HEL55
entrez
126393
canonical
uniprot
O14558
canonical
ensembl
ENSG00000004776
resolver
ensp
ENSP00000004982
resolver
enst
ENST00000004982
resolver
genesymbol
HEL55
resolver
genesymbol
HSPB6
resolver
hgnc
HGNC:26511
resolver
uniprot
O14551
resolver
uniprot
Q6NVI3
resolver
uniprot
Q96MG9
resolver
uniprot
V9HWB6
resolver
uniprot_entry
HSPB6_HUMAN
resolver
uniprot_entry
V9HWB6_HUMAN
resolver
uniprot_sec
O14551
resolver
uniprot_sec
Q6NVI3
resolver
uniprot_sec
Q96MG9
resolver
amino_acid_sequence
MEIPVPVQPSWLRRASAPLPGLSAPGRLFDQRFGEGLLEAELAALCPTTLAPYYLRAPSVALPVAQVPTDPGHFSVLLDVKHFSPEEIAVKVVGEHVEVHARHEERPDEHGFVAREFHRRYRLPPGVDPAAVTSALSPEGVLSIQAAPASAQAPPPAAAK
uniprot
proteins
function
FUNCTION: Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Seems to have versatile functions in various biological processes. Plays a role in regulating muscle function such as smooth muscle vasorelaxation and cardiac myocyte contractility. May regulate myocardial angiogenesis implicating KDR. Overexpression mediates cardioprotection and angiogenesis after induced damage. Stabilizes monomeric YWHAZ thereby supporting YWHAZ chaperone-like activity. {ECO:0000269|PubMed:14717697, ECO:0000269|PubMed:19845507, ECO:0000269|PubMed:20843828, ECO:0000269|PubMed:22427880, ECO:0000305, ECO:0000305|PubMed:22794279}.
uniprot
proteins
mass_dalton
17136
uniprot
proteins
mutagenesis
MUTAGEN 3; /note="I->G: Increases homodimer-based self-association properties; increases chaperone activity; when associated with G-5."; /evidence="ECO:0000269|PubMed:24382496"; MUTAGEN 5; /note="V->G: Increases homodimer-based self-association properties; increases chaperone activity; when associated with G-3."; /evidence="ECO:0000269|PubMed:24382496"; MUTAGEN 67; /note="V->G: No effect on homodimer-based self-association properties; no effect on chaperone activity."; /evidence="ECO:0000269|PubMed:24382496"; MUTAGEN 134; /note="S->Q: Decreases heteromer formation with CRYAB.
uniprot
proteins
post_translational_modification
PTM: The N-terminus is blocked. {ECO:0000269|PubMed:8195168}.; PTM: Phosphorylated at Ser-16 by PKA and probably PKD1K; required to protect cardiomyocytes from apoptosis. {ECO:0000250|UniProtKB:P97541, ECO:0000250|UniProtKB:Q5EBG6, ECO:0000305|PubMed:26443497}.
uniprot
proteins
protein_family
Small heat shock protein (HSP20) family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14717697
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18790732
uniprot
proteins
pubmed
19464326
uniprot
proteins
pubmed
19568960
uniprot
proteins
pubmed
19777375
uniprot
proteins
pubmed
19845507
uniprot
proteins
pubmed
20843828
uniprot
proteins
pubmed
21334344
uniprot
proteins
pubmed
21641913
uniprot
proteins
pubmed
22002549
uniprot
proteins
pubmed
22427880
uniprot
proteins
pubmed
22794279
uniprot
proteins
pubmed
23948568
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24382496
uniprot
proteins
pubmed
26098708
uniprot
proteins
pubmed
26443497
uniprot
proteins
pubmed
27717639
uniprot
proteins
pubmed
8195168
uniprot
proteins
sequence_length
160
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19464326}. Nucleus {ECO:0000269|PubMed:19464326}. Secreted {ECO:0000269|PubMed:22427880}. Note=Translocates to nuclear foci during heat shock. {ECO:0000269|PubMed:19464326}.
uniprot
proteins