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HUMAN:HS71A

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) HSPA1A (synonyms: HSPA1, HSX70)
Protein Name(s) Heat shock 70 kDa protein 1A (ECO:0000312 with HGNC:HGNC:5232)

Heat shock 70 kDa protein 1 HSP70-1 (ECO:0000303 with PMID:14656967[1], ECO:0000303 with PMID:2538825[2]) HSP70.1

External Links
UniProt P0DMV8
EMBL M11717
M59828
BA000025
AF134726
AK304652
DQ451402
AL671762
BC002453
M24743
X04676
X04677
CCDS CCDS34414.1
PIR A29160
A45871
I59139
I79540
RefSeq NP_005336.3
NP_005337.2
UniGene Hs.274402
Hs.702139
Hs.719966
Hs.743411
PDB 1HJO
1S3X
1XQS
2E88
2E8A
2LMG
3A8Y
3ATU
3ATV
3AY9
3D2E
3D2F
3JXU
3LOF
4IO8
4J8F
4PO2
4WV5
4WV7
PDBsum 1HJO
1S3X
1XQS
2E88
2E8A
2LMG
3A8Y
3ATU
3ATV
3AY9
3D2E
3D2F
3JXU
3LOF
4IO8
4J8F
4PO2
4WV5
4WV7
ProteinModelPortal P0DMV8
SMR P0DMV8
IntAct P0DMV8
MINT MINT-96699
BindingDB P0DMV8
ChEMBL CHEMBL5460
SwissPalm P0DMV8
DMDM 147744565
REPRODUCTION-2DPAGE IPI00304925
DNASU 3303
Ensembl ENST00000375651
ENST00000400040
ENST00000430065
ENST00000433487
ENST00000441618
GeneID 3303
3304
KEGG hsa:3303
hsa:3304
CTD 3303
3304
H-InvDB HIX0058169
HIX0058187
HIX0166160
HGNC HGNC:5232
HPA CAB008640
CAB017451
CAB032815
HPA052504
MIM 140550
603012
neXtProt NX_P0DMV8
HOGENOM HOG000228135
HOVERGEN HBG051845
KO K03283
OrthoDB EOG7PCJGF
TreeFam TF105042
Reactome R-HSA-168330
R-HSA-3371453
R-HSA-3371568
R-HSA-3371571
R-HSA-450408
ChiTaRS HSPA1A
HSPA1B
GeneWiki HSPA1A
NextBio 13103
PRO PR:P0DMV8
Proteomes UP000005640
CleanEx HS_HSPA1A
ExpressionAtlas P0DMV8
GO GO:0072562
GO:0005814
GO:0005737
GO:0005829
GO:0005925
GO:0016234
GO:0005739
GO:0005654
GO:0048471
GO:0005524
GO:0016887
GO:0042623
GO:0055131
GO:0019899
GO:0001664
GO:0031072
GO:0042826
GO:0044183
GO:0005102
GO:0031625
GO:0051082
GO:0001618
GO:0046034
GO:0070370
GO:0034605
GO:0034599
GO:0010467
GO:0060548
GO:1902236
GO:2001240
GO:0090084
GO:1901029
GO:0031397
GO:1902380
GO:0010628
GO:0032757
GO:1904722
GO:0051092
GO:0070434
GO:1903265
GO:0042026
GO:0050821
GO:1900034
GO:0043488
GO:0031396
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 ECO ID ECO term name with/from Aspect Extension Notes Status

involved_in

GO:0007041

lysosomal transport

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q61696

P

Seeded From UniProt

complete

involved_in

GO:0034620

cellular response to unfolded protein

PMID:20625543[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0051131

chaperone-mediated protein complex assembly

PMID:10811660[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:11785981[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0097718

disordered domain specific binding

PMID:11785981[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P21758

F

Seeded From UniProt

complete

enables

GO:0045296

cadherin binding

PMID:25468996[6]

ECO:0007005

high throughput direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0031249

denatured protein binding

PMID:21909508[7]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P42858

F

Seeded From UniProt

complete

part_of

GO:0032991

protein-containing complex

PMID:23349634[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0030512

negative regulation of transforming growth factor beta receptor signaling pathway

PMID:24613385[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0032436

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

PMID:24613385[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0050821

protein stabilization

PMID:21909508[7]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0031396

regulation of protein ubiquitination

PMID:16809764[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042826

histone deacetylase binding

PMID:16809764[10]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q9BY41

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:24790089[11]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0042026

protein refolding

PMID:27708256[12]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0090063

positive regulation of microtubule nucleation

PMID:27137183[13]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1901673

regulation of mitotic spindle assembly

PMID:27137183[13]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005813

centrosome

PMID:27137183[13]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0031625

ubiquitin protein ligase binding

PMID:15603737[14]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:O60260

F

Seeded From UniProt

complete

enables

GO:0031072

heat shock protein binding

PMID:23921388[15]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P25685

F

Seeded From UniProt

complete

enables

GO:0019899

enzyme binding

PMID:23921388[15]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q8WXB1

F

Seeded From UniProt

complete

part_of

GO:0048471

perinuclear region of cytoplasm

PMID:15603737[14]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0016234

inclusion body

PMID:15603737[14]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0044183

protein folding chaperone

PMID:15603737[14]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016887

ATPase activity

PMID:23921388[15]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:23921388[15]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:2001240

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

PMID:17167422[16]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0090084

negative regulation of inclusion body assembly

PMID:15603737[14]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0046034

ATP metabolic process

PMID:23921388[15]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042026

protein refolding

PMID:15603737[14]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0010628

positive regulation of gene expression

PMID:25281747[17]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

has_regulation_target:(UniProtKB:Q12809)

Seeded From UniProt

complete

enables

GO:0055131

C3HC4-type RING finger domain binding

PMID:25281747[17]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q6ZRF8

F

Seeded From UniProt

complete

enables

GO:0031072

heat shock protein binding

PMID:17182002[18]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q8WXX5

F

Seeded From UniProt

complete

enables

GO:0005102

signaling receptor binding

PMID:24790089[11]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q9HC29

F

occurs_in:(CL:0011108)

Seeded From UniProt

complete

involved_in

GO:0051092

positive regulation of NF-kappaB transcription factor activity

PMID:24790089[11]

ECO:0000315

mutant phenotype evidence used in manual assertion

UniProtKB:Q9HC29

P

Seeded From UniProt

complete

involved_in

GO:0070434

positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway

PMID:24790089[11]

ECO:0000315

mutant phenotype evidence used in manual assertion

UniProtKB:Q9HC29

P

Seeded From UniProt

complete

involved_in

GO:0050821

protein stabilization

PMID:24790089[11]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

has_regulation_target:(UniProtKB:Q9HC29)

Seeded From UniProt

complete

involved_in

GO:1903265

positive regulation of tumor necrosis factor-mediated signaling pathway

PMID:24790089[11]

ECO:0000315

mutant phenotype evidence used in manual assertion

UniProtKB:Q9HC29

P

Seeded From UniProt

complete

involved_in

GO:0033120

positive regulation of RNA splicing

PMID:20625543[3]

ECO:0000314

direct assay evidence used in manual assertion

P

has_regulation_target:(UniProtKB:P17861)

Seeded From UniProt

complete

involved_in

GO:1902380

positive regulation of endoribonuclease activity

PMID:20625543[3]

ECO:0000314

direct assay evidence used in manual assertion

P

has_regulation_target:(UniProtKB:O75460)

Seeded From UniProt

complete

involved_in

GO:1901029

negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway

PMID:20625543[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1902236

negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway

PMID:20625543[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0001664

G protein-coupled receptor binding

PMID:12150907[19]

ECO:0000314

direct assay evidence used in manual assertion

F

has_direct_input:(UniProtKB:O15354)

Seeded From UniProt

complete

part_of

GO:0070062

extracellular exosome

PMID:23533145[20]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0031625

ubiquitin protein ligase binding

PMID:12150907[19]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:O60260

F

Seeded From UniProt

complete

part_of

GO:0031982

vesicle

PMID:19190083[21]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(CL:0002202)

Seeded From UniProt

complete

involved_in

GO:1902236

negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway

PMID:12150907[19]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:12150907[19]

ECO:0000303

author statement without traceable support used in manual assertion

F

has_input:(UniProtKB:O15354)

Seeded From UniProt

complete

involved_in

GO:0031397

negative regulation of protein ubiquitination

PMID:12150907[19]

ECO:0000314

direct assay evidence used in manual assertion

P

has_regulation_target:(UniProtKB:O15354)

Seeded From UniProt

complete

colocalizes_with

GO:0000151

ubiquitin ligase complex

PMID:12150907[19]

ECO:0000314

direct assay evidence used in manual assertion

C

part_of:(UBERON:0000955)

Seeded From UniProt

complete

part_of

GO:0005925

focal adhesion

PMID:21423176[22]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(CL:0000057)

Seeded From UniProt

complete

involved_in

GO:0090084

negative regulation of inclusion body assembly

PMID:21231916[23]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0072562

blood microparticle

PMID:22516433[24]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0070370

cellular heat acclimation

PMID:21231916[23]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0070062

extracellular exosome

PMID:19199708[25]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(UBERON:0001831)

Seeded From UniProt

complete

part_of

GO:0070062

extracellular exosome

PMID:20458337[26]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0070062

extracellular exosome

PMID:20458337[26]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(CL:0000639)

Seeded From UniProt

complete

involved_in

GO:0060548

negative regulation of cell death

PMID:21231916[23]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

happens_during:(GO:0034605)

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:21231916[23]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042623

ATPase activity, coupled

PMID:21231916[23]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0042026

protein refolding

PMID:21231916[23]

ECO:0000314

direct assay evidence used in manual assertion

P

has_input:(UniProtKB:P04637)

Seeded From UniProt

complete

involved_in

GO:0034605

cellular response to heat

PMID:24061851[27]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0031072

heat shock protein binding

PMID:21231916[23]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q8NHS0

F

Seeded From UniProt

complete

enables

GO:0031072

heat shock protein binding

PMID:21231916[23]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q7Z6W7

F

Seeded From UniProt

complete

enables

GO:0031072

heat shock protein binding

PMID:21231916[23]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:O75190

F

Seeded From UniProt

complete

enables

GO:0031072

heat shock protein binding

PMID:21231916[23]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:O75953

F

Seeded From UniProt

complete

enables

GO:0031072

heat shock protein binding

PMID:21231916[23]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q9UDY4

F

Seeded From UniProt

complete

enables

GO:0031072

heat shock protein binding

PMID:21231916[23]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P25686

F

Seeded From UniProt

complete

enables

GO:0031072

heat shock protein binding

PMID:21231916[23]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P25685

F

Seeded From UniProt

complete

enables

GO:0031072

heat shock protein binding

PMID:21231916[23]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q8WW22

F

Seeded From UniProt

complete

enables

GO:0031072

heat shock protein binding

PMID:21231916[23]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:O60884

F

Seeded From UniProt

complete

enables

GO:0031072

heat shock protein binding

PMID:21231916[23]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P31689

F

Seeded From UniProt

complete

NOT|involved_in

GO:0010941

regulation of cell death

PMID:21231916[23]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21231916[23]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005814

centriole

PMID:24061851[27]

ECO:0000314

direct assay evidence used in manual assertion

C

part_of:(CL:0000540)

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:24061851[27]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0032757

positive regulation of interleukin-8 production

PMID:24790089[11]

ECO:0000315

mutant phenotype evidence used in manual assertion

UniProtKB:Q9HC29

P

Seeded From UniProt

complete

enables

GO:0003714

transcription corepressor activity

PMID:9499401[28]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0097201

negative regulation of transcription from RNA polymerase II promoter in response to stress

PMID:9499401[28]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0048471

perinuclear region of cytoplasm

PMID:10205060[29]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0047485

protein N-terminus binding

PMID:9553041[30]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P19544

F

Seeded From UniProt

complete

involved_in

GO:0045648

positive regulation of erythrocyte differentiation

PMID:17167422[16]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

PMID:22681889[31]

ECO:0007005

high throughput direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

PMID:22658674[32]

ECO:0007005

high throughput direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0043066

negative regulation of apoptotic process

PMID:17167422[16]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:1990904

ribonucleoprotein complex

PMID:17289661[33]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0030308

negative regulation of cell growth

PMID:9553041[30]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0016607

nuclear speck

PMID:9553041[30]

ECO:0000314

direct assay evidence used in manual assertion

C

part_of:(CL:0000653)

Seeded From UniProt

complete

part_of

GO:0016235

aggresome

PMID:15885686[34]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0008285

negative regulation of cell population proliferation

PMID:9553041[30]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

colocalizes_with

GO:0008180

COP9 signalosome

PMID:18850735[35]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006986

response to unfolded protein

PMID:10859165[36]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006402

mRNA catabolic process

PMID:10205060[29]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:9553041[30]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:10859165[36]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:17167422[16]

ECO:0000314

direct assay evidence used in manual assertion

C

exists_during:(GO:0030218)

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:10205060[29]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:1901673

regulation of mitotic spindle assembly

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000453125
UniProtKB:P0DMV8
UniProtKB:P0DMV9

P

Seeded From UniProt

complete

enables

GO:0051787

misfolded protein binding

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:95835
PANTHER:PTN002321897
RGD:2843
UniProtKB:P11021

F

Seeded From UniProt

complete

involved_in

GO:0051085

chaperone cofactor-dependent protein refolding

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
MGI:MGI:105384
PANTHER:PTN002321897

P

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
MGI:MGI:105384
PANTHER:PTN002321897
RGD:2843
RGD:621725
SGD:S000000004
SGD:S000000171
SGD:S000000905
SGD:S000001106
SGD:S000001556
SGD:S000002388
SGD:S000003571
SGD:S000003947
SGD:S000005153
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P11142
UniProtKB:P17066
UniProtKB:P34931
UniProtKB:P54652

F

Seeded From UniProt

complete

enables

GO:0044183

protein folding chaperone

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
PANTHER:PTN002321897
UniProtKB:P0DMV8
UniProtKB:P0DMV9

F

Seeded From UniProt

complete

enables

GO:0042623

ATPase activity, coupled

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:105384
PANTHER:PTN002321897
RGD:621725
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P17066

F

Seeded From UniProt

complete

involved_in

GO:0042026

protein refolding

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002321897
SGD:S000000004
SGD:S000000756
SGD:S000003806
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P11142
UniProtKB:P17066
UniProtKB:P34931
UniProtKB:P54652

P

Seeded From UniProt

complete

involved_in

GO:0034620

cellular response to unfolded protein

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
PANTHER:PTN002321897
UniProtKB:P0DMV8

P

Seeded From UniProt

complete

involved_in

GO:0034605

cellular response to heat

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

CGD:CAL0000184706
PANTHER:PTN002321897
RGD:621725
SGD:S000000905
UniProtKB:A5I640
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P17066

P

Seeded From UniProt

complete

part_of

GO:0032991

protein-containing complex

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000453103
RGD:2840
UniProtKB:P0DMV8
UniProtKB:P0DMV9

C

Seeded From UniProt

complete

involved_in

GO:0032436

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000453125
UniProtKB:P0DMV8

P

Seeded From UniProt

complete

enables

GO:0031625

ubiquitin protein ligase binding

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000453103
UniProtKB:P0DMV8
UniProtKB:P0DMV9

F

Seeded From UniProt

complete

enables

GO:0031072

heat shock protein binding

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002321897
RGD:1311806
UniProtKB:K7NTP5
UniProtKB:O73885
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P11142
UniProtKB:P17066
UniProtKB:P34931
UniProtKB:Q8IB24

F

Seeded From UniProt

complete

enables

GO:0016887

ATPase activity

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
EcoGene:EG12130
EcoGene:EG13653
PANTHER:PTN002321897
PomBase:SPAC664.11
RGD:621725
SGD:S000000004
SGD:S000000171
SGD:S000002388
SGD:S000003571
SGD:S000003806
SGD:S000005153
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P11021
UniProtKB:P11142
WB:WBGene00002005

F

Seeded From UniProt

complete

colocalizes_with

GO:0008180

COP9 signalosome

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000453103
UniProtKB:P0DMV8
UniProtKB:P17066
UniProtKB:P48741

C

Seeded From UniProt

complete

involved_in

GO:0006986

response to unfolded protein

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002321897
RGD:1593284
RGD:2840
SGD:S000001556
SGD:S000003571
UniProtKB:P0DMV8

P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN002321762
PomBase:SPBC1709.05
RGD:2840
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P17066
UniProtKB:P34931
UniProtKB:Q0VDF9

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
FB:FBgn0266599
MGI:MGI:105384
MGI:MGI:96244
PANTHER:PTN002321897
PomBase:SPCC1739.13
RGD:1311806
RGD:2843
RGD:621725
SGD:S000000004
SGD:S000000905
SGD:S000001106
SGD:S000002388
SGD:S000003947
UniProtKB:O73885
UniProtKB:P08106
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P17066
UniProtKB:P22953
UniProtKB:Q27975
UniProtKB:Q8IB24
WB:WBGene00002005

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000453103
RGD:2840
UniProtKB:P0DMV8
UniProtKB:P0DMV9

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:21873635[37]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10241
EcoGene:EG12130
PANTHER:PTN002321897
RGD:621725
SGD:S000001556
SGD:S000003947
TAIR:locus:2101222
TAIR:locus:2121022
TAIR:locus:2135897
TAIR:locus:2144801
UniProtKB:P08106
UniProtKB:P0DMV8
UniProtKB:P0DMV9
UniProtKB:P11142
UniProtKB:Q7SX63

F

Seeded From UniProt

complete

involved_in

GO:0046718

viral entry into host cell

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0001618

P

Seeded From UniProt

complete

involved_in

GO:0034599

cellular response to oxidative stress

PMID:24252804[38]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0050821

protein stabilization

PMID:24252804[38]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

has_input:(UniProtKB:P37840)

Seeded From UniProt

complete

enables

GO:0051082

unfolded protein binding

PMID:16130169[39]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0043066

negative regulation of apoptotic process

PMID:16130169[39]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005783

endoplasmic reticulum

PMID:16130169[39]

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:16130169[39]

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:16130169[39]

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:1904813

ficolin-1-rich granule lumen

Reactome:R-HSA-6800434

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:1900034

regulation of cellular response to heat

Reactome:R-HSA-3371571
Reactome:R-HSA-3371453

ECO:0000304

author statement supported by traceable reference used in manual assertion


P

Seeded From UniProt

complete

involved_in

GO:0043488

regulation of mRNA stability

Reactome:R-HSA-450408

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043312

neutrophil degranulation

Reactome:R-HSA-6798695

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0042623

ATPase activity, coupled

Reactome:R-HSA-3371422

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

Reactome:R-HSA-5618110
Reactome:R-HSA-5618107
Reactome:R-HSA-5618105
Reactome:R-HSA-5618098
Reactome:R-HSA-5618085
Reactome:R-HSA-5252079
Reactome:R-HSA-5252041
Reactome:R-HSA-5251959
Reactome:R-HSA-5251942
Reactome:R-HSA-450580
Reactome:R-HSA-450551
Reactome:R-HSA-3371590
Reactome:R-HSA-3371503
Reactome:R-HSA-3371422

ECO:0000304

author statement supported by traceable reference used in manual assertion














C

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

Reactome:R-HSA-5252041
Reactome:R-HSA-5251955
Reactome:R-HSA-5082384
Reactome:R-HSA-5082369
Reactome:R-HSA-5082356
Reactome:R-HSA-3371554
Reactome:R-HSA-3371518
Reactome:R-HSA-3371467

ECO:0000304

author statement supported by traceable reference used in manual assertion








C

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

Reactome:R-HSA-6800434

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

part_of

GO:0005856

cytoskeleton

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0206

C

Seeded From UniProt

complete

enables

GO:0001618

virus receptor activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-1183

F

Seeded From UniProt

complete

part_of

GO:0005815

microtubule organizing center

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0048

C

Seeded From UniProt

complete

Notes

References

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

  1. Xie, T et al. (2003) Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse. Genome Res. 13 2621-36 PubMed GONUTS page
  2. Sargent, CA et al. (1989) Human major histocompatibility complex contains genes for the major heat shock protein HSP70. Proc. Natl. Acad. Sci. U.S.A. 86 1968-72 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 3.4 Gupta, S et al. (2010) HSP72 protects cells from ER stress-induced apoptosis via enhancement of IRE1alpha-XBP1 signaling through a physical interaction. PLoS Biol. 8 e1000410 PubMed GONUTS page
  4. Weaver, AJ et al. (2000) Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone. J. Biol. Chem. 275 23045-52 PubMed GONUTS page
  5. 5.0 5.1 Nakamura, T et al. (2002) HSP90, HSP70, and GAPDH directly interact with the cytoplasmic domain of macrophage scavenger receptors. Biochem. Biophys. Res. Commun. 290 858-64 PubMed GONUTS page
  6. Guo, Z et al. (2014) E-cadherin interactome complexity and robustness resolved by quantitative proteomics. Sci Signal 7 rs7 PubMed GONUTS page
  7. 7.0 7.1 Chakrabortee, S et al. (2012) Intrinsically disordered proteins as molecular shields. Mol Biosyst 8 210-9 PubMed GONUTS page
  8. Cloutier, P et al. (2013) A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity. PLoS Genet. 9 e1003210 PubMed GONUTS page
  9. 9.0 9.1 Shang, Y et al. (2014) Hsp70 and Hsp90 oppositely regulate TGF-β signaling through CHIP/Stub1. Biochem. Biophys. Res. Commun. 446 387-92 PubMed GONUTS page
  10. 10.0 10.1 Lee, H et al. (2006) Histone deacetylase 8 safeguards the human ever-shorter telomeres 1B (hEST1B) protein from ubiquitin-mediated degradation. Mol. Cell. Biol. 26 5259-69 PubMed GONUTS page
  11. 11.0 11.1 11.2 11.3 11.4 11.5 11.6 Mohanan, V & Grimes, CL (2014) The molecular chaperone HSP70 binds to and stabilizes NOD2, an important protein involved in Crohn disease. J. Biol. Chem. 289 18987-98 PubMed GONUTS page
  12. Seo, JH et al. (2016) ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation. Nat Commun 7 12882 PubMed GONUTS page
  13. 13.0 13.1 13.2 Fang, CT et al. (2016) HSP70 regulates the function of mitotic centrosomes. Cell. Mol. Life Sci. 73 3949-60 PubMed GONUTS page
  14. 14.0 14.1 14.2 14.3 14.4 14.5 Kalia, SK et al. (2004) BAG5 inhibits parkin and enhances dopaminergic neuron degeneration. Neuron 44 931-45 PubMed GONUTS page
  15. 15.0 15.1 15.2 15.3 15.4 Jakobsson, ME et al. (2013) Identification and characterization of a novel human methyltransferase modulating Hsp70 protein function through lysine methylation. J. Biol. Chem. 288 27752-63 PubMed GONUTS page
  16. 16.0 16.1 16.2 16.3 Ribeil, JA et al. (2007) Hsp70 regulates erythropoiesis by preventing caspase-3-mediated cleavage of GATA-1. Nature 445 102-5 PubMed GONUTS page
  17. 17.0 17.1 Roder, K et al. (2014) RING finger protein RNF207, a novel regulator of cardiac excitation. J. Biol. Chem. 289 33730-40 PubMed GONUTS page
  18. Han, C et al. (2007) HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain. Biochem. Biophys. Res. Commun. 353 280-5 PubMed GONUTS page
  19. 19.0 19.1 19.2 19.3 19.4 19.5 Imai, Y et al. (2002) CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol. Cell 10 55-67 PubMed GONUTS page
  20. Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
  21. Kesimer, M et al. (2009) Characterization of exosome-like vesicles released from human tracheobronchial ciliated epithelium: a possible role in innate defense. FASEB J. 23 1858-68 PubMed GONUTS page
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  24. Bastos-Amador, P et al. (2012) Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. J Proteomics 75 3574-84 PubMed GONUTS page
  25. Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page
  26. 26.0 26.1 Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
  27. 27.0 27.1 27.2 Khalouei, S et al. (2014) Stress-induced localization of HSPA6 (HSP70B') and HSPA1A (HSP70-1) proteins to centrioles in human neuronal cells. Cell Stress Chaperones 19 321-7 PubMed GONUTS page
  28. 28.0 28.1 Shi, Y et al. (1998) Molecular chaperones as HSF1-specific transcriptional repressors. Genes Dev. 12 654-66 PubMed GONUTS page
  29. 29.0 29.1 29.2 Laroia, G et al. (1999) Control of mRNA decay by heat shock-ubiquitin-proteasome pathway. Science 284 499-502 PubMed GONUTS page
  30. 30.0 30.1 30.2 30.3 30.4 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
  31. Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page
  32. Castello, A et al. (2012) Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 149 1393-406 PubMed GONUTS page
  33. Jønson, L et al. (2007) Molecular composition of IMP1 ribonucleoprotein granules. Mol. Cell Proteomics 6 798-811 PubMed GONUTS page
  34. 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
  35. 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
  36. 36.0 36.1 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
  37. 37.00 37.01 37.02 37.03 37.04 37.05 37.06 37.07 37.08 37.09 37.10 37.11 37.12 37.13 37.14 37.15 37.16 37.17 37.18 37.19 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  38. 38.0 38.1 Dias, V et al. (2013) The role of oxidative stress in Parkinson's disease. J Parkinsons Dis 3 461-91 PubMed GONUTS page
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[7d38fb9010b0922893729690] /wiki/index.php/HUMAN:HS71A Error from line 252 of /usr/local/github/wiki-extensions/wiki-extensions-hulab/AnnotationLinks/AnnotationLinks.php: Call to a member function getIdentifier() on null

Backtrace:

#0 /usr/local/github/wiki-extensions/wiki-extensions-hulab/AnnotationLinks/AnnotationLinks.php(70): AnnotationLinks::getQuickGOannotations(string, array)
#1 /var/www/html/go/wiki/includes/parser/Parser.php(3888): AnnotationLinks::renderAnnotations(NULL, array, Parser, PPFrame_DOM)
#2 /var/www/html/go/wiki/includes/parser/Preprocessor_DOM.php(1362): Parser->extensionSubstitution(array, PPFrame_DOM)
#3 /var/www/html/go/wiki/includes/parser/Parser.php(2942): PPFrame_DOM->expand(DOMElement, integer)
#4 /var/www/html/go/wiki/includes/parser/Parser.php(1293): Parser->replaceVariables(string)
#5 /var/www/html/go/wiki/includes/parser/Parser.php(443): Parser->internalParse(string)
#6 /var/www/html/go/wiki/includes/content/WikitextContent.php(323): Parser->parse(string, Title, ParserOptions, boolean, boolean, integer)
#7 /var/www/html/go/wiki/includes/content/AbstractContent.php(516): WikitextContent->fillParserOutput(Title, integer, ParserOptions, boolean, ParserOutput)
#8 /var/www/html/go/wiki/includes/content/ContentHandler.php(1324): AbstractContent->getParserOutput(Title, integer, ParserOptions)
#9 /usr/local/github/wiki-extensions/wiki-extensions-hulab/CirrusSearch/includes/Updater.php(348): ContentHandler->getParserOutputForIndexing(WikiPage, ParserCache)
#10 /usr/local/github/wiki-extensions/wiki-extensions-hulab/CirrusSearch/includes/Updater.php(407): CirrusSearch\Updater::buildDocument(CirrusSearch, WikiPage, CirrusSearch\Connection, integer, integer, integer)
#11 /usr/local/github/wiki-extensions/wiki-extensions-hulab/CirrusSearch/includes/Updater.php(205): CirrusSearch\Updater->buildDocumentsForPages(array, integer)
#12 /usr/local/github/wiki-extensions/wiki-extensions-hulab/CirrusSearch/includes/Updater.php(83): CirrusSearch\Updater->updatePages(array, integer)
#13 /usr/local/github/wiki-extensions/wiki-extensions-hulab/CirrusSearch/includes/Job/LinksUpdate.php(52): CirrusSearch\Updater->updateFromTitle(Title)
#14 /usr/local/github/wiki-extensions/wiki-extensions-hulab/CirrusSearch/includes/Job/Job.php(99): CirrusSearch\Job\LinksUpdate->doJob()
#15 /var/www/html/go/wiki/includes/jobqueue/JobRunner.php(296): CirrusSearch\Job\Job->run()
#16 /var/www/html/go/wiki/includes/jobqueue/JobRunner.php(193): JobRunner->executeJob(CirrusSearch\Job\LinksUpdate, Wikimedia\Rdbms\LBFactorySimple, BufferingStatsdDataFactory, integer)
#17 /var/www/html/go/wiki/includes/MediaWiki.php(1002): JobRunner->run(array)
#18 /var/www/html/go/wiki/includes/MediaWiki.php(988): MediaWiki->triggerSyncJobs(integer, MediaWiki\Logger\LegacyLogger)
#19 /var/www/html/go/wiki/includes/MediaWiki.php(912): MediaWiki->triggerJobs()
#20 /var/www/html/go/wiki/includes/MediaWiki.php(727): MediaWiki->restInPeace(string, boolean)
#21 /var/www/html/go/wiki/includes/MediaWiki.php(750): MediaWiki->{closure}()
#22 /var/www/html/go/wiki/includes/MediaWiki.php(557): MediaWiki->doPostOutputShutdown(string)
#23 /var/www/html/go/wiki/index.php(42): MediaWiki->run()
#24 {main}

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