HSP33

Hsp33 protein

Identifiers

Symbol

Hsp33

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe
PDBsum	structure summary

Hsp33 protein is a molecular chaperone, distinguished from all other known chaperones by its mode of functional regulation. Its activity is redox regulated. Hsp33 is a cytoplasmically localized protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidizing conditions like H₂O₂ cause disulphide bonds to form in Hsp33, a process that leads to the activation of its chaperone function^[1].

References

^ Jakob U, Muse W, Eser M, Bardwell JC (1999). "Chaperone activity with a redox switch". Cell 96 (3): 341–352. doi:10.1016/S0092-8674(00)80547-4. PMID 10025400.

Posttranslational modification

Chaperones/
protein folding

Heat shock proteins/ Chaperonins	Hsp10/GroES (Early pregnancy factor) · Hsp27 · Hsp47 · HSP60/GroEL Hsp40/DnaJ (A1, A2, A3, B1, B2, B11, B4, B6, B9, C1, C3, C5, C6, C7, C10, C11, C13, C14, C19) Hsp70 (1A, 1B, 1L, 2, 4, 4L, 5, 6, 7, 8, 9, 12A, 14) Hsp90 (α₁, α₂, β, ER, TRAP1)

Other	Alpha crystallin · Clusterin · Survival of motor neuron (SMN1, SMN2)

Protein targeting

Signal peptide

Ubiquitin

E1 Ubiquitin-activating enzyme (UBA1, UBA2, UBA3, UBA5, UBA6, UBA7, ATG7, NAE1, SAE1)

E2 Ubiquitin-conjugating enzyme (A • B • C • D1, D2, D3 • E1, E2, E3 • G1, G2 • H • I • J1, J2 • K • L1, L2, L3, L4, L6 • M • N • O • Q1, Q2 • R1 (CDC34), R2 • S • V1, V2 • Z)

E3 Ubiquitin ligase (VHL, Cullin, CBL, MDM2, FANCL, UBR1)

Deubiquitinating enzyme: Ataxin 3 • USP6 • CYLD

ATG3 • BIRC6 • UFC1

Other

SUMO protein

see also posttranslational modification disorders
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

This article incorporates text from the public domain Pfam and InterPro IPR000397