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Protein

Heat shock 70 kDa protein 1B

Gene

Hspa1a

more
Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei71 – 711ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 154ATPBy similarity
Nucleotide bindingi202 – 2043ATPBy similarity
Nucleotide bindingi268 – 2758ATPBy similarity
Nucleotide bindingi339 – 3424ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • NF-kappaB binding Source: RGD
  • protease binding Source: RGD

GO - Biological processi

  • defense response Source: RGD
  • negative regulation of apoptotic process Source: RGD
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: RGD
  • negative regulation of vasoconstriction Source: RGD
  • positive regulation of T cell mediated cytotoxicity Source: RGD
  • response to unfolded protein Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-3371453. Regulation of HSF1-mediated heat shock response.
R-RNO-3371568. Attenuation phase.
R-RNO-3371571. HSF1-dependent transactivation.
R-RNO-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock 70 kDa protein 1B
Alternative name(s):
Heat shock 70 kDa protein 1
Short name:
HSP70-1
Short name:
HSP70.1
Gene namesi
Name:Hspa1a
Synonyms:Hsp70-1, Hspa1
AND
Name:Hspa1b
Synonyms:Hsp70-2, Hspa2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 20

Organism-specific databases

RGDi2840. Hspa1b.

Subcellular locationi

  • Cytoplasm By similarity

  • Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.By similarity

GO - Cellular componenti

  • apical plasma membrane Source: RGD
  • basolateral plasma membrane Source: RGD
  • cytosol Source: RGD
  • nucleus Source: RGD
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 641640Heat shock 70 kDa protein 1BPRO_0000433116Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei108 – 1081N6-acetyllysineBy similarity
Modified residuei246 – 2461N6-acetyllysineBy similarity
Modified residuei348 – 3481N6-acetyllysineBy similarity
Modified residuei561 – 5611N6,N6,N6-trimethyllysine; by METTL21ABy similarity
Modified residuei631 – 6311PhosphoserineBy similarity
Modified residuei633 – 6331PhosphoserineBy similarity
Modified residuei636 – 6361PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Expressioni

Tissue specificityi

HSPA1B is testis-specific.

Inductioni

By heat shock.

Gene expression databases

ExpressionAtlasiP0DMW1. baseline and differential.

Interactioni

Subunit structurei

Component of the CatSper complex. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C and TSC2. Interacts with TERT; the interaction occurs in the absence of the RNA component, TERC, and dissociates once the TERT complex has formed. Interacts with METTL21A. Interacts with TRIM5 (via B30.2/SPRY domain). Interacts with PARK2. Interacts with FOXP3. Interacts with NOD2; the interaction enhances NOD2 stability. Interacts with DNAJC9 (via J domain). Interacts with ATF5; the interaction protects ATF5 from degradation via proteasome-dependent and caspase-dependent processes (By similarity).By similarity

GO - Molecular functioni

  • NF-kappaB binding Source: RGD
  • protease binding Source: RGD

Protein-protein interaction databases

MINTiMINT-240978.

Structurei

3D structure databases

ProteinModelPortaliP0DMW1.
SMRiP0DMW1. Positions 1-619.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

GeneTreeiENSGT00840000130142.
ENSGT00840000130709.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
KOiK03283.
OrthoDBiEOG7PCJGF.
PhylomeDBiP0DMW1.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0DMW1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKKTAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL
60 70 80 90 100
IGDAAKNQVA LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVVNDGDK
110 120 130 140 150
PKVQVNYKGE NRSFYPEEIS SMVLTKMKEI AEAYLGHPVT NAVITVPAYF
160 170 180 190 200
NDSQRQATKD AGVIAGLNVL RIINEPTAAA IAYGLDRTGK GERNVLIFDL
210 220 230 240 250
GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVSH FVEEFKRKHK
260 270 280 290 300
KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA
310 320 330 340 350
RFEELCSDLF RGTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL
360 370 380 390 400
QDFFNGRDLN KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS
410 420 430 440 450
LGLETAGGVM TALIKRNSTI PTKQTQTFTT YSDNQPGVLI QVYEGERAMT
460 470 480 490 500
RDNNLLGRFE LSGIPPAPRG VPQIEVTFDI DANGILNVTA TDKSTGKANK
510 520 530 540 550
ITITNDKGRL SKEEIERMVQ EAERYKAEDE VQRERVAAKN ALESYAFNMK
560 570 580 590 600
SAVEDEGLKG KISEADKKKV LDKCQEVISW LDSNTLAEKE EFVHKREELE
610 620 630 640
RVCNPIISGL YQGAGAPGAG GFGAQAPKGG SGSGPTIEEV D
Length:641
Mass (Da):70,185
Last modified:May 27, 2015 - v1
Checksum:i2D745B1013F64E7B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 722KR → NG in CAA52328 (PubMed:8086479).Curated
Sequence conflicti71 – 722KR → NG in CAA53140 (PubMed:8141767).Curated
Sequence conflicti110 – 1101E → K in CAA53140 (PubMed:8141767).Curated
Sequence conflicti204 – 2041T → R in CAA53140 (PubMed:8141767).Curated
Sequence conflicti227 – 2271H → D in AAA17441 (PubMed:8271311).Curated
Sequence conflicti262 – 2676RLRTAC → PLADGV in CAA53140 (PubMed:8141767).Curated
Sequence conflicti408 – 4081G → A in CAA52328 (PubMed:8086479).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L16764 mRNA. Translation: AAA17441.1.
X74271 Genomic DNA. Translation: CAA52328.1.
X75357 Genomic DNA. Translation: CAA53140.1.
X77207 Genomic DNA. Translation: CAA54422.1.
BX883045 Genomic DNA. Translation: CAE83977.1.
PIRiI54542.
RefSeqiNP_114177.2. NM_031971.2.
NP_997669.1. NM_212504.1.
UniGeneiRn.1950.
Rn.228581.

Genome annotation databases

EnsembliENSRNOT00000049667; ENSRNOP00000050605; ENSRNOG00000045654.
ENSRNOT00000061950; ENSRNOP00000067749; ENSRNOG00000045654.
ENSRNOT00000081924; ENSRNOP00000075599; ENSRNOG00000050647.
GeneIDi24472.
294254.
KEGGirno:24472.
rno:294254.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L16764 mRNA. Translation: AAA17441.1.
X74271 Genomic DNA. Translation: CAA52328.1.
X75357 Genomic DNA. Translation: CAA53140.1.
X77207 Genomic DNA. Translation: CAA54422.1.
BX883045 Genomic DNA. Translation: CAE83977.1.
PIRiI54542.
RefSeqiNP_114177.2. NM_031971.2.
NP_997669.1. NM_212504.1.
UniGeneiRn.1950.
Rn.228581.

3D structure databases

ProteinModelPortaliP0DMW1.
SMRiP0DMW1. Positions 1-619.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-240978.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000049667; ENSRNOP00000050605; ENSRNOG00000045654.
ENSRNOT00000061950; ENSRNOP00000067749; ENSRNOG00000045654.
ENSRNOT00000081924; ENSRNOP00000075599; ENSRNOG00000050647.
GeneIDi24472.
294254.
KEGGirno:24472.
rno:294254.

Organism-specific databases

CTDi3303.
3304.
RGDi2840. Hspa1b.

Phylogenomic databases

GeneTreeiENSGT00840000130142.
ENSGT00840000130709.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
KOiK03283.
OrthoDBiEOG7PCJGF.
PhylomeDBiP0DMW1.

Enzyme and pathway databases

ReactomeiR-RNO-3371453. Regulation of HSF1-mediated heat shock response.
R-RNO-3371568. Attenuation phase.
R-RNO-3371571. HSF1-dependent transactivation.
R-RNO-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.

Miscellaneous databases

PROiP0DMW1.

Gene expression databases

ExpressionAtlasiP0DMW1. baseline and differential.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and expression of stress-inducible rat hsp70 in normal and injured rat brain."
    Longo F.M., Wang S., Narasimhan P., Zhang J.S., Chen J., Massa S.M., Sharp F.R.
    J. Neurosci. Res. 36:325-335(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Cloning, nucleotide sequence and expression of rat heat inducible hsp70 gene."
    Lisowska K., Krawczyk Z., Widlak W., Wolniczek P., Wisniewski J.
    Biochim. Biophys. Acta 1219:64-72(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  3. "Isolation of a novel inducible rat heat shock protein (HSP70) gene and its expression during ischaemia/hypoxia and heat shock."
    Mestril R., Chi S.H., Sayen M.R., Dillmann W.H.
    Biochem. J. 298:561-569(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Wistar.
    Tissue: Spleen.
  4. "Comparative analysis of the three major histocompatibility complex-linked heat shock protein 70 (Hsp70) genes of the rat."
    Walter L., Rauh F., Guenther E.
    Immunogenetics 40:325-330(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: LEW.1W/GUN.
  5. "The genomic sequence and comparative analysis of the rat major histocompatibility complex."
    Hurt P., Walter L., Sudbrak R., Klages S., Mueller I., Shiina T., Inoko H., Lehrach H., Guenther E., Reinhardt R., Himmelbauer H.
    Genome Res. 14:631-639(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.

Entry informationi

Entry nameiHS71B_RAT
AccessioniPrimary (citable) accession number: P0DMW1
Secondary accession number(s): P42853, Q07439, Q63256
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2015
Last sequence update: May 27, 2015
Last modified: June 8, 2016
This is version 12 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. 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.