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P04792 (HSPB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 176. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:HSPB1
Synonyms:HSP27, HSP28
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in stress resistance and actin organization.

Subunit structure

Interacts with TGFB1I1 By similarity. Associates with alpha- and beta-tubulin, microtubules and CRYAB. Interacts with HSPB8 and HSPBAP1. Ref.3 Ref.24

Subcellular location

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. Ref.3 Ref.33

Tissue specificity

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. Ref.16

Induction

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). Ref.27

Post-translational modification

Phosphorylated in MCF-7 cells on exposure to protein kinase C activators and heat shock. Ref.14 Ref.15 Ref.17 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.34

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.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.40 Ref.41

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.40

Sequence similarities

Belongs to the small heat shock protein (HSP20) family.

Sequence caution

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

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

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

Ontologies

Keywords
   Biological processStress response
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   DiseaseCharcot-Marie-Tooth disease
Disease mutation
Neurodegeneration
Neuropathy
   Molecular functionChaperone
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cellular component movement

Traceable author statement PubMed 16130169. Source: UniProtKB

cellular response to vascular endothelial growth factor stimulus

Inferred from mutant phenotype PubMed 18440775. Source: BHF-UCL

gene expression

Traceable author statement. Source: Reactome

intracellular signal transduction

Inferred from mutant phenotype PubMed 18440775. Source: BHF-UCL

mRNA metabolic process

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Traceable author statement PubMed 16130169. Source: UniProtKB

negative regulation of intrinsic apoptotic signaling pathway in response to oxidative stress

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of protein kinase activity

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of protein serine/threonine kinase activity

Inferred from sequence or structural similarity. Source: GOC

positive regulation of angiogenesis

Inferred from mutant phenotype PubMed 18440775. Source: BHF-UCL

positive regulation of blood vessel endothelial cell migration

Inferred from mutant phenotype PubMed 18440775. Source: BHF-UCL

positive regulation of endothelial cell chemotaxis

Inferred from mutant phenotype PubMed 18440775. Source: BHF-UCL

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

Inferred from mutant phenotype PubMed 18440775. Source: BHF-UCL

positive regulation of interleukin-1 beta production

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of tumor necrosis factor biosynthetic process

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of translational initiation

Traceable author statement PubMed 10859165. Source: ProtInc

response to unfolded protein

Non-traceable author statement Ref.16. Source: UniProtKB

response to virus

Inferred from expression pattern Ref.27. Source: UniProtKB

retina homeostasis

Inferred from expression pattern PubMed 23580065. Source: UniProt

   Cellular_componentZ disc

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.33. Source: UniProtKB

cytoskeleton

Traceable author statement PubMed 16130169. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 22664934PubMed 23580065. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708. Source: UniProt

nucleus

Inferred from direct assay Ref.33. Source: UniProtKB

plasma membrane

Inferred from electronic annotation. Source: Ensembl

proteasome complex

Inferred from sequence or structural similarity. Source: BHF-UCL

spindle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionidentical protein binding

Inferred from physical interaction PubMed 11003656PubMed 22365833. Source: IntAct

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein kinase C binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein kinase C inhibitor activity

Inferred from sequence or structural similarity. Source: BHF-UCL

protein kinase binding

Inferred from physical interaction Ref.22. Source: UniProtKB

ubiquitin binding

Inferred from sequence or structural similarity. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 205205Heat shock protein beta-1
PRO_0000125927

Regions

Region70 – 205136Interaction with TGFB1I1 By similarity

Amino acid modifications

Modified residue151Phosphoserine; by MAPKAPK2 and MAPKAPK3 Ref.20 Ref.22 Ref.23 Ref.26 Ref.30 Ref.31 Ref.37
Modified residue261Phosphoserine By similarity
Modified residue651Phosphoserine Ref.26 Ref.37
Modified residue781Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5 Ref.17 Ref.20 Ref.22 Ref.23 Ref.25 Ref.34 Ref.37
Modified residue821Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5 Ref.14 Ref.17 Ref.20 Ref.22 Ref.23 Ref.25 Ref.28 Ref.32 Ref.34 Ref.37 Ref.39
Modified residue831Phosphoserine Ref.28
Modified residue861Phosphoserine By similarity
Modified residue1231N6-acetyllysine Ref.36
Modified residue1991Phosphoserine Ref.31 Ref.32 Ref.37

Natural variations

Natural variant1271R → W in HMN2B. Ref.40
VAR_018506
Natural variant1351S → F in CMT2F and HMN2B. Ref.40
VAR_018507
Natural variant1361R → W in CMT2F. Ref.40
VAR_018508
Natural variant1511T → I in HMN2B. Ref.40
VAR_018509
Natural variant1641T → A in CMT2F. Ref.41
VAR_067085
Natural variant1821P → L in HMN2B. Ref.40
VAR_018510

Experimental info

Mutagenesis151S → D: Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-78 and D-82. Ref.23
Mutagenesis781S → D: Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-15 and D-82. Ref.23
Mutagenesis821S → D: Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-15 and D-78. Ref.23
Sequence conflict101L → I AA sequence Ref.13
Sequence conflict1091L → R in AAH12292. Ref.12
Sequence conflict1211T → S in AAH12292. Ref.12
Sequence conflict1271R → L in AAH12292. Ref.12

Secondary structure

................. 205
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04792 [UniParc].

