UniProt ID | HSPB1_HUMAN | |
---|---|---|
UniProt AC | P04792 | |
Protein Name | Heat shock protein beta-1 | |
Gene Name | HSPB1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 205 | |
Subcellular Localization | Cytoplasm . Nucleus . Cytoplasm, cytoskeleton, spindle . 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 o | |
Protein Description | Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. [PubMed: 10383393] | |
Protein Sequence | MTERRVPFSLLRGPSWDPFRDWYPHSRLFDQAFGLPRLPEEWSQWLGGSSWPGYVRPLPPAAIESPAVAAPAYSRALSRQLSSGVSEIRHTADRWRVSLDVNHFAPDELTVKTKDGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTQVSSSLSPEGTLTVEAPMPKLATQSNEITIPVTFESRAQLGGPEAAKSDETAAK | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
5 | Methylation | ---MTERRVPFSLLR ---CCCCCCCCHHHC | 33.94 | 58854747 | |
9 | Phosphorylation | TERRVPFSLLRGPSW CCCCCCCHHHCCCCC | 22.03 | 20886841 | |
12 | Methylation | RVPFSLLRGPSWDPF CCCCHHHCCCCCCCC | 61.34 | 24129315 | |
15 | Phosphorylation | FSLLRGPSWDPFRDW CHHHCCCCCCCCHHC | 47.11 | 19664994 | |
23 | Phosphorylation | WDPFRDWYPHSRLFD CCCCHHCCCCHHHHH | 8.71 | 23927012 | |
26 | Phosphorylation | FRDWYPHSRLFDQAF CHHCCCCHHHHHHHH | 26.61 | 23927012 | |
37 | Methylation | DQAFGLPRLPEEWSQ HHHHCCCCCCHHHHH | 68.84 | 26494247 | |
43 | Phosphorylation | PRLPEEWSQWLGGSS CCCCHHHHHHHCCCC | 18.11 | 20873877 | |
49 | Phosphorylation | WSQWLGGSSWPGYVR HHHHHCCCCCCCCCC | 27.68 | 26356563 | |
50 | Phosphorylation | SQWLGGSSWPGYVRP HHHHCCCCCCCCCCC | 40.33 | 26657352 | |
54 | Phosphorylation | GGSSWPGYVRPLPPA CCCCCCCCCCCCCHH | 6.82 | 26356563 | |
56 | Methylation | SSWPGYVRPLPPAAI CCCCCCCCCCCHHHC | 20.67 | 54556783 | |
65 | Phosphorylation | LPPAAIESPAVAAPA CCHHHCCCCCCHHHH | 16.43 | 28355574 | |
73 | Phosphorylation | PAVAAPAYSRALSRQ CCCHHHHHHHHHHHH | 9.53 | 26657352 | |
74 | O-linked_Glycosylation | AVAAPAYSRALSRQL CCHHHHHHHHHHHHH | 17.12 | 32574038 | |
74 | Phosphorylation | AVAAPAYSRALSRQL CCHHHHHHHHHHHHH | 17.12 | 26657352 | |
78 | Phosphorylation | PAYSRALSRQLSSGV HHHHHHHHHHHHCCC | 19.59 | 20201521 | |
82 | Phosphorylation | RALSRQLSSGVSEIR HHHHHHHHCCCHHHH | 19.39 | 19664994 | |
83 | Phosphorylation | ALSRQLSSGVSEIRH HHHHHHHCCCHHHHH | 52.37 | 22167270 | |
86 | Phosphorylation | RQLSSGVSEIRHTAD HHHHCCCHHHHHCCC | 30.72 | 23927012 | |
89 | Methylation | SSGVSEIRHTADRWR HCCCHHHHHCCCCEE | 19.63 | 115367653 | |
91 | Phosphorylation | GVSEIRHTADRWRVS CCHHHHHCCCCEEEE | 22.02 | 30183078 | |
98 | Phosphorylation | TADRWRVSLDVNHFA CCCCEEEEEECCCCC | 15.41 | 30266825 | |
110 | Phosphorylation | HFAPDELTVKTKDGV CCCCCCCEEEECCCE | 20.22 | 23403867 | |
112 | Ubiquitination | APDELTVKTKDGVVE CCCCCEEEECCCEEE | 44.62 | 21906983 | |
112 | 2-Hydroxyisobutyrylation | APDELTVKTKDGVVE CCCCCEEEECCCEEE | 44.62 | - | |
112 | Malonylation | APDELTVKTKDGVVE CCCCCEEEECCCEEE | 44.62 | 26320211 | |
112 | Acetylation | APDELTVKTKDGVVE CCCCCEEEECCCEEE | 44.62 | 23236377 | |
113 | Phosphorylation | PDELTVKTKDGVVEI CCCCEEEECCCEEEE | 29.99 | 20068231 | |
114 | 2-Hydroxyisobutyrylation | DELTVKTKDGVVEIT CCCEEEECCCEEEEC | 46.93 | - | |
114 | Sumoylation | DELTVKTKDGVVEIT CCCEEEECCCEEEEC | 46.93 | - | |
114 | Malonylation | DELTVKTKDGVVEIT CCCEEEECCCEEEEC | 46.93 | 26320211 | |
114 | Acetylation | DELTVKTKDGVVEIT CCCEEEECCCEEEEC | 46.93 | 26051181 | |
114 | Glycation | DELTVKTKDGVVEIT CCCEEEECCCEEEEC | 46.93 | - | |
114 | Sumoylation | DELTVKTKDGVVEIT CCCEEEECCCEEEEC | 46.93 | - | |
114 | Ubiquitination | DELTVKTKDGVVEIT CCCEEEECCCEEEEC | 46.93 | - | |
121 | Phosphorylation | KDGVVEITGKHEERQ CCCEEEECCCCCCCC | 27.03 | 20068231 | |
123 | Glycation | GVVEITGKHEERQDE CEEEECCCCCCCCCC | 38.91 | - | |
123 | Acetylation | GVVEITGKHEERQDE CEEEECCCCCCCCCC | 38.91 | 19608861 | |
123 | Ubiquitination | GVVEITGKHEERQDE CEEEECCCCCCCCCC | 38.91 | 19608861 | |
123 | 2-Hydroxyisobutyrylation | GVVEITGKHEERQDE CEEEECCCCCCCCCC | 38.91 | - | |
123 | Malonylation | GVVEITGKHEERQDE CEEEECCCCCCCCCC | 38.91 | 26320211 | |
133 | Phosphorylation | ERQDEHGYISRCFTR CCCCCCCCEEEEEEC | 9.53 | 24927040 | |
135 | Phosphorylation | QDEHGYISRCFTRKY CCCCCCEEEEEECCC | 17.95 | 28152594 | |
139 | Phosphorylation | GYISRCFTRKYTLPP CCEEEEEECCCCCCC | 29.85 | - | |
141 | Acetylation | ISRCFTRKYTLPPGV EEEEEECCCCCCCCC | 39.26 | 26051181 | |
141 | Ubiquitination | ISRCFTRKYTLPPGV EEEEEECCCCCCCCC | 39.26 | - | |
142 | Phosphorylation | SRCFTRKYTLPPGVD EEEEECCCCCCCCCC | 15.37 | 23663014 | |
143 | Phosphorylation | RCFTRKYTLPPGVDP EEEECCCCCCCCCCH | 35.50 | 26657352 | |
151 | Phosphorylation | LPPGVDPTQVSSSLS CCCCCCHHHCCCCCC | 36.82 | 23663014 | |
154 | Phosphorylation | GVDPTQVSSSLSPEG CCCHHHCCCCCCCCC | 12.37 | 23663014 | |
155 | Phosphorylation | VDPTQVSSSLSPEGT CCHHHCCCCCCCCCC | 36.12 | 23663014 | |
156 | Phosphorylation | DPTQVSSSLSPEGTL CHHHCCCCCCCCCCE | 25.92 | 23663014 | |
158 | Phosphorylation | TQVSSSLSPEGTLTV HHCCCCCCCCCCEEE | 23.89 | 23663014 | |
162 | Phosphorylation | SSLSPEGTLTVEAPM CCCCCCCCEEEECCC | 20.00 | 23663014 | |
164 | Phosphorylation | LSPEGTLTVEAPMPK CCCCCCEEEECCCCC | 19.01 | 23663014 | |
171 | Ubiquitination | TVEAPMPKLATQSNE EEECCCCCCCCCCCE | 44.49 | - | |
174 | O-linked_Glycosylation | APMPKLATQSNEITI CCCCCCCCCCCEEEE | 42.86 | 32574038 | |
174 | Phosphorylation | APMPKLATQSNEITI CCCCCCCCCCCEEEE | 42.86 | 30266825 | |
176 | O-linked_Glycosylation | MPKLATQSNEITIPV CCCCCCCCCEEEEEE | 31.88 | 32574038 | |
176 | Phosphorylation | MPKLATQSNEITIPV CCCCCCCCCEEEEEE | 31.88 | 30266825 | |
180 | Phosphorylation | ATQSNEITIPVTFES CCCCCEEEEEEEECC | 17.04 | 30266825 | |
180 | O-linked_Glycosylation | ATQSNEITIPVTFES CCCCCEEEEEEEECC | 17.04 | 32574038 | |
184 | Phosphorylation | NEITIPVTFESRAQL CEEEEEEEECCHHHH | 19.14 | 30266825 | |
184 | O-linked_Glycosylation | NEITIPVTFESRAQL CEEEEEEEECCHHHH | 19.14 | 32574038 | |
187 | O-linked_Glycosylation | TIPVTFESRAQLGGP EEEEEECCHHHHCCC | 28.82 | 32574038 | |
187 | Phosphorylation | TIPVTFESRAQLGGP EEEEEECCHHHHCCC | 28.82 | 30266825 | |
198 | Sumoylation | LGGPEAAKSDETAAK HCCCHHHCCHHHCCC | 66.54 | - | |
198 | 2-Hydroxyisobutyrylation | LGGPEAAKSDETAAK HCCCHHHCCHHHCCC | 66.54 | - | |
198 | Malonylation | LGGPEAAKSDETAAK HCCCHHHCCHHHCCC | 66.54 | 26320211 | |
198 | Ubiquitination | LGGPEAAKSDETAAK HCCCHHHCCHHHCCC | 66.54 | 2190698 | |
198 | Sumoylation | LGGPEAAKSDETAAK HCCCHHHCCHHHCCC | 66.54 | - | |
198 | Acetylation | LGGPEAAKSDETAAK HCCCHHHCCHHHCCC | 66.54 | 26051181 | |
199 | O-linked_Glycosylation | GGPEAAKSDETAAK- CCCHHHCCHHHCCC- | 35.63 | 32574038 | |
199 | Phosphorylation | GGPEAAKSDETAAK- CCCHHHCCHHHCCC- | 35.63 | 29255136 | |
202 | Phosphorylation | EAAKSDETAAK---- HHHCCHHHCCC---- | 36.58 | 30266825 | |
205 | Ubiquitination | KSDETAAK------- CCHHHCCC------- | 59.41 | - | |
205 | Acetylation | KSDETAAK------- CCHHHCCC------- | 59.41 | 156059 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
15 | S | Phosphorylation | Kinase | MAPKAPK3 | Q16644 | Uniprot |
15 | S | Phosphorylation | Kinase | MAPK2 | P49137 | PhosphoELM |
15 | S | Phosphorylation | Kinase | PRKG1 | Q13976-2 | GPS |
78 | S | Phosphorylation | Kinase | PRKACA | P17612 | GPS |
78 | S | Phosphorylation | Kinase | MAPK-FAMILY | - | GPS |
78 | S | Phosphorylation | Kinase | MAPKAPK5 | Q8IW41 | Uniprot |
78 | S | Phosphorylation | Kinase | MAPKAPK3 | Q16644 | Uniprot |
78 | S | Phosphorylation | Kinase | MAPK2 | P49137 | PhosphoELM |
78 | S | Phosphorylation | Kinase | RPS6KB2 | Q9UBS0 | GPS |
78 | S | Phosphorylation | Kinase | PRKG1 | Q13976-2 | GPS |
82 | S | Phosphorylation | Kinase | PRKD1 | Q15139 | PSP |
82 | S | Phosphorylation | Kinase | PRKD2 | Q9BZL6 | GPS |
82 | S | Phosphorylation | Kinase | RPS6KB2 | Q9UBS0 | GPS |
82 | S | Phosphorylation | Kinase | PRKG1 | Q13976-2 | GPS |
82 | S | Phosphorylation | Kinase | MAPK2 | P49137 | PhosphoELM |
82 | S | Phosphorylation | Kinase | AKT1 | P31749 | PSP |
82 | S | Phosphorylation | Kinase | MAPK-FAMILY | - | GPS |
82 | S | Phosphorylation | Kinase | MAPKAPK3 | Q16644 | Uniprot |
82 | S | Phosphorylation | Kinase | PRKACA | P17612 | GPS |
82 | S | Phosphorylation | Kinase | MAPKAPK5 | Q8IW41 | Uniprot |
82 | S | Phosphorylation | Kinase | PKD1 | P98161 | PhosphoELM |
143 | T | Phosphorylation | Kinase | PRKG1 ISOFORM ALPHA | - | GPS |
143 | T | Phosphorylation | Kinase | PRKG2 | Q13237 | GPS |
143 | T | Phosphorylation | Kinase | PRKACA | P17612 | GPS |
143 | T | Phosphorylation | Kinase | PRKACB | P22694 | GPS |
143 | T | Phosphorylation | Kinase | PRKG1 | Q13976-2 | GPS |
176 | S | Phosphorylation | Kinase | MAPK14 | Q16539 | GPS |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HSPB1_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of HSPB1_HUMAN !! |
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Acetylation | |
Reference | PubMed |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123, AND MASS SPECTROMETRY. | |
"Substrate and functional diversity of lysine acetylation revealed bya 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). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-123, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND MASSSPECTROMETRY. | |
"PKA-induced F-actin rearrangement requires phosphorylation of Hsp27by the MAPKAP kinase MK5."; Kostenko S., Johannessen M., Moens U.; Cell. Signal. 21:712-718(2009). Cited for: PHOSPHORYLATION AT SER-78 AND SER-82. | |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND MASSSPECTROMETRY. | |
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-82 AND SER-199,AND MASS SPECTROMETRY. | |
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-65; SER-82 ANDSER-199, AND MASS SPECTROMETRY. | |
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-82, AND MASSSPECTROMETRY. | |
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND MASSSPECTROMETRY. | |
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-65; SER-82;SER-83 AND SER-199, AND MASS SPECTROMETRY. | |
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND MASSSPECTROMETRY. | |
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-82, AND MASSSPECTROMETRY. | |
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-82 AND SER-83,AND MASS SPECTROMETRY. | |
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-65 AND SER-82,AND MASS SPECTROMETRY. | |
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND MASSSPECTROMETRY. | |
"Heat shock protein 27 is associated with freedom from graftvasculopathy 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). Cited for: PHOSPHORYLATION AT SER-78 AND SER-82, AND MASS SPECTROMETRY. | |
"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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASSSPECTROMETRY. | |
"Regulation of Hsp27 oligomerization, chaperone function, andprotective activity against oxidative stress/tumor necrosis factoralpha 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). Cited for: PHOSPHORYLATION AT SER-15; SER-78 AND SER-82, AND MUTAGENESIS OFSER-15; SER-78 AND SER-82. | |
"A comparison of the substrate specificity of MAPKAP kinase-2 andMAPKAP kinase-3 and their activation by cytokines and cellularstress."; Clifton A.D., Young P.R., Cohen P.; FEBS Lett. 392:209-214(1996). Cited for: PHOSPHORYLATION AT SER-15; SER-78 AND SER-82. | |
"Identification of MAPKAP kinase 2 as a major enzyme responsible forthe 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). Cited for: PHOSPHORYLATION AT SER-15; SER-78 AND SER-82 BY MAPKAPK2. | |
"Human HSP27 is phosphorylated at serines 78 and 82 by heat shock andmitogen-activated kinases that recognize the same amino acid motif asS6 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). Cited for: PROTEIN SEQUENCE OF 76-89, AND PHOSPHORYLATION AT SER-78 AND SER-82. |