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P11142

- HSP7C_HUMAN

UniProt

P11142 - HSP7C_HUMAN

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Protein

Heat shock cognate 71 kDa protein

Gene

HSPA8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. 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) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase CHIP.3 Publications

Sites

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

Regions

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

GO - Molecular functioni

  1. ATPase activity Source: BHF-UCL
  2. ATPase activity, coupled Source: UniProtKB
  3. ATP binding Source: BHF-UCL
  4. enzyme binding Source: BHF-UCL
  5. G-protein coupled receptor binding Source: ParkinsonsUK-UCL
  6. heat shock protein binding Source: BHF-UCL
  7. MHC class II protein complex binding Source: UniProt
  8. poly(A) RNA binding Source: UniProtKB
  9. ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
  10. unfolded protein binding Source: UniProt

GO - Biological processi

  1. ATP catabolic process Source: BHF-UCL
  2. axon guidance Source: Reactome
  3. chaperone mediated protein folding requiring cofactor Source: Ensembl
  4. clathrin coat disassembly Source: Ensembl
  5. gene expression Source: Reactome
  6. membrane organization Source: Reactome
  7. mRNA metabolic process Source: Reactome
  8. mRNA processing Source: UniProtKB-KW
  9. negative regulation of fibril organization Source: BHF-UCL
  10. negative regulation of transcription, DNA-templated Source: UniProtKB
  11. neurotransmitter secretion Source: Reactome
  12. post-Golgi vesicle-mediated transport Source: Reactome
  13. protein folding Source: UniProtKB
  14. protein refolding Source: UniProt
  15. regulation of cell cycle Source: Ensembl
  16. response to unfolded protein Source: UniProtKB
  17. RNA metabolic process Source: Reactome
  18. RNA splicing Source: UniProtKB-KW
  19. synaptic transmission Source: Reactome
  20. transcription, DNA-templated Source: UniProtKB-KW
  21. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Repressor

Keywords - Biological processi

Host-virus interaction, mRNA processing, mRNA splicing, Stress response, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_19287. Lysosome Vesicle Biogenesis.
REACT_19400. Golgi Associated Vesicle Biogenesis.
REACT_200624. Attenuation phase.
REACT_200775. HSF1-dependent transactivation.
REACT_200780. Regulation of HSF1-mediated heat shock response.
REACT_22292. CHL1 interactions.
REACT_23947. GABA synthesis, release, reuptake and degradation.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock cognate 71 kDa protein
Alternative name(s):
Heat shock 70 kDa protein 8
Lipopolysaccharide-associated protein 1
Short name:
LAP-1
Short name:
LPS-associated protein 1
Gene namesi
Name:HSPA8
Synonyms:HSC70, HSP73, HSPA10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:5241. HSPA8.

Subcellular locationi

Cytoplasm. Melanosome. Nucleusnucleolus. Cell membrane
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock.

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane Source: Reactome
  3. cytosol Source: UniProt
  4. extracellular space Source: UniProt
  5. extracellular vesicular exosome Source: UniProtKB
  6. focal adhesion Source: UniProtKB
  7. intracellular Source: UniProtKB
  8. membrane Source: UniProtKB
  9. nucleus Source: UniProtKB
  10. plasma membrane Source: Reactome
  11. Prp19 complex Source: UniProtKB
  12. ribonucleoprotein complex Source: UniProtKB
  13. spliceosomal complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi561 – 5611K → R: Complete loss of in vitro methylation by METTL21A. 2 Publications

Organism-specific databases

PharmGKBiPA29507.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 646645Heat shock cognate 71 kDa proteinPRO_0000078270Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei108 – 1081N6-acetyllysineBy similarity
Modified residuei153 – 1531Phosphoserine1 Publication
Modified residuei246 – 2461N6-acetyllysine1 Publication
Modified residuei319 – 3191N6-acetyllysine; alternate1 Publication
Modified residuei319 – 3191N6-succinyllysine; alternateBy similarity
Modified residuei328 – 3281N6-acetyllysineBy similarity
Modified residuei362 – 3621Phosphoserine1 Publication
Modified residuei512 – 5121N6-acetyllysine; alternateBy similarity
Modified residuei512 – 5121N6-succinyllysine; alternateBy similarity
Modified residuei524 – 5241N6-acetyllysineBy similarity
Modified residuei561 – 5611N6,N6,N6-trimethyllysine; by METTL21A2 Publications
Modified residuei589 – 5891N6-acetyllysine1 Publication
Modified residuei597 – 5971N6-acetyllysine1 Publication
Modified residuei601 – 6011N6-acetyllysine1 Publication

Post-translational modificationi

Acetylated.4 Publications
ISGylated.2 Publications
Trimethylation at Lys-561 reduces fibrillar SNCA binding.

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP11142.
PaxDbiP11142.
PeptideAtlasiP11142.
PRIDEiP11142.

2D gel databases

DOSAC-COBS-2DPAGEP11142.
OGPiP11142.
REPRODUCTION-2DPAGEIPI00003865.
SWISS-2DPAGEP11142.
UCD-2DPAGEP11142.

PTM databases

PhosphoSiteiP11142.

Miscellaneous databases

PMAP-CutDBP11142.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Inductioni

Constitutively synthesized.

Gene expression databases

BgeeiP11142.
CleanExiHS_HSPA8.
ExpressionAtlasiP11142. baseline and differential.
GenevestigatoriP11142.

Organism-specific databases

HPAiCAB002056.

Interactioni

Subunit structurei

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with PACRG. Interacts with HSPH1/HSP105. Interacts with IRAK1BP1 and BAG1. Interacts with DNAJC7 and DNAJB14 (via J domain). Interacts (via C-terminus) with the E3 ligase CHIP forming a 210 kDa complex of one CHIP and two HSPA8 molecules. Interacts with CITED1 (via N-terminus); the interaction suppresses the association of CITED1 to p300/CBP and Smad-mediated transcription transactivation. Component of the PRP19-CDC5L splicing complex composed of a core complex comprising a homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts with SV40 VP1. Interacts with TRIM5. Part of a complex composed at least of ASCL2, C11orf30/EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity. Interacts with METTL21A. Following LPS binding, may form a complex with CXCR4, GDF5 and HSP90AA1. Interacts with PARK2.15 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q99IB83EBI-351896,EBI-6927928From a different organism.
ACTBP607092EBI-351896,EBI-353944
AICDAQ9GZX72EBI-351896,EBI-3834328
ARRB1P494074EBI-351896,EBI-743313
ARRB2P321214EBI-351896,EBI-714559
ATP13A2Q9NQ112EBI-351896,EBI-6308763
BAG1Q9993310EBI-351896,EBI-1030678
BAG2O958163EBI-351896,EBI-355275
EBNA-LPQ8AZK73EBI-351896,EBI-1185167From a different organism.
EGFRP005335EBI-351896,EBI-297353
GAKO149765EBI-351896,EBI-714707
LDHAP003384EBI-351896,EBI-372327
LRRK2Q5S0075EBI-351896,EBI-5323863
MP034854EBI-351896,EBI-2547543From a different organism.
STUB1Q9UNE75EBI-351896,EBI-357085

Protein-protein interaction databases

BioGridi109544. 301 interactions.
IntActiP11142. 92 interactions.
MINTiMINT-4998609.
STRINGi9606.ENSP00000227378.

Structurei

Secondary structure

1
646
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 104Combined sources
Beta strandi13 – 2210Combined sources
Beta strandi25 – 284Combined sources
Beta strandi36 – 405Combined sources
Beta strandi42 – 443Combined sources
Beta strandi49 – 524Combined sources
Helixi53 – 575Combined sources
Turni58 – 614Combined sources
Helixi63 – 653Combined sources
Helixi70 – 734Combined sources
Helixi81 – 866Combined sources
Helixi87 – 893Combined sources
Beta strandi91 – 977Combined sources
Beta strandi100 – 1078Combined sources
Beta strandi110 – 1145Combined sources
Helixi116 – 13520Combined sources
Beta strandi141 – 1466Combined sources
Helixi152 – 16413Combined sources
Beta strandi168 – 1747Combined sources
Helixi175 – 1828Combined sources
Helixi185 – 1873Combined sources
Beta strandi193 – 2008Combined sources
Beta strandi205 – 2139Combined sources
Beta strandi216 – 22510Combined sources
Helixi230 – 24920Combined sources
Helixi253 – 2553Combined sources
Helixi257 – 27418Combined sources
Beta strandi277 – 28812Combined sources
Beta strandi291 – 2988Combined sources
Helixi299 – 3057Combined sources
Helixi307 – 3126Combined sources
Helixi314 – 32310Combined sources
Helixi328 – 3303Combined sources
Beta strandi333 – 3386Combined sources
Helixi339 – 3424Combined sources
Helixi344 – 35310Combined sources
Turni354 – 3563Combined sources
Beta strandi357 – 3604Combined sources
Turni365 – 3673Combined sources
Helixi368 – 38013Combined sources
Beta strandi641 – 6444Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AGYX-ray1.85C/D/F639-646[»]
3AGZX-ray2.51C/D/E/F639-646[»]
3ESKX-ray2.05B635-646[»]
3FZFX-ray2.20A4-381[»]
3FZHX-ray2.00A4-381[»]
3FZKX-ray2.10A4-381[»]
3FZLX-ray2.20A4-381[»]
3FZMX-ray2.30A4-381[»]
3LDQX-ray1.90A4-381[»]
3M3ZX-ray2.10A4-381[»]
4H5NX-ray1.86A/B2-384[»]
4H5RX-ray1.64A/B2-384[»]
4H5TX-ray1.90A2-384[»]
4H5VX-ray1.75A2-384[»]
4H5WX-ray1.94A/B2-384[»]
4HWIX-ray2.27A5-381[»]
ProteinModelPortaliP11142.
SMRiP11142. Positions 1-621.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11142.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni186 – 377192Interaction with BAG1Add
BLAST

Domaini

The N-terminal 1-386 residues constitute the ATPase domain, while residues 387-646 form the peptide-binding domain.1 Publication

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiCOG0443.
GeneTreeiENSGT00750000117237.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP11142.
KOiK03283.
OMAiGENKIFT.
OrthoDBiEOG7PCJGF.
PhylomeDBiP11142.
TreeFamiTF105042.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P11142-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL
60 70 80 90 100
IGDAAKNQVA MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR
110 120 130 140 150
PKVQVEYKGE TKSFYPEEVS SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF
160 170 180 190 200
NDSQRQATKD AGTIAGLNVL RIINEPTAAA IAYGLDKKVG AERNVLIFDL
210 220 230 240 250
GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH FIAEFKRKHK
260 270 280 290 300
KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA
310 320 330 340 350
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL
360 370 380 390 400
QDFFNGKELN KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS
410 420 430 440 450
LGIETAGGVM TVLIKRNTTI PTKQTQTFTT YSDNQPGVLI QVYEGERAMT
460 470 480 490 500
KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI DANGILNVSA VDKSTGKENK
510 520 530 540 550
ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN SLESYAFNMK
560 570 580 590 600
ATVEDEKLQG KINDEDKQKI LDKCNEIINW LDKNQTAEKE EFEHQQKELE
610 620 630 640
KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD
Length:646
Mass (Da):70,898
Last modified:July 1, 1989 - v1
Checksum:i9AA27B210730670C
GO
Isoform 2 (identifier: P11142-2) [UniParc]FASTAAdd to Basket

Also known as: HSC54

The sequence of this isoform differs from the canonical sequence as follows:
     464-616: Missing.

Show »
Length:493
Mass (Da):53,518
Checksum:iBA2CFBD68F17784E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321D → Y.
Corresponds to variant rs11551602 [ dbSNP | Ensembl ].
VAR_049619
Natural varianti459 – 4591F → L.
Corresponds to variant rs11551598 [ dbSNP | Ensembl ].
VAR_049620

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei464 – 616153Missing in isoform 2. 1 PublicationVSP_002427Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00371 Genomic DNA. Translation: CAA68445.1.
AB034951 mRNA. Translation: BAB18615.1.
AF352832 mRNA. Translation: AAK17898.1.
BC016179 mRNA. Translation: AAH16179.1.
BC016660 mRNA. Translation: AAH16660.1.
BC019816 mRNA. Translation: AAH19816.1.
CCDSiCCDS44754.1. [P11142-2]
CCDS8440.1. [P11142-1]
PIRiA27077.
RefSeqiNP_006588.1. NM_006597.5. [P11142-1]
NP_694881.1. NM_153201.3. [P11142-2]
XP_006718894.1. XM_006718831.1. [P11142-1]
UniGeneiHs.180414.

Genome annotation databases

EnsembliENST00000227378; ENSP00000227378; ENSG00000109971. [P11142-1]
ENST00000453788; ENSP00000404372; ENSG00000109971. [P11142-2]
ENST00000532636; ENSP00000437125; ENSG00000109971. [P11142-1]
ENST00000534624; ENSP00000432083; ENSG00000109971. [P11142-1]
GeneIDi3312.
KEGGihsa:3312.
UCSCiuc001pyo.3. human. [P11142-1]
uc001pyp.3. human. [P11142-2]

Polymorphism databases

DMDMi123648.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00371 Genomic DNA. Translation: CAA68445.1 .
AB034951 mRNA. Translation: BAB18615.1 .
AF352832 mRNA. Translation: AAK17898.1 .
BC016179 mRNA. Translation: AAH16179.1 .
BC016660 mRNA. Translation: AAH16660.1 .
BC019816 mRNA. Translation: AAH19816.1 .
CCDSi CCDS44754.1. [P11142-2 ]
CCDS8440.1. [P11142-1 ]
PIRi A27077.
RefSeqi NP_006588.1. NM_006597.5. [P11142-1 ]
NP_694881.1. NM_153201.3. [P11142-2 ]
XP_006718894.1. XM_006718831.1. [P11142-1 ]
UniGenei Hs.180414.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3AGY X-ray 1.85 C/D/F 639-646 [» ]
3AGZ X-ray 2.51 C/D/E/F 639-646 [» ]
3ESK X-ray 2.05 B 635-646 [» ]
3FZF X-ray 2.20 A 4-381 [» ]
3FZH X-ray 2.00 A 4-381 [» ]
3FZK X-ray 2.10 A 4-381 [» ]
3FZL X-ray 2.20 A 4-381 [» ]
3FZM X-ray 2.30 A 4-381 [» ]
3LDQ X-ray 1.90 A 4-381 [» ]
3M3Z X-ray 2.10 A 4-381 [» ]
4H5N X-ray 1.86 A/B 2-384 [» ]
4H5R X-ray 1.64 A/B 2-384 [» ]
4H5T X-ray 1.90 A 2-384 [» ]
4H5V X-ray 1.75 A 2-384 [» ]
4H5W X-ray 1.94 A/B 2-384 [» ]
4HWI X-ray 2.27 A 5-381 [» ]
ProteinModelPortali P11142.
SMRi P11142. Positions 1-621.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109544. 301 interactions.
IntActi P11142. 92 interactions.
MINTi MINT-4998609.
STRINGi 9606.ENSP00000227378.

Chemistry

BindingDBi P11142.
ChEMBLi CHEMBL1275223.

PTM databases

PhosphoSitei P11142.

Polymorphism databases

DMDMi 123648.

2D gel databases

DOSAC-COBS-2DPAGE P11142.
OGPi P11142.
REPRODUCTION-2DPAGE IPI00003865.
SWISS-2DPAGE P11142.
UCD-2DPAGE P11142.

Proteomic databases

MaxQBi P11142.
PaxDbi P11142.
PeptideAtlasi P11142.
PRIDEi P11142.

Protocols and materials databases

DNASUi 3312.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000227378 ; ENSP00000227378 ; ENSG00000109971 . [P11142-1 ]
ENST00000453788 ; ENSP00000404372 ; ENSG00000109971 . [P11142-2 ]
ENST00000532636 ; ENSP00000437125 ; ENSG00000109971 . [P11142-1 ]
ENST00000534624 ; ENSP00000432083 ; ENSG00000109971 . [P11142-1 ]
GeneIDi 3312.
KEGGi hsa:3312.
UCSCi uc001pyo.3. human. [P11142-1 ]
uc001pyp.3. human. [P11142-2 ]

Organism-specific databases

CTDi 3312.
GeneCardsi GC11M122982.
H-InvDB HIX0033867.
HGNCi HGNC:5241. HSPA8.
HPAi CAB002056.
MIMi 600816. gene.
neXtProti NX_P11142.
PharmGKBi PA29507.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0443.
GeneTreei ENSGT00750000117237.
HOGENOMi HOG000228135.
HOVERGENi HBG051845.
InParanoidi P11142.
KOi K03283.
OMAi GENKIFT.
OrthoDBi EOG7PCJGF.
PhylomeDBi P11142.
TreeFami TF105042.

Enzyme and pathway databases

Reactomei REACT_19287. Lysosome Vesicle Biogenesis.
REACT_19400. Golgi Associated Vesicle Biogenesis.
REACT_200624. Attenuation phase.
REACT_200775. HSF1-dependent transactivation.
REACT_200780. Regulation of HSF1-mediated heat shock response.
REACT_22292. CHL1 interactions.
REACT_23947. GABA synthesis, release, reuptake and degradation.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSi HSPA8. human.
EvolutionaryTracei P11142.
GeneWikii HSPA8.
GenomeRNAii 3312.
NextBioi 13136.
PMAP-CutDB P11142.
PROi P11142.
SOURCEi Search...

Gene expression databases

Bgeei P11142.
CleanExi HS_HSPA8.
ExpressionAtlasi P11142. baseline and differential.
Genevestigatori P11142.

Family and domain databases

Gene3Di 1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProi IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view ]
Pfami PF00012. HSP70. 1 hit.
[Graphical view ]
PRINTSi PR00301. HEATSHOCK70.
SUPFAMi SSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEi PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure and expression of a human gene coding for a 71 kd heat shock 'cognate' protein."
    Dworniczak B.P., Mirault M.-E.
    Nucleic Acids Res. 15:5181-5197(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  2. "Molecular and functional characterization of HSC54, a novel variant of human heat shock cognate protein 70."
    Tsukahara F., Yoshioka T., Muraki T.
    Mol. Pharmacol. 58:1257-1263(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  3. "Complete coding sequence of human HSC70."
    Niswonger M.L., Berk L.R., Srivastava P.K.
    Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta and Skin.
  5. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-49; 57-71; 77-102; 103-155; 160-188; 221-247; 273-311; 326-342; 349-416; 424-447; 452-493; 510-517; 540-550; 570-597 AND 602-646, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  6. Cited for: PROTEIN SEQUENCE OF 2-49; 57-72; 78-88; 113-188; 221-247; 300-319; 326-342; 349-357; 362-384; 424-447; 452-469; 510-517; 540-550 AND 584-609, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma and Ovarian carcinoma.
  7. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 4-49; 57-71; 77-88; 113-126; 129-155; 160-187; 221-246; 300-311; 329-342; 362-384; 424-447; 540-550 AND 574-583, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  8. "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
    Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
    Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 50-55; 103-107 AND 580-596.
  9. "Identification of the 70kD heat shock cognate protein (Hsc70) and alpha-actinin-1 as novel phosphotyrosine-containing proteins in T lymphocytes."
    Egerton M., Moritz R.L., Druker B., Kelso A., Simpson R.J.
    Biochem. Biophys. Res. Commun. 224:666-674(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 77-86; 221-236 AND 302-311.
  10. "A newly uncovered group of distantly related lysine methyltransferases preferentially interact with molecular chaperones to regulate their activity."
    Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.
    PLoS Genet. 9:E1003210-E1003210(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 551-567, METHYLATION AT LYS-561, MUTAGENESIS OF LYS-561, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "Intracellular localization and partial amino acid sequence of a stress-inducible 40-kDa protein in HeLa cells."
    Hattori H., Liu Y.-C., Tohnai I., Ueda M., Kaneda T., Kobayashi T., Tanabe K., Ohtsuka K.
    Cell Struct. Funct. 17:77-86(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  12. Cited for: INTERACTION WITH BAG1, DOMAIN.
  13. "Expression and location of Hsp70/Hsc-binding anti-apoptotic protein BAG-1 and its variants in normal tissues and tumor cell lines."
    Takayama S., Krajewski S., Krajewska M., Kitada S., Zapata J.M., Kochel K., Knee D., Scudiero D., Tudor G., Miller G.J., Miyashita T., Yamada M., Reed J.C.
    Cancer Res. 58:3116-3131(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BAG1.
  14. "HSC70 interactions with SV40 viral proteins differ between permissive and nonpermissive mammalian cells."
    Sainis L., Angelidis C., Pagoulatos G.N., Lazaridis L.
    Cell Stress Chaperones 5:132-138(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SV40 VP1.
  15. "The MSG1 non-DNA-binding transactivator binds to the p300/CBP coactivators, enhancing their functional link to the Smad transcription factors."
    Yahata T., de Caestecker M.P., Lechleider R.J., Andriole S., Roberts A.B., Isselbacher K.J., Shioda T.
    J. Biol. Chem. 275:8825-8834(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CITED1.
  16. Cited for: FUNCTION, IDENTIFICATION AS LPS RECEPTOR, INTERACTION WITH CXCR4; GDF5 AND HSP90AA1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  17. "A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death."
    Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.
    J. Biol. Chem. 278:51901-51910(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PACRG.
  18. Cited for: ISGYLATION.
  19. Cited for: INTERACTION WITH TSC2, IDENTIFICATION BY MASS SPECTROMETRY.
  20. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  21. "HERC5 is an IFN-induced HECT-type E3 protein ligase that mediates type I IFN-induced ISGylation of protein targets."
    Wong J.J., Pung Y.F., Sze N.S., Chin K.C.
    Proc. Natl. Acad. Sci. U.S.A. 103:10735-10740(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HERC5, ISGYLATION.
  22. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  23. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  24. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Identification and characterization of a novel nuclear protein complex involved in nuclear hormone receptor-mediated gene regulation."
    Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., Samuels H.H.
    J. Biol. Chem. 284:7542-7552(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH HCFC1; MKI67; C11ORF30; MATR3; ZNF335; TUBB2A; CCAR2; ASCL2; RBBP5 AND WDR5.
  26. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  27. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-246; LYS-319; LYS-589; LYS-597 AND LYS-601, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "Hsp70 interacts with the retroviral restriction factor TRIM5alpha and assists the folding of TRIM5alpha."
    Hwang C.Y., Holl J., Rajan D., Lee Y., Kim S., Um M., Kwon K.S., Song B.
    J. Biol. Chem. 285:7827-7837(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM5.
  29. Cited for: IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L COMPLEX, SUBCELLULAR LOCATION.
  30. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "The E3 ubiquitin ligase CHIP and the molecular chaperone Hsc70 form a dynamic, tethered complex."
    Smith M.C., Scaglione K.M., Assimon V.A., Patury S., Thompson A.D., Dickey C.A., Southworth D.R., Paulson H.L., Gestwicki J.E., Zuiderweg E.R.
    Biochemistry 52:5354-5364(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH CHIP.
  34. "Identification and characterization of a novel human methyltransferase modulating Hsp70 function through lysine methylation."
    Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S., Melki R., Falnes P.O.
    J. Biol. Chem. 288:27752-27763(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-561, MUTAGENESIS OF LYS-561, INTERACTION WITH METTL21A.
  35. "Endoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligase."
    Matsumura Y., Sakai J., Skach W.R.
    J. Biol. Chem. 288:31069-31079(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN ERAD, INTERACTION WITH CHIP.
  36. "High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy."
    Hasson S.A., Kane L.A., Yamano K., Huang C.H., Sliter D.A., Buehler E., Wang C., Heman-Ackah S.M., Hessa T., Guha R., Martin S.E., Youle R.J.
    Nature 504:291-295(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PARK2.
  37. "Electrostatic interactions of Hsp-organizing protein tetratricopeptide domains with Hsp70 and Hsp90: computational analysis and protein engineering."
    Kajander T., Sachs J.N., Goldman A., Regan L.
    J. Biol. Chem. 284:25364-25374(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-634.
  38. Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 4-381 IN COMPLEXES WITH ATP AND ATP ANALOGS.
  39. Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 4-381 IN COMPLEXES WITH ATP ANALOGS.

Entry informationi

Entry nameiHSP7C_HUMAN
AccessioniPrimary (citable) accession number: P11142
Secondary accession number(s): Q9H3R6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 26, 2014
This is version 184 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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