RAT:HSP71

Species (Taxon ID)	Rattus norvegicus (Rat). (10116)
Gene Name(s)	Hspa1b (synonyms: Hsp70-2, Hspa2)
Protein Name(s)	Heat shock 70 kDa protein 1A/1B Heat shock 70 kDa protein 1/2 HSP70-1/HSP70-2 HSP70.1/HSP70.2
External Links
UniProt	Q07439
EMBL	L16764 X77208 X77207 X74271 X75357 BX883045 BX883045
PIR	I54542
RefSeq	NP_114177.2 NP_997669.1
UniGene	Rn.1950 Rn.228581
ProteinModelPortal	Q07439
SMR	Q07439
BioGrid	246633
IntAct	Q07439
MINT	MINT-240978
STRING	10116.ENSRNOP00000050605
PhosphoSite	Q07439
PaxDb	Q07439
PRIDE	Q07439
Ensembl	ENSRNOT00000049667 ENSRNOT00000061950
GeneID	24472 294254
KEGG	rno:24472 rno:294254
CTD	3303 3304
RGD	1593284 2840
eggNOG	COG0443
GeneTree	ENSGT00750000117237
HOGENOM	HOG000228135
HOVERGEN	HBG051845
InParanoid	Q07439
KO	K03283
OMA	NANAEVE
OrthoDB	EOG7PCJGF
PhylomeDB	Q07439
Reactome	REACT_196424 REACT_206546 REACT_216105 REACT_216489
NextBio	603417
PRO	PR:Q07439
Proteomes	UP000002494
Genevestigator	Q07439
GO	GO:0016324 GO:0016323 GO:0005737 GO:0005829 GO:0016607 GO:0005634 GO:0048471 GO:0043234 GO:0005524 GO:0051059 GO:0002020 GO:0006952 GO:0006402 GO:0043066 GO:0030308 GO:0008285 GO:0043154 GO:0045906 GO:0030182 GO:0045666 GO:0001916 GO:0045471 GO:0002931 GO:0009612 GO:0009314 GO:0006986
Gene3D	1.20.1270.10 2.60.34.10
InterPro	IPR018181 IPR029048 IPR029047 IPR013126
Pfam	PF00012
PRINTS	PR00301
SUPFAM	SSF100920 SSF100934
PROSITE	PS00297 PS00329 PS01036

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0000166	nucleotide binding	GO_REF:0000037	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
	GO:0001916	positive regulation of T cell mediated cytotoxicity	PMID:10679071^[1]	IDA: Inferred from Direct Assay		P	Seeded From UniProt	complete
	GO:0002020	protease binding	PMID:16397188^[2]	IPI: Inferred from Physical Interaction	RGD:733294	F	Seeded From UniProt	complete
	GO:0003674	molecular_function	GO_REF:0000015	ND: No biological Data available		F	Seeded From UniProt	complete
	GO:0005515	protein binding	PMID:16135962^[3]	IPI: Inferred from Physical Interaction	RGD:3171	F	Seeded From UniProt	complete
	GO:0005515	protein binding	PMID:9553041^[4]	IPI: Inferred from Physical Interaction	UniProtKB:P49952	F	Seeded From UniProt	complete
	GO:0005524	ATP binding	GO_REF:0000037	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0067	F	Seeded From UniProt	complete
	GO:0005575	cellular_component	GO_REF:0000015	ND: No biological Data available		C	Seeded From UniProt	complete
	GO:0005634	nucleus	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P08107	C	Seeded From UniProt	complete
	GO:0005634	nucleus	PMID:15543931^[5]	IDA: Inferred from Direct Assay		C	Seeded From UniProt	complete
	GO:0005737	cytoplasm	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P08107	C	Seeded From UniProt	complete
	GO:0005737	cytoplasm	GO_REF:0000037	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0963	C	Seeded From UniProt	complete
	GO:0005737	cytoplasm	GO_REF:0000039	IEA: Inferred from Electronic Annotation	UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
	GO:0005829	cytosol	PMID:16135962^[3]	IDA: Inferred from Direct Assay		C	Seeded From UniProt	complete
	GO:0005829	cytosol	PMID:16609151^[6]	IDA: Inferred from Direct Assay		C	Seeded From UniProt	complete
	GO:0006402	mRNA catabolic process	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P08107	P	Seeded From UniProt	complete
	GO:0006950	response to stress	GO_REF:0000037	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0346	P	Seeded From UniProt	complete
	GO:0006952	defense response	PMID:11820796^[7]	IDA: Inferred from Direct Assay		P	Seeded From UniProt	complete
	GO:0006986	response to unfolded protein	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P08107	P	Seeded From UniProt	complete
	GO:0006986	response to unfolded protein	PMID:12397389^[8]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt	complete
	GO:0006986	response to unfolded protein	PMID:8271311^[9]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt	complete
	GO:0008285	negative regulation of cell proliferation	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P08107	P	Seeded From UniProt	complete
	GO:0009612	response to mechanical stimulus	PMID:20809232^[10]	IEP: Inferred from Expression Pattern		P	Seeded From UniProt	complete
	GO:0016323	basolateral plasma membrane	PMID:16609151^[6]	IDA: Inferred from Direct Assay		C	Seeded From UniProt	complete
	GO:0016324	apical plasma membrane	PMID:16609151^[6]	IDA: Inferred from Direct Assay		C	Seeded From UniProt	complete
	GO:0016607	nuclear speck	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P08107	C	Seeded From UniProt	complete
	GO:0030308	negative regulation of cell growth	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P08107	P	Seeded From UniProt	complete
	GO:0043066	negative regulation of apoptotic process	PMID:16397188^[2]	IDA: Inferred from Direct Assay		P	Seeded From UniProt	complete
	GO:0043154	negative regulation of cysteine-type endopeptidase activity involved in apoptotic process	PMID:16397188^[2]	IDA: Inferred from Direct Assay		P	Seeded From UniProt	complete
	GO:0043234	protein complex	PMID:16135962^[3]	IDA: Inferred from Direct Assay		C	Seeded From UniProt	complete
	GO:0045906	negative regulation of vasoconstriction	PMID:15381648^[11]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt	complete
	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:P08107	C	Seeded From UniProt	complete
	GO:0051059	NF-kappaB binding	PMID:16135962^[3]	IPI: Inferred from Physical Interaction	RGD:70498	F	Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ Dressel, R et al. (2000) Heat shock protein 70 is able to prevent heat shock-induced resistance of target cells to CTL. J. Immunol. 164 2362-71 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Matsumori, Y et al. (2006) Reduction of caspase-8 and -9 cleavage is associated with increased c-FLIP and increased binding of Apaf-1 and Hsp70 after neonatal hypoxic/ischemic injury in mice overexpressing Hsp70. Stroke 37 507-12 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Chen, HW et al. (2005) In vivo heat shock protein assembles with septic liver NF-kappaB/I-kappaB complex regulating NF-kappaB activity. Shock 24 232-8 PubMed GONUTS page
↑ Maheswaran, S et al. (1998) Inhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70. Genes Dev. 12 1108-20 PubMed GONUTS page
↑ Cvoro, A et al. (2004) Intracellular localization of constitutive and inducible heat shock protein 70 in rat liver after in vivo heat stress. Mol. Cell. Biochem. 265 27-35 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Fekete, A et al. (2006) Sex differences in heat shock protein 72 expression and localization in rats following renal ischemia-reperfusion injury. Am. J. Physiol. Renal Physiol. 291 F806-11 PubMed GONUTS page
↑ Csont, T et al. (2002) Hyperlipidemia induced by high cholesterol diet inhibits heat shock response in rat hearts. Biochem. Biophys. Res. Commun. 290 1535-8 PubMed GONUTS page
↑ Neuhofer, W et al. (2002) Heat shock protein 72, a chaperone abundant in renal papilla, counteracts urea-mediated inhibition of enzymes. Pflugers Arch. 445 67-73 PubMed GONUTS page
↑ Longo, FM et al. (1993) cDNA cloning and expression of stress-inducible rat hsp70 in normal and injured rat brain. J. Neurosci. Res. 36 325-35 PubMed GONUTS page
↑ Arai, C et al. (2010) HSPA1A is upregulated in periodontal ligament at early stage of tooth movement in rats. Histochem. Cell Biol. 134 337-43 PubMed GONUTS page
↑ Nikaido, H et al. (2004) Potential role for heat shock protein 72 in antagonizing cerebral vasospasm after rat subarachnoid hemorrhage. Circulation 110 1839-46 PubMed GONUTS page

