P04792 (HSPB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	HSPB1
Synonyms:	HSP27, HSP28

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	205 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Cytoplasm › cytoskeleton › spindle. 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 regeneration 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 Distal hereditary motor neuronopathy 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 process	Stress response
Cellular component	Cytoplasm Cytoskeleton Nucleus
Disease	Charcot-Marie-Tooth disease Disease mutation Neurodegeneration Neuropathy
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell death Inferred from electronic annotation. Source: UniProtKB-KW cellular component movement Traceable author statement PubMed 16130169. Source: UniProtKB gene expression Traceable author statement. Source: Reactome intracellular protein kinase cascade 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 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 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 cascade 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
Cellular_component	Z disc Inferred from electronic annotation. Source: Compara cell surface Inferred from direct assay PubMed 12493773. Source: UniProtKB cytoskeleton Traceable author statement PubMed 16130169. Source: UniProtKB cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay Ref.33. Source: UniProtKB plasma membrane Inferred from electronic annotation. Source: Compara proteasome complex Inferred from sequence or structural similarity. Source: BHF-UCL spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	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 ubiquitin binding Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DAXX	Q9UER7	3	EBI-352682,EBI-77321
HSPB8	Q9UJY1	3	EBI-352682,EBI-739074
MAPKAPK2	P49137	2	EBI-352682,EBI-993299
MAPKAPK3	Q16644	2	EBI-352682,EBI-1384657
MAPKAPK5	Q8IW41	2	EBI-352682,EBI-1201460
MME	P08473	4	EBI-352682,EBI-353759

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 205

205

Heat shock protein beta-1

PRO_0000125927

Regions

Region

70 – 205

136

Interaction with TGFB1I1 By similarity

Amino acid modifications

Modified residue

15

1

Phosphoserine; by MAPKAPK2 and MAPKAPK3 Ref.20 Ref.22 Ref.23 Ref.26 Ref.30 Ref.31 Ref.37

Modified residue

26

1

Phosphoserine By similarity

Modified residue

65

1

Phosphoserine Ref.26 Ref.37

Modified residue

78

1

Phosphoserine; by MAPKAPK2, MAPKAPK3 and MAPKAPK5 Ref.17 Ref.20 Ref.22 Ref.23 Ref.25 Ref.34 Ref.37

Modified residue

82

1

Phosphoserine; 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 residue

83

1

Phosphoserine Ref.28

Modified residue

123

1

N6-acetyllysine Ref.36

Modified residue

199

1

Phosphoserine Ref.31 Ref.32 Ref.37

Natural variations

Natural variant

127

1

R → W in HMN2B. Ref.40

VAR_018506

Natural variant

135

1

S → F in CMT2F and HMN2B. Ref.40

VAR_018507

Natural variant

136

1

R → W in CMT2F. Ref.40

VAR_018508

Natural variant

151

1

T → I in HMN2B. Ref.40

VAR_018509

Natural variant

164

1

T → A in CMT2F. Ref.41

VAR_067085

Natural variant

182

1

P → L in HMN2B. Ref.40

VAR_018510

Experimental info

Mutagenesis

15

1

S → D: Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-78 and D-82. Ref.23

Mutagenesis

78

1

S → D: Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-15 and D-82. Ref.23

Mutagenesis

82

1

S → D: Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-15 and D-78. Ref.23

Sequence conflict

10

1

L → I AA sequence Ref.13

Sequence conflict

109

1

L → R in AAH12292. Ref.12

Sequence conflict

121

1

T → S in AAH12292. Ref.12

Sequence conflict

127

1

R → L in AAH12292. Ref.12

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

205

Helix Strand Turn

Details...

Beta strand

94 – 100

7

Turn

102 – 104

3

Beta strand

107 – 114

8

Beta strand

117 – 124

8

Beta strand

136 – 143

8

Helix

150 – 152

3

Beta strand

154 – 157

4

Beta strand

161 – 168

8

Sequences

	Sequence		Length	Mass (Da)
	P04792 [UniParc]. Last modified September 26, 2001. Version 2. Checksum: 1B4DC44A6F6606D5	FASTA	205	22,783
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, 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, 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, MASS SPECTROMETRY. 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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. , 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.

Web resources

Inherited peripheral neuropathies mutation db

GeneReviews

NIEHS SNPs

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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.

IPI

IPI00025512.

PIR

HHHU27. S12102.

RefSeq

NP_001531.1. NM_001540.3.

UniGene

Hs.520973.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3Q9P	X-ray	2.00	A	90-171	[»]
3Q9Q	X-ray	2.20	A/B	90-171	[»]

ProteinModelPortal

P04792.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-412N.

IntAct

P04792. 40 interactions.

MINT

MINT-1368692.

PTM databases

PhosphoSite

P04792.

Polymorphism databases

DMDM

19855073.

2D gel databases

DOSAC-COBS-2DPAGE

P04792.

OGP

P04792.

REPRODUCTION-2DPAGE

IPI00025512.
P04792.

SWISS-2DPAGE

P04792.

UCD-2DPAGE

P04792.

Proteomic databases

PaxDb

P04792.

PeptideAtlas

P04792.

PRIDE

P04792.

Protocols and materials databases

DNASU

3315.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000248553; ENSP00000248553; ENSG00000106211.

GeneID

3315.

KEGG

hsa:3315.

UCSC

uc003uew.3. human.

Organism-specific databases

CTD

3315.

GeneCards

GC07P075931.

HGNC

HGNC:5246. HSPB1.

HPA

CAB004439.
CAB047331.
HPA000497.

MIM

602195. gene.
606595. phenotype.
608634. phenotype.

neXtProt

NX_P04792.

Orphanet

99940. Autosomal dominant Charcot-Marie-Tooth disease type 2F.
139525. Distal hereditary motor neuropathy type 2.

PharmGKB

PA29511.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG307785.

HOVERGEN

HBG054766.

InParanoid

P04792.

KO

K04455.

OMA

RTPSWDP.

OrthoDB

EOG4DR9DF.

PhylomeDB

P04792.

Enzyme and pathway databases

Pathway_Interaction_DB

p38_mk2pathway. p38 signaling mediated by MAPKAP kinases.
vegfr1_2_pathway. Signaling events mediated by VEGFR1 and VEGFR2.
p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.

Reactome

REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

P04792.

Bgee

P04792.

CleanEx

HS_HSPB1.

Genevestigator

P04792.

Family and domain databases

InterPro

IPR002068. a-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR008978. HSP20-like_chaperone.
[Graphical view]

Pfam

PF00011. HSP20. 1 hit.
[Graphical view]

PIRSF

PIRSF036514. Sm_HSP_B1. 1 hit.

PRINTS

PR00299. ACRYSTALLIN.

SUPFAM

SSF49764. HSP20_chap. 1 hit.

PROSITE

PS01031. HSP20. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P04792.

ChEMBL

CHEMBL5976.

ChiTaRS

HSPB1. human.

GenomeRNAi

3315.

NextBio

13148.

SOURCE

Search...

Entry information

Entry name

HSPB1_HUMAN

Accession

Primary (citable) accession number: P04792
Secondary accession number(s): B2R4N8 , 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:	May 29, 2013
This is version 166 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.