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Reviewed, UniProtKB/Swiss-Prot P04792 (HSPB1_HUMAN)

Last modified July 7, 2009. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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.

Binary interactions

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 Ref.22 Ref.24 Ref.25 Ref.28 Ref.29 Ref.30
Modified residue261Phosphoserine By similarity
Modified residue651Phosphoserine Ref.22 Ref.29
Modified residue781Phosphoserine Ref.15 Ref.20
Modified residue821Phosphoserine 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 residue831Phosphoserine Ref.19 Ref.24
Modified residue1231N6-acetyllysine Ref.23
Modified residue1991Phosphoserine Ref.29 Ref.30

Natural variations

Natural variant1271R → W in HMN2B. Ref.32
VAR_018506
Natural variant1351S → F in CMT2F and HMN2B.
VAR_018507
Natural variant1361R → W in CMT2F. Ref.32
VAR_018508
Natural variant1511T → I in HMN2B. Ref.32
VAR_018509
Natural variant1821P → L in HMN2B. Ref.32
VAR_018510

Experimental info

Sequence conflict101L → I AA sequence Ref.11
Sequence conflict1091L → R in AAH12292. Ref.10
Sequence conflict1211T → S in AAH12292. Ref.10
Sequence conflict1271R → L in AAH12292. Ref.10

Sequences

Sequence LengthMass (Da)Tools
P04792-1 [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: 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. 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: 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. 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: 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.

Cross-references

Sequence databases

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.
IPIIPI00025512.
PIRHHHU27. S12102.
RefSeqNP_001531.1.
UniGeneHs.520973

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

DIPDIP:412N.
IntActP04792. 24 interactions.

PTM databases

PhosphoSiteP04792.

2-D gel databases

SWISS-2DPAGEP04792.
Aarhus/Ghent-2DPAGE4110. IEF.
5102. IEF.
6104. IEF.
Cornea-2DPAGEP04792.
DOSAC-COBS-2DPAGEP04792.
HSC-2DPAGEP04792.
OGPP04792.
REPRODUCTION-2DPAGEIPI00025512.
P04792.

Proteomic databases

PeptideAtlasP04792.
PRIDEP04792.

Genome annotation databases

EnsemblENSG00000106211. Homo sapiens. [Contig view]
GeneID3315.
KEGGhsa:3315.
UCSCuc003uew.1. human.

Organism-specific databases

GeneCardsGC07P075769.
H-InvDBHIX0006788.
HGNCHGNC:5246. HSPB1.
HPACAB002061.
CAB004439.
HPA000497.
MIM602195. gene.
606595. phenotype.
608634. phenotype.
Orphanet64746. Autosomal dominant Charcot-Marie-Tooth disease, type 2.
99940. Autosomal dominant Charcot-Marie-Tooth disease, type 2F.
139525. Distal hereditary motor neuropathy, type 2.
PharmGKBPA29511.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP04792.
HOVERGENP04792.
OMAP04792. VTFEARA.

Enzyme and pathway databases

Pathway_Interaction_DBp38_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

ArrayExpressP04792.
BgeeP04792.
CleanExHS_HSPB1.

Family and domain databases

InterProIPR001436. Alpha-crystallin/HSP.
IPR002068. Hsp20.
[Graphical view]
PfamPF00011. HSP20. 1 hit.
[Graphical view]
PRINTSPR00299. ACRYSTALLIN.
PROSITEPS01031. HSP20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio13148.
SOURCESearch...

Entry information

Entry nameHSPB1_HUMAN
AccessionPrimary (citable) accession number: P04792
Secondary accession number(s): Q6FI47 expand/collapse secondary AC list , 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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 7

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents