HUMAN:HSP71

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	HSPA1B (synonyms: HSPA1, HSX70)
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	P08107
EMBL	M59828 M59830 M11717 AF134726 AF134726 BA000025 BA000025 AK304652 DQ388429 DQ451402 AL662834 AL662834 AL671762 AL671762 AL929592 AL929592 BC002453 BC009322 BC018740 BC057397 BC063507 M24743 M24744 X04676 X04677
CCDS	CCDS34414.1 CCDS34415.1
PIR	A29160 A45871 I59139 I79540
RefSeq	NP_005336.3 NP_005337.2
UniGene	Hs.274402 Hs.702139 Hs.719966
PDB	1HJO 1S3X 1XQS 2E88 2E8A 2LMG 3A8Y 3ATU 3ATV 3AY9 3D2E 3D2F 3JXU 3LOF 4IO8 4J8F 4PO2
PDBsum	1HJO 1S3X 1XQS 2E88 2E8A 2LMG 3A8Y 3ATU 3ATV 3AY9 3D2E 3D2F 3JXU 3LOF 4IO8 4J8F 4PO2
ProteinModelPortal	P08107
SMR	P08107
BioGrid	109535 109536
DIP	DIP-211N
IntAct	P08107
MINT	MINT-96699
STRING	9606.ENSP00000364802
BindingDB	P08107
ChEMBL	CHEMBL5460
TCDB	1.A.33.1.3
PhosphoSite	P08107
DMDM	147744565
DOSAC-COBS-2DPAGE	P08107
OGP	P08107
REPRODUCTION-2DPAGE	IPI00304925
SWISS-2DPAGE	P08107
UCD-2DPAGE	P08107
MaxQB	P08107
PaxDb	P08107
PRIDE	P08107
DNASU	3303
Ensembl	ENST00000375650 ENST00000375651 ENST00000391548 ENST00000391555 ENST00000400040 ENST00000430065 ENST00000433487 ENST00000441618 ENST00000445736 ENST00000450744
GeneID	3303 3304
KEGG	hsa:3303 hsa:3304
UCSC	uc003nxj.3
CTD	3303 3304
GeneCards	GC06P031850 GC06P031853 GC06Pi31794 GC06Pi31806 GC06Pj31770 GC06Pj31782 GC06Pk31765 GC06Pk31777 GC06Pn31773 GC06Pn31785
H-InvDB	HIX0058169 HIX0058187 HIX0166160
HGNC	HGNC:5232 HGNC:5233
HPA	CAB008640 CAB017451 CAB032815 HPA052504
MIM	140550 603012
neXtProt	NX_P08107
PharmGKB	PA29499
eggNOG	COG0443
GeneTree	ENSGT00750000117237
HOGENOM	HOG000228135
HOVERGEN	HBG051845
InParanoid	P08107
KO	K03283
OMA	MAKSTAI
OrthoDB	EOG7PCJGF
PhylomeDB	P08107
TreeFam	TF105042
Reactome	REACT_200624 REACT_200775 REACT_200780 REACT_25325 REACT_6198
ChiTaRS	HSPA1A HSPA1B
EvolutionaryTrace	P08107
GeneWiki	HSPA1A
NextBio	13103
PRO	PR:P08107
Proteomes	UP000005640 UP000005640
Bgee	P08107
CleanEx	HS_HSPA1A
ExpressionAtlas	P08107
Genevestigator	P08107
GO	GO:0016235 GO:0072562 GO:0005814 GO:0005737 GO:0005829 GO:0005783 GO:0070062 GO:0005925 GO:0016234 GO:0005739 GO:0016607 GO:0005634 GO:0048471 GO:0030529 GO:0031982 GO:0005524 GO:0016887 GO:0042623 GO:0003725 GO:0019899 GO:0001664 GO:0031072 GO:0044822 GO:0044183 GO:0047485 GO:0031625 GO:0051082 GO:0001618 GO:0006200 GO:0070370 GO:0034605 GO:0034599 GO:0010467 GO:0006402 GO:0016071 GO:0043066 GO:0060548 GO:0030308 GO:0008285 GO:2001240 GO:0090084 GO:0031397 GO:0045648 GO:0042026 GO:0050821 GO:0006986 GO:0016070
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:0016887	ATPase activity	PMID:23975754^[1]	IDA: Inferred from Direct Assay		F	Fig. 6	complete CACAO 8862
	GO:0000166	nucleotide binding	GO_REF:0000037	IEA: Inferred from Electronic Annotation	UniProtKB-KW:KW-0547	F	Seeded From UniProt	complete
	GO:0005515	protein binding	PMID:12853476^[2]	IPI: Inferred from Physical Interaction	UniProtKB:Q99615	F	Seeded From UniProt	complete
	GO:0005515	protein binding	PMID:15603737^[3]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UL15	F	Seeded From UniProt	complete
	GO:0005515	protein binding	PMID:15657067^[4]	IPI: Inferred from Physical Interaction	UniProtKB:P00533	F	Seeded From UniProt	complete
	GO:0005515	protein binding	PMID:15671022^[5]	IPI: Inferred from Physical Interaction	UniProtKB:P37840	F	Seeded From UniProt	complete
	GO:0005515	protein binding	PMID:16275660^[6]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UNE7	F	Seeded From UniProt	complete
	GO:0005515	protein binding	PMID:17167422^[7]	IPI: Inferred from Physical Interaction	UniProtKB:P15976	F	Seeded From UniProt	complete
	GO:0005515	protein binding	PMID:17342744^[8]	IPI: Inferred from Physical Interaction	UniProtKB:P08473	F	Seeded From UniProt	complete
	GO:0005515	protein binding	PMID:18555782^[9]	IPI: Inferred from Physical Interaction	UniProtKB:P32589	F	Seeded From UniProt	complete
	GO:0005515	protein binding	PMID:18975920^[10]	IPI: Inferred from Physical Interaction	UniProtKB:P37840	F	Seeded From UniProt	complete
	GO:0005515	protein binding	PMID:20029029^[11]	IPI: Inferred from Physical Interaction	UniProtKB:P00533	F	Seeded From UniProt	complete
