caspase-9, -2 and -3. Involved in macrophage pyroptosis, a caspase-1-dependent inflammatory form of cell death and is the major constituent of the ASC pyroptosome which forms upon potassium depletion and rapidly recruits and activates caspase-1. In innate immune response believed to act as an integral adapter in the assembly of the inflammasome which activates caspase-1 leading to processing and secretion of proinflammatory cytokines. The function as activating adapter in different types of inflammasomes is mediated by the DAPIN and CARD domains and their homotypic interactions. Required for recruitment of caspase-1 to inflammasomes containing certain pattern recognition receptors, such as NLRP2, NLRP3, AIM2 and probably IFI16. In the NLRP1 and NLRC4 inflammasomes seems not be required but facilitates the processing of procaspase-1. In cooperation with NOD2 involved in an inflammasome activated by bacterial muramyl dipeptide leading to caspase-1 activation. May be involved in DDX58-triggered proinflammatory responses and inflammasome activation. In collaboration with AIM2 which detects cytosolic double-stranded DNA may also be involved in a caspase-1-independent cell death that involves caspase-8. In adaptive immunity may be involved in maturation of dendritic cells to stimulate T-cell immunity and in cytoskeletal rearrangements coupled to chemotaxis and antigen uptake may be involved in post-transcriptional regulation of the guanine nucleotide exchange factor DOCK2; the latter function is proposed to involve the nuclear form. Also involved in transcriptional activation of cytokines and chemokines independent of the inflammasome; this function may involve AP-1, NF-kappa-B, MAPK and caspase-8 signaling pathways. For regulation of NF-kappa-B activating and inhibiting functions have been reported. Modulates NF-kappa-B induction at the level of the IKK complex by inhibiting kinase activity of CHUK and IKBK. Proposed to compete with RIPK2 for association with CASP1 thereby down-regulating CASP1-mediated RIPK2-dependent NF-kappa-B activation and activating interleukin-1 beta processing.4 Publications

GO - Molecular functioni

  1. peptidase activator activity involved in apoptotic process Source: MGI
  2. protein homodimerization activity Source: HGNC
  3. Pyrin domain binding Source: HGNC

GO - Biological processi

  1. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  2. activation of innate immune response Source: UniProtKB
  3. apoptotic process Source: MGI
  4. cellular response to interleukin-1 Source: MGI
  5. cellular response to lipopolysaccharide Source: MGI
  6. cellular response to tumor necrosis factor Source: MGI
  7. defense response to Gram-negative bacterium Source: MGI
  8. defense response to virus Source: MGI
  9. inflammatory response Source: MGI
  10. innate immune response Source: UniProtKB-KW
  11. interleukin-1 beta production Source: MGI
  12. intrinsic apoptotic signaling pathway by p53 class mediator Source: MGI
  13. intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator Source: MGI
  14. macropinocytosis Source: UniProtKB
  15. myeloid dendritic cell activation Source: MGI
  16. myeloid dendritic cell activation involved in immune response Source: UniProtKB
  17. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  18. negative regulation of interferon-beta production Source: MGI
  19. negative regulation of NF-kappaB transcription factor activity Source: MGI
  20. negative regulation of protein serine/threonine kinase activity Source: MGI
  21. positive regulation of actin filament polymerization Source: UniProtKB
  22. positive regulation of activated T cell proliferation Source: UniProtKB
  23. positive regulation of adaptive immune response Source: MGI
  24. positive regulation of antigen processing and presentation of peptide antigen via MHC class II Source: UniProtKB
  25. positive regulation of apoptotic process Source: MGI
  26. positive regulation of chemokine secretion Source: UniProtKB
  27. positive regulation of cysteine-type endopeptidase activity Source: MGI
  28. positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: HGNC
  29. positive regulation of defense response to virus by host Source: UniProtKB
  30. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  31. positive regulation of extrinsic apoptotic signaling pathway Source: MGI
  32. positive regulation of interferon-gamma production Source: UniProtKB
  33. positive regulation of interleukin-10 secretion Source: MGI
  34. positive regulation of interleukin-1 beta secretion Source: UniProtKB
  35. positive regulation of interleukin-6 production Source: UniProtKB
  36. positive regulation of interleukin-6 secretion Source: MGI
  37. positive regulation of interleukin-8 secretion Source: MGI
  38. positive regulation of JNK cascade Source: MGI
  39. positive regulation of NF-kappaB transcription factor activity Source: MGI
  40. positive regulation of phagocytosis Source: UniProtKB
  41. positive regulation of release of cytochrome c from mitochondria Source: MGI
  42. positive regulation of sequence-specific DNA binding transcription factor activity Source: MGI
  43. positive regulation of T cell activation Source: MGI
  44. positive regulation of T cell migration Source: UniProtKB
  45. positive regulation of tumor necrosis factor production Source: MGI
  46. regulation of apoptotic process Source: MGI
  47. regulation of autophagy Source: MGI
  48. regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
  49. regulation of inflammatory response Source: MGI
  50. regulation of intrinsic apoptotic signaling pathway Source: MGI
  51. regulation of protein stability Source: UniProtKB
  52. regulation of Rac GTPase activity Source: UniProtKB
  53. regulation of tumor necrosis factor-mediated signaling pathway Source: MGI
  54. response to bacterium Source: MGI
  55. tumor necrosis factor-mediated signaling pathway Source: MGI
Complete GO annotation...

Keywords - Biological processi

Apoptosis, Immunity, Inflammatory response, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_198644. The NLRP3 inflammasome.
REACT_198662. The AIM2 inflammasome.

Names & Taxonomyi

Protein namesi
Recommended name:
Apoptosis-associated speck-like protein containing a CARD
Short name:
mASC
Alternative name(s):
PYD and CARD domain-containing protein
Gene namesi
Name:Pycard
Synonyms:Asc
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1931465. Pycard.

Subcellular locationi

Cytoplasm 2 Publications. Endoplasmic reticulum By similarity. Mitochondrion By similarity. Nucleus By similarity
Note: Upstream of caspase activation, a redistribution from the cytoplasm to the aggregates occurs. These appear as hollow, perinuclear spherical, ball-like structures. Upon NLRP3 inflammasome activation redistributes to the perinuclear space localizing to endoplasmic reticulum and mitochondria. Localized primarily to the nucleus in resting monocytes/macrophages and rapidly redistributed to the cytoplasm upon pathogen infection (By similarity). Localized to large cytoplasmic aggregate appearing as a speck containing AIM2, PYCARD, CASP8 and bacterial DNA after infection with Francisella tularensis.By similarity

GO - Cellular componenti

  1. AIM2 inflammasome complex Source: UniProtKB
  2. cytoplasm Source: HGNC
  3. cytosol Source: MGI
  4. endoplasmic reticulum Source: UniProtKB-SubCell
  5. extracellular region Source: MGI
  6. mitochondrion Source: MGI
  7. neuronal cell body Source: Ensembl
  8. NLRP1 inflammasome complex Source: MGI
  9. NLRP3 inflammasome complex Source: UniProtKB
  10. nucleolus Source: MGI
  11. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Mitochondrion, Nucleus

Pathology & Biotechi

Disruption phenotypei

Increased resistance to endotoxic shock and severe defects in caspase-1 activation and interleukin-1 beta and interleukin-18 production in macrophages in response to several pro-inflammatory molecules.2 Publications

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 193193Apoptosis-associated speck-like protein containing a CARDPRO_0000064693Add
BLAST

Post-translational modificationi

Phosphorylated.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9EPB4.
PaxDbiQ9EPB4.
PRIDEiQ9EPB4.

PTM databases

PhosphoSiteiQ9EPB4.

Expressioni

Tissue specificityi

Expressed in small intestine, colon, thymus, spleen, brain, heart, skeletal muscle, kidney, lung and liver.

Developmental stagei

Strongly expressed at E9.5 in the telencephalon, thalamic areas of the diencephalon, heart and liver.

Gene expression databases

BgeeiQ9EPB4.
CleanExiMM_PYCARD.
ExpressionAtlasiQ9EPB4. baseline and differential.
GenevestigatoriQ9EPB4.

Interactioni

Subunit structurei

Self-associates; enforced oligomerization induces apoptosis, NF-kappa-B regulation and interleukin-1 beta seceretion. Homooligomers can form disk-like particles of approximately 12 nm diameter and approximately 1 nm height. Component of several inflammasomes containing one pattern recognition receptor/sensor, such as NLRP1, NLRP2, NLRP3, AIM2, MEFV or NOD2, and probably NLRC4, NLRP12 or IFI16. Major component of the ASC pyroptosome, a 1-2 um supramolecular assembly (one per macrophage cell) which consists of oligomerized PYCARD dimers and CASP1. Interacts with CASP1 (precursor form); the interaction induces activation of CASP1 leading to the processing of interleukin-1 beta; PYCARD competes with RIPK2 for binding to CASP1. Interacts with NLRP3; the interaction requires the homooligomerization of NLRP3. Interacts with NLRP2, NLRC4, MEFV, CARD16, AIM2, IFI16, NOD2, DDX58, RIPK2, PYDC1, PYDC2, NLRP10, CASP8, CHUK, IKBKB and BAX.1 Publication

Protein-protein interaction databases

DIPiDIP-27619N.
IntActiQ9EPB4. 3 interactions.
STRINGi10090.ENSMUSP00000033056.

Structurei

3D structure databases

ProteinModelPortaliQ9EPB4.
SMRiQ9EPB4. Positions 1-193.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9191DAPINPROSITE-ProRule annotationAdd
BLAST
Domaini105 – 19389CARDPROSITE-ProRule annotationAdd
BLAST

Domaini

The DAPIN domain mediates homotypic interactions with DAPIN domains of proteins such as of NLRP3, PYDC1 and AIM2.By similarity
The CARD domain mediates interaction with CASP1 and NLRC4.By similarity

Sequence similaritiesi

Contains 1 CARD domain.PROSITE-ProRule annotation
Contains 1 DAPIN domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG39139.
GeneTreeiENSGT00440000033973.
HOGENOMiHOG000034090.
HOVERGENiHBG018739.
InParanoidiQ9EPB4.
KOiK12799.
OMAiMGCTRDA.
OrthoDBiEOG786H4P.
PhylomeDBiQ9EPB4.
TreeFamiTF337882.

Family and domain databases

Gene3Di1.10.533.10. 2 hits.
InterProiIPR001315. CARD.
IPR004020. DAPIN.
IPR011029. DEATH-like_dom.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
PF02758. PYRIN. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 2 hits.
PROSITEiPS50209. CARD. 1 hit.
PS50824. DAPIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9EPB4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGRARDAILD ALENLSGDEL KKFKMKLLTV QLREGYGRIP RGALLQMDAI
60 70 80 90 100
DLTDKLVSYY LESYGLELTM TVLRDMGLQE LAEQLQTTKE ESGAVAAAAS
110 120 130 140 150
VPAQSTARTG HFVDQHRQAL IARVTEVDGV LDALHGSVLT EGQYQAVRAE
160 170 180 190
TTSQDKMRKL FSFVPSWNLT CKDSLLQALK EIHPYLVMDL EQS
Length:193
Mass (Da):21,459
Last modified:March 1, 2001 - v1
Checksum:i2A4EA40194870B31
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti159 – 1591K → E in BAB31341. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032249 mRNA. Translation: BAB16609.1.
AF310104 mRNA. Translation: AAG30287.1.
AK009852 mRNA. Translation: BAB26543.1.
AK007742 mRNA. Translation: BAB25229.1.
AK018682 mRNA. Translation: BAB31341.1.
BC008252 mRNA. Translation: AAH08252.1.
CCDSiCCDS21888.1.
RefSeqiNP_075747.3. NM_023258.4.
UniGeneiMm.24163.

Genome annotation databases

EnsembliENSMUST00000033056; ENSMUSP00000033056; ENSMUSG00000030793.
GeneIDi66824.
KEGGimmu:66824.
UCSCiuc009jxu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB032249 mRNA. Translation: BAB16609.1.
AF310104 mRNA. Translation: AAG30287.1.
AK009852 mRNA. Translation: BAB26543.1.
AK007742 mRNA. Translation: BAB25229.1.
AK018682 mRNA. Translation: BAB31341.1.
BC008252 mRNA. Translation: AAH08252.1.
CCDSiCCDS21888.1.
RefSeqiNP_075747.3. NM_023258.4.
UniGeneiMm.24163.