[PMID:10679071-1] Dressel, R et al. (2000) Heat shock protein 70 is able to prevent heat shock-induced resistance of target cells to CTL. J. Immunol. 164 2362-71 PubMed GONUTS page

[PMID:16397188-2] 2.0 ^2.1 ^2.2 Matsumori, Y et al. (2006) Reduction of caspase-8 and -9 cleavage is associated with increased c-FLIP and increased binding of Apaf-1 and Hsp70 after neonatal hypoxic/ischemic injury in mice overexpressing Hsp70. Stroke 37 507-12 PubMed GONUTS page

[PMID:16135962-3] 3.0 ^3.1 ^3.2 ^3.3 Chen, HW et al. (2005) In vivo heat shock protein assembles with septic liver NF-kappaB/I-kappaB complex regulating NF-kappaB activity. Shock 24 232-8 PubMed GONUTS page

[PMID:9553041-4] Maheswaran, S et al. (1998) Inhibition of cellular proliferation by the Wilms tumor suppressor WT1 requires association with the inducible chaperone Hsp70. Genes Dev. 12 1108-20 PubMed GONUTS page

[PMID:15543931-5] Cvoro, A et al. (2004) Intracellular localization of constitutive and inducible heat shock protein 70 in rat liver after in vivo heat stress. Mol. Cell. Biochem. 265 27-35 PubMed GONUTS page

[PMID:16609151-6] 6.0 ^6.1 ^6.2 Fekete, A et al. (2006) Sex differences in heat shock protein 72 expression and localization in rats following renal ischemia-reperfusion injury. Am. J. Physiol. Renal Physiol. 291 F806-11 PubMed GONUTS page

[PMID:11820796-7] Csont, T et al. (2002) Hyperlipidemia induced by high cholesterol diet inhibits heat shock response in rat hearts. Biochem. Biophys. Res. Commun. 290 1535-8 PubMed GONUTS page

[PMID:12397389-8] Neuhofer, W et al. (2002) Heat shock protein 72, a chaperone abundant in renal papilla, counteracts urea-mediated inhibition of enzymes. Pflugers Arch. 445 67-73 PubMed GONUTS page

[PMID:8271311-9] Longo, FM et al. (1993) cDNA cloning and expression of stress-inducible rat hsp70 in normal and injured rat brain. J. Neurosci. Res. 36 325-35 PubMed GONUTS page

[PMID:20809232-10] Arai, C et al. (2010) HSPA1A is upregulated in periodontal ligament at early stage of tooth movement in rats. Histochem. Cell Biol. 134 337-43 PubMed GONUTS page

[PMID:15381648-11] Nikaido, H et al. (2004) Potential role for heat shock protein 72 in antagonizing cerebral vasospasm after rat subarachnoid hemorrhage. Circulation 110 1839-46 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

RAT:HSP71

Contents

Annotations

Notes

References

a

b

c

d

e

g

m

n

o

p

r

s

v

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools