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P04792

- HSPB1_HUMAN

UniProt

P04792 - HSPB1_HUMAN

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Protein

Heat shock protein beta-1

Gene

HSPB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Involved in stress resistance and actin organization.

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. poly(A) RNA binding Source: UniProtKB
  3. protein kinase binding Source: UniProtKB
  4. protein kinase C binding Source: BHF-UCL
  5. protein kinase C inhibitor activity Source: BHF-UCL
  6. ubiquitin binding Source: BHF-UCL

GO - Biological processi

  1. cell death Source: UniProtKB-KW
  2. cellular component movement Source: UniProtKB
  3. cellular response to vascular endothelial growth factor stimulus Source: BHF-UCL
  4. gene expression Source: Reactome
  5. intracellular signal transduction Source: BHF-UCL
  6. mRNA metabolic process Source: Reactome
  7. negative regulation of apoptotic process Source: UniProtKB
  8. negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: BHF-UCL
  9. negative regulation of protein kinase activity Source: BHF-UCL
  10. platelet aggregation Source: UniProtKB
  11. positive regulation of angiogenesis Source: BHF-UCL
  12. positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
  13. positive regulation of endothelial cell chemotaxis Source: BHF-UCL
  14. positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  15. positive regulation of interleukin-1 beta production Source: BHF-UCL
  16. positive regulation of tumor necrosis factor biosynthetic process Source: BHF-UCL
  17. regulation of I-kappaB kinase/NF-kappaB signaling Source: BHF-UCL
  18. regulation of translational initiation Source: ProtInc
  19. response to unfolded protein Source: UniProtKB
  20. response to virus Source: UniProtKB
  21. retina homeostasis Source: UniProt
  22. RNA metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Enzyme and pathway databases

ReactomeiREACT_228166. VEGFA-VEGFR2 Pathway.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein beta-1
Short name:
HspB1
Alternative name(s):
28 kDa heat shock protein
Estrogen-regulated 24 kDa protein
Heat shock 27 kDa protein
Short name:
HSP 27
Stress-responsive protein 27
Short name:
SRP27
Gene namesi
Name:HSPB1
Synonyms:HSP27, HSP28
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:5246. HSPB1.

Subcellular locationi

Cytoplasm. Nucleus. Cytoplasmcytoskeletonspindle
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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB
  3. cytosol Source: Reactome
  4. extracellular space Source: UniProt
  5. extracellular vesicular exosome Source: UniProtKB
  6. focal adhesion Source: UniProtKB
  7. nucleus Source: UniProtKB
  8. plasma membrane Source: Ensembl
  9. proteasome complex Source: BHF-UCL
  10. Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

Charcot-Marie-Tooth disease 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. Nerve conduction velocities are normal or slightly reduced. 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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti135 – 1351S → F in CMT2F and HMN2B. 1 Publication
VAR_018507
Natural varianti136 – 1361R → W in CMT2F. 1 Publication
VAR_018508
Natural varianti164 – 1641T → A in CMT2F. 1 Publication
VAR_067085
Neuronopathy, distal hereditary motor, 2B (HMN2B) [MIM:608634]: A neuromuscular disorder. Distal hereditary motor neuronopathies constitute 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti127 – 1271R → W in HMN2B. 1 Publication
VAR_018506
Natural varianti135 – 1351S → F in CMT2F and HMN2B. 1 Publication
VAR_018507
Natural varianti151 – 1511T → I in HMN2B. 1 Publication
VAR_018509
Natural varianti182 – 1821P → L in HMN2B. 1 Publication
VAR_018510

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi15 – 151S → D: Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-78 and D-82. 1 Publication
Mutagenesisi78 – 781S → D: Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-15 and D-82. 1 Publication
Mutagenesisi82 – 821S → D: Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-15 and D-78. 1 Publication

Keywords - Diseasei

Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

Organism-specific databases

MIMi606595. phenotype.
608634. phenotype.
Orphaneti99940. Autosomal dominant Charcot-Marie-Tooth disease type 2F.
139525. Distal hereditary motor neuropathy type 2.
PharmGKBiPA29511.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 205205Heat shock protein beta-1PRO_0000125927Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151Phosphoserine; by MAPKAPK2 and MAPKAPK37 Publications
Modified residuei26 – 261PhosphoserineBy similarity
Modified residuei65 – 651Phosphoserine2 Publications
Modified residuei78 – 781Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK57 Publications
Modified residuei82 – 821Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK511 Publications
Modified residuei83 – 831Phosphoserine1 Publication
Modified residuei86 – 861PhosphoserineBy similarity
Modified residuei123 – 1231N6-acetyllysine1 Publication
Modified residuei199 – 1991Phosphoserine3 Publications

Post-translational modificationi

Phosphorylated in MCF-7 cells on exposure to protein kinase C activators and heat shock.
Phosphorylation by MAPKAPK2 and MAPKAPK3 in response to stress leads to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair its chaperone activity and ability to protect against oxidative stress effectively. Phosphorylation by MAPKAPK5 in response to PKA stimulation induces F-actin rearrangement.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP04792.
PaxDbiP04792.
PeptideAtlasiP04792.
PRIDEiP04792.

2D gel databases

DOSAC-COBS-2DPAGEP04792.
OGPiP04792.
REPRODUCTION-2DPAGEIPI00025512.
P04792.
SWISS-2DPAGEP04792.
UCD-2DPAGEP04792.

PTM databases

PhosphoSiteiP04792.

Expressioni

Tissue specificityi

Detected in all tissues tested: skeletal muscle, heart, aorta, large intestine, small intestine, stomach, esophagus, bladder, adrenal gland, thyroid, pancreas, testis, adipose tissue, kidney, liver, spleen, cerebral cortex, blood serum and cerebrospinal fluid. Highest levels are found in the heart and in tissues composed of striated and smooth muscle.1 Publication

Inductioni

Expressed in response to environmental stresses such as heat shock, or estrogen stimulation in MCF-7 cells. Up-regulated in response to enterovirus 71 (EV71) infection (at protein level).1 Publication

Gene expression databases

BgeeiP04792.
CleanExiHS_HSPB1.
ExpressionAtlasiP04792. baseline and differential.
GenevestigatoriP04792.

Organism-specific databases

HPAiCAB004439.
CAB047330.
CAB047331.
CAB047332.
HPA000497.

Interactioni

Subunit structurei

Interacts with TGFB1I1 (By similarity). Associates with alpha- and beta-tubulin, microtubules and CRYAB. Interacts with HSPB8 and HSPBAP1.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-352682,EBI-352682
BAG3O958173EBI-352682,EBI-747185
CALRP277972EBI-352682,EBI-1049597
CRYABP025112EBI-352682,EBI-739060
DAXXQ9UER74EBI-352682,EBI-77321
DFFAO002732EBI-352682,EBI-727171
EFTUD2Q150292EBI-352682,EBI-357897
EGFRP005333EBI-352682,EBI-297353
EIF4A2Q142402EBI-352682,EBI-73473
EIF4G2P783443EBI-352682,EBI-296519
FKBP4Q027902EBI-352682,EBI-1047444
FTH1P027942EBI-352682,EBI-713259
G6PDP114132EBI-352682,EBI-4289891
GSTO1P784172EBI-352682,EBI-712083
HSPB8Q9UJY13EBI-352682,EBI-739074
HUWE1Q7Z6Z73EBI-352682,EBI-625934
IGBP1P783183EBI-352682,EBI-1055954
MAPKAPK2P491373EBI-352682,EBI-993299
MAPKAPK3Q166443EBI-352682,EBI-1384657
MAPKAPK5Q8IW412EBI-352682,EBI-1201460
MMEP084734EBI-352682,EBI-353759
PAF1Q8N7H52EBI-352682,EBI-2607770
PGM2Q96G032EBI-352682,EBI-4399372
RAB43Q86YS62EBI-352682,EBI-4401730
SF3A3Q128742EBI-352682,EBI-1051880
SNW1Q135733EBI-352682,EBI-632715
SPIN1Q9Y6572EBI-352682,EBI-727129
TP53P046373EBI-352682,EBI-366083
TPT1P136932EBI-352682,EBI-1783169
XRCC5P130102EBI-352682,EBI-357997
YWHAZP631044EBI-352682,EBI-347088

Protein-protein interaction databases

BioGridi109547. 111 interactions.
DIPiDIP-412N.
IntActiP04792. 287 interactions.
MINTiMINT-1368692.

Structurei

Secondary structure

1
205
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi86 – 883Combined sources
Beta strandi94 – 1007Combined sources
Turni102 – 1043Combined sources
Beta strandi107 – 1148Combined sources
Beta strandi117 – 1248Combined sources
Beta strandi136 – 1438Combined sources
Helixi150 – 1523Combined sources
Beta strandi154 – 1574Combined sources
Beta strandi161 – 1688Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q9PX-ray2.00A90-171[»]
3Q9QX-ray2.20A/B90-171[»]
4MJHX-ray2.60A/C84-176[»]
B/D179-186[»]
ProteinModelPortaliP04792.
SMRiP04792. Positions 18-188.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni70 – 205136Interaction with TGFB1I1By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the small heat shock protein (HSP20) family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG307785.
HOVERGENiHBG054766.
InParanoidiP04792.
KOiK04455.
OMAiDQSFGMP.
OrthoDBiEOG7WHHBK.
PhylomeDBiP04792.
TreeFamiTF105049.

Family and domain databases

Gene3Di2.60.40.790. 2 hits.
InterProiIPR002068. a-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PfamiPF00011. HSP20. 1 hit.
[Graphical view]
PIRSFiPIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P04792-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTERRVPFSL LRGPSWDPFR DWYPHSRLFD QAFGLPRLPE EWSQWLGGSS
60 70 80 90 100
WPGYVRPLPP AAIESPAVAA PAYSRALSRQ LSSGVSEIRH TADRWRVSLD
110 120 130 140 150
VNHFAPDELT VKTKDGVVEI TGKHEERQDE HGYISRCFTR KYTLPPGVDP
160 170 180 190 200
TQVSSSLSPE GTLTVEAPMP KLATQSNEIT IPVTFESRAQ LGGPEAAKSD

ETAAK
Length:205
Mass (Da):22,783
Last modified:September 26, 2001 - v2
Checksum:i1B4DC44A6F6606D5
GO

Sequence cautioni

The sequence AAA62175.1 differs from that shown. Reason: Frameshift at position 194. Curated
The sequence AAB20722.1 differs from that shown. Reason: Frameshift at position 194. Curated
The sequence CAA34498.1 differs from that shown. Reason: Frameshift at position 194. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti10 – 101L → I AA sequence (PubMed:2295696)Curated
Sequence conflicti109 – 1091L → R in AAH12292. (PubMed:15489334)Curated
Sequence conflicti121 – 1211T → S in AAH12292. (PubMed:15489334)Curated
Sequence conflicti127 – 1271R → L in AAH12292. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti127 – 1271R → W in HMN2B. 1 Publication
VAR_018506
Natural varianti135 – 1351S → F in CMT2F and HMN2B. 1 Publication
VAR_018507
Natural varianti136 – 1361R → W in CMT2F. 1 Publication
VAR_018508
Natural varianti151 – 1511T → I in HMN2B. 1 Publication
VAR_018509
Natural varianti164 – 1641T → A in CMT2F. 1 Publication
VAR_067085
Natural varianti182 – 1821P → L in HMN2B. 1 Publication
VAR_018510

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L39370 Genomic DNA. Translation: AAA62175.1. Frameshift.
X54079 mRNA. Translation: CAA38016.1.
Z23090 mRNA. Translation: CAA80636.1.
AB020027 mRNA. Translation: BAB17232.1.
U90906 mRNA. Translation: AAB51056.1.
CR407614 mRNA. Translation: CAG28542.1.
CR536489 mRNA. Translation: CAG38728.1.
BT019888 mRNA. Translation: AAV38691.1.
AK311894 mRNA. Translation: BAG34835.1.
DQ379985 Genomic DNA. Translation: ABC88475.1.
AC006388 Genomic DNA. No translation available.
CH471220 Genomic DNA. Translation: EAW71803.1.
BC000510 mRNA. Translation: AAH00510.1.
BC012292 mRNA. Translation: AAH12292.1.
BC012768 mRNA. Translation: AAH12768.1.
BC014920 mRNA. Translation: AAH14920.1.
BC073768 mRNA. Translation: AAH73768.1.
X16477 mRNA. Translation: CAA34498.1. Frameshift.
S74571 mRNA. Translation: AAB20722.1. Frameshift.
CCDSiCCDS5583.1.
PIRiS12102. HHHU27.
RefSeqiNP_001531.1. NM_001540.3.
UniGeneiHs.520973.

Genome annotation databases

EnsembliENST00000248553; ENSP00000248553; ENSG00000106211.
GeneIDi3315.
KEGGihsa:3315.
UCSCiuc003uew.3. human.

Polymorphism databases

DMDMi19855073.

Cross-referencesi

Web resourcesi

Inherited peripheral neuropathies mutation db
NIEHS SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L39370 Genomic DNA. Translation: AAA62175.1 . Frameshift.
X54079 mRNA. Translation: CAA38016.1 .
Z23090 mRNA. Translation: CAA80636.1 .
AB020027 mRNA. Translation: BAB17232.1 .
U90906 mRNA. Translation: AAB51056.1 .
CR407614 mRNA. Translation: CAG28542.1 .
CR536489 mRNA. Translation: CAG38728.1 .
BT019888 mRNA. Translation: AAV38691.1 .
AK311894 mRNA. Translation: BAG34835.1 .
DQ379985 Genomic DNA. Translation: ABC88475.1 .
AC006388 Genomic DNA. No translation available.
CH471220 Genomic DNA. Translation: EAW71803.1 .
BC000510 mRNA. Translation: AAH00510.1 .
BC012292 mRNA. Translation: AAH12292.1 .
BC012768 mRNA. Translation: AAH12768.1 .
BC014920 mRNA. Translation: AAH14920.1 .
BC073768 mRNA. Translation: AAH73768.1 .
X16477 mRNA. Translation: CAA34498.1 . Frameshift.
S74571 mRNA. Translation: AAB20722.1 . Frameshift.
CCDSi CCDS5583.1.
PIRi S12102. HHHU27.
RefSeqi NP_001531.1. NM_001540.3.
UniGenei Hs.520973.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3Q9P X-ray 2.00 A 90-171 [» ]
3Q9Q X-ray 2.20 A/B 90-171 [» ]
4MJH X-ray 2.60 A/C 84-176 [» ]
B/D 179-186 [» ]
ProteinModelPortali P04792.
SMRi P04792. Positions 18-188.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109547. 111 interactions.
DIPi DIP-412N.
IntActi P04792. 287 interactions.
MINTi MINT-1368692.

Chemistry

BindingDBi P04792.
ChEMBLi CHEMBL5976.

PTM databases

PhosphoSitei P04792.

Polymorphism databases

DMDMi 19855073.

2D gel databases

DOSAC-COBS-2DPAGE P04792.
OGPi P04792.
REPRODUCTION-2DPAGE IPI00025512.
P04792.
SWISS-2DPAGE P04792.
UCD-2DPAGE P04792.

Proteomic databases

MaxQBi P04792.
PaxDbi P04792.
PeptideAtlasi P04792.
PRIDEi P04792.

Protocols and materials databases

DNASUi 3315.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000248553 ; ENSP00000248553 ; ENSG00000106211 .
GeneIDi 3315.
KEGGi hsa:3315.
UCSCi uc003uew.3. human.

Organism-specific databases

CTDi 3315.
GeneCardsi GC07P075931.
GeneReviewsi HSPB1.
HGNCi HGNC:5246. HSPB1.
HPAi CAB004439.
CAB047330.
CAB047331.
CAB047332.
HPA000497.
MIMi 602195. gene.
606595. phenotype.
608634. phenotype.
neXtProti NX_P04792.
Orphaneti 99940. Autosomal dominant Charcot-Marie-Tooth disease type 2F.
139525. Distal hereditary motor neuropathy type 2.
PharmGKBi PA29511.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG307785.
HOVERGENi HBG054766.
InParanoidi P04792.
KOi K04455.
OMAi DQSFGMP.
OrthoDBi EOG7WHHBK.
PhylomeDBi P04792.
TreeFami TF105049.

Enzyme and pathway databases

Reactomei REACT_228166. VEGFA-VEGFR2 Pathway.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.

Miscellaneous databases

ChiTaRSi HSPB1. human.
GeneWikii Hsp27.
GenomeRNAii 3315.
NextBioi 13148.
PROi P04792.
SOURCEi Search...

Gene expression databases

Bgeei P04792.
CleanExi HS_HSPB1.
ExpressionAtlasi P04792. baseline and differential.
Genevestigatori P04792.

Family and domain databases

Gene3Di 2.60.40.790. 2 hits.
InterProi IPR002068. a-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR008978. HSP20-like_chaperone.
[Graphical view ]
Pfami PF00011. HSP20. 1 hit.
[Graphical view ]
PIRSFi PIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSi PR00299. ACRYSTALLIN.
SUPFAMi SSF49764. SSF49764. 1 hit.
PROSITEi PS01031. HSP20. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and organization of genes encoding the human 27 kDa heat shock protein."
    Hickey E., Brandon S.E., Potter R., Stein G., Stein J., Weber L.A.
    Nucleic Acids Res. 14:4127-4145(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "cDNA sequence of a human heat shock protein HSP27."
    Carper S.W., Rocheleau T.A., Storm F.K.
    Nucleic Acids Res. 18:6457-6457(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  3. "Small heat shock protein 27 (HSP27) associates with tubulin/microtubules in HeLa cells."
    Hino M., Kurogi K., Okubo M.-A., Murata-Hori M., Hosoya H.
    Biochem. Biophys. Res. Commun. 271:164-169(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, SUBUNIT.
    Tissue: Cervix carcinoma.
  4. "Identification of a new cDNA sequence from human breast carcinoma cells encoding the 28kDa heat shock protein."
    Briolay J., Chareyron P., Mehlen P., Arrigo A.
    Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary carcinoma.
  5. "Large-scale concatenation cDNA sequencing."
    Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
    Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skeletal muscle.
  9. NIEHS SNPs program
    Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  10. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  12. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung, Ovary, Pancreas, Skin and Uterus.
  13. "Identification of two related markers for common acute lymphoblastic leukemia as heat shock proteins."
    Strahler J.R., Kuick R., Eckerskorn C., Lottspeich F., Richardson B.C., Fox D.A., Stoolman L.M., Hanson C.A., Nichols D., Tueche H.J., Hanash S.M.
    J. Clin. Invest. 85:200-207(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 5-12; 97-112; 141-154 AND 172-188.
  14. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 6-37; 57-75; 80-89; 97-127 AND 141-188, PHOSPHORYLATION AT SER-82, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  15. "The 28-kDa protein whose phosphorylation is induced by protein kinase C activators in MCF-7 cells belongs to the family of low molecular mass heat shock proteins and is the estrogen-regulated 24-kDa protein."
    Faucher C., Capdevielle J., Canal I., Ferrara P., Mazarguil H., McGuire W.L., Darbon J.-M.
    J. Biol. Chem. 268:15168-15173(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 13-20; 38-46; 97-110; 141-154 AND 172-186, PHOSPHORYLATION.
    Tissue: Mammary carcinoma.
  16. "Copurification of small heat shock protein with alpha B crystallin from human skeletal muscle."
    Kato K., Shinohara H., Goto S., Inaguma Y., Morishita R., Asano T.
    J. Biol. Chem. 267:7718-7725(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 21-59; 93-98; 129-134 AND 178-193, ASSOCIATION WITH CRYAB, TISSUE SPECIFICITY.
    Tissue: Pectoralis muscle.
  17. "Human HSP27 is phosphorylated at serines 78 and 82 by heat shock and mitogen-activated kinases that recognize the same amino acid motif as S6 kinase II."
    Landry J., Lambert H., Zhou M., Lavoie J.N., Hickey E., Weber L.A., Anderson C.W.
    J. Biol. Chem. 267:794-803(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 76-89, PHOSPHORYLATION AT SER-78 AND SER-82.
  18. "Induction of the estrogen-regulated '24K' protein by heat shock."
    Fuqua S.A.W., Blum-Salingaros M., McGuire W.L.
    Cancer Res. 49:4126-4129(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 109-205.
    Tissue: Mammary carcinoma.
  19. "The 29-kDa proteins phosphorylated in thrombin-activated human platelets are forms of the estrogen receptor-related 27-kDa heat shock protein."
    Mendelsohn M.E., Zhu Y., O'Neill S.
    Proc. Natl. Acad. Sci. U.S.A. 88:11212-11216(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 122-205.
  20. "Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins."
    Stokoe D., Engel K., Campbell D.G., Cohen P., Gaestel M.
    FEBS Lett. 313:307-313(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-15; SER-78 AND SER-82 BY MAPKAPK2.
  21. "Small heat shock proteins are molecular chaperones."
    Jakob U., Gaestel M., Engel K., Buchner J.
    J. Biol. Chem. 268:1517-1520(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY MAPKAPK2.
  22. "A comparison of the substrate specificity of MAPKAP kinase-2 and MAPKAP kinase-3 and their activation by cytokines and cellular stress."
    Clifton A.D., Young P.R., Cohen P.
    FEBS Lett. 392:209-214(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-15; SER-78 AND SER-82.
  23. "Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation."
    Rogalla T., Ehrnsperger M., Preville X., Kotlyarov A., Lutsch G., Ducasse C., Paul C., Wieske M., Arrigo A.P., Buchner J., Gaestel M.
    J. Biol. Chem. 274:18947-18956(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-15; SER-78 AND SER-82, MUTAGENESIS OF SER-15; SER-78 AND SER-82.
  24. "Identification and characterization of a novel protein from Sertoli cells, PASS1, that associates with mammalian small stress protein hsp27."
    Liu C., Gilmont R.R., Benndorf R., Welsh M.J.
    J. Biol. Chem. 275:18724-18731(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSPBAP1.
  25. "Heat shock protein 27 is associated with freedom from graft vasculopathy after human cardiac transplantation."
    De Souza A.I., Wait R., Mitchell A.G., Banner N.R., Dunn M.J., Rose M.L.
    Circ. Res. 97:192-198(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-78 AND SER-82, IDENTIFICATION BY MASS SPECTROMETRY.
  26. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-65, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection."
    Leong W.F., Chow V.T.
    Cell. Microbiol. 8:565-580(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, IDENTIFICATION BY MASS SPECTROMETRY.
  28. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  29. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  30. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  31. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  32. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  33. "HSPB7 is a SC35 speckle resident small heat shock protein."
    Vos M.J., Kanon B., Kampinga H.H.
    Biochim. Biophys. Acta 1793:1343-1353(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  34. "PKA-induced F-actin rearrangement requires phosphorylation of Hsp27 by the MAPKAP kinase MK5."
    Kostenko S., Johannessen M., Moens U.
    Cell. Signal. 21:712-718(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-78 AND SER-82.
  35. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  36. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  37. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-65; SER-78; SER-82 AND SER-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  38. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  39. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  40. Cited for: VARIANTS CMT2F PHE-135 AND TRP-136, VARIANTS HMN2B TRP-127; PHE-135; ILE-151 AND LEU-182.
  41. "The mutational spectrum in a cohort of Charcot-Marie-Tooth disease type 2 among the Han Chinese in Taiwan."
    Lin K.P., Soong B.W., Yang C.C., Huang L.W., Chang M.H., Lee I.H., Antonellis A., Lee Y.C.
    PLoS ONE 6:E29393-E29393(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT CMT2F ALA-164.

Entry informationi

Entry nameiHSPB1_HUMAN
AccessioniPrimary (citable) accession number: P04792
Secondary accession number(s): B2R4N8
, Q6FI47, Q96C20, Q96EI7, Q9UC31, Q9UC34, Q9UC35, Q9UC36
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: September 26, 2001
Last modified: November 26, 2014
This is version 183 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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