Variant position: 7 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 205 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human MTERRV PFSLLRGPSWDPFRDWYP-HSR
Mouse MTERRV PFSLLRSPSWEPFRDWYPAHS
Rat MTERRV PFSLLRSPSWEPFRDWYPAHS
Pig MTERRV PFSLLRSPSWDPFRDWYPAHS
Bovine MAERRV PFSLLRGPSWDPFRDWYPAHS
Chicken MAERRV PFTFLTSPSWEPFRDWYH-GS
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Type Positions Description
1 – 205 Heat shock protein beta-1
12 – 12 Omega-N-methylarginine
15 – 15 Phosphoserine; by MAPKAPK2 and MAPKAPK3
26 – 26 Phosphoserine
15 – 15 S -> D. Mimicks phosphorylation state, leading to dreased ability to act as molecular chaperones; when associated with D-78 and D-82.
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)
Cited for: PROTEIN SEQUENCE OF 76-89; PHOSPHORYLATION AT SER-78 AND SER-82;
Identification of MAPKAP kinase 2 as a major enzyme responsible for the 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;
A comparison of the substrate specificity of MAPKAP kinase-2 and MAPKAP kinase-3 and their activation by cytokines and cellular stress.
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;
Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha 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: FUNCTION; SUBUNIT; PHOSPHORYLATION AT SER-15; SER-78 AND SER-82; MUTAGENESIS OF SER-15; SER-78 AND SER-82;
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)
Cited for: PHOSPHORYLATION AT SER-78 AND SER-82; IDENTIFICATION BY MASS SPECTROMETRY;
PKA-induced F-actin rearrangement requires phosphorylation of Hsp27 by the MAPKAP kinase MK5.
Kostenko S.; Johannessen M.; Moens U.;
Cell. Signal. 21:712-718(2009)
Cited for: FUNCTION; PHOSPHORYLATION AT SER-78 AND SER-82;
Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
Olsen J.V.; Vermeulen M.; Santamaria A.; Kumar C.; Miller M.L.; Jensen L.J.; Gnad F.; Cox J.; Jensen T.S.; Nigg E.A.; Brunak S.; Mann M.;
Sci. Signal. 3:RA3-RA3(2010)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-65; SER-78; SER-82 AND SER-199; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS];
Toward a comprehensive characterization of a human cancer cell phosphoproteome.
Zhou H.; Di Palma S.; Preisinger C.; Peng M.; Polat A.N.; Heck A.J.; Mohammed S.;
J. Proteome Res. 12:260-271(2013)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-78; SER-82; SER-86; THR-174; SER-176 AND SER-199; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS];
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
Bian Y.; Song C.; Cheng K.; Dong M.; Wang F.; Huang J.; Sun D.; Wang L.; Ye M.; Zou H.;
J. Proteomics 96:253-262(2014)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-78; SER-82; SER-86; SER-98 AND SER-199; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS];
Axonal Neuropathies due to Mutations in Small Heat Shock Proteins: Clinical, Genetic, and Functional Insights into Novel Mutations.
Echaniz-Laguna A.; Geuens T.; Petiot P.; Pereon Y.; Adriaenssens E.; Haidar M.; Capponi S.; Maisonobe T.; Fournier E.; Dubourg O.; Degos B.; Salachas F.; Lenglet T.; Eymard B.; Delmont E.; Pouget J.; Juntas Morales R.; Goizet C.; Latour P.; Timmerman V.; Stojkovic T.;
Hum. Mutat. 38:556-568(2017)
Cited for: VARIANTS HMN2B SER-7; LEU-39; ASP-53; TRP-127; ARG-128; ILE-151; 175-GLN--LYS-205 DEL; ILE-180 AND LEU-187; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANTS HMN2B SER-7; ASP-53; ARG-128 AND LEU-187;
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