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P63017

- HSP7C_MOUSE

UniProt

P63017 - HSP7C_MOUSE

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Protein

Heat shock cognate 71 kDa protein

Gene
Hspa8, Hsc70, Hsc73
Organism
Mus musculus (Mouse)
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 By similarity. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion By similarity.

Sites

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

Regions

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

GO - Molecular functioni

  1. ATPase activity, coupled Source: MGI
  2. ATP binding Source: UniProtKB-KW
  3. protein binding Source: IntAct
  4. unfolded protein binding Source: MGI

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. chaperone mediated protein folding requiring cofactor Source: MGI
  3. clathrin coat disassembly Source: MGI
  4. mRNA processing Source: UniProtKB-KW
  5. negative regulation of transcription, DNA-templated Source: UniProtKB
  6. protein folding Source: MGI
  7. regulation of cell cycle Source: MGI
  8. response to stress Source: UniProtKB-KW
  9. RNA splicing Source: UniProtKB-KW
  10. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Repressor

Keywords - Biological processi

mRNA processing, mRNA splicing, Stress response, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_213550. HSF1-dependent transactivation.
REACT_222185. Regulation of HSF1-mediated heat shock response.
REACT_223784. Attenuation phase.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock cognate 71 kDa protein
Alternative name(s):
Heat shock 70 kDa protein 8
Gene namesi
