HSPB1
entrez
3315
canonical
uniprot
P04792
canonical
ensembl
ENSG00000106211
resolver
ensp
ENSP00000248553
resolver
enst
ENST00000248553
resolver
genesymbol
HEL-S-102
resolver
genesymbol
HSPB1
resolver
genesymbol_syn
HSP27
resolver
genesymbol_syn
HSP28
resolver
hgnc
HGNC:5246
resolver
uniprot
B2R4N8
resolver
uniprot
Q6FI47
resolver
uniprot
Q96C20
resolver
uniprot
Q96EI7
resolver
uniprot
Q9UC31
resolver
uniprot
Q9UC34
resolver
uniprot
Q9UC35
resolver
uniprot
Q9UC36
resolver
uniprot
V9HW43
resolver
uniprot_entry
HSPB1_HUMAN
resolver
uniprot_entry
V9HW43_HUMAN
resolver
uniprot_sec
B2R4N8
resolver
uniprot_sec
Q6FI47
resolver
uniprot_sec
Q96C20
resolver
uniprot_sec
Q96EI7
resolver
uniprot_sec
Q9UC31
resolver
uniprot_sec
Q9UC34
resolver
uniprot_sec
Q9UC35
resolver
uniprot_sec
Q9UC36
resolver
amino_acid_sequence
MTERRVPFSLLRGPSWDPFRDWYPHSRLFDQAFGLPRLPEEWSQWLGGSSWPGYVRPLPPAAIESPAVAAPAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQSNEITIPVTFESRAQLGGPEAAKSDETAAK
uniprot
proteins
disease_involvement
DISEASE: Charcot-Marie-Tooth disease, axonal, type 2F (CMT2F) [MIM:606595]: A dominant axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Onset of Charcot-Marie-Tooth disease type 2F is between 15 and 25 years with muscle weakness and atrophy usually beginning in feet and legs (peroneal distribution). Upper limb involvement occurs later. {ECO:0000269|PubMed:15122254, ECO:0000269|PubMed:20178975, ECO:0000269|PubMed:22176143, ECO:0000269|PubMed:22206013, ECO:0000269|PubMed:23728742}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Neuronopathy, distal hereditary motor, autosomal dominant 3 (HMND3) [MIM:608634]: A form of distal hereditary motor neuronopathy, a heterogeneous group of neuromuscular disorders caused by selective degeneration of motor neurons in the anterior horn of the spinal cord, without sensory deficit in the posterior horn. The overall clinical picture consists of a classical distal muscular atrophy syndrome in the legs without clinical sensory loss. The disease starts with weakness and wasting of distal muscles of the anterior tibial and peroneal compartments of the legs. Later on, weakness and atrophy may expand to the proximal muscles of the lower limbs and/or to the distal upper limbs. {ECO:0000269|PubMed:15122254, ECO:0000269|PubMed:18832141, ECO:0000269|PubMed:18952241, ECO:0000269|PubMed:20178975, ECO:0000269|PubMed:20870250, ECO:0000269|PubMed:22176143, ECO:0000269|PubMed:23643870, ECO:0000269|PubMed:23728742, ECO:0000269|PubMed:23948568, ECO:0000269|PubMed:25965061, ECO:0000269|PubMed:28144995}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state (PubMed:10383393, PubMed:20178975). Plays a role in stress resistance and actin organization (PubMed:19166925). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (PubMed:23728742). {ECO:0000269|PubMed:10383393, ECO:0000269|PubMed:19166925, ECO:0000269|PubMed:20178975, ECO:0000269|PubMed:23728742}.
uniprot
proteins
mass_dalton
22783
uniprot
proteins
mutagenesis
MUTAGEN 15; /note="S->D: Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-78 and D-82."; /evidence="ECO:0000269|PubMed:10383393"; MUTAGEN 78; /note="S->D: Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-15 and D-82."; /evidence="ECO:0000269|PubMed:10383393"; MUTAGEN 82; /note="S->D: Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-15 and D-78."; /evidence="ECO:0000269|PubMed:10383393
uniprot
proteins
post_translational_modification
PTM: Phosphorylated upon exposure to protein kinase C activators and heat shock (PubMed:8325890). Phosphorylation by MAPKAPK2 and MAPKAPK3 in response to stress dissociates HSPB1 from large small heat-shock protein (sHsps) oligomers and impairs its chaperone activity and ability to protect against oxidative stress effectively. Phosphorylation by MAPKAPK5 in response to PKA stimulation induces F-actin rearrangement (PubMed:1332886, PubMed:19166925, PubMed:8093612). {ECO:0000269|PubMed:1332886, ECO:0000269|PubMed:19166925, ECO:0000269|PubMed:8093612, ECO:0000269|PubMed:8325890}.
uniprot
proteins
protein_family
Small heat shock protein (HSP20) family
uniprot
proteins
pubmed
10383393
uniprot
proteins
pubmed
10751411
uniprot
proteins
pubmed
10777697
uniprot
proteins
pubmed
11342557
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
1332886
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15122254
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
1560006
uniprot
proteins
pubmed
15976317
uniprot
proteins
pubmed
16548883
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
1730670
uniprot
proteins
pubmed
1763035
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
18832141
uniprot
proteins
pubmed
18952241
uniprot
proteins
pubmed
19166925
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19464326
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20178975
uniprot
proteins
pubmed
20870250
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22176143
uniprot
proteins
pubmed
22206013
uniprot
proteins
pubmed
2243808
uniprot
proteins
pubmed
2295696
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23643870
uniprot
proteins
pubmed
23728742
uniprot
proteins
pubmed
23948568
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
25965061
uniprot
proteins
pubmed
2743305
uniprot
proteins
pubmed
27492805
uniprot
proteins
pubmed
28144995
uniprot
proteins
pubmed
3714473
uniprot
proteins
pubmed
8093612
uniprot
proteins
pubmed
8325890
uniprot
proteins
pubmed
8774846
uniprot
proteins
pubmed
9110174
uniprot
proteins
sequence_length
205
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10777697, ECO:0000269|PubMed:28144995}. Nucleus {ECO:0000269|PubMed:19464326}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:10777697}. Note=Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. {ECO:0000269|PubMed:19464326}.
uniprot
proteins