3D structure databases

ProteinModelPortaliQ9EPB4.
SMRiQ9EPB4. Positions 1-193.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-27619N.
IntActiQ9EPB4. 3 interactions.
STRINGi10090.ENSMUSP00000033056.

PTM databases

PhosphoSiteiQ9EPB4.

Proteomic databases

MaxQBiQ9EPB4.
PaxDbiQ9EPB4.
PRIDEiQ9EPB4.

Protocols and materials databases

DNASUi66824.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033056; ENSMUSP00000033056; ENSMUSG00000030793.
GeneIDi66824.
KEGGimmu:66824.
UCSCiuc009jxu.2. mouse.

Organism-specific databases

CTDi29108.
MGIiMGI:1931465. Pycard.

Phylogenomic databases

eggNOGiNOG39139.
GeneTreeiENSGT00440000033973.
HOGENOMiHOG000034090.
HOVERGENiHBG018739.
InParanoidiQ9EPB4.
KOiK12799.
OMAiMGCTRDA.
OrthoDBiEOG786H4P.
PhylomeDBiQ9EPB4.
TreeFamiTF337882.

Enzyme and pathway databases

ReactomeiREACT_198644. The NLRP3 inflammasome.
REACT_198662. The AIM2 inflammasome.

Miscellaneous databases

NextBioi322743.
PROiQ9EPB4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EPB4.
CleanExiMM_PYCARD.
ExpressionAtlasiQ9EPB4. baseline and differential.
GenevestigatoriQ9EPB4.

Family and domain databases

Gene3Di1.10.533.10. 2 hits.
InterProiIPR001315. CARD.
IPR004020. DAPIN.
IPR011029. DEATH-like_dom.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
PF02758. PYRIN. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 2 hits.
PROSITEiPS50209. CARD. 1 hit.
PS50824. DAPIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Murine ortholog of ASC, a CARD-containing protein, self-associates and exhibits restricted distribution in developing mouse embryos."
    Masumoto J., Taniguchi S., Nakayama K., Ayukawa K., Sagara J.
    Exp. Cell Res. 262:128-133(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Thymus.
  2. "Pycard a PYD and CARD containing molecule."
    Martinon F., Hofmann K., Tschopp J.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Pancreas and Tongue.
  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. "ASC is essential for LPS-induced activation of procaspase-1 independently of TLR-associated signal adaptor molecules."
    Yamamoto M., Yaginuma K., Tsutsui H., Sagara J., Guan X., Seki E., Yasuda K., Yamamoto M., Akira S., Nakanishi K., Noda T., Taniguchi S.
    Genes Cells 9:1055-1067(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "Differential activation of the inflammasome by caspase-1 adaptors ASC and Ipaf."
    Mariathasan S., Newton K., Monack D.M., Vucic D., French D.M., Lee W.P., Roose-Girma M., Erickson S., Dixit V.M.
    Nature 430:213-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  7. "The inflammasome adaptor ASC regulates the function of adaptive immune cells by controlling Dock2-mediated Rac activation and actin polymerization."
    Ippagunta S.K., Malireddi R.K., Shaw P.J., Neale G.A., Walle L.V., Green D.R., Fukui Y., Lamkanfi M., Kanneganti T.D.
    Nat. Immunol. 12:1010-1016(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "AIM2/ASC triggers caspase-8-dependent apoptosis in Francisella-infected caspase-1-deficient macrophages."
    Pierini R., Juruj C., Perret M., Jones C.L., Mangeot P., Weiss D.S., Henry T.
    Cell Death Differ. 19:1709-1721(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CASP8.

Entry informationi

Entry nameiASC_MOUSE
AccessioniPrimary (citable) accession number: Q9EPB4
Secondary accession number(s): Q9D2W9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: March 1, 2001
Last modified: February 4, 2015
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.