[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1093/nar/14.10.4127; PubMed=3714473 [NCBI, ExPASy, EBI, Israel, Japan] Hickey E., Brandon S.E., Potter R., Stein G., Stein J., Weber L.A.; "Sequence and organization of genes encoding the human 27 kDa heat shock protein."; Nucleic Acids Res. 14:4127-4145(1986).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Lung; DOI=10.1093/nar/18.21.6457; PubMed=2243808 [NCBI, ExPASy, EBI, Israel, Japan] Carper S.W., Rocheleau T.A., Storm F.K.; "cDNA sequence of a human heat shock protein HSP27."; Nucleic Acids Res. 18:6457-6457(1990).
[3]	NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND SUBUNIT. TISSUE=Cervix carcinoma; DOI=10.1006/bbrc.2000.2553; PubMed=10777697 [NCBI, ExPASy, EBI, Israel, Japan] Hino M., Kurogi K., Okubo M.-A., Murata-Hori M., Hosoya H.; "Small heat shock protein 27 (HSP27) associates with tubulin/microtubules in HeLa cells."; Biochem. Biophys. Res. Commun. 271:164-169(2000).
[4]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Mammary carcinoma; Briolay J., Chareyron P., Mehlen P., Arrigo A.; "Identification of a new cDNA sequence from human breast carcinoma cells encoding the 28kDa heat shock protein."; Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Brain; PubMed=9110174 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Large-scale concatenation cDNA sequencing."; Genome Res. 7:353-358(1997).
[6]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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.; "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."; Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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.; "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[8]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. NIEHS SNPs program; Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
[9]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature01782; PubMed=12853948 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The DNA sequence of human chromosome 7."; Nature 424:157-164(2003).
[10]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Lung, Ovary, Pancreas, Skin, and Uterus; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[11]	PROTEIN SEQUENCE OF 5-12; 97-112; 141-154 AND 172-188. PubMed=2295696 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Identification of two related markers for common acute lymphoblastic leukemia as heat shock proteins."; J. Clin. Invest. 85:200-207(1990).
[12]	PROTEIN SEQUENCE OF 13-20; 38-46; 97-110; 141-154 AND 172-186, AND PHOSPHORYLATION. TISSUE=Mammary carcinoma; PubMed=8325890 [NCBI, ExPASy, EBI, Israel, Japan] Faucher C., Capdevielle J., Canal I., Ferrara P., Mazarguil H., McGuire W.L., Darbon J.-M.; "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."; J. Biol. Chem. 268:15168-15173(1993).
[13]	PROTEIN SEQUENCE OF 21-59; 93-98; 129-134 AND 178-193, ASSOCIATION WITH CRYAB, AND TISSUE SPECIFICITY. TISSUE=Pectoralis muscle; PubMed=1560006 [NCBI, ExPASy, EBI, Israel, Japan] Kato K., Shinohara H., Goto S., Inaguma Y., Morishita R., Asano T.; "Copurification of small heat shock protein with alpha B crystallin from human skeletal muscle."; J. Biol. Chem. 267:7718-7725(1992).
[14]	PROTEIN SEQUENCE OF 76-89, AND PHOSPHORYLATION AT SER-78 AND SER-82. PubMed=1730670 [NCBI, ExPASy, EBI, Israel, Japan] Landry J., Lambert H., Zhou M., Lavoie J.N., Hickey E., Weber L.A., Anderson C.W.; "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."; J. Biol. Chem. 267:794-803(1992).
[15]	NUCLEOTIDE SEQUENCE [MRNA] OF 109-205. TISSUE=Mammary carcinoma; PubMed=2743305 [NCBI, ExPASy, EBI, Israel, Japan] Fuqua S.A.W., Blum-Salingaros M., McGuire W.L.; "Induction of the estrogen-regulated '24K' protein by heat shock."; Cancer Res. 49:4126-4129(1989).
[16]	NUCLEOTIDE SEQUENCE [MRNA] OF 122-205. PubMed=1763035 [NCBI, ExPASy, EBI, Israel, Japan] Mendelsohn M.E., Zhu Y., O'Neill S.; "The 29-kDa proteins phosphorylated in thrombin-activated human platelets are forms of the estrogen receptor-related 27-kDa heat shock protein."; Proc. Natl. Acad. Sci. U.S.A. 88:11212-11216(1991).
[17]	INTERACTION WITH HSPBAP1. DOI=10.1074/jbc.M001981200; PubMed=10751411 [NCBI, ExPASy, EBI, Israel, Japan] Liu C., Gilmont R.R., Benndorf R., Welsh M.J.; "Identification and characterization of a novel protein from Sertoli cells, PASS1, that associates with mammalian small stress protein hsp27."; J. Biol. Chem. 275:18724-18731(2000).
[18]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0404720101; PubMed=15302935 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.; "Large-scale characterization of HeLa cell nuclear phosphoproteins."; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
[19]	PHOSPHORYLATION AT SER-78 AND SER-82, AND MASS SPECTROMETRY. DOI=10.1161/01.RES.0000174815.10996.08; PubMed=15976317 [NCBI, ExPASy, EBI, Israel, Japan] De Souza A.I., Wait R., Mitchell A.G., Banner N.R., Dunn M.J., Rose M.L.; "Heat shock protein 27 is associated with freedom from graft vasculopathy after human cardiac transplantation."; Circ. Res. 97:192-198(2005).
[20]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND MASS SPECTROMETRY. TISSUE=Hepatocyte; DOI=10.1002/pmic.200401217; PubMed=16097034 [NCBI, ExPASy, EBI, Israel, Japan] Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J.; "Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC."; Proteomics 5:3589-3599(2005).
[21]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-65 AND SER-82, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[22]	ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.molcel.2006.06.026; PubMed=16916647 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey."; Mol. Cell 23:607-618(2006).
[23]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-82 AND SER-83, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan] Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."; Nat. Biotechnol. 24:1285-1292(2006).
[24]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-82, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0507066103; PubMed=16565220 [NCBI, ExPASy, EBI, Israel, Japan] Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; "Phosphoproteome analysis of the human mitotic spindle."; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
[25]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan] Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; "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."; J. Proteome Res. 6:4150-4162(2007).
[26]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND MASS SPECTROMETRY. DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan] Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Anal. Sci. 24:161-166(2008).
[27]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-82, AND MASS SPECTROMETRY. TISSUE=Platelet; DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan] Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.; "Phosphoproteome of resting human platelets."; J. Proteome Res. 7:526-534(2008).
[28]	VARIANTS CMT2F PHE-135 AND TRP-136, AND VARIANTS DHMN TRP-127; PHE-135; ILE-151 AND LEU-182. DOI=10.1038/ng1354; PubMed=15122254 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy."; Nat. Genet. 36:602-606(2004).

Comments

FUNCTION: Involved in stress resistance and actin organization.
SUBUNIT: Interacts with TGFB1I1 (By similarity). Associates with alpha- and beta-tubulin, microtubules and CRYAB. Interacts with HSPB8 and HSPBAP1.
INTERACTION:
Self; NbExp=1; IntAct=EBI-352682, EBI-352682;
Q9UER7:DAXX; NbExp=1; IntAct=EBI-352682, EBI-77321;
P15991:HSPB1 (xeno); NbExp=1; IntAct=EBI-352682, EBI-1559114;
Q9UJY1:HSPB8; NbExp=1; IntAct=EBI-352682, EBI-739074;
Q13418:ILK; NbExp=1; IntAct=EBI-352682, EBI-747644;
Q9Y5V3:MAGED1; NbExp=1; IntAct=EBI-352682, EBI-716006;
O54992:Mapkapk5 (xeno); NbExp=1; IntAct=EBI-352682, EBI-1202132;
P08473:MME; NbExp=1; IntAct=EBI-352682, EBI-353759;
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells. Translocates to the nucleus during heat shock.
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.
INDUCTION: Expressed in response to environmental stresses such as heat shock, or estrogen stimulation in MCF-7 cells.
PTM: Phosphorylated in MCF-7 cells on exposure to protein kinase C activators and heat shock.
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.
DISEASE: Defects in HSPB1 are a cause of distal hereditary motor neuropathy (dHMN) [MIM:608634]. Distal HMN is a pure motor peripheral neuropathy without sensory abnormalities.
SIMILARITY: Belongs to the small heat shock protein (HSP20) family.
SEQUENCE CAUTION:
- Sequence=AAA62175.1; Type=Frameshift; Positions=194;
- Sequence=AAB20722.1; Type=Frameshift; Positions=194;
- Sequence=CAA34498.1; Type=Frameshift; Positions=194;
WEB RESOURCE: Name=Inherited peripheral neuropathies mutation db; URL="http://www.molgen.ua.ac.be/CMTMutations/";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=HSPB1";.
WEB RESOURCE: Name=NIEHS SNPs; URL="http://egp.gs.washington.edu/data/hspb1/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

L39370; AAA62175.1; ALT_FRAME; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X54079; CAA38016.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z23090; CAA80636.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB020027; BAB17232.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U90906; AAB51056.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR407614; CAG28542.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CR536489; CAG38728.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019888; AAV38691.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ379985; ABC88475.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC006388; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
BC000510; AAH00510.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012292; AAH12292.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012768; AAH12768.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC014920; AAH14920.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC073768; AAH73768.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X16477; CAA34498.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S74571; AAB20722.1; ALT_FRAME; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

S12102; HHHU27.

