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Q14790 (CASP8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 180. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Caspase-8

Short name=CASP-8
EC=3.4.22.61
Alternative name(s):
Apoptotic cysteine protease
Apoptotic protease Mch-5
CAP4
FADD-homologous ICE/ced-3-like protease
FADD-like ICE
Short name=FLICE
ICE-like apoptotic protease 5
MORT1-associated ced-3 homolog
Short name=MACH

Cleaved into the following 2 chains:

  1. Caspase-8 subunit p18
  2. Caspase-8 subunit p10
Gene names
Name:CASP8
Synonyms:MCH5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex. Ref.7 Ref.13 Ref.26

Catalytic activity

Strict requirement for Asp at position P1 and has a preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-(Gly/Ser/Ala). Ref.26

Enzyme regulation

Probably negatively regulated by RFFL through proteasomal degradation. Inhibited by the effector protein NleF that is produced by pathogenic E.coli; this inhibits apoptosis. Ref.26

Subunit structure

Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 18 kDa (p18) and a 10 kDa (p10) subunit. Interacts with FADD, CFLAR and PEA15. Isoform 9 interacts at the endoplasmic reticulum with a complex containing BCAP31, BAP29, BCL2 and/or BCL2L1. Interacts with TNFAIP8L2 By similarity. Interacts with CASP8AP2. Interacts with RFFL. Interacts with human cytomegalovirus/HHV-5 protein vICA/UL36; this interaction inhibits CASP8 activation. Interacts with NleF from pathogenic E.coli. Ref.8 Ref.16 Ref.17 Ref.18 Ref.20 Ref.23 Ref.26 Ref.28

Subcellular location

Cytoplasm.

Tissue specificity

Isoform 1, isoform 5 and isoform 7 are expressed in a wide variety of tissues. Highest expression in peripheral blood leukocytes, spleen, thymus and liver. Barely detectable in brain, testis and skeletal muscle.

Domain

Isoform 9 contains a N-terminal extension that is required for interaction with the BCAP31 complex.

Post-translational modification

Generation of the subunits requires association with the death-inducing signaling complex (DISC), whereas additional processing is likely due to the autocatalytic activity of the activated protease. GZMB and CASP10 can be involved in these processing events.

Phosphorylation on Ser-387 during mitosis by CDK1 inhibits activation by proteolysis and prevents apoptosis. This phosphorylation occurs in cancer cell lines, as well as in primary breast tissues and lymphocytes.

Polymorphism

Genetic variations in CASP8 are associated with reduced risk of lung cancer [MIM:211980] in a population of Han Chinese subjects. Genetic variations are also associated with decreased risk of cancer of various other forms including esophageal, gastric, colorectal, cervical, and breast, acting in an allele dose-dependent manner.

Involvement in disease

Caspase-8 deficiency (CASP8D) [MIM:607271]: Disorder resembling autoimmune lymphoproliferative syndrome (ALPS). It is characterized by lymphadenopathy, splenomegaly, and defective CD95-induced apoptosis of peripheral blood lymphocytes (PBLs). It leads to defects in activation of T-lymphocytes, B-lymphocytes, and natural killer cells leading to immunodeficiency characterized by recurrent sinopulmonary and herpes simplex virus infections and poor responses to immunization.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.29

Sequence similarities

Belongs to the peptidase C14A family.

Contains 2 DED (death effector) domains.

Sequence caution

The sequence CAA66858.1 differs from that shown. Reason:

The sequence CAA66859.1 differs from that shown. Reason:

Ontologies

Keywords
   Biological processApoptosis
Host-virus interaction
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
   Molecular functionHydrolase
Protease
Thiol protease
   PTMAcetylation
Phosphoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processB cell activation

Traceable author statement PubMed 18309324. Source: UniProtKB

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

T cell activation

Traceable author statement PubMed 18309324. Source: UniProtKB

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

activation of cysteine-type endopeptidase activity

Inferred from direct assay PubMed 18387192. Source: BHF-UCL

activation of cysteine-type endopeptidase activity involved in apoptotic process

Traceable author statement. Source: Reactome

angiogenesis

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from mutant phenotype PubMed 22891283. Source: UniProtKB

apoptotic signaling pathway

Inferred from mutant phenotype PubMed 11101870. Source: BHF-UCL

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

cellular response to mechanical stimulus

Inferred from expression pattern PubMed 19593445. Source: UniProtKB

cellular response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

execution phase of apoptosis

Inferred from mutant phenotype PubMed 21737330. Source: UniProtKB

extrinsic apoptotic signaling pathway

Inferred from direct assay PubMed 21785459. Source: UniProtKB

extrinsic apoptotic signaling pathway via death domain receptors

Inferred from Biological aspect of Ancestor. Source: RefGenome

heart development

Inferred from electronic annotation. Source: Ensembl

hepatocyte apoptotic process

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway

Traceable author statement. Source: Reactome

macrophage differentiation

Traceable author statement PubMed 18309324. Source: UniProtKB

natural killer cell activation

Traceable author statement PubMed 18309324. Source: UniProtKB

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 17047155. Source: UniProtKB

neural tube formation

Inferred from electronic annotation. Source: Ensembl

nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway

Traceable author statement. Source: Reactome

nucleotide-binding oligomerization domain containing signaling pathway

Traceable author statement. Source: Reactome

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 12884866. Source: UniProtKB

positive regulation of extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of macrophage differentiation

Inferred from mutant phenotype PubMed 17047155. Source: UniProtKB

positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway

Traceable author statement. Source: Reactome

positive regulation of proteolysis

Inferred from direct assay PubMed 18387192. Source: BHF-UCL

protein heterooligomerization

Inferred from electronic annotation. Source: Ensembl

proteolysis

Inferred from direct assay PubMed 12888622. Source: UniProtKB

proteolysis involved in cellular protein catabolic process

Inferred from mutant phenotype PubMed 10521396. Source: BHF-UCL

regulation of extrinsic apoptotic signaling pathway in absence of ligand

Traceable author statement. Source: Reactome

regulation of thymocyte apoptotic process

Inferred from electronic annotation. Source: Ensembl

response to antibiotic

Inferred from electronic annotation. Source: Ensembl

response to cobalt ion

Inferred from electronic annotation. Source: Ensembl

response to cold

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to tumor necrosis factor

Inferred from mutant phenotype PubMed 10521396. Source: BHF-UCL

syncytiotrophoblast cell differentiation involved in labyrinthine layer development

Traceable author statement PubMed 18309324. Source: UniProtKB

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCD95 death-inducing signaling complex

Inferred from direct assay PubMed 11717445. Source: UniProtKB

Noc1p-Noc2p complex

Inferred from electronic annotation. Source: Ensembl

cell body

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

cytoskeleton

Traceable author statement PubMed 10891503. Source: ProtInc

cytosol

Inferred from direct assay PubMed 17167422. Source: UniProtKB

death-inducing signaling complex

Inferred from direct assay PubMed 21803845. Source: UniProtKB

membrane raft

Inferred from electronic annotation. Source: Ensembl

microtubule organizing center

Inferred from direct assay. Source: HPA

mitochondrial outer membrane

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay. Source: HPA

neuron projection

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay. Source: HPA

ripoptosome

Inferred from direct assay PubMed 21737330. Source: UniProtKB

   Molecular_functioncysteine-type endopeptidase activity

Inferred from direct assay PubMed 19240112. Source: UniProtKB

cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 21737330. Source: UniProtKB

cysteine-type endopeptidase activity involved in apoptotic signaling pathway

Inferred from mutant phenotype PubMed 11717445. Source: UniProtKB

cysteine-type peptidase activity

Traceable author statement Ref.1. Source: ProtInc

death effector domain binding

Inferred from physical interaction PubMed 11717445. Source: UniProtKB

peptidase activity

Inferred from mutant phenotype PubMed 17047155. Source: UniProtKB

protease binding

Inferred from physical interaction. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.1. Source: IntAct

ubiquitin protein ligase binding

Inferred from physical interaction Ref.20. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14790-1)

Also known as: Alpha-1;

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.
Isoform 2 (identifier: Q14790-2)

Also known as: Alpha-2; MCH5-beta;

The sequence of this isoform differs from the canonical sequence as follows:
     184-198: Missing.
Isoform 3 (identifier: Q14790-3)

Also known as: Alpha-3;

The sequence of this isoform differs from the canonical sequence as follows:
     184-267: Missing.
Isoform 4 (identifier: Q14790-4)

Also known as: Alpha-4;

The sequence of this isoform differs from the canonical sequence as follows:
     102-102: R → RFHFCRMSWAEANSQCQTQSVPFWRRVDHLLIR
     184-198: Missing.
Isoform 5 (identifier: Q14790-5)

Also known as: Beta-1;

The sequence of this isoform differs from the canonical sequence as follows:
     199-235: GEELCGVMTISDSPREQDSESQTLDKVYQMKSKPRGY → DFGQSLPNEKQTSGILSDHQQSQFCKSTGESAQTSQH
     236-479: Missing.
Isoform 6 (identifier: Q14790-6)

Also known as: Beta-2;

The sequence of this isoform differs from the canonical sequence as follows:
     184-220: ERSSSLEGSPDEFSNGEELCGVMTISDSPREQDSESQ → DFGQSLPNEKQTSGILSDHQQSQFCKSTGESAQTSQH
     221-479: Missing.
Isoform 7 (identifier: Q14790-7)

Also known as: Beta-3; 8L;

The sequence of this isoform differs from the canonical sequence as follows:
     269-276: ALTTTFEE → TVEPKREK
     277-479: Missing.
Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.
Isoform 8 (identifier: Q14790-8)

Also known as: Beta-4;

The sequence of this isoform differs from the canonical sequence as follows:
     184-198: Missing.
     269-276: ALTTTFEE → TVEPKREK
     277-479: Missing.
Isoform 9 (identifier: Q14790-9)

Also known as: 8L;

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEGGRRARVVIESKRNFFLGAFPTPFPAEHVELGRLGDSETAMVPGKGGADYILLPFKKM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 216216
PRO_0000004628
Chain217 – 374158Caspase-8 subunit p18
PRO_0000004629
Propeptide375 – 38410
PRO_0000004630
Chain385 – 47995Caspase-8 subunit p10
PRO_0000004631

Regions

Domain2 – 8079DED 1
Domain100 – 17778DED 2

Sites

Active site3171
Active site3601

Amino acid modifications

Modified residue1881Phosphoserine By similarity
Modified residue2111Phosphoserine By similarity
Modified residue2241N6-acetyllysine By similarity
Modified residue3341Phosphotyrosine Ref.21
Modified residue3871Phosphoserine; by CDK1 Ref.24

Natural variations

Alternative sequence11M → MEGGRRARVVIESKRNFFLG AFPTPFPAEHVELGRLGDSE TAMVPGKGGADYILLPFKKM in isoform 9.
VSP_000808
Alternative sequence1021R → RFHFCRMSWAEANSQCQTQS VPFWRRVDHLLIR in isoform 4.
VSP_000809
Alternative sequence184 – 26784Missing in isoform 3.
VSP_000813
Alternative sequence184 – 22037ERSSS…DSESQ → DFGQSLPNEKQTSGILSDHQ QSQFCKSTGESAQTSQH in isoform 6.
VSP_000811
Alternative sequence184 – 19815Missing in isoform 2, isoform 4 and isoform 8.
VSP_000810
Alternative sequence199 – 23537GEELC…KPRGY → DFGQSLPNEKQTSGILSDHQ QSQFCKSTGESAQTSQH in isoform 5.
VSP_000814
Alternative sequence221 – 479259Missing in isoform 6.
VSP_000812
Alternative sequence236 – 479244Missing in isoform 5.
VSP_000815
Alternative sequence269 – 2768ALTTTFEE → TVEPKREK in isoform 7 and isoform 8.
VSP_000816
Alternative sequence277 – 479203Missing in isoform 7 and isoform 8.
VSP_000817
Natural variant2191S → T. Ref.9
Corresponds to variant rs35976359 [ dbSNP | Ensembl ].
VAR_025816
Natural variant2481R → W in CASP8D. Ref.29
Corresponds to variant rs17860424 [ dbSNP | Ensembl ].
VAR_014204
Natural variant2851D → H Associated with protection against breast cancer; also associated with a lower risk of cutaneous melanoma. Ref.3 Ref.4 Ref.6 Ref.9 Ref.30 Ref.31 Ref.34
Corresponds to variant rs1045485 [ dbSNP | Ensembl ].
VAR_020127

Experimental info

Mutagenesis731D → A: Abolishes binding to FLASH. Induces NF-kappa-B activation. Ref.22
Mutagenesis3871S → A: Impaired CDK1-mediated phosphorylation and enhanced apoptosis.
Sequence conflict2941E → D in AAD24962. Ref.5
Sequence conflict3311A → P in AAC50602. Ref.2
Sequence conflict3311A → P in AAD24962. Ref.5
Sequence conflict343 – 3442LK → FG in AAL87631. Ref.8
Isoform 9:
Sequence conflict141K → R in AAL87628. Ref.8

Secondary structure

.......................................................... 479
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha-1) [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 7A5FEAA6B39B582F

FASTA47955,391
        10         20         30         40         50         60 
MDFSRNLYDI GEQLDSEDLA SLKFLSLDYI PQRKQEPIKD ALMLFQRLQE KRMLEESNLS 

        70         80         90        100        110        120 
FLKELLFRIN RLDLLITYLN TRKEEMEREL QTPGRAQISA YRVMLYQISE EVSRSELRSF 

       130        140        150        160        170        180 
KFLLQEEISK CKLDDDMNLL DIFIEMEKRV ILGEGKLDIL KRVCAQINKS LLKIINDYEE 

       190        200        210        220        230        240 
FSKERSSSLE GSPDEFSNGE ELCGVMTISD SPREQDSESQ TLDKVYQMKS KPRGYCLIIN 

       250        260        270        280        290        300 
NHNFAKAREK VPKLHSIRDR NGTHLDAGAL TTTFEELHFE IKPHDDCTVE QIYEILKIYQ 

       310        320        330        340        350        360 
LMDHSNMDCF ICCILSHGDK GIIYGTDGQE APIYELTSQF TGLKCPSLAG KPKVFFIQAC 

       370        380        390        400        410        420 
QGDNYQKGIP VETDSEEQPY LEMDLSSPQT RYIPDEADFL LGMATVNNCV SYRNPAEGTW 

       430        440        450        460        470 
YIQSLCQSLR ERCPRGDDIL TILTEVNYEV SNKDDKKNMG KQMPQPTFTL RKKLVFPSD 

« Hide

Isoform 2 (Alpha-2) (MCH5-beta) [UniParc].

Checksum: 7F52F14ADE6A02B6
Show »

FASTA46453,768
Isoform 3 (Alpha-3) [UniParc].

Checksum: 2787AE831A2B36EF
Show »

FASTA39545,929
Isoform 4 (Alpha-4) [UniParc].

Checksum: 68136650A49159D9
Show »

FASTA49657,701
Isoform 5 (Beta-1) [UniParc].

Checksum: 7C9013CEA85A77DE
Show »

FASTA23527,484
Isoform 6 (Beta-2) [UniParc].

Checksum: F3DA0380D12006C7
Show »

FASTA22025,862
Isoform 7 (Beta-3) (8L) [UniParc].

Checksum: 227ED77718788F92
Show »

FASTA27632,330
Isoform 8 (Beta-4) [UniParc].

Checksum: 19ACAE80171E0572
Show »

FASTA26130,707
Isoform 9 (8L) [UniParc].

Checksum: 54402ECFA9FE5E14
Show »

FASTA53861,836

References

« Hide 'large scale' references
[1]"Involvement of MACH, a novel MORT1/FADD-interacting protease, in Fas/APO-1- and TNF receptor-induced cell death."
Boldin M.P., Goncharov T.M., Goltsev Y.V., Wallach D.
Cell 85:803-815(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 5; 6; 7 AND 8).
Tissue: B-cell and Thymus.
[2]"FLICE, a novel FADD-homologous ICE/CED-3-like protease, is recruited to the CD95 (Fas/APO-1) death-inducing signaling complex."
Muzio M., Chinnaiyan A.M., Kischkel F.C., O'Rourke K., Shevchenko A., Ni J., Scaffidi C., Bretz J.D., Zhang M., Gentz R., Mann M., Krammer P.H., Peter M.E., Dixit V.M.
Cell 85:817-827(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[3]"In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains."
Fernandes-Alnemri T., Armstrong R.C., Krebs J.F., Srinivasula S.M., Wang L., Bullrich F., Fritz L.C., Trapani J.A., Tomaselli K.J., Litwack G., Alnemri E.S.
Proc. Natl. Acad. Sci. U.S.A. 93:7464-7469(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANT HIS-285.
Tissue: T-cell.
[4]"FLAME-1, a novel FADD-like anti-apoptotic molecule that regulates Fas/TNFR1-induced apoptosis."
Srinivasula S.M., Ahmad M., Ottilie S., Bullrich F., Banks S., Wang Y., Fernandes-Alnemri T., Croce C.M., Litwack G., Tomaselli K.J., Armstrong R.C., Alnemri E.S.
J. Biol. Chem. 272:18542-18545(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT HIS-285.
[5]"Structure and chromosome localization of the human CASP8 gene."
Grenet J., Teitz T., Wei T., Valentine V., Kidd V.J.
Gene 226:225-232(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Cloning and characterization of three novel genes, ALS2CR1, ALS2CR2, and ALS2CR3, in the juvenile amyotrophic lateral sclerosis (ALS2) critical region at chromosome 2q33-q34: candidate genes for ALS2."
Hadano S., Yanagisawa Y., Skaug J., Fichter K., Nasir J., Martindale D., Koop B.F., Scherer S.W., Nicholson D.W., Rouleau G.A., Ikeda J.-E., Hayden M.R.
Genomics 71:200-213(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-285.
[7]"Characterization of caspase-8L: a novel isoform of caspase-8 that behaves as an inhibitor of the caspase cascade."
Himeji D., Horiuchi T., Tsukamoto H., Hayashi K., Watanabe T., Harada M.
Blood 99:4070-4078(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), FUNCTION (ISOFORM 7).
Tissue: Leukocyte.
[8]"The procaspase-8 isoform, procaspase-8L, recruited to the BAP31 complex at the endoplasmic reticulum."
Breckenridge D.G., Nguyen M., Kuppig S., Reth M., Shore G.C.
Proc. Natl. Acad. Sci. U.S.A. 99:4331-4336(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 9), INTERACTION OF ISOFORM 9 WITH BCAP31 AT THE ENDOPLASMIC RETICULUM.
[9]NIEHS SNPs program
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-219 AND HIS-285.
[10]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
Tissue: Leukocyte.
[12]"Molecular ordering of the Fas-apoptotic pathway: the Fas/APO-1 protease Mch5 is a CrmA-inhibitable protease that activates multiple Ced-3/ICE-like cysteine proteases."
Srinivasula S.M., Ahmad M., Fernandes-Alnemri T., Litwack G., Alnemri E.S.
Proc. Natl. Acad. Sci. U.S.A. 93:14486-14491(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, PROTEOLYTIC PROCESSING.
[13]"FLICE induced apoptosis in a cell-free system. Cleavage of caspase zymogens."
Muzio M., Salvesen G.S., Dixit V.M.
J. Biol. Chem. 272:2952-2956(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"FLICE is activated by association with the CD95 death-inducing signaling complex (DISC)."
Medema J.P., Scaffidi C., Kischkel F.C., Shevchenko A., Mann M., Krammer P.H., Peter M.E.
EMBO J. 16:2794-2804(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[15]"Dominant expression of a novel splice variant of caspase-8 in human peripheral blood lymphocytes."
Horiuchi T., Himeji D., Tsukamoto H., Harashima S., Hashimura C., Hayashi K.
Biochem. Biophys. Res. Commun. 272:877-881(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION (ISOFORM 7).
[16]"p28 Bap31, a Bcl-2/Bcl-XL- and procaspase-8-associated protein in the endoplasmic reticulum."
Ng F.W.H., Nguyen M., Kwan T., Branton P.E., Nicholson D.W., Cromlish J.A., Shore G.C.
J. Cell Biol. 139:327-338(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BCL2; BCL2L1 AND BCAP31.
[17]"PED/PEA-15: an anti-apoptotic molecule that regulates FAS/TNFR1-induced apoptosis."
Condorelli G., Vigliotta G., Cafieri A., Trencia A., Andalo P., Oriente F., Miele C., Caruso M., Formisano P., Beguinot F.
Oncogene 18:4409-4415(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PEA15.
[18]"A cytomegalovirus-encoded inhibitor of apoptosis that suppresses caspase-8 activation."
Skaletskaya A., Bartle L.M., Chittenden T., McCormick A.L., Mocarski E.S., Goldmacher V.S.
Proc. Natl. Acad. Sci. U.S.A. 98:7829-7834(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HHV-5 PROTEIN UL36.
[19]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
[20]"Suppression of caspase-8- and -10-associated RING proteins results in sensitization to death ligands and inhibition of tumor cell growth."
McDonald E.R. III, El-Deiry W.S.
Proc. Natl. Acad. Sci. U.S.A. 101:6170-6175(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RFFL.
[21]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-334, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Role of FLASH in caspase-8-mediated activation of NF-kappaB: dominant-negative function of FLASH mutant in NF-kappaB signaling pathway."
Jun J.-I., Chung C.-W., Lee H.-J., Pyo J.-O., Lee K.N., Kim N.-S., Kim Y.S., Yoo H.-S., Lee T.-H., Kim E., Jung Y.-K.
Oncogene 24:688-696(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-73.
[23]"FLASH links the CD95 signaling pathway to the cell nucleus and nuclear bodies."
Milovic-Holm K., Krieghoff E., Jensen K., Will H., Hofmann T.G.
EMBO J. 26:391-401(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CASP8P2.
[24]"Cdk1/cyclin B1 controls Fas-mediated apoptosis by regulating caspase-8 activity."
Matthess Y., Raab M., Sanhaji M., Lavrik I.N., Strebhardt K.
Mol. Cell. Biol. 30:5726-5740(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-387 BY CDK1.
[25]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"The E.coli effector protein NleF is a caspase inhibitor."
Blasche S., Moertl M., Steuber H., Siszler G., Nisa S., Schwarz F., Lavrik I., Gronewold T.M.A., Maskos K., Donnenberg M.S., Ullmann D., Uetz P., Koegl M.
PLoS ONE 0:0-0(2013)
Cited for: INTERACTION WITH E.COLI NLEF, CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION.
[27]"The three-dimensional structure of caspase-8: an initiator enzyme in apoptosis."
Blanchard H., Kodandapani L., Mittl P.R.E., Di Marco S., Krebs J.F., Wu J.C., Tomaselli K.J., Gruetter M.G.
Structure 7:1125-1133(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[28]"The atomic-resolution structure of human caspase-8, a key activator of apoptosis."
Watt W., Koeplinger K.A., Mildner A.M., Heinrikson R.L., Tomasselli A.G., Watenpaugh K.D.
Structure 7:1135-1143(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 211-479, SUBUNIT.
[29]"Pleiotropic defects in lymphocyte activation caused by caspase-8 mutations lead to human immunodeficiency."
Chun H.J., Zheng L., Ahmad M., Wang J., Speirs C.K., Siegel R.M., Dale J.K., Puck J., Davis J., Hall C.G., Skoda-Smith S., Atkinson T.P., Straus S.E., Lenardo M.J.
Nature 419:395-399(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CASP8D TRP-248.
[30]"Association of a common variant of the CASP8 gene with reduced risk of breast cancer."
MacPherson G., Healey C.S., Teare M.D., Balasubramanian S.P., Reed M.W.R., Pharoah P.D., Ponder B.A.J., Meuth M., Bhattacharyya N.P., Cox A.
J. Natl. Cancer Inst. 96:1866-1869(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIS-285, PROTECTION AGAINST BREAST CANCER.
[31]"A common coding variant in CASP8 is associated with breast cancer risk."
The Kathleen Cunningham foundation consortium for research into familial breast cancer, Breast cancer association consortium
Cox A., Dunning A.M., Garcia-Closas M., Balasubramanian S., Reed M.W.R., Pooley K.A., Scollen S., Baynes C., Ponder B.A.J., Chanock S., Lissowska J., Brinton L., Peplonska B., Southey M.C., Hopper J.L., McCredie M.R.E., Giles G.G., Fletcher O. expand/collapse author list , Johnson N., dos Santos Silva I., Gibson L., Bojesen S.E., Nordestgaard B.G., Axelsson C.K., Torres D., Hamann U., Justenhoven C., Brauch H., Chang-Claude J., Kropp S., Risch A., Wang-Gohrke S., Schuermann P., Bogdanova N., Doerk T., Fagerholm R., Aaltonen K., Blomqvist C., Nevanlinna H., Seal S., Renwick A., Stratton M.R., Rahman N., Sangrajrang S., Hughes D., Odefrey F., Brennan P., Spurdle A.B., Chenevix-Trench G., Beesley J., Mannermaa A., Hartikainen J., Kataja V., Kosma V.M., Couch F.J., Olson J.E., Goode E.L., Broeks A., Schmidt M.K., Hogervorst F.B.L., Van't Veer L.J., Kang D., Yoo K.-Y., Noh D.-Y., Ahn S.-H., Wedren S., Hall P., Low Y.-L., Liu J., Milne R.L., Ribas G., Gonzalez-Neira A., Benitez J., Sigurdson A.J., Stredrick D.L., Alexander B.H., Struewing J.P., Pharoah P.D.P., Easton D.F.
Nat. Genet. 39:352-358(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIS-285, PROTECTION AGAINST BREAST CANCER.
[32]Erratum
The Kathleen Cunningham foundation consortium for research into familial breast cancer, Breast cancer association consortium
Cox A., Dunning A.M., Garcia-Closas M., Balasubramanian S., Reed M.W.R., Pooley K.A., Scollen S., Baynes C., Ponder B.A.J., Chanock S., Lissowska J., Brinton L., Peplonska B., Southey M.C., Hopper J.L., McCredie M.R.E., Giles G.G., Fletcher O. expand/collapse author list , Johnson N., dos Santos Silva I., Gibson L., Bojesen S.E., Nordestgaard B.G., Axelsson C.K., Torres D., Hamann U., Justenhoven C., Brauch H., Chang-Claude J., Kropp S., Risch A., Wang-Gohrke S., Schuermann P., Bogdanova N., Doerk T., Fagerholm R., Aaltonen K., Blomqvist C., Nevanlinna H., Seal S., Renwick A., Stratton M.R., Rahman N., Sangrajrang S., Hughes D., Odefrey F., Brennan P., Spurdle A.B., Chenevix-Trench G., Beesley J., Mannermaa A., Hartikainen J., Kataja V., Kosma V.M., Couch F.J., Olson J.E., Goode E.L., Broeks A., Schmidt M.K., Hogervorst F.B.L., Van't Veer L.J., Kang D., Yoo K.-Y., Noh D.-Y., Ahn S.-H., Wedren S., Hall P., Low Y.-L., Liu J., Milne R.L., Ribas G., Gonzalez-Neira A., Benitez J., Sigurdson A.J., Stredrick D.L., Alexander B.H., Struewing J.P., Pharoah P.D.P., Easton D.F.
Nat. Genet. 39:688-688(2007)
[33]"A six-nucleotide insertion-deletion polymorphism in the CASP8 promoter is associated with susceptibility to multiple cancers."
Sun T., Gao Y., Tan W., Ma S., Shi Y., Yao J., Guo Y., Yang M., Zhang X., Zhang Q., Zeng C., Lin D.
Nat. Genet. 39:605-613(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN PROTECTION AGAINST LUNG CANCER.
[34]"Genetic variants and haplotypes of the caspase-8 and caspase-10 genes contribute to susceptibility to cutaneous melanoma."
Li C., Zhao H., Hu Z., Liu Z., Wang L.-E., Gershenwald J.E., Prieto V.G., Lee J.E., Duvic M., Grimm E.A., Wei Q.
Hum. Mutat. 29:1443-1451(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIS-285, RISK FACTOR FOR CUTANEOUS MELANOMA.
+Additional computationally mapped references.

Web resources

CASP8base

CASP8 mutation db

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98172 mRNA. Translation: CAA66853.1.
X98173 mRNA. Translation: CAA66854.1.
X98174 mRNA. Translation: CAA66855.1.
X98175 mRNA. Translation: CAA66856.1.
X98176 mRNA. Translation: CAA66857.1.
X98177 mRNA. Translation: CAA66858.1. Sequence problems.
X98178 mRNA. Translation: CAA66859.1. Sequence problems.
U58143 mRNA. Translation: AAC50602.1.
U60520 mRNA. Translation: AAC50645.1.
AF009620 mRNA. Translation: AAB70913.1.
AF102146 expand/collapse EMBL AC list , AF102139, AF102140, AF102141, AF102142, AF102143, AF102144, AF102145 Genomic DNA. Translation: AAD24962.1.
AB038985 Genomic DNA. Translation: BAB32555.1.
AF380342 mRNA. Translation: AAK57437.1.
AF422925 mRNA. Translation: AAL87628.1.
AF422926 mRNA. Translation: AAL87629.1.
AF422927 mRNA. Translation: AAL87630.1.
AF422928 mRNA. Translation: AAL87631.1.
AF422929 mRNA. Translation: AAL87632.1.
DQ355026 Genomic DNA. Translation: ABC67468.1.
AC007256 Genomic DNA. Translation: AAY24225.1.
BC028223 mRNA. No translation available.
CCDSCCDS2342.1. [Q14790-1]
CCDS2343.1. [Q14790-2]
CCDS2345.1. [Q14790-5]
CCDS42798.1. [Q14790-9]
CCDS42799.1. [Q14790-4]
RefSeqNP_001073593.1. NM_001080124.1. [Q14790-2]
NP_001073594.1. NM_001080125.1. [Q14790-9]
NP_001219.2. NM_001228.4. [Q14790-4]
NP_203519.1. NM_033355.3. [Q14790-1]
NP_203520.1. NM_033356.3. [Q14790-2]
NP_203522.1. NM_033358.3. [Q14790-5]
XP_005246943.1. XM_005246886.1. [Q14790-1]
XP_005246944.1. XM_005246887.1. [Q14790-1]
XP_005246945.1. XM_005246888.1. [Q14790-1]
XP_005246946.1. XM_005246889.1. [Q14790-1]
XP_005246947.1. XM_005246890.1. [Q14790-1]
XP_005246948.1. XM_005246891.2. [Q14790-1]
XP_005246949.1. XM_005246892.1. [Q14790-2]
XP_006712852.1. XM_006712789.1. [Q14790-1]
XP_006712853.1. XM_006712790.1. [Q14790-1]
XP_006712856.1. XM_006712793.1. [Q14790-5]
UniGeneHs.599762.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F9EX-ray2.90A/C/E/G/I/K222-374[»]
B/D/F/H/J/L390-478[»]
1I4EX-ray3.00B222-479[»]
1QDUX-ray2.80A/C/E/G/I/K222-374[»]
B/D/F/H/J/L390-477[»]
1QTNX-ray1.20A211-374[»]
B385-479[»]
2C2ZX-ray1.95A218-374[»]
B376-479[»]
2FUNX-ray3.00B/D222-479[»]
2K7ZNMR-A217-479[»]
2Y1LX-ray1.80A/C218-374[»]
B/D376-479[»]
3H11X-ray1.90B217-479[»]
3KJNX-ray1.80A211-374[»]
B385-479[»]
3KJQX-ray1.80A211-374[»]
B385-479[»]
4JJ7X-ray1.18A217-479[»]
ProteinModelPortalQ14790.
SMRQ14790. Positions 223-479.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107291. 91 interactions.
DIPDIP-30915N.
IntActQ14790. 67 interactions.
MINTMINT-91645.

Chemistry

BindingDBQ14790.
ChEMBLCHEMBL3776.
GuidetoPHARMACOLOGY1624.

Protein family/group databases

MEROPSC14.009.

PTM databases

PhosphoSiteQ14790.

Polymorphism databases

DMDM2493531.

Proteomic databases

MaxQBQ14790.
PaxDbQ14790.
PRIDEQ14790.

Protocols and materials databases

DNASU841.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264274; ENSP00000264274; ENSG00000064012. [Q14790-3]
ENST00000264275; ENSP00000264275; ENSG00000064012. [Q14790-4]
ENST00000323492; ENSP00000325722; ENSG00000064012. [Q14790-2]
ENST00000358485; ENSP00000351273; ENSG00000064012. [Q14790-9]
ENST00000392258; ENSP00000376087; ENSG00000064012. [Q14790-5]
ENST00000392259; ENSP00000376088; ENSG00000064012. [Q14790-5]
ENST00000392263; ENSP00000376091; ENSG00000064012. [Q14790-2]
ENST00000392266; ENSP00000376094; ENSG00000064012. [Q14790-6]
ENST00000432109; ENSP00000412523; ENSG00000064012. [Q14790-1]
GeneID841.
KEGGhsa:841.
UCSCuc002uxo.1. human. [Q14790-5]
uc002uxp.1. human. [Q14790-4]
uc002uxq.1. human. [Q14790-2]
uc002uxr.1. human. [Q14790-1]
uc002uxt.1. human. [Q14790-9]
uc002uxv.1. human. [Q14790-8]
uc010fte.1. human. [Q14790-6]
uc010ftf.2. human. [Q14790-3]

Organism-specific databases

CTD841.
GeneCardsGC02P202062.
HGNCHGNC:1509. CASP8.
HPACAB002047.
HPA001302.
HPA005688.
HPA006191.
MIM211980. phenotype.
601763. gene.
607271. phenotype.
neXtProtNX_Q14790.
Orphanet275517. Autoimmune lymphoproliferative syndrome with recurrent infections.
PharmGKBPA26092.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG303276.
HOVERGENHBG050803.
InParanoidQ14790.
KOK04398.
OMAIFIEMEK.
OrthoDBEOG7CRTQM.
PhylomeDBQ14790.
TreeFamTF102023.

Enzyme and pathway databases

BRENDA3.4.22.61. 2681.
ReactomeREACT_578. Apoptosis.
REACT_6900. Immune System.
SignaLinkQ14790.

Gene expression databases

ArrayExpressQ14790.
BgeeQ14790.
GenevestigatorQ14790.

Family and domain databases

Gene3D1.10.533.10. 2 hits.
3.40.50.1460. 1 hit.
InterProIPR029030. Caspase-like_dom.
IPR011029. DEATH-like_dom.
IPR001875. DED.
IPR011600. Pept_C14_caspase.
IPR001309. Pept_C14_ICE_p20.
IPR016129. Pept_C14_ICE_p20_AS.
IPR002138. Pept_C14_p10.
IPR015917. Pept_C14A_p45_core.
[Graphical view]
PfamPF01335. DED. 2 hits.
PF00656. Peptidase_C14. 1 hit.
[Graphical view]
PRINTSPR00376. IL1BCENZYME.
SMARTSM00115. CASc. 1 hit.
SM00031. DED. 2 hits.
[Graphical view]
SUPFAMSSF47986. SSF47986. 2 hits.
PROSITEPS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
PS50168. DED. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCASP8. human.
EvolutionaryTraceQ14790.
GeneWikiCaspase_8.
GenomeRNAi841.
NextBio3510.
PMAP-CutDBQ14790.
PROQ14790.
SOURCESearch...

Entry information

Entry nameCASP8_HUMAN
AccessionPrimary (citable) accession number: Q14790
Secondary accession number(s): O14676 expand/collapse secondary AC list , Q14791, Q14792, Q14793, Q14794, Q14795, Q14796, Q15780, Q15806, Q53TT5, Q8TDI1, Q8TDI2, Q8TDI3, Q8TDI4, Q8TDI5, Q96T22, Q9C0K4, Q9UQ81
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 180 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM