Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyTRAF domain-like8040736 3001027 SCOP2B (2022-06-29)
ASCOP2B SuperfamilyTrimerization domain of TRAF8039390 3001589 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyTRAF domain-like8040736 3001027 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyTrimerization domain of TRAF8039390 3001589 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyTRAF domain-like8040736 3001027 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyTrimerization domain of TRAF8039390 3001589 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AMATHe1czyA1 A: beta sandwichesX: Immunoglobulin-like beta-sandwichH: TRAF domain-like (From Topology)T: TRAF domain-likeF: MATHECOD (1.6)
BMATHe1czyB1 A: beta sandwichesX: Immunoglobulin-like beta-sandwichH: TRAF domain-like (From Topology)T: TRAF domain-likeF: MATHECOD (1.6)
CMATHe1czyC1 A: beta sandwichesX: Immunoglobulin-like beta-sandwichH: TRAF domain-like (From Topology)T: TRAF domain-likeF: MATHECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C
PF21355TRAF/meprin, MATH domain (TRAF-mep_MATH)TRAF/meprin, MATH domainIntracellular TRAFs and extracellular meprins share a conserved region of about 180 residues, the the meprin and TRAF homology (MATH) domain which adopts a beta-sandwich structure. This is the MATH domain of TNF receptor-associated factors (TRAFs) an ...Intracellular TRAFs and extracellular meprins share a conserved region of about 180 residues, the the meprin and TRAF homology (MATH) domain which adopts a beta-sandwich structure. This is the MATH domain of TNF receptor-associated factors (TRAFs) and meprins. In TRAFS, it is essential for self-association and receptor interaction [1-3]. Meprins are mammalian tissue-specific metalloendopeptidases involved developmental, normal and pathological processes.
Domain
D, E
PF05297Herpesvirus latent membrane protein 1 (LMP1) (Herpes_LMP1)Herpesvirus latent membrane protein 1 (LMP1)- Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B, C
TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED PROTEIN 2
D, E
LATENT MEMBRANE PROTEIN 1-

Pharos: Disease Associations Pharos Homepage Annotation

ChainsDrug Target  Associated Disease
A, B, C
PharosQ12933

Protein Modification Annotation

Modified Residue(s)
ChainResidue(s)Description
D, E
ACE RESIDAA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354

PSI-MOD :  N-acetyl-L-alanine MOD:00050 , N-acetyl-L-aspartic acid MOD:00051 , N-acetyl-L-cysteine MOD:00052 , N-acetyl-S-archeol-cysteine MOD:00897 , N-acetyl-L-glutamic acid MOD:00053 , N-acetyl-L-glutamine MOD:00054 , N-acetylglycine MOD:00055 , N-acetyl-L-methionine MOD:00058 , N-acetyl-L-proline MOD:00059 , N-acetyl-L-serine MOD:00060 , N,O-diacetylated L-serine MOD:00648 , N-acetyl-L-threonine MOD:00061 , N-acetyl-L-tyrosine MOD:00062 , N-acetyl-L-valine MOD:00063 , N2-acetyl-L-arginine MOD:00359