Reviewed, UniProtKB/Swiss-Prot P04792 (HSPB1_HUMAN)

Names and origin

Protein names

Recommended name:
    Heat shock protein beta-1
      Short name=HspB1
Alternative name(s):
    Heat shock 27 kDa protein
    HSP 27
    Stress-responsive protein 27
      Short name=SRP27
    Estrogen-regulated 24 kDa protein
    28 kDa heat shock protein

Gene names

Name:	HSPB1
Synonyms:	HSP27, HSP28

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	205 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Subcellular location	Cytoplasm. Nucleus. Spindle. Note: Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells. Translocates to the nucleus during heat shock. Ref.3
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.14
Induction	Expressed in response to environmental stresses such as heat shock, or estrogen stimulation in MCF-7 cells.
Post-translational modification	Phosphorylated in MCF-7 cells on exposure to protein kinase C activators and heat shock. Ref.12 Ref.13 Ref.15 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30
Involvement in disease	Defects in HSPB1 are the cause of Charcot-Marie-Tooth disease type 2F (CMT2F) [MIM:606595]. CMT2F is a form of Charcot-Marie-Tooth disease, the most common inherited disorder of the peripheral nervous system. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathy or CMT1, and primary peripheral axonal neuropathy or 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. CMT2F onset is between 15 and 25 years with muscle weakness and atrophy usually beginning in feet and legs (peroneal distribution). Upper limb involvement occurs later. CMT2F inheritance is autosomal dominant. Ref.32 Defects in HSPB1 are a cause of distal hereditary motor neuronopathy type 2B (HMN2B) [MIM:608634]. Distal hereditary motor neuronopathies constitute a heterogeneous group of neuromuscular disorders caused by selective impairment 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. Ref.32
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 Nucleus
Disease	Charcot-Marie-Tooth disease Disease mutation Neurodegeneration Neuropathy
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	anti-apoptosis Traceable author statement. Source: UniProtKB cell death Inferred from electronic annotation. Source: UniProtKB-KW cell motion Traceable author statement. Source: UniProtKB regulation of translational initiation Traceable author statement. Source: ProtInc response to heat Inferred from electronic annotation. Source: InterPro response to unfolded protein Traceable author statement. Source: ProtInc
Cellular component	cell surface Inferred from direct assay. Source: UniProtKB cytoplasm Traceable author statement. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	identical protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		1	EBI-352682,EBI-352682
DAXX	Q9UER7	1	EBI-352682,EBI-77321
HSPB1	P15991	1	EBI-352682,EBI-1559114	From a different organism.
HSPB8	Q9UJY1	1	EBI-352682,EBI-739074
ILK	Q13418	1	EBI-352682,EBI-747644
MAGED1	Q9Y5V3	1	EBI-352682,EBI-716006
Mapkapk5	O54992	1	EBI-352682,EBI-1202132	From a different organism.
MME	P08473	1	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 Ref.22 Ref.24 Ref.25 Ref.28 Ref.29 Ref.30
	Modified residue	26	1	Phosphoserine By similarity
	Modified residue	65	1	Phosphoserine Ref.22 Ref.29
	Modified residue	78	1	Phosphoserine Ref.15 Ref.20
	Modified residue	82	1	Phosphoserine Ref.12 Ref.15 Ref.20 Ref.21 Ref.22 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30
	Modified residue	83	1	Phosphoserine Ref.19 Ref.24
	Modified residue	123	1	N6-acetyllysine Ref.23
	Modified residue	199	1	Phosphoserine Ref.29 Ref.30
Natural variations
	Natural variant	127	1	R → W in HMN2B. Ref.32		VAR_018506
	Natural variant	135	1	S → F in CMT2F and HMN2B.		VAR_018507
	Natural variant	136	1	R → W in CMT2F. Ref.32		VAR_018508
	Natural variant	151	1	T → I in HMN2B. Ref.32		VAR_018509
	Natural variant	182	1	P → L in HMN2B. Ref.32		VAR_018510
Experimental info
	Sequence conflict	10	1	L → I AA sequence Ref.11
	Sequence conflict	109	1	L → R in AAH12292. Ref.10
	Sequence conflict	121	1	T → S in AAH12292. Ref.10
	Sequence conflict	127	1	R → L in AAH12292. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	P04792-1 [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: 3714473] [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: 2243808] [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: 10777697] [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: 9110174] [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]	NIEHS SNPs program Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]	"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: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung, Ovary, Pancreas, Skin and Uterus.
[11]	"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: 2295696] [Abstract] Cited for: PROTEIN SEQUENCE OF 5-12; 97-112; 141-154 AND 172-188.
[12]	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.
[13]	"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: 8325890] [Abstract] Cited for: PROTEIN SEQUENCE OF 13-20; 38-46; 97-110; 141-154 AND 172-186, PHOSPHORYLATION. Tissue: Mammary carcinoma.
[14]	"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: 1560006] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-59; 93-98; 129-134 AND 178-193, ASSOCIATION WITH CRYAB, TISSUE SPECIFICITY. Tissue: Pectoralis muscle.
[15]	"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: 1730670] [Abstract] Cited for: PROTEIN SEQUENCE OF 76-89, PHOSPHORYLATION AT SER-78 AND SER-82.
[16]	"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: 2743305] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 109-205. Tissue: Mammary carcinoma.
[17]	"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: 1763035] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 122-205.
[18]	"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: 10751411] [Abstract] Cited for: INTERACTION WITH HSPBAP1.
[19]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY. Tissue: Epithelium.
[20]	"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: 15976317] [Abstract] Cited for: PHOSPHORYLATION AT SER-78 AND SER-82, MASS SPECTROMETRY.
[21]	"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC." Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J. Proteomics 5:3589-3599(2005) [PubMed: 16097034] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, MASS SPECTROMETRY. Tissue: Hepatocyte.
[22]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-65 AND SER-82, MASS SPECTROMETRY. Tissue: Epithelium.
[23]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123, MASS SPECTROMETRY. Tissue: Epithelium.
[24]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-82 AND SER-83, MASS SPECTROMETRY. Tissue: Epithelium.
[25]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-82, MASS SPECTROMETRY. Tissue: Epithelium.
[26]	"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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, MASS SPECTROMETRY. Tissue: Epithelium.
[27]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, MASS SPECTROMETRY.
[28]	"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: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-82, MASS SPECTROMETRY. Tissue: Platelet.
[29]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-65; SER-82 AND SER-199, MASS SPECTROMETRY.
[30]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-82 AND SER-199, MASS SPECTROMETRY.
[31]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[32]	"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: 15122254] [Abstract] Cited for: VARIANTS CMT2F PHE-135 AND TRP-136, VARIANTS HMN2B TRP-127; PHE-135; ILE-151 AND LEU-182.
+	Additional computationally mapped references.

Web resources

Inherited peripheral neuropathies mutation db

GeneReviews

NIEHS SNPs

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. DQ379985 Genomic DNA. Translation: ABC88475.1. AC006388 Genomic DNA. No translation available. 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.
UniGene	Hs.520973
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:412N.
IntAct	P04792. 24 interactions.
PTM databases
PhosphoSite	P04792.
2-D gel databases
SWISS-2DPAGE	P04792.
Aarhus/Ghent-2DPAGE	4110. IEF. 5102. IEF. 6104. IEF.
Cornea-2DPAGE	P04792.
DOSAC-COBS-2DPAGE	P04792.
HSC-2DPAGE	P04792.
OGP	P04792.
REPRODUCTION-2DPAGE	IPI00025512. P04792.
Proteomic databases
PeptideAtlas	P04792.
PRIDE	P04792.
Genome annotation databases
Ensembl	ENSG00000106211. Homo sapiens. [Contig view]
GeneID	3315.
KEGG	hsa:3315.
UCSC	uc003uew.1. human.
Organism-specific databases
GeneCards	GC07P075769.
H-InvDB	HIX0006788.
HGNC	HGNC:5246. HSPB1.
HPA	CAB002061. CAB004439. HPA000497.
MIM	602195. gene. 606595. phenotype. 608634. phenotype.
Orphanet	64746. Autosomal dominant Charcot-Marie-Tooth disease, type 2. 99940. Autosomal dominant Charcot-Marie-Tooth disease, type 2F. 139525. Distal hereditary motor neuropathy, type 2.
PharmGKB	PA29511.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P04792.
HOVERGEN	P04792.
OMA	P04792. VTFEARA.
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.
Gene expression databases
ArrayExpress	P04792.
Bgee	P04792.
CleanEx	HS_HSPB1.
Family and domain databases
InterPro	IPR001436. Alpha-crystallin/HSP. IPR002068. Hsp20. [Graphical view]
Pfam	PF00011. HSP20. 1 hit. [Graphical view]
PRINTS	PR00299. ACRYSTALLIN.
PROSITE	PS01031. HSP20. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	13148.
SOURCE	Search...

Entry information

Entry name

HSPB1_HUMAN

Accession

Primary (citable) accession number: P04792
Secondary accession number(s): 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:	July 7, 2009
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)