	GO:0005515	protein binding	PMID:21081504^[12]	IPI: Inferred from Physical Interaction	UniProtKB:Q9CRB9	F	Seeded From UniProt	complete
	GO:0005515	protein binding	PMID:21887822^[13]	IPI: Inferred from Physical Interaction	UniProtKB:P53350	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:0005634	nucleus	PMID:10205060^[14]	IDA: Inferred from Direct Assay		C	Seeded From UniProt	complete
	GO:0005634	nucleus	PMID:17167422^[7]	IDA: Inferred from Direct Assay		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:0005737	cytoplasm	PMID:10859165^[15]	IDA: Inferred from Direct Assay		C	Seeded From UniProt	complete
	GO:0005737	cytoplasm	PMID:16130169^[16]	TAS: Traceable Author Statement		C	Seeded From UniProt	complete
	GO:0005737	cytoplasm	PMID:9553041^[17]	IDA: Inferred from Direct Assay		C	Seeded From UniProt	complete
	GO:0005739	mitochondrion	PMID:16130169^[16]	TAS: Traceable Author Statement		C	Seeded From UniProt	complete
	GO:0005783	endoplasmic reticulum	PMID:16130169^[16]	TAS: Traceable Author Statement		C	Seeded From UniProt	complete
	GO:0005829	cytosol	Reactome:REACT_25267	TAS: Traceable Author Statement		C	Seeded From UniProt	complete
	GO:0005829	cytosol	Reactome:REACT_25315	TAS: Traceable Author Statement		C	Seeded From UniProt	complete
	GO:0006402	mRNA catabolic process	PMID:10205060^[14]	IDA: Inferred from Direct Assay		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:0006986	response to unfolded protein	PMID:10859165^[15]	IDA: Inferred from Direct Assay		P	Seeded From UniProt	complete
	GO:0008285	negative regulation of cell proliferation	PMID:9553041^[17]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt	complete
	GO:0010467	gene expression	Reactome:REACT_71	TAS: Traceable Author Statement		P	Seeded From UniProt	complete
	GO:0016070	RNA metabolic process	Reactome:REACT_21257	TAS: Traceable Author Statement		P	Seeded From UniProt	complete
	GO:0016071	mRNA metabolic process	Reactome:REACT_20605	TAS: Traceable Author Statement		P	Seeded From UniProt	complete
	GO:0016234	inclusion body	PMID:15603737^[3]	IDA: Inferred from Direct Assay		C	Seeded From UniProt	complete
	GO:0016235	aggresome	PMID:15885686^[18]	IDA: Inferred from Direct Assay		C	Seeded From UniProt	complete
	GO:0016607	nuclear speck	PMID:9553041^[17]	IDA: Inferred from Direct Assay		C	Seeded From UniProt	complete
	GO:0030308	negative regulation of cell growth	PMID:9553041^[17]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt	complete
	GO:0030529	ribonucleoprotein complex	PMID:17289661^[19]	IDA: Inferred from Direct Assay		C	Seeded From UniProt	complete
	GO:0031625	ubiquitin protein ligase binding	PMID:15603737^[3]	IPI: Inferred from Physical Interaction	UniProtKB:O60260	F	Seeded From UniProt	complete
	GO:0042026	protein refolding	PMID:15603737^[3]	IDA: Inferred from Direct Assay		P	Seeded From UniProt	complete
	GO:0043066	negative regulation of apoptotic process	PMID:16130169^[16]	TAS: Traceable Author Statement		P	Seeded From UniProt	complete
	GO:0043066	negative regulation of apoptotic process	PMID:17167422^[7]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt	complete
	GO:0044183	protein binding involved in protein folding	PMID:15603737^[3]	IDA: Inferred from Direct Assay		F	Seeded From UniProt	complete
	GO:0045648	positive regulation of erythrocyte differentiation	PMID:17167422^[7]	IMP: Inferred from Mutant Phenotype		P	Seeded From UniProt	complete
	GO:0047485	protein N-terminus binding	PMID:9553041^[17]	IPI: Inferred from Physical Interaction	UniProtKB:P19544	F	Seeded From UniProt	complete
	GO:0048471	perinuclear region of cytoplasm	PMID:10205060^[14]	IDA: Inferred from Direct Assay		C	Seeded From UniProt	complete
	GO:0048471	perinuclear region of cytoplasm	PMID:15603737^[3]	IDA: Inferred from Direct Assay		C	Seeded From UniProt	complete
	GO:0051082	unfolded protein binding	PMID:16130169^[16]	TAS: Traceable Author Statement		F	Seeded From UniProt	complete
	GO:0090084	negative regulation of inclusion body assembly	PMID:15603737^[3]	IDA: Inferred from Direct Assay		P	Seeded From UniProt	complete
colocalizes_with	GO:0008180	COP9 signalosome	PMID:18850735^[20]	IDA: Inferred from Direct Assay		C	Seeded From UniProt	complete
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Notes

References

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

↑ Kharenko, OA et al. (2013) Identification and characterization of interactions between abscisic acid and human heat shock protein 70 family members. J. Biochem. 154 383-91 PubMed GONUTS page
↑ Brychzy, A et al. (2003) Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system. EMBO J. 22 3613-23 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 Kalia, SK et al. (2004) BAG5 inhibits parkin and enhances dopaminergic neuron degeneration. Neuron 44 931-45 PubMed GONUTS page
↑ Thelemann, A et al. (2005) Phosphotyrosine signaling networks in epidermal growth factor receptor overexpressing squamous carcinoma cells. Mol. Cell Proteomics 4 356-76 PubMed GONUTS page
↑ Dedmon, MM et al. (2005) Heat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar species. J. Biol. Chem. 280 14733-40 PubMed GONUTS page
↑ Grelle, G et al. (2006) Identification of VCP/p97, carboxyl terminus of Hsp70-interacting protein (CHIP), and amphiphysin II interaction partners using membrane-based human proteome arrays. Mol. Cell Proteomics 5 234-44 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 Ribeil, JA et al. (2007) Hsp70 regulates erythropoiesis by preventing caspase-3-mediated cleavage of GATA-1. Nature 445 102-5 PubMed GONUTS page
↑ Dall'Era, MA et al. (2007) HSP27 and HSP70 interact with CD10 in C4-2 prostate cancer cells. Prostate 67 714-21 PubMed GONUTS page
↑ Polier, S et al. (2008) Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell 133 1068-79 PubMed GONUTS page
↑ Luk, KC et al. (2008) Interactions between Hsp70 and the hydrophobic core of alpha-synuclein inhibit fibril assembly. Biochemistry 47 12614-25 PubMed GONUTS page
↑ Deribe, YL et al. (2009) Regulation of epidermal growth factor receptor trafficking by lysine deacetylase HDAC6. Sci Signal 2 ra84 PubMed GONUTS page
↑ Darshi, M et al. (2011) ChChd3, an inner mitochondrial membrane protein, is essential for maintaining crista integrity and mitochondrial function. J. Biol. Chem. 286 2918-32 PubMed GONUTS page
↑ Chen, YJ et al. (2011) Proteomic identification of Hsp70 as a new Plk1 substrate in arsenic trioxide-induced mitotically arrested cells. Proteomics 11 4331-45 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 Laroia, G et al. (1999) Control of mRNA decay by heat shock-ubiquitin-proteasome pathway. Science 284 499-502 PubMed GONUTS page
↑ ^15.0 ^15.1 Cuesta, R et al. (2000) Chaperone hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes. Genes Dev. 14 1460-70 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 ^16.3 ^16.4 Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 ^17.3 ^17.4 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
↑ Kallijärvi, J et al. (2005) TRIM37 defective in mulibrey nanism is a novel RING finger ubiquitin E3 ligase. Exp. Cell Res. 308 146-55 PubMed GONUTS page
↑ Jønson, L et al. (2007) Molecular composition of IMP1 ribonucleoprotein granules. Mol. Cell Proteomics 6 798-811 PubMed GONUTS page
↑ Fang, L et al. (2008) Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry. J. Proteome Res. 7 4914-25 PubMed GONUTS page

[PMID:23975754-1] Kharenko, OA et al. (2013) Identification and characterization of interactions between abscisic acid and human heat shock protein 70 family members. J. Biochem. 154 383-91 PubMed GONUTS page

[PMID:12853476-2] Brychzy, A et al. (2003) Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system. EMBO J. 22 3613-23 PubMed GONUTS page

[PMID:15603737-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 ^3.6 Kalia, SK et al. (2004) BAG5 inhibits parkin and enhances dopaminergic neuron degeneration. Neuron 44 931-45 PubMed GONUTS page

[PMID:15657067-4] Thelemann, A et al. (2005) Phosphotyrosine signaling networks in epidermal growth factor receptor overexpressing squamous carcinoma cells. Mol. Cell Proteomics 4 356-76 PubMed GONUTS page

[PMID:15671022-5] Dedmon, MM et al. (2005) Heat shock protein 70 inhibits alpha-synuclein fibril formation via preferential binding to prefibrillar species. J. Biol. Chem. 280 14733-40 PubMed GONUTS page

[PMID:16275660-6] Grelle, G et al. (2006) Identification of VCP/p97, carboxyl terminus of Hsp70-interacting protein (CHIP), and amphiphysin II interaction partners using membrane-based human proteome arrays. Mol. Cell Proteomics 5 234-44 PubMed GONUTS page

[PMID:17167422-7] 7.0 ^7.1 ^7.2 ^7.3 Ribeil, JA et al. (2007) Hsp70 regulates erythropoiesis by preventing caspase-3-mediated cleavage of GATA-1. Nature 445 102-5 PubMed GONUTS page

[PMID:17342744-8] Dall'Era, MA et al. (2007) HSP27 and HSP70 interact with CD10 in C4-2 prostate cancer cells. Prostate 67 714-21 PubMed GONUTS page

[PMID:18555782-9] Polier, S et al. (2008) Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell 133 1068-79 PubMed GONUTS page

[PMID:18975920-10] Luk, KC et al. (2008) Interactions between Hsp70 and the hydrophobic core of alpha-synuclein inhibit fibril assembly. Biochemistry 47 12614-25 PubMed GONUTS page

[PMID:20029029-11] Deribe, YL et al. (2009) Regulation of epidermal growth factor receptor trafficking by lysine deacetylase HDAC6. Sci Signal 2 ra84 PubMed GONUTS page

[PMID:21081504-12] Darshi, M et al. (2011) ChChd3, an inner mitochondrial membrane protein, is essential for maintaining crista integrity and mitochondrial function. J. Biol. Chem. 286 2918-32 PubMed GONUTS page

[PMID:21887822-13] Chen, YJ et al. (2011) Proteomic identification of Hsp70 as a new Plk1 substrate in arsenic trioxide-induced mitotically arrested cells. Proteomics 11 4331-45 PubMed GONUTS page

[PMID:10205060-14] 14.0 ^14.1 ^14.2 Laroia, G et al. (1999) Control of mRNA decay by heat shock-ubiquitin-proteasome pathway. Science 284 499-502 PubMed GONUTS page

[PMID:10859165-15] 15.0 ^15.1 Cuesta, R et al. (2000) Chaperone hsp27 inhibits translation during heat shock by binding eIF4G and facilitating dissociation of cap-initiation complexes. Genes Dev. 14 1460-70 PubMed GONUTS page

[PMID:16130169-16] 16.0 ^16.1 ^16.2 ^16.3 ^16.4 Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page

[PMID:9553041-17] 17.0 ^17.1 ^17.2 ^17.3 ^17.4 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:15885686-18] Kallijärvi, J et al. (2005) TRIM37 defective in mulibrey nanism is a novel RING finger ubiquitin E3 ligase. Exp. Cell Res. 308 146-55 PubMed GONUTS page

[PMID:17289661-19] Jønson, L et al. (2007) Molecular composition of IMP1 ribonucleoprotein granules. Mol. Cell Proteomics 6 798-811 PubMed GONUTS page

[PMID:18850735-20] Fang, L et al. (2008) Characterization of the human COP9 signalosome complex using affinity purification and mass spectrometry. J. Proteome Res. 7 4914-25 PubMed GONUTS page

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HUMAN:HSP71

Contents

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