CPLM-002158

Genbank Nucleotide ID

Heat shock protein beta-1

Protein Synonyms/Alias

HspB1; 28 kDa heat shock protein; Estrogen-regulated 24 kDa protein; Heat shock 27 kDa protein; HSP 27; Stress-responsive protein 27; SRP27

Homo sapiens (Human)

Position	Peptide	Type	References
112	APDELTVKTKDGVVE	ubiquitination	[1, 2, 3]
114	DELTVKTKDGVVEIT	glycation	[4]
114	DELTVKTKDGVVEIT	ubiquitination	[1, 3, 5, 6]
123	GVVEITGKHEERQDE	acetylation	[7, 8, 9, 10]
123	GVVEITGKHEERQDE	glycation	[4]
123	GVVEITGKHEERQDE	ubiquitination	[1, 3]
141	ISRCFTRKYTLPPGV	ubiquitination	[3]
171	TVEAPMPKLATQSNE	ubiquitination	[1, 3]
198	LGGPEAAKSDETAAK	ubiquitination	[1, 3, 6, 11, 12]

[1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[4] Heat-shock protein 27 (Hsp27) as a target of methylglyoxal in gastrointestinal cancer.
Oya-Ito T, Naito Y, Takagi T, Handa O, Matsui H, Yamada M, Shima K, Yoshikawa T.
Biochim Biophys Acta. 2011 Jul;1812(7):769-81. [PMID: 21497196]
[5] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[7] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
[8] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[9] Proteome-wide prediction of acetylation substrates.
Basu A, Rose KL, Zhang J, Beavis RC, Ueberheide B, Garcia BA, Chait B, Zhao Y, Hunt DF, Segal E, Allis CD, Hake SB.
Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13785-90. [PMID: 19666589]
[10] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
[11] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[12] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]

Functional Description

Involved in stress resistance and actin organization.

REGION 70 205 Interaction with TGFB1I1 (By similarity).
MOD_RES 15 15 Phosphoserine; by MAPKAPK2 and MAPKAPK3.
MOD_RES 26 26 Phosphoserine (By similarity).
MOD_RES 65 65 Phosphoserine.
MOD_RES 78 78 Phosphoserine; by MAPKAPK2, MAPKAPK3 and
MOD_RES 82 82 Phosphoserine; by MAPKAPK2, MAPKAPK3 and
MOD_RES 83 83 Phosphoserine.
MOD_RES 86 86 Phosphoserine (By similarity).
MOD_RES 123 123 N6-acetyllysine.
MOD_RES 199 199 Phosphoserine.

3D-structure; Acetylation; Chaperone; Charcot-Marie-Tooth disease; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Neurodegeneration; Neuropathy; Nucleus; Phosphoprotein; Reference proteome; Stress response.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0009986; C:cell surface; IDA:UniProtKB.
GO:0005856; C:cytoskeleton; TAS:UniProtKB.
GO:0005829; C:cytosol; TAS:Reactome.
GO:0005634; C:nucleus; IDA:UniProtKB.
GO:0005886; C:plasma membrane; IEA:Compara.
GO:0000502; C:proteasome complex; ISS:BHF-UCL.
GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO:0030018; C:Z disc; IEA:Compara.
GO:0005080; F:protein kinase C binding; ISS:BHF-UCL.
GO:0008426; F:protein kinase C inhibitor activity; ISS:BHF-UCL.
GO:0043130; F:ubiquitin binding; ISS:BHF-UCL.
GO:0008219; P:cell death; IEA:UniProtKB-KW.
GO:0006928; P:cellular component movement; TAS:UniProtKB.
GO:0010467; P:gene expression; TAS:Reactome.
GO:0007243; P:intracellular protein kinase cascade; IMP:BHF-UCL.
GO:0016071; P:mRNA metabolic process; TAS:Reactome.
GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IMP:BHF-UCL.
GO:0038033; P:positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway; IMP:BHF-UCL.
GO:0032731; P:positive regulation of interleukin-1 beta production; ISS:BHF-UCL.
GO:0042535; P:positive regulation of tumor necrosis factor biosynthetic process; ISS:BHF-UCL.
GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB cascade; ISS:BHF-UCL.
GO:0006446; P:regulation of translational initiation; TAS:ProtInc.
GO:0006986; P:response to unfolded protein; NAS:UniProtKB.
GO:0009615; P:response to virus; IEP:UniProtKB.

IPR002068; a-crystallin/Hsp20_dom.
IPR001436; Alpha-crystallin/HSP.
IPR008978; HSP20-like_chaperone.

PR00299; ACRYSTALLIN.