HSP47

HSP47
serpín peptidasa inhibidor, clado H (heat shock protein 47), miembro 1, (collagen binding protein 1)
HUGO 1546
Símbolo SERPINH1
Símbolos alt. CBP1, CBP2, SERPINH2
Datos genéticos
Locus Cr. 11 q13.5
Bases de datos
Entrez 871
OMIM 600943
RefSeq NM_004353
UniProt P50454

HSP47 (por las siglas en inglés de Heat shock protein 47, proteína de choque térmico 47) es una serpina, es decir, una proteína inhibidora de serín proteasas, que actúa en la célula como caperona para el compuesto químico colágeno.[1]

La proteína Hsp47 desempeña su función en el retículo endoplásmico.

Referencias

  1. ↑ Dafforn T, Della M, Miller A (2001). «The molecular interactions of heat shock protein 47 (Hsp47) and their implications for collagen biosynthesis». J Biol Chem 276 (52):  pp. 49310-9. PMID 11592970. 

Enlaces externos


Wikimedia foundation. 2010.

Игры ⚽ Поможем сделать НИР

Mira otros diccionarios:

  • Heat shock protein 47 — Heat shock protein 47, also known as SERPINH1 is a serpin which serves as a human chaperone protein for collagen.cite web | title = Entrez Gene: SERPINH1 serpin peptidase inhibitor, clade H (heat shock protein 47), member 1, (collagen binding… …   Wikipedia

  • Chaperone (protein) — A top view of the GroES/GroEL bacterial chaperone complex model In molecular biology, chaperones are proteins that assist the non covalent folding or unfolding and the assembly or disassembly of other macromolecular structures, but do not occur… …   Wikipedia

  • Serpin — Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The name serpin is derived from this activity serine protease inhibitors. [cite journal |author=R. Carrell and J.… …   Wikipedia

  • Protein targeting — This article deals with protein targeting in eukaryotes except where noted. Protein targeting or protein sorting is the mechanism by which a cell transports proteins to the appropriate positions in the cell or outside of it. Sorting targets can… …   Wikipedia

  • Protein folding — Protein thermodynamics redirects here. For the thermodynamics of reactions catalyzed by proteins, see Enzyme. Protein before and after folding. Protein folding is the process by which a protein structure assumes its functional shape or… …   Wikipedia

  • Hsp70 — protein Structure of the ATPase fragment of a 70K heat shock cognate protein.[1] Identifiers Symbol …   Wikipedia

  • Clusterin — Identifiers Symbols CLU; APOJ; CLI; KUB1; MGC24903; SGP 2; SGP2; SP 40; TRPM 2; TRPM2 External IDs …   Wikipedia

  • GroES — Heat shock 10kDa protein 1 (chaperonin 10) Identifiers Symbols HSPE1; CPN10; EPF; GROES; HSP10 External IDs …   Wikipedia

  • Chaperonin — Chaperonins are proteins that fold and unfold other proteins. Newly made proteins usually must fold from a linear chain of amino acids into a three dimensional form. Chaperonins belong to a large class of molecules that assist protein folding,… …   Wikipedia

  • Deubiquitinating enzyme — Deubiquitinating enzymes (DUBs) are a large group of proteases[1] (more than 60 known) that regulate ubiquitin dependent metabolic pathways by cleaving ubiquitin protein bonds. DUBs are also commonly referred to as deubiquitinating peptidases,… …   Wikipedia

Compartir el artículo y extractos

Link directo
… Do a right-click on the link above
and select “Copy Link”