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HUMAN:HSPB1

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) HSPB1 (synonyms: HSP27, HSP28)
Protein Name(s) Heat shock protein beta-1

HspB1 28 kDa heat shock protein Estrogen-regulated 24 kDa protein Heat shock 27 kDa protein HSP 27 Stress-responsive protein 27 SRP27

External Links
UniProt P04792
EMBL L39370
X54079
Z23090
AB020027
U90906
CR407614
CR536489
BT019888
AK311894
DQ379985
AC006388
CH471220
BC000510
BC012292
BC012768
BC014920
BC073768
X16477
S74571
CCDS CCDS5583.1
PIR S12102
RefSeq NP_001531.1
UniGene Hs.520973
PDB 3Q9P
3Q9Q
4MJH
PDBsum 3Q9P
3Q9Q
4MJH
ProteinModelPortal P04792
SMR P04792
BioGrid 109547
DIP DIP-412N
IntAct P04792
MINT MINT-1368692
BindingDB P04792
ChEMBL CHEMBL5976
PhosphoSite P04792
DMDM 19855073
DOSAC-COBS-2DPAGE P04792
OGP P04792
REPRODUCTION-2DPAGE IPI00025512
P04792
SWISS-2DPAGE P04792
UCD-2DPAGE P04792
MaxQB P04792
PaxDb P04792
PeptideAtlas P04792
PRIDE P04792
DNASU 3315
Ensembl ENST00000248553
GeneID 3315
KEGG hsa:3315
UCSC uc003uew.3
CTD 3315
GeneCards GC07P075931
GeneReviews HSPB1
HGNC HGNC:5246
HPA CAB004439
CAB047330
CAB047331
CAB047332
HPA000497
MIM 602195
606595
608634
neXtProt NX_P04792
Orphanet 99940
139525
PharmGKB PA29511
eggNOG NOG307785
HOVERGEN HBG054766
InParanoid P04792
KO K04455
OMA HTSDRWR
OrthoDB EOG7WHHBK
PhylomeDB P04792
TreeFam TF105049
Reactome REACT_228166
REACT_25325
ChiTaRS HSPB1
GeneWiki Hsp27
GenomeRNAi 3315
NextBio 13148
PRO PR:P04792
Proteomes UP000005640
Bgee P04792
CleanEx HS_HSPB1
ExpressionAtlas P04792
Genevestigator P04792
GO GO:0005737
GO:0005856
GO:0005829
GO:0005615
GO:0070062
GO:0005925
GO:0005634
GO:0005886
GO:0000502
GO:0005819
GO:0030018
GO:0042802
GO:0044822
GO:0019901
GO:0005080
GO:0008426
GO:0043130
GO:0006928
GO:0035924
GO:0010467
GO:0035556
GO:0016071
GO:0043066
GO:1902176
GO:0006469
GO:0070527
GO:0045766
GO:0043536
GO:2001028
GO:0038033
GO:0032731
GO:0042535
GO:0043122
GO:0006446
GO:0006986
GO:0009615
GO:0001895
GO:0016070
Gene3D 2.60.40.790
InterPro IPR002068
IPR001436
IPR008978
Pfam PF00011
PIRSF PIRSF036514
PRINTS PR00299
SUPFAM SSF49764
PROSITE PS01031

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0046596

regulation of viral entry into host cell

PMID:24098578[1]

ECO:0000314

P

Figure 1

complete
CACAO 8960

involved_in

GO:0010506

regulation of autophagy

PMID:25962073[2]

ECO:0000303

author statement without traceable support used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:28144995[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0042803

protein homodimerization activity

PMID:28144995[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:20178975[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0044183

protein folding chaperone

PMID:20178975[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0061077

chaperone-mediated protein folding

PMID:20178975[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0070062

extracellular exosome

PMID:23533145[5]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0070527

platelet aggregation

PMID:23382103[6]

ECO:0007001

high throughput mutant phenotypic evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005925

focal adhesion

PMID:21423176[7]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(CL:0000057)

Seeded From UniProt

complete

part_of

GO:0070062

extracellular exosome

PMID:19199708[8]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(UBERON:0001831)

Seeded From UniProt

complete

part_of

GO:0070062

extracellular exosome

PMID:19056867[9]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(UBERON:0001088)

Seeded From UniProt

complete

part_of

GO:0005615

extracellular space

PMID:23580065[10]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(UBERON:0001827)

Seeded From UniProt

complete

part_of

GO:0005615

extracellular space

PMID:22664934[11]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(UBERON:0001827)

Seeded From UniProt

complete

involved_in

GO:0001895

retina homeostasis

PMID:23580065[10]

ECO:0007007

high throughput expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0099641

anterograde axonal protein transport

PMID:23728742[12]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0001932

regulation of protein phosphorylation

PMID:23728742[12]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:23948568[13]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0061077

chaperone-mediated protein folding

PMID:23948568[13]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:2001028

positive regulation of endothelial cell chemotaxis

PMID:18440775[14]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

occurs_in:(CL:0002618)

Seeded From UniProt

complete

involved_in

GO:1902176

negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P14602

P

Seeded From UniProt

complete

involved_in

GO:0045766

positive regulation of angiogenesis

PMID:18440775[14]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

occurs_in:(CL:0002618)

Seeded From UniProt

complete

involved_in

GO:0043536

positive regulation of blood vessel endothelial cell migration

PMID:18440775[14]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

occurs_in:(CL:0002618)

Seeded From UniProt

complete

enables

GO:0043130

ubiquitin binding

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P42930

F

Seeded From UniProt

complete

involved_in

GO:0043122

regulation of I-kappaB kinase/NF-kappaB signaling

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P14602

P

Seeded From UniProt

complete

involved_in

GO:0042535

positive regulation of tumor necrosis factor biosynthetic process

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P14602

P

Seeded From UniProt

complete

involved_in

GO:0038033

positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway

PMID:18440775[14]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

occurs_in:(CL:0002618)

Seeded From UniProt

complete

involved_in

GO:0035924

cellular response to vascular endothelial growth factor stimulus

PMID:18440775[14]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

occurs_in:(CL:0002618)

Seeded From UniProt

complete

involved_in

GO:0035556

intracellular signal transduction

PMID:18440775[14]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

occurs_in:(CL:0002618)

Seeded From UniProt

complete

involved_in

GO:0032731

positive regulation of interleukin-1 beta production

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P14602

P

Seeded From UniProt

complete

enables

GO:0008426

protein kinase C inhibitor activity

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P14602

F

Seeded From UniProt

complete

involved_in

GO:0006469

negative regulation of protein kinase activity

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P14602

P

Seeded From UniProt

complete

enables

GO:0005080

protein kinase C binding

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P14602

F

Seeded From UniProt

complete

part_of

GO:0000502

proteasome complex

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P42930

C

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

PMID:22658674[15]

ECO:0007005

high throughput direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0019901

protein kinase binding

PMID:8774846[16]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q16644

F

Seeded From UniProt

complete

enables

GO:0019901

protein kinase binding

PMID:8774846[16]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P49137

F

Seeded From UniProt

complete

involved_in

GO:0009615

response to virus

PMID:16548883[17]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006986

response to unfolded protein

PMID:1560006[18]

ECO:0000303

author statement without traceable support used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:19464326[19]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:19464326[19]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:25277244[20]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P04792

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:25036637[21]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P04792

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:22365833[22]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P04792

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:11003656[23]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P04792

F

Seeded From UniProt

complete

involved_in

GO:0071901

negative regulation of protein serine/threonine kinase activity

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0008426

P

Seeded From UniProt

complete

involved_in

GO:0071901

negative regulation of protein serine/threonine kinase activity

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0008426

P

Seeded From UniProt

complete

part_of

GO:1904115

axon cytoplasm

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0099641

C

Seeded From UniProt

complete

involved_in

GO:2001234

negative regulation of apoptotic signaling pathway

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P14602
ensembl:ENSMUSP00000005077

P

Seeded From UniProt

complete

involved_in

GO:1902176

negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P14602
ensembl:ENSMUSP00000005077

P

Seeded From UniProt

complete

part_of

GO:0043292

contractile fiber

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P14602
ensembl:ENSMUSP00000005077

C

Seeded From UniProt

complete

involved_in

GO:0043122

regulation of I-kappaB kinase/NF-kappaB signaling

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P14602
ensembl:ENSMUSP00000005077

P

Seeded From UniProt

complete

involved_in

GO:0042535

positive regulation of tumor necrosis factor biosynthetic process

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P14602
ensembl:ENSMUSP00000005077

P

Seeded From UniProt

complete

involved_in

GO:0032731

positive regulation of interleukin-1 beta production

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P14602
ensembl:ENSMUSP00000005077

P

Seeded From UniProt

complete

part_of

GO:0030018

Z disc

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P14602
ensembl:ENSMUSP00000005077

C

Seeded From UniProt

complete

enables

GO:0008426

protein kinase C inhibitor activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P14602
ensembl:ENSMUSP00000005077

F

Seeded From UniProt

complete

involved_in

GO:0006469

negative regulation of protein kinase activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P14602
ensembl:ENSMUSP00000005077

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P14602
ensembl:ENSMUSP00000005077

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P14602
ensembl:ENSMUSP00000005077

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P14602
ensembl:ENSMUSP00000005077

C

Seeded From UniProt

complete

enables

GO:0005080

protein kinase C binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P14602
ensembl:ENSMUSP00000005077

F

Seeded From UniProt

complete

involved_in

GO:0006986

response to unfolded protein

PMID:10859165[24]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006446

regulation of translational initiation

PMID:10859165[24]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:10859165[24]
PMID:16130169[25]

ECO:0000304

author statement supported by traceable reference used in manual assertion


C

Seeded From UniProt

complete

involved_in

GO:0043066

negative regulation of apoptotic process

PMID:16130169[25]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005856

cytoskeleton

PMID:16130169[25]

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0043488

regulation of mRNA stability

Reactome:R-HSA-450408

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

Reactome:R-HSA-5687121
Reactome:R-HSA-5218916
Reactome:R-HSA-450580
Reactome:R-HSA-450551

ECO:0000304

author statement supported by traceable reference used in manual assertion




C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

part_of

GO:0005856

cytoskeleton

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0206

C

Seeded From UniProt

complete

part_of

GO:0005819

spindle

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0251

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Tsou, YL et al. (2013) Heat shock protein 90: role in enterovirus 71 entry and assembly and potential target for therapy. PLoS ONE 8 e77133 PubMed GONUTS page
  2. Matsumoto, T et al. (2015) Small Heat Shock Protein Beta-1 (HSPB1) Is Upregulated and Regulates Autophagy and Apoptosis of Renal Tubular Cells in Acute Kidney Injury. PLoS ONE 10 e0126229 PubMed GONUTS page
  3. 3.0 3.1 Echaniz-Laguna, A et al. (2017) Axonal Neuropathies due to Mutations in Small Heat Shock Proteins: Clinical, Genetic, and Functional Insights into Novel Mutations. Hum. Mutat. 38 556-568 PubMed GONUTS page
  4. 4.0 4.1 4.2 Almeida-Souza, L et al. (2010) Increased monomerization of mutant HSPB1 leads to protein hyperactivity in Charcot-Marie-Tooth neuropathy. J. Biol. Chem. 285 12778-86 PubMed GONUTS page
  5. Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
  6. Fröbel, J et al. (2013) Platelet proteome analysis reveals integrin-dependent aggregation defects in patients with myelodysplastic syndromes. Mol. Cell Proteomics 12 1272-80 PubMed GONUTS page
  7. Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page
  8. Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page
  9. Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
  10. 10.0 10.1 Pieragostino, D et al. (2013) Shotgun proteomics reveals specific modulated protein patterns in tears of patients with primary open angle glaucoma naïve to therapy. Mol Biosyst 9 1108-16 PubMed GONUTS page
  11. Böhm, D et al. (2012) Comparison of tear protein levels in breast cancer patients and healthy controls using a de novo proteomic approach. Oncol. Rep. 28 429-38 PubMed GONUTS page
  12. 12.0 12.1 Holmgren, A et al. (2013) Charcot-Marie-Tooth causing HSPB1 mutations increase Cdk5-mediated phosphorylation of neurofilaments. Acta Neuropathol. 126 93-108 PubMed GONUTS page
  13. 13.0 13.1 Nefedova, VV et al. (2013) Structure and properties of G84R and L99M mutants of human small heat shock protein HspB1 correlating with motor neuropathy. Arch. Biochem. Biophys. 538 16-24 PubMed GONUTS page
  14. 14.0 14.1 14.2 14.3 14.4 14.5 Evans, IM et al. (2008) Vascular endothelial growth factor induces heat shock protein (HSP) 27 serine 82 phosphorylation and endothelial tubulogenesis via protein kinase D and independent of p38 kinase. Cell. Signal. 20 1375-84 PubMed GONUTS page
  15. Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
  16. 16.0 16.1 Clifton, AD et al. (1996) A comparison of the substrate specificity of MAPKAP kinase-2 and MAPKAP kinase-3 and their activation by cytokines and cellular stress. FEBS Lett. 392 209-14 PubMed GONUTS page
  17. Leong, WF & Chow, VT (2006) Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection. Cell. Microbiol. 8 565-80 PubMed GONUTS page
  18. Kato, K et al. (1992) Copurification of small heat shock protein with alpha B crystallin from human skeletal muscle. J. Biol. Chem. 267 7718-25 PubMed GONUTS page
  19. 19.0 19.1 Vos, MJ et al. (2009) HSPB7 is a SC35 speckle resident small heat shock protein. Biochim. Biophys. Acta 1793 1343-53 PubMed GONUTS page
  20. Katsogiannou, M et al. (2014) The functional landscape of Hsp27 reveals new cellular processes such as DNA repair and alternative splicing and proposes novel anticancer targets. Mol. Cell Proteomics 13 3585-601 PubMed GONUTS page
  21. Taipale, M et al. (2014) A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways. Cell 158 434-48 PubMed GONUTS page
  22. Hegele, A et al. (2012) Dynamic protein-protein interaction wiring of the human spliceosome. Mol. Cell 45 567-80 PubMed GONUTS page
  23. Charette, SJ et al. (2000) Inhibition of Daxx-mediated apoptosis by heat shock protein 27. Mol. Cell. Biol. 20 7602-12 PubMed GONUTS page
  24. 24.0 24.1 24.2 Cuesta, R et al. (2000) Chaperone hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes. Genes Dev. 14 1460-70 PubMed GONUTS page
  25. 25.0 25.1 25.2 Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page