NP_001531.1; -.

3D structure databases

ModBase

P04792.

Protein-protein interaction databases

DIP

DIP:412N; -.

IntAct

P04792; -.

PTM databases

PhosphoSite

P04792; -.

2D gel databases

SWISS-2DPAGE

P04792; -.

Aarhus/Ghent-2DPAGE

4110; IEF.
5102; IEF.
6104; IEF.

P04792; -.

P04792; -.

P04792; -.

P04792; -.

IPI00025512; -.
P04792; -.

Organism-specific databases

HIX0006788; -.

HGNC:5246; HSPB1.

CAB002061; -.
CAB004439; -.
HPA000497; -.

MIM

602195; gene. [NCBI / EBI]
606595; phenotype. [NCBI / EBI]
608634; phenotype. [NCBI / EBI]

Orphanet

64746; Charcot-Marie-Tooth disease, type 2, autosomal dominant.
99940; Charcot-Marie-Tooth disease, type 2F, autosomal dominant.
139525; Neuropathy, motor, distal, hereditary, type 2.

PharmGKB

PA29511; -.

GeneCards

P04792.

Gene expression databases

ArrayExpress

P04792; -.

CleanEx

HS_HSPB1; -.

Ontologies

GO:0009986;	Cellular component: cell surface (inferred from direct assay from UniProtKB).
GO:0005737;	Cellular component: cytoplasm (traceable author statement from UniProtKB).
GO:0005856;	Cellular component: cytoskeleton (traceable author statement from UniProtKB).
GO:0042802;	Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0006916;	Biological process: anti-apoptosis (traceable author statement from UniProtKB).
GO:0006928;	Biological process: cell motion (traceable author statement from UniProtKB).
GO:0006446;	Biological process: regulation of translational initiation (traceable author statement from ProtInc).
GO:0006986;	Biological process: response to unfolded protein (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR001436; Alpha-crystallin/HSP.
IPR002068; Hsp20.
Graphical view of domain structure.

Pfam

PF00011; HSP20; 1.
Pfam graphical view of domain structure.

PRINTS

PR00299; ACRYSTALLIN.

PROSITE

PS01031; HSP20; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

P04792; -.

Genome annotation databases

Ensembl

ENSG00000106211; Homo sapiens. [Contig view]

GeneID

3315; -.

KEGG

hsa:3315; -.

Phylogenomic databases

HOGENOM

P04792; -.

HOVERGEN

P04792; -.

Other

P04792; -.

13148; -.

HSPB1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Charcot-Marie-Tooth disease; Cytoplasm; Direct protein sequencing; Disease mutation; Nucleus; Phosphoprotein; Stress response.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 205`	`205`	`Heat shock protein beta-1.`	`PRO_0000125927`
`REGION`	`70 205`	`136`	`Interaction with TGFB1I1 (By similarity).`
`MOD_RES`	`15 15`		`Phosphoserine.`
`MOD_RES`	`26 26`		`Phosphoserine (By similarity).`
`MOD_RES`	`65 65`		`Phosphoserine.`
`MOD_RES`	`78 78`		`Phosphoserine.`
`MOD_RES`	`82 82`		`Phosphoserine.`
`MOD_RES`	`83 83`		`Phosphoserine.`
`MOD_RES`	`123 123`		`N6-acetyllysine.`
`VARIANT`	`127 127`	`1`	`R -> W (in dHMN).`	`VAR_018506`
`VARIANT`	`135 135`	`1`	`S -> F (in CMT2F and dHMN).`	`VAR_018507`
`VARIANT`	`136 136`	`1`	`R -> W (in CMT2F).`	`VAR_018508`
`VARIANT`	`151 151`	`1`	`T -> I (in dHMN).`	`VAR_018509`
`VARIANT`	`182 182`	`1`	`P -> L (in dHMN).`	`VAR_018510`
`CONFLICT`	`10 10`		`L -> I (in Ref. 11; AA sequence).`
`CONFLICT`	`109 109`		`L -> R (in Ref. 10; AAH12292).`
`CONFLICT`	`121 121`		`T -> S (in Ref. 10; AAH12292).`
`CONFLICT`	`127 127`		`R -> L (in Ref. 10; AAH12292).`

Sequence information

Length: 205 AA [This is the length of the unprocessed precursor]

Molecular weight: 22783 Da [This is the MW of the unprocessed precursor]

CRC64: 1B4DC44A6F6606D5 [This is a checksum on the sequence]

        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

P04792 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools