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Protein

Heat shock protein beta-8

Gene

Hspb8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Displays temperature-dependent chaperone activity.

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Enzyme and pathway databases

ReactomeiR-MMU-3371571. HSF1-dependent transactivation.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock protein beta-8
Short name:
HspB8
Alternative name(s):
Alpha-crystallin C chain
Small stress protein-like protein HSP22
Gene namesi
Name:Hspb8
Synonyms:Cryac, Hsp22
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2135756. Hspb8.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Translocates to nuclear foci during heat shock.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 196196Heat shock protein beta-8PRO_0000125947Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241PhosphoserineBy similarity
Modified residuei57 – 571PhosphoserineBy similarity
Modified residuei63 – 631PhosphothreonineBy similarity
Modified residuei87 – 871PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9JK92.
MaxQBiQ9JK92.
PaxDbiQ9JK92.
PRIDEiQ9JK92.

PTM databases

iPTMnetiQ9JK92.
PhosphoSiteiQ9JK92.

Expressioni

Tissue specificityi

Highly expressed in skeletal muscle, heart, uterus, liver, lung and ovary. Low levels found in stomach and brain. Not detected in small intestine, large intestine, kidney, spleen and testis. In the ovary, expression is concentrated in the endometrium and in the connective tissue between the circular and longitudinal muscles of the myometrium.1 Publication

Developmental stagei

Detected in developing heart throughout embryonic development but only detected in developing liver close to time of birth. In the adult ovary, expression is highest during decidualization and early pregnancy.1 Publication

Inductioni

By progesterone.1 Publication

Gene expression databases

BgeeiQ9JK92.
CleanExiMM_HSPB8.
GenevisibleiQ9JK92. MM.

Interactioni

Subunit structurei

Monomer. Interacts with HSPB1 (By similarity). Interacts with DNAJB6 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9JK92. 2 interactions.
MINTiMINT-4098152.
STRINGi10090.ENSMUSP00000037007.

Structurei

3D structure databases

ProteinModelPortaliQ9JK92.
SMRiQ9JK92. Positions 18-170.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the small heat shock protein (HSP20) family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
GeneTreeiENSGT00760000119238.
HOGENOMiHOG000233955.
HOVERGENiHBG054766.
InParanoidiQ9JK92.
KOiK08879.
OMAiPFGESSF.
OrthoDBiEOG7WHHBK.
PhylomeDBiQ9JK92.
TreeFamiTF105049.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR002068. A-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527. PTHR11527. 1 hit.
PfamiPF00011. HSP20. 1 hit.
[Graphical view]
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JK92-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADGQLPFPC SYPSRLRRDP FRDSPLSSRL LDDGFGMDPF PDDLTAPWPE
60 70 80 90 100
WALPRLSSAW PGTLRSGMVP RGPPATARFG VPAEGRSPPP FPGEPWKVCV
110 120 130 140 150
NVHSFKPEEL MVKTKDGYVE VSGKHEEKQQ EGGIVSKNFT KKIQLPAEVD
160 170 180 190
PATVFASLSP EGLLIIEAPQ VPPYSPFGES SFNNELPQDN QEVTCS
Length:196
Mass (Da):21,533
Last modified:October 1, 2000 - v1
Checksum:iADE847E9E70D7DAC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF250139 mRNA. Translation: AAF65563.1.
AF273453 mRNA. Translation: AAG00233.1.
AK005052 mRNA. Translation: BAB23778.1.
BC011219 mRNA. Translation: AAH11219.1.
CCDSiCCDS19600.1.
RefSeqiNP_109629.1. NM_030704.3.
UniGeneiMm.21549.

Genome annotation databases

EnsembliENSMUST00000036991; ENSMUSP00000037007; ENSMUSG00000041548.
GeneIDi80888.
KEGGimmu:80888.
UCSCiuc008zez.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF250139 mRNA. Translation: AAF65563.1.
AF273453 mRNA. Translation: AAG00233.1.
AK005052 mRNA. Translation: BAB23778.1.
BC011219 mRNA. Translation: AAH11219.1.
CCDSiCCDS19600.1.
RefSeqiNP_109629.1. NM_030704.3.
UniGeneiMm.21549.

3D structure databases

ProteinModelPortaliQ9JK92.
SMRiQ9JK92. Positions 18-170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JK92. 2 interactions.
MINTiMINT-4098152.
STRINGi10090.ENSMUSP00000037007.

PTM databases

iPTMnetiQ9JK92.
PhosphoSiteiQ9JK92.

Proteomic databases

EPDiQ9JK92.
MaxQBiQ9JK92.
PaxDbiQ9JK92.
PRIDEiQ9JK92.

Protocols and materials databases

DNASUi80888.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000036991; ENSMUSP00000037007; ENSMUSG00000041548.
GeneIDi80888.
KEGGimmu:80888.
UCSCiuc008zez.1. mouse.

Organism-specific databases

CTDi26353.
MGIiMGI:2135756. Hspb8.

Phylogenomic databases

eggNOGiKOG3591. Eukaryota.
ENOG410YERS. LUCA.
GeneTreeiENSGT00760000119238.
HOGENOMiHOG000233955.
HOVERGENiHBG054766.
InParanoidiQ9JK92.
KOiK08879.
OMAiPFGESSF.
OrthoDBiEOG7WHHBK.
PhylomeDBiQ9JK92.
TreeFamiTF105049.

Enzyme and pathway databases

ReactomeiR-MMU-3371571. HSF1-dependent transactivation.

Miscellaneous databases

PROiQ9JK92.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JK92.
CleanExiMM_HSPB8.
GenevisibleiQ9JK92. MM.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR002068. A-crystallin/Hsp20_dom.
IPR001436. Alpha-crystallin/HSP.
IPR031107. HSP20.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PANTHERiPTHR11527. PTHR11527. 1 hit.
PfamiPF00011. HSP20. 1 hit.
[Graphical view]
PRINTSiPR00299. ACRYSTALLIN.
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS01031. HSP20. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "HSP22, a new member of the small heat shock protein superfamily, interacts with mimic of phosphorylated HSP27 (3DHSP27)."
    Benndorf R., Sun X., Gilmont R.R., Biederman K.J., Molloy M.P., Goodmurphy C.W., Cheng H., Andrews P.C., Welsh M.J.
    J. Biol. Chem. 276:26753-26761(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH HSPB1.
    Strain: C57BL/6J.
    Tissue: Heart.
  2. "Increased expression of a novel heat shock protein transcript in the mouse uterus during decidualization and in response to progesterone."
    Bany B.M., Schultz G.A.
    Biol. Reprod. 64:284-292(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION.
    Strain: CD-1.
    Tissue: Decidua.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Liver.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart and Liver.

Entry informationi

Entry nameiHSPB8_MOUSE
AccessioniPrimary (citable) accession number: Q9JK92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.