UAS family, ETEA subfamily; composed of proteins similar to human ETEA protein, the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. ETEA shows homology to Fas-associated factor 1 (FAF1); both containing UAS and UBX (ubiquitin-associated) domains. Compared to FAF1, however, ETEA lacks the ubiquitin-associated UBA domain and a nuclear targeting domain. The function of ETEA is still unknown. A yeast two-hybrid assay showed that it can interact with Fas. Because of its homology to FAF1, it is postulated that ETEA could be involved in modulating Fas-mediated apoptosis of T-cells and eosinophils of atopic dermatitis patients, making them more resistant to apoptosis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158533976 154 FYQGTYSQALNDAKRELRFLLVYLHGDDHQDSDEFCRNALCAPEVISLINSRMLFWACSTNKPEGYRVSQALRENTYPFL 233
Cdd:cd02991    1 FYQGTYSQALNDAKQELRFLLVYLHGDDHQDTDEFCRNTLCAPEVIEYINTRMLFWACSVAKPEGYRVSQALRERTYPFL 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 158533976 234 AMIMLKDRRMTVVGRLEGLIQPDDLINQLTFIMDAN 269
Cdd:cd02991   81 AMIMLKDNRMTIVGRLEGLIQPEDLINRLTFIMDAN 116

UBA-like TAP-C domain found in FAS-associated factor 2 (FAF2) and similar proteins; FAF2, also called protein ETEA, UBX domain-containing protein 3B, or UBX domain-containing protein 8, is the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. FAF2 shows homology to Fas-associated factor 1 (FAF1). Both of them contain N-terminal ubiquitin-associated (UBA)-like domain, UAS and ubiquitin-like (UBX) domains. Compared to FAF1, however, FAF2 lacks the nuclear targeting domain. The function of FAF2 remains unclear. A yeast two-hybrid assay showed that it can interact with Fas. Because of its homology to FAF1, it is postulated that FAF2 could be involved in modulating Fas-mediated apoptosis of T-cells and eosinophils of atopic dermatitis patients, making them more resistant to apoptosis.

                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 158533976  15 EKLLQFQDLTGIESMEQCRLALEQHNWNMEAAVQDRLN 52
Cdd:cd14414    1 EKLLQFQDLTGIEDMDQCREVLERHNWDIEAAVQDRLN 38

UAS family, ETEA subfamily; composed of proteins similar to human ETEA protein, the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. ETEA shows homology to Fas-associated factor 1 (FAF1); both containing UAS and UBX (ubiquitin-associated) domains. Compared to FAF1, however, ETEA lacks the ubiquitin-associated UBA domain and a nuclear targeting domain. The function of ETEA is still unknown. A yeast two-hybrid assay showed that it can interact with Fas. Because of its homology to FAF1, it is postulated that ETEA could be involved in modulating Fas-mediated apoptosis of T-cells and eosinophils of atopic dermatitis patients, making them more resistant to apoptosis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158533976 154 FYQGTYSQALNDAKRELRFLLVYLHGDDHQDSDEFCRNALCAPEVISLINSRMLFWACSTNKPEGYRVSQALRENTYPFL 233
Cdd:cd02991    1 FYQGTYSQALNDAKQELRFLLVYLHGDDHQDTDEFCRNTLCAPEVIEYINTRMLFWACSVAKPEGYRVSQALRERTYPFL 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 158533976 234 AMIMLKDRRMTVVGRLEGLIQPDDLINQLTFIMDAN 269
Cdd:cd02991   81 AMIMLKDNRMTIVGRLEGLIQPEDLINRLTFIMDAN 116

UAS domain;

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158533976   141 HSFEEKYGrahPVFYQGTYSQALNDAKRELRFLLVYLHGDDHQDSDEFCRNALCAPEVISLINSRMLFWACSTNKPEGYR 220
Cdd:smart00594   1 KLFRPPYG---PLFYQGSLEAAKQEASRQRRLLWLYLHSQDSPDSQVFNRDVLCNEAVKSLIRENFIFWQVDVDTSEGQR 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 158533976   221 VSQALRENTYPFLAMIMLKD--RRMTVVGRLEGLIQPDDLINQLT 263
Cdd:smart00594  78 VSQFYKLDSFPYVAIVDPRTgqRVIEWVGVVEGEISPEELMTFLE 122

UBA-like domain;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 158533976   15 EKLLQFQDLTGIeSMEQCRLALEQHNWNMEAAVQDRLNEQEG 56
Cdd:pfam14555   2 ELIAQFQAITGA-DEEVARQYLEAHNWDLEAAVNAFFDDGEA 42

UAS family, ETEA subfamily; composed of proteins similar to human ETEA protein, the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. ETEA shows homology to Fas-associated factor 1 (FAF1); both containing UAS and UBX (ubiquitin-associated) domains. Compared to FAF1, however, ETEA lacks the ubiquitin-associated UBA domain and a nuclear targeting domain. The function of ETEA is still unknown. A yeast two-hybrid assay showed that it can interact with Fas. Because of its homology to FAF1, it is postulated that ETEA could be involved in modulating Fas-mediated apoptosis of T-cells and eosinophils of atopic dermatitis patients, making them more resistant to apoptosis.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158533976 154 FYQGTYSQALNDAKRELRFLLVYLHGDDHQDSDEFCRNALCAPEVISLINSRMLFWACSTNKPEGYRVSQALRENTYPFL 233
Cdd:cd02991    1 FYQGTYSQALNDAKQELRFLLVYLHGDDHQDTDEFCRNTLCAPEVIEYINTRMLFWACSVAKPEGYRVSQALRERTYPFL 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 158533976 234 AMIMLKDRRMTVVGRLEGLIQPDDLINQLTFIMDAN 269
Cdd:cd02991   81 AMIMLKDNRMTIVGRLEGLIQPEDLINRLTFIMDAN 116

Ubiquitin regulatory domain X (UBX) found in FAS associated factor 2 (FAF2, also known as UBXN3B) and similar proteins; UBX domain-containing protein 3B (UBXN3B), also termed protein ETEA, or FAF2, or UBX domain-containing protein 8 (UBXD8), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. FAF2 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. The p97-UBXD8 complex destabilizes mRNA by promoting release of ubiquitinated the RNA-binding protein HuR from messenger ribonucleoprotein (mRNP). Moreover, FAF2 is the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. A yeast two-hybrid assay showed that FAF2 can interact with Fas.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158533976 362 VKIIFKLPNDSRVERRFHFSQSLTVIHDFLFSLKESPEKFQIEANFPRRVLPCVPSEEWPNPPTLQEAGLSHTEVLFVQD 441
Cdd:cd16120    1 VKILFKLPNGTRLERRFLKSDSLKVLYDFVFSHEDSPDKFQLVTNFPRRVLPCQPTEEQPNPPTLEEAGLGKSEVLFVQD 80

UBA-like TAP-C domain found in FAS-associated factor 2 (FAF2) and similar proteins; FAF2, also called protein ETEA, UBX domain-containing protein 3B, or UBX domain-containing protein 8, is the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. FAF2 shows homology to Fas-associated factor 1 (FAF1). Both of them contain N-terminal ubiquitin-associated (UBA)-like domain, UAS and ubiquitin-like (UBX) domains. Compared to FAF1, however, FAF2 lacks the nuclear targeting domain. The function of FAF2 remains unclear. A yeast two-hybrid assay showed that it can interact with Fas. Because of its homology to FAF1, it is postulated that FAF2 could be involved in modulating Fas-mediated apoptosis of T-cells and eosinophils of atopic dermatitis patients, making them more resistant to apoptosis.

                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 158533976  15 EKLLQFQDLTGIESMEQCRLALEQHNWNMEAAVQDRLN 52
Cdd:cd14414    1 EKLLQFQDLTGIEDMDQCREVLERHNWDIEAAVQDRLN 38

UBA-like domain found in FAS-associated factor FAF1, FAF2 and similar proteins; FAF1, also called UBX domain-containing protein 12 or UBX domain-containing protein 3A, is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. FAF1 is widely expressed in adult and embryonic tissues, and in tumor cell lines, and is localized not only in the cytoplasm where it interacts with Fas, but also in the nucleus. FAF1 contains phosphorylation sites for protein kinase CK2 within the nuclear targeting domain. Phosphorylation influences nuclear localization of FAF1 but does not affect its potentiation of Fas-induced apoptosis. Other functions have also been attributed to FAF1. It inhibits nuclear factor-kappaB (NF-kappaB) by interfering with the nuclear translocation of the p65 subunit. Although the precise role of FAF1 in the ubiquitination pathway remains unclear, FAF1 interacts with valosin-containing protein (VCP) which is involved in the ubiquitin-proteosome pathway. FAF2, also called protein ETEA, UBX domain-containing protein 3B, or UBX domain-containing protein 8, is the translation product of a highly expressed gene in the T-cells and eosinophils of atopic dermatitis patients compared with those of normal individuals. FAF2 shows homology to Fas-associated factor 1 (FAF1). Both of them contain N-terminal ubiquitin-associated (UBA)-like domain, UAS and ubiquitin-like (UBX) domains. Compared to FAF1, however, FAF2 lacks the nuclear targeting domain. The function of FAF2 remains unclear. A yeast two-hybrid assay showed that it can interact with Fas. Because of its homology to FAF1, it is postulated that FAF2 could be involved in modulating Fas-mediated apoptosis of T-cells and eosinophils of atopic dermatitis patients, making them more resistant to apoptosis.

                         10        20        30
                 ....*....|....*....|....*....|..
gi 158533976  20 FQDLTGIESMEQCRLALEQHNWNMEAAVQDRL 51
Cdd:cd14353    1 FQSITGIEDSDQCRQILEAHNWDLEAAIQTAL 32

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 7 (UBXN7) and similar proteins; UBXN7, also termed UBX domain-containing protein 7 (UBXD7), belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN7 functions as a ubiquitin-binding adaptor that mediates the interaction between the AAA+ ATPase p97 (also known as VCP or Cdc48) and the transcription factor HIF1-alpha. It binds only to the active, NEDD8- or Rub1-modified form of cullins. In addition to having a UBX domain, UBXD7 contains a ubiquitin-associated (UBA), ubiquitin-associating (UAS), and ubiquitin-interacting motif (UIM) domains. Either UBA or UIM could serve as a docking site for neddylated-cullins. UBA domain is required for binding ubiquitylated-protein substrates, while the UIM motif is responsible for the binding to cullin RING ligases (CRLs), and the UBX domain is essential for p97 binding.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158533976 363 KIIFKLPNDSRVERRFHFSQSLTVIHDFLFSLKESPEKFQIEANFPRRVLPCVPSEEwpnppTLQEAGLSHTEVLFVQD 441
Cdd:cd01773    3 KLMLRFPDGKREQLSLPASAKLKALVKYVSSKGYPNERYELVTNFPRRKLSHLDYDI-----TLKEAGLCPQETIFVQE 76

UAS family, FAS-associated factor 1 (FAF1) subfamily; FAF1 contains a UAS domain of unknown function N-terminal to a ubiquitin-associated UBX domain. FAF1 also contains ubiquitin-associated UBA and nuclear targeting domains, N-terminal to the UAS domain. FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. It is widely expressed in adult and embryonic tissues, and in tumor cell lines, and is localized not only in the cytoplasm where it interacts with Fas, but also in the nucleus. FAF1 contains phosphorylation sites for protein kinase CK2 within the nuclear targeting domain. Phosphorylation influences nuclear localization of FAF1 but does not affect its potentiation of Fas-induced apoptosis. Other functions have also been attributed to FAF1. It inhibits nuclear factor-kB (NF-kB) by interfering with the nuclear translocation of the p65 subunit. FAF1 also interacts with valosin-containing protein (VCP), which is involved in the ubiquitin-proteosome pathway.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158533976 154 FYQGTYSQALNDA----KRELRFLLVYLHGDDHQDSDEFCRNALCAPEVISLINSRMLFWA-------------CSTNKP 216
Cdd:cd02990    1 FFIGSLEAAFQEAcyrkARDRKLLAIYLHHDESVLSNVFCSQLLCAESIVQYLSQNFITWGwdmtkesnkarflSSCTRH 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 158533976 217 EGYRVSQALRE---NTYPFLAMIMLKDRRMTVVGRLEGLIQPDDLINQLTFIMD 267
Cdd:cd02990   81 FGSVAAQTIRNiktDQLPAILIIMGKRSSNEVLNVIQGNTGVDELLMRLIEAME 134

UBA-like domain found in FAS-associated factor 1 (FAF1) and similar proteins; FAF1, also called UBX domain-containing protein 12 or UBX domain-containing protein 3A, is a multi-functional Fas associating protein that contains an N-terminal ubiquitin-associated (UBA)-like domain, UAS and ubiquitin-like (UBX) domains, p150 subunit of a chromatin assembly factor like domain (CAF) and a novel nuclear localization signal (NLS). FAF1 is an apoptotic signaling molecule that acts downstream in the Fas signal transduction pathway. It interacts with the cytoplasmic domain of Fas, but not to a Fas mutant that is deficient in signal transduction. FAF1 is widely expressed in adult and embryonic tissues, and in tumor cell lines, and is localized not only in the cytoplasm where it interacts with Fas, but also in the nucleus. FAF1 contains phosphorylation sites for protein kinase CK2 within the nuclear targeting domain. Phosphorylation influences nuclear localization of FAF1 but does not affect its potentiation of Fas-induced apoptosis. Other functions have also been attributed to FAF1. It inhibits nuclear factor-kappaB (NF-kappaB) by interfering with the nuclear translocation of the p65 subunit. Although the precise role of FAF1 in the ubiquitination pathway remains unclear, FAF1 interacts with valosin-containing protein (VCP) which is involved in the ubiquitin-proteosome pathway.

                         10        20
                 ....*....|....*....|....*....
gi 158533976  20 FQDLTGIESMEQCRLALEQHNWNMEAAVQ 48
Cdd:cd14413    1 FQACTGIEDIDECIMLLEQNNWNLVAAVN 29

UBX domain; This domain is present in ubiquitin-regulatory proteins and is a general Cdc48-interacting module.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158533976  362 VKIIFKLPNDSRVERRFHFSQSLTVIHDFLFS-LKESPEKFQIEANFPRRVLpcvpSEEWPNpPTLQEAGLSHTEVLFVQ 440
Cdd:pfam00789   5 TRLQIRLPDGSRLVRRFNSSDKLQTVYDFVDSnRYDDLEPFSLNTPFPRRPL----TDLDYS-KTLKEAGLLPNSTLVLE 79

UBA domain-like superfamily; The ubiquitin-associated (UBA) domain-like superfamily contains alpha-helical structural homology ubiquitin-binding domains, including UBA domains and coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domains which share a common three-helical bundle architecture. UBA domains are commonly occurring sequence motifs found in proteins involved in ubiquitin-mediated proteolysis. They contribute to ubiquitin (Ub) binding or ubiquitin-like (UbL) domain binding. However, some kinds of UBA domains can only bind the UbL domain, but not the Ub domain. UBA domains are normally comprised of compact three-helix bundles which contain a conserved GF/Y-loop. They can bind polyubiquitin with high affinity. They also bind monoubiquitin and other proteins. Most UBA domain-containing proteins have one UBA domain, but some harbor two or three UBA domains. CUE domain containing proteins are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. This superfamily also includes many UBA-like domains found in AMP-activated protein kinase (AMPK) related kinases, the NXF family of mRNA nuclear export factors, elongation factor Ts (EF-Ts), nascent polypeptide-associated complex subunit alpha (NACA) and similar proteins. Although many UBA-like domains may have a conserved TG but not GF/Y-loop, they still show a high level of structural and sequence similarity with three-helical ubiquitin binding domains.

                         10        20
                 ....*....|....*....|....*....
gi 158533976  20 FQDLTGIESmEQCRLALEQHNWNMEAAVQ 48
Cdd:cd00194    1 LVDITGASQ-EEAQQALEACGGNLNIAAN 28