Last modified September 26, 2001. Version 2.
Checksum: 1B4DC44A6F6606D5

FASTA20522,783
        10         20         30         40         50         60 
MTERRVPFSL LRGPSWDPFR DWYPHSRLFD QAFGLPRLPE EWSQWLGGSS WPGYVRPLPP 

        70         80         90        100        110        120 
AAIESPAVAA PAYSRALSRQ LSSGVSEIRH TADRWRVSLD VNHFAPDELT VKTKDGVVEI 

       130        140        150        160        170        180 
TGKHEERQDE HGYISRCFTR KYTLPPGVDP TQVSSSLSPE GTLTVEAPMP KLATQSNEIT 

       190        200 
IPVTFESRAQ LGGPEAAKSD ETAAK 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy."
Evgrafov O.V., Mersiyanova I., Irobi J., Van Den Bosch L., Dierick I., Leung C.L., Schagina O., Verpoorten N., Van Impe K., Fedotov V., Dadali E., Auer-Grumbach M., Windpassinger C., Wagner K., Mitrovic Z., Hilton-Jones D., Talbot K., Martin J.-J. expand/collapse author list , Vasserman N., Tverskaya S., Polyakov A., Liem R.K.H., Gettemans J., Robberecht W., De Jonghe P., Timmerman V.
Nat. Genet. 36:602-606(2004) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRHHHU27. S12102.
RefSeqNP_001531.1. NM_001540.3.
UniGeneHs.520973.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3Q9PX-ray2.00A90-171[»]
3Q9QX-ray2.20A/B90-171[»]
ProteinModelPortalP04792.
SMRP04792. Positions 18-188.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109547. 90 interactions.
DIPDIP-412N.
IntActP04792. 58 interactions.
MINTMINT-1368692.

Chemistry

BindingDBP04792.
ChEMBLCHEMBL5976.

PTM databases

PhosphoSiteP04792.

Polymorphism databases

DMDM19855073.

2D gel databases

DOSAC-COBS-2DPAGEP04792.
OGPP04792.
REPRODUCTION-2DPAGEIPI00025512.
P04792.
SWISS-2DPAGEP04792.
UCD-2DPAGEP04792.

Proteomic databases

PaxDbP04792.
PeptideAtlasP04792.
PRIDEP04792.

Protocols and materials databases

DNASU3315.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000248553; ENSP00000248553; ENSG00000106211.
GeneID3315.
KEGGhsa:3315.
UCSCuc003uew.3. human.

Organism-specific databases

CTD3315.
GeneCardsGC07P075931.
HGNCHGNC:5246. HSPB1.
HPACAB004439.
CAB047330.
CAB047331.
CAB047332.
HPA000497.
MIM602195. gene.
606595. phenotype.
608634. phenotype.
neXtProtNX_P04792.
Orphanet99940. Autosomal dominant Charcot-Marie-Tooth disease type 2F.
139525. Distal hereditary motor neuropathy type 2.
PharmGKBPA29511.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG307785.
HOVERGENHBG054766.
InParanoidP04792.
KOK04455.
OMARTPSWDP.
OrthoDBEOG7WHHBK.
PhylomeDBP04792.
TreeFamTF105049.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP04792.
BgeeP04792.
CleanExHS_HSPB1.
GenevestigatorP04792.

Family and domain databases

Gene3D2.60.40.790. 2 hits.
InterProIPR002068. a-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PfamPF00011. HSP20. 1 hit.
[Graphical view]
PIRSFPIRSF036514. Sm_HSP_B1. 1 hit.
PRINTSPR00299. ACRYSTALLIN.
SUPFAMSSF49764. SSF49764. 1 hit.
PROSITEPS01031. HSP20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHSPB1. human.
GeneWikiHsp27.
GenomeRNAi3315.
NextBio13148.
PROP04792.
SOURCESearch...

Entry information

Entry nameHSPB1_HUMAN
AccessionPrimary (citable) accession number: P04792
Secondary accession number(s): B2R4N8 expand/collapse secondary AC list , Q6FI47, Q96C20, Q96EI7, Q9UC31, Q9UC34, Q9UC35, Q9UC36
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: September 26, 2001
Last modified: April 16, 2014
This is version 176 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM