Protein: P11142

UniprotKB AC UniprotKB ID Gene name Full name Species Curated set
P11142 (Uniprot) HSP7C_HUMAN HSPA8 Heat shock cognate 71 kDa protein human No
Uniprot: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). The co-chaperones have been shown to not only regulate different steps of the ATPase cycle of HSP70, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661, PubMed:23018488). The affinity of HSP70 for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. HSP70 goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 (PubMed:24318877, PubMed:27474739, PubMed:24121476, PubMed:26865365). Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:10722728, PubMed:11276205). Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase STUB1 (PubMed:23990462). more..
GO ID 1 Function 1 Module ID 1 GO ID 2 Function 2 Module ID 2 Association Probability (PrOnto) Interaction Probability (PrOnto)
GO:0006725 cellular aromatic compound metabolic process 395 GO:0007165 signal transduction 534, 609 5.44e-126 5.27e-27
Module ID (MoonGO) GO ID (BP) GO Name
2 GO:0044267 cellular protein metabolic process
2 GO:0010467 gene expression
2 GO:0006139 nucleobase-containing compound metabolic process
2 GO:0060255 regulation of macromolecule metabolic process
2 GO:0007165 signal transduction
24 GO:0016070 RNA metabolic process
24 GO:0006464 cellular protein modification process
24 GO:0034654 nucleobase-containing compound biosynthetic process
24 GO:0006796 phosphate-containing compound metabolic process
24 GO:0031325 positive regulation of cellular metabolic process
24 GO:0010604 positive regulation of macromolecule metabolic process
24 GO:0051173 positive regulation of nitrogen compound metabolic process
24 GO:2000112 regulation of cellular macromolecule biosynthetic process
24 GO:0010468 regulation of gene expression
24 GO:0019219 regulation of nucleobase-containing compound metabolic process
24 GO:0051246 regulation of protein metabolic process
24 GO:0007165 signal transduction
155 GO:0006464 cellular protein modification process
155 GO:0060255 regulation of macromolecule metabolic process
157 GO:0034645 cellular macromolecule biosynthetic process
157 GO:0044267 cellular protein metabolic process
157 GO:0090304 nucleic acid metabolic process
192 GO:0034645 cellular macromolecule biosynthetic process
192 GO:0006464 cellular protein modification process
192 GO:0010467 gene expression
192 GO:0090304 nucleic acid metabolic process
192 GO:0009893 positive regulation of metabolic process
192 GO:0060255 regulation of macromolecule metabolic process
192 GO:0007165 signal transduction
211 GO:0034645 cellular macromolecule biosynthetic process
211 GO:0044271 cellular nitrogen compound biosynthetic process
211 GO:0090304 nucleic acid metabolic process
211 GO:0060255 regulation of macromolecule metabolic process
237 GO:0022607 cellular component assembly
237 GO:0034645 cellular macromolecule biosynthetic process
237 GO:0044271 cellular nitrogen compound biosynthetic process
237 GO:0006464 cellular protein modification process
237 GO:0051649 establishment of localization in cell
237 GO:0010467 gene expression
237 GO:0031324 negative regulation of cellular metabolic process
237 GO:0010605 negative regulation of macromolecule metabolic process
237 GO:0051172 negative regulation of nitrogen compound metabolic process
237 GO:0090304 nucleic acid metabolic process
237 GO:0033365 protein localization to organelle
237 GO:0015031 protein transport
237 GO:0050790 regulation of catalytic activity
237 GO:0051128 regulation of cellular component organization
283 GO:0006464 cellular protein modification process
283 GO:0060255 regulation of macromolecule metabolic process
300 GO:0016070 RNA metabolic process
300 GO:0044271 cellular nitrogen compound biosynthetic process
300 GO:0031325 positive regulation of cellular metabolic process
300 GO:0010604 positive regulation of macromolecule metabolic process
300 GO:0051173 positive regulation of nitrogen compound metabolic process
300 GO:2000112 regulation of cellular macromolecule biosynthetic process
300 GO:0010468 regulation of gene expression
300 GO:0019219 regulation of nucleobase-containing compound metabolic process
326 GO:0044267 cellular protein metabolic process
337 GO:0022607 cellular component assembly
337 GO:0035556 intracellular signal transduction
337 GO:0006468 protein phosphorylation
337 GO:0060255 regulation of macromolecule metabolic process
395 GO:0006139 nucleobase-containing compound metabolic process
395 GO:0019538 protein metabolic process
434 GO:0044267 cellular protein metabolic process
485 GO:0034645 cellular macromolecule biosynthetic process
485 GO:0090304 nucleic acid metabolic process
534 GO:0007166 cell surface receptor signaling pathway
534 GO:0006464 cellular protein modification process
534 GO:0033554 cellular response to stress
534 GO:0010467 gene expression
534 GO:0006796 phosphate-containing compound metabolic process
534 GO:0060255 regulation of macromolecule metabolic process
534 GO:0009966 regulation of signal transduction
534 GO:0009628 response to abiotic stimulus
545 GO:0044267 cellular protein metabolic process
545 GO:0006139 nucleobase-containing compound metabolic process
551 GO:0034645 cellular macromolecule biosynthetic process
551 GO:0090304 nucleic acid metabolic process
551 GO:0034654 nucleobase-containing compound biosynthetic process
551 GO:0010604 positive regulation of macromolecule metabolic process
551 GO:0051173 positive regulation of nitrogen compound metabolic process
609 GO:0007166 cell surface receptor signaling pathway
609 GO:0006464 cellular protein modification process
609 GO:0071310 cellular response to organic substance
609 GO:0031325 positive regulation of cellular metabolic process
609 GO:0010604 positive regulation of macromolecule metabolic process
609 GO:0051173 positive regulation of nitrogen compound metabolic process
609 GO:0051246 regulation of protein metabolic process
609 GO:0006355 regulation of transcription, DNA-templated
747 GO:0010467 gene expression
747 GO:0090304 nucleic acid metabolic process
774 GO:0006464 cellular protein modification process
774 GO:0060255 regulation of macromolecule metabolic process
833 GO:0034645 cellular macromolecule biosynthetic process
833 GO:0006464 cellular protein modification process
833 GO:0006796 phosphate-containing compound metabolic process
833 GO:0060255 regulation of macromolecule metabolic process
Module ID (MoonGO) GO ID (CC) GO Name
2 GO:0005829 cytosol
2 GO:0005634 nucleus
24 GO:0005829 cytosol
24 GO:0005654 nucleoplasm
155 GO:0005634 nucleus
157 GO:0005654 nucleoplasm
162 GO:0005634 nucleus
192 GO:0005829 cytosol
192 GO:0005654 nucleoplasm
211 GO:0005829 cytosol
211 GO:0031981 nuclear lumen
237 GO:0005829 cytosol
237 GO:0012505 endomembrane system
237 GO:0005615 extracellular space
237 GO:0043232 intracellular non-membrane-bounded organelle
237 GO:0070013 intracellular organelle lumen
237 GO:0044428 nuclear part
237 GO:0031982 vesicle
283 GO:0012505 endomembrane system
283 GO:0044428 nuclear part
300 GO:0070013 intracellular organelle lumen
300 GO:0044428 nuclear part
317 GO:0005829 cytosol
326 GO:0005829 cytosol
326 GO:0005634 nucleus
337 GO:0005829 cytosol
337 GO:0043232 intracellular non-membrane-bounded organelle
337 GO:0005634 nucleus
346 GO:0043232 intracellular non-membrane-bounded organelle
346 GO:0005634 nucleus
395 GO:0005634 nucleus
434 GO:0005829 cytosol
434 GO:0070062 extracellular exosome
434 GO:0005634 nucleus
485 GO:0043232 intracellular non-membrane-bounded organelle
485 GO:0005634 nucleus
501 GO:0031090 organelle membrane
534 GO:0005829 cytosol
534 GO:0012505 endomembrane system
534 GO:0005654 nucleoplasm
545 GO:0005829 cytosol
545 GO:0005634 nucleus
545 GO:0031982 vesicle
551 GO:0005829 cytosol
551 GO:0005615 extracellular space
551 GO:0043232 intracellular non-membrane-bounded organelle
551 GO:0005654 nucleoplasm
551 GO:0031982 vesicle
609 GO:0005829 cytosol
609 GO:0043232 intracellular non-membrane-bounded organelle
609 GO:0070013 intracellular organelle lumen
609 GO:0005634 nucleus
609 GO:0005886 plasma membrane
729 GO:0005829 cytosol
729 GO:0005634 nucleus
747 GO:0070013 intracellular organelle lumen
747 GO:0005634 nucleus
774 GO:0005634 nucleus
833 GO:0005829 cytosol
GO ID (BP) GO Name Evidence Code (GO EC)
GO:0000398 mRNA splicing, via spliceosome TAS
GO:0006351 transcription, DNA-templated IEA
GO:0006457 protein folding NAS
GO:0006479 protein methylation TAS
GO:0006986 response to unfolded protein NAS
GO:0007269 neurotransmitter secretion TAS
GO:0009267 cellular response to starvation TAS
GO:0016032 viral process IEA
GO:0031647 regulation of protein stability IMP
GO:0042026 protein refolding IDA
GO:0043254 regulation of protein complex assembly TAS
GO:0043312 neutrophil degranulation TAS
GO:0043488 regulation of mRNA stability TAS
GO:0044829 positive regulation by host of viral genome replication IEA
GO:0045892 negative regulation of transcription, DNA-templated IDA
GO:0046034 ATP metabolic process IDA
GO:0048026 positive regulation of mRNA splicing, via spliceosome IEA
GO:0051085 chaperone mediated protein folding requiring cofactor IEA
GO:0051726 regulation of cell cycle IEA
GO:0061024 membrane organization TAS
GO:0061635 regulation of protein complex stability ISS
GO:0061684 chaperone-mediated autophagy TAS
GO:0061738 late endosomal microautophagy IEA
GO:0061740 protein targeting to lysosome involved in chaperone-mediated autophagy TAS
GO:0061741 chaperone-mediated protein transport involved in chaperone-mediated autophagy NAS
GO:0072318 clathrin coat disassembly IEA
GO:1900034 regulation of cellular response to heat TAS
GO:1902904 negative regulation of supramolecular fiber organization IDA
GO:1904589 regulation of protein import TAS
GO:1904764 chaperone-mediated autophagy translocation complex disassembly ISS
GO ID (CC) GO Name Evidence Code (GO EC)
GO:0000151 ubiquitin ligase complex IDA
GO:0000974 Prp19 complex IDA
GO:0005576 extracellular region TAS
GO:0005615 extracellular space IDA
GO:0005622 intracellular NAS
GO:0005634 nucleus IDA
GO:0005654 nucleoplasm TAS
GO:0005681 spliceosomal complex IEA
GO:0005730 nucleolus IEA
GO:0005765 lysosomal membrane ISS
GO:0005770 late endosome IEA
GO:0005829 cytosol TAS
GO:0005886 plasma membrane TAS
GO:0005925 focal adhesion IDA
GO:0016020 membrane IDA
GO:0030529 intracellular ribonucleoprotein complex IDA
GO:0031012 extracellular matrix IDA
GO:0034774 secretory granule lumen TAS
GO:0042470 melanosome IEA
GO:0043202 lysosomal lumen TAS
GO:0043209 myelin sheath IEA
GO:0061202 clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane TAS
GO:0070062 extracellular exosome IDA
GO:0072562 blood microparticle IDA
GO:0098575 lumenal side of lysosomal membrane TAS
GO:0098793 presynapse IEA
GO:1904813 ficolin-1-rich granule lumen TAS
GO ID 1 Component 1 GO ID 2 Component 2 Association Probability (PrOnto) Interaction Probability (PrOnto)
GO:0000151 ubiquitin ligase complex GO:0005576 extracellular region 7.25e-11 4.98e-07
GO:0000151 ubiquitin ligase complex GO:0005886 plasma membrane 2.77e-20 3.36e-26
GO:0000151 ubiquitin ligase complex GO:0016020 membrane 6.01e-29 2.12e-49
GO:0005576 extracellular region GO:0005622 intracellular 8.27e-38 5.46e-09
GO:0005576 extracellular region GO:0005634 nucleus 4.48e-91 1.28e-107
GO:0005576 extracellular region GO:0005654 nucleoplasm 6.62e-72 7.68e-98
GO:0005576 extracellular region GO:0005730 nucleolus 6.04e-15 4.85e-05
GO:0005615 extracellular space GO:0005622 intracellular 1.63e-10 4.39e-07
GO:0005615 extracellular space GO:0005634 nucleus 6.26e-54 1.10e-77
GO:0005615 extracellular space GO:0005654 nucleoplasm 1.00e-49 3.88e-77
GO:0005615 extracellular space GO:0005730 nucleolus 6.97e-10 1.36e-14
GO:0005622 intracellular GO:0005886 plasma membrane 0.00e+00 9.14e-55
GO:0005622 intracellular GO:0016020 membrane 1.69e-220 1.49e-57
GO:0005634 nucleus GO:0005765 lysosomal membrane 3.45e-10 9.81e-32
GO:0005634 nucleus GO:0005770 late endosome 4.75e-02 1.57e-04
GO:0005634 nucleus GO:0005886 plasma membrane 5.35e-300 7.52e-165
GO:0005634 nucleus GO:0016020 membrane 0.00e+00 4.39e-236
GO:0005634 nucleus GO:0031012 extracellular matrix 1.58e-13 4.18e-03
GO:0005634 nucleus GO:0070062 extracellular exosome 6.30e-13 4.54e-26
GO:0005634 nucleus GO:0098793 presynapse 3.45e-05 2.45e-27
GO:0005654 nucleoplasm GO:0005765 lysosomal membrane 7.59e-07 1.29e-14
GO:0005654 nucleoplasm GO:0005886 plasma membrane 9.14e-199 6.17e-196
GO:0005654 nucleoplasm GO:0016020 membrane 5.76e-255 1.32e-206
GO:0005654 nucleoplasm GO:0031012 extracellular matrix 2.78e-09 4.74e-33
GO:0005654 nucleoplasm GO:0070062 extracellular exosome 3.37e-20 1.23e-35
GO:0005654 nucleoplasm GO:0098793 presynapse 2.80e-05 4.49e-75
GO:0005681 spliceosomal complex GO:0005886 plasma membrane 3.11e-19 7.74e-95
GO:0005681 spliceosomal complex GO:0016020 membrane 6.04e-13 3.30e-19
GO:0005730 nucleolus GO:0005886 plasma membrane 7.70e-47 3.09e-07
GO:0005730 nucleolus GO:0016020 membrane 8.89e-46 1.83e-10
GO:0005829 cytosol GO:0031012 extracellular matrix 4.46e-06 5.18e-08
GO:0005886 plasma membrane GO:0030529 intracellular ribonucleoprotein complex 1.50e-65 9.46e-34
Interactor Also a MoonDB EMF protein
BAG3_HUMAN No
SGTA_HUMAN No
KEAP1_HUMAN No
CHIP_HUMAN Yes: Q9UNE7 (MoonDB)
MOS_HUMAN No
EGFR_HUMAN Yes: P00533 (MoonDB)
AGO2_HUMAN No
MLF2_HUMAN Yes: Q15773 (MoonDB)
HSF2_HUMAN No
PSMD2_HUMAN Yes: Q13200 (MoonDB)
AASD1_HUMAN No
ACTB_HUMAN No
ANDR_HUMAN Yes: P10275 (MoonDB)
ANR40_HUMAN No
AOFB_HUMAN No
ARIP4_HUMAN No
ARMC5_HUMAN No
AT132_HUMAN No
ATM_HUMAN No
ATPA_HUMAN No
B4DE84_HUMAN No
BAG1_HUMAN No
BAG2_HUMAN No
BAG4_HUMAN No
BRCA1_HUMAN No
CACP_HUMAN No
CAPZB_HUMAN No
CC117_HUMAN No
CCAR2_HUMAN No
CD5R1_HUMAN No
CDK10_HUMAN No
CDK9_HUMAN No
CFLAR_HUMAN No
CLCN2_HUMAN No
CO7A1_HUMAN No
COPG1_HUMAN No
COPG2_HUMAN No
CT194_HUMAN No
CTCFL_HUMAN No
DCP1B_HUMAN No
DDX11_HUMAN No
DET1_HUMAN No
DNJB2_HUMAN No
DNJB6_HUMAN No
DPP3_HUMAN No
DYN3_HUMAN No
E2AK4_HUMAN No
EF2_HUMAN No
EIPR1_HUMAN No
ENC1_HUMAN No
ENOA_HUMAN Yes: P06733 (MoonDB)
ERBB2_HUMAN Yes: P04626 (MoonDB)
ERCC2_HUMAN No
ERH_HUMAN No
F16P1_HUMAN No
FANCC_HUMAN No
FBH1_HUMAN No
GBB1_HUMAN No
GBB2_HUMAN No
GBB3_HUMAN No
GBB4_HUMAN No
GCH1_HUMAN No
GCP3_HUMAN No
GCR_HUMAN No
GNA13_HUMAN No
GNAL_HUMAN No
GNAZ_HUMAN No
GNB5_HUMAN No
GRK6_HUMAN No
GTD2A_HUMAN No
HCFC1_HUMAN No
HDAC6_HUMAN No
HEMGN_HUMAN No
HLTF_HUMAN No
HPBP1_HUMAN No
HS105_HUMAN No
HSF1_HUMAN Yes: Q00613 (MoonDB)
HSP72_HUMAN No
IKKE_HUMAN No
IL32_HUMAN No
IRF3_HUMAN No
IRS4_HUMAN No
JUN_HUMAN No
KC1E_HUMAN No
KCJ11_HUMAN No
KLH38_HUMAN No
KLHL1_HUMAN No
KSR2_HUMAN No
M3K8_HUMAN No
MCM5_HUMAN No
MCM7_HUMAN No
MDM2_HUMAN Yes: Q00987 (MoonDB)
MERL_HUMAN No
MK08_HUMAN No
MLF1_HUMAN Yes: P58340 (MoonDB)
MUTYH_HUMAN No
NAL12_HUMAN No
NAT10_HUMAN No
NDKB_HUMAN No
NHLC1_HUMAN No
NISCH_HUMAN No
NMI_HUMAN No
NOA1_HUMAN No
NOD1_HUMAN No
NPHP4_HUMAN No
NUCG_HUMAN No
OGA_HUMAN No
P53_HUMAN Yes: P04637 (MoonDB)
PADI4_HUMAN No
PDPK1_HUMAN Yes: O15530 (MoonDB)
PGTA_HUMAN No
PHC1_HUMAN No
PHS_HUMAN Yes: P61457 (MoonDB)
PIWL1_HUMAN No
PIWL2_HUMAN No
PIWL4_HUMAN No
PRAME_HUMAN No
PRDM1_HUMAN No
PRS6B_HUMAN No
PRS7_HUMAN No
Q308M6_HUMAN No
Q573B4_HUMAN No
Q59FJ7_HUMAN No
Q59FP4_HUMAN No
Q59GL9_HUMAN No
Q5C8S5_HUMAN No
Q5ULA9_HUMAN No
Q7Z4G2_HUMAN No
Q86WA0_HUMAN No
Q8IZN1_HUMAN No
Q8N5Q5_HUMAN No
Q8WYX9_HUMAN No
Q96S08_HUMAN No
Q9NPV4_HUMAN No
Q9UMP2_HUMAN No
RA51D_HUMAN No
RAD51_HUMAN No
RAF1_HUMAN Yes: P04049 (MoonDB)
RAG1_HUMAN No
REC8_HUMAN No
RFC1_HUMAN No
RGS11_HUMAN No
RGS2_HUMAN No
RPC1_HUMAN No
SETB1_HUMAN No
SF3B3_HUMAN No
SIM2_HUMAN No
SIR6_HUMAN No
SKP2_HUMAN No
SMRD2_HUMAN No
SRP68_HUMAN No
SRRT_HUMAN No
STIP1_HUMAN No
T4S1_HUMAN No
TADA3_HUMAN No
TBB1_HUMAN No
TBX22_HUMAN No
TELT_HUMAN No
TESK2_HUMAN No
TET3_HUMAN No
TF3C5_HUMAN No
TFDP3_HUMAN No
TGM2_HUMAN No
TRI17_HUMAN No
TRI38_HUMAN No
TTC1_HUMAN No
U5S1_HUMAN No
UBB_HUMAN Yes: P0CG47 (MoonDB)
UBC_HUMAN Yes: P0CG48 (MoonDB)
UBP18_HUMAN No
UBP49_HUMAN No
WSB2_HUMAN No
ZBT20_HUMAN No
ZN215_HUMAN No
PMID Article Title
1286667 Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes.
1586970 Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells.
3037489 Structure and expression of a human gene coding for a 71 kd heat shock 'cognate' protein.
8713105 Identification of the 70kD heat shock cognate protein (Hsc70) and alpha-actinin-1 as novel phosphotyrosine-containing proteins in T lymphocytes.
9305631 BAG-1 modulates the chaperone activity of Hsp70/Hsc70.
9499401 Molecular chaperones as HSF1-specific transcriptional repressors.
9679980 Expression and location of Hsp70/Hsc-binding anti-apoptotic protein BAG-1 and its variants in normal tissues and tumor cell lines.
10722728 The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors.
11093761 Molecular and functional characterization of HSC54, a novel variant of human heat shock cognate protein 70.
11147964 HSC70 interactions with SV40 viral proteins differ between permissive and nonpermissive mammalian cells.
11276205 A CD14-independent LPS receptor cluster.
14532270 A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death.
15489334 The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
15708368 Small glutamine-rich tetratricopeptide repeat-containing protein is composed of three structural units with distinct functions.
15936278 HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome.
15963462 Phosphorylation and binding partner analysis of the TSC1-TSC2 complex.
16139798 Proteomic identification of proteins conjugated to ISG15 in mouse and human cells.
16815975 HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets.
17081065 Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes.
17182002 HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain.
17289661 Molecular composition of IMP1 ribonucleoprotein granules.
17525332 ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.
19131338 Identification and characterization of a novel nuclear protein complex involved in nuclear hormone receptor-mediated gene regulation.
19256508 Novel adenosine-derived inhibitors of 70 kDa heat shock protein, discovered through structure-based design.
19413330 Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
19586912 Electrostatic interactions of Hsp-organizing protein tetratricopeptide domains with Hsp70 and Hsp90: computational analysis and protein engineering.
19608861 Lysine acetylation targets protein complexes and co-regulates major cellular functions.
19690332 Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
20053985 Hsp70 interacts with the retroviral restriction factor TRIM5alpha and assists the folding of TRIM5alpha.
20068231 Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
20176811 Molecular architecture of the human Prp19/CDC5L complex.
21148293 The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508.
21150129 A novel ER J-protein DNAJB12 accelerates ER-associated degradation of membrane proteins including CFTR.
21269460 Initial characterization of the human central proteome.
21526763 Adenosine-derived inhibitors of 78 kDa glucose regulated protein (Grp78) ATPase: insights into isoform selectivity.
22814378 N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.
23018488 A novel mammalian ER-located J-protein, DNAJB14, can accelerate ERAD of misfolded membrane proteins.
23186163 Toward a comprehensive characterization of a human cancer cell phosphoproteome.
23349634 A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity.
23865999 The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex.
23921388 Identification and characterization of a novel human methyltransferase modulating Hsp70 function through lysine methylation.
23973223 The ubiquitin ligase Stub1 negatively modulates regulatory T cell suppressive activity by promoting degradation of the transcription factor Foxp3.
23990462 Endoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligase.
24121476 HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.
24122553 The co-chaperone DNAJC12 binds to Hsc70 and is upregulated by endoplasmic reticulum stress.
24129315 Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.
24270810 High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy.
24275569 An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
24318877 Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro.
24732912 Expression of DNAJB12 or DNAJB14 causes coordinate invasion of the nucleus by membranes associated with a novel nuclear pore structure.
24880125 Degradation of AF1Q by chaperone-mediated autophagy.
25114211 Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.
25218447 Uncovering global SUMOylation signaling networks in a site-specific manner.
25281747 RING finger protein RNF207, a novel regulator of cardiac excitation.
25944712 N-terminome analysis of the human mitochondrial proteome.
26865365 The human HSP70 family of chaperones: where do we stand?
27346687 DNAJC21 mutations link a cancer-prone bone marrow failure syndrome to corruption in 60S ribosome subunit maturation.
27474739 Non-canonical interactions between heat shock cognate protein 70 (Hsc70) and Bcl2-associated anthanogene (BAG) co-chaperones are important for client release.
27708256 ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation.
27916661 Tetrameric assembly of K(+) channels requires ER-located chaperone proteins.
No results found.
Domain Name Domain ID Source
A27077 A27077 PIR
Hsp_70_fam IPR013126 InterPro
Heat_shock_70_CS IPR018181 InterPro
HSP70_peptide-bd_sf IPR029047 InterPro
HSP70_C_sf IPR029048 InterPro
HSP70 PF00012 Pfam
HEATSHOCK70 PR00301 PRINTS
HSP70_1 PS00297 PROSITE
HSP70_2 PS00329 PROSITE
HSP70_3 PS01036 PROSITE
SSF100920 SSF100920 SUPFAM
SSF100934 SSF100934 SUPFAM