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1h8c

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1h8c, 20 NMR models ()

Structural annotation:
Resources:	CATH : 1H8Ca00 InterPro : Ipr001012, Ipr006577 Pfam : PF00789 SCOP : d1h8ca_ UniProt : Q9UNN5

Functional annotation:
Cellular component:	CD95 death-inducing signaling complex perinuclear region of cytoplasm cytosol nucleus
Biological process:	positive regulation of protein complex assembly regulation of protein catabolic process positive regulation of apoptosis apoptosis cell death proteasomal ubiquitin-dependent protein catabolic process cytoplasmic sequestering of NF-kappaB
Molecular function:	Hsp70/Hsc70 protein inhibitor activity protein binding heat shock protein binding protein kinase binding NF-kappaB binding protein kinase CK2 regulator activity

Evolutionary conservation:

Toggle Conservation Colors:	Rows = identical sequences:
Further Information:	Caveats, Explanation, Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

UBX DOMAIN FROM HUMAN FAF1

Publication Abstract from PubMed

The UBX domain is an 80 amino acid residue module that is present typically at the carboxyl terminus of a variety of eukaryotic proteins. In an effort to elucidate the function of UBX domains, we solved the three-dimensional structure of the UBX domain of human Fas-associated factor-1 (FAF1) by NMR spectroscopy. The structure has a beta-Grasp fold characterised by a beta-beta-alpha-beta-beta-alpha-beta secondary-structure organisation. The five beta strands are arranged into a mixed sheet in the order 21534. The longer first helix packs across the first three strands of the sheet, and a second shorter 3(10) helix is located in an extended loop connecting strands 4 and 5. In the absence of significant sequence similarity, the UBX domain can be superimposed with ubiquitin with an r.m.s.d. of 1.9 A, suggesting that the two structures share the same superfold, and an evolutionary relationship. However, the absence of a carboxyl-terminal extension containing a double glycine motif and of suitably positioned lysine side-chains makes it highly unlikely that UBX domains are either conjugated to other proteins or part of mixed UBX-ubiquitin chains. Database searches revealed that most UBX domain-containing proteins belong to one of four evolutionarily conserved families represented by the human FAF1, p47, Y33K, and Rep8 proteins. A role of the UBX domain in ubiquitin-related processes is suggested.

The UBX domain: a widespread ubiquitin-like module., Buchberger A, Howard MJ, Proctor M, Bycroft M, J Mol Biol. 2001 Mar 16;307(1):17-24. PMID:11243799

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1h8c is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Buchberger A, Howard MJ, Proctor M, Bycroft M. The UBX domain: a widespread ubiquitin-like module. J Mol Biol. 2001 Mar 16;307(1):17-24. PMID:11243799 doi:10.1006/jmbi.2000.4462
Ryu SW, Chae SK, Lee KJ, Kim E. Identification and characterization of human Fas associated factor 1, hFAF1. Biochem Biophys Res Commun. 1999 Aug 27;262(2):388-94. PMID:10462485 doi:10.1006/bbrc.1999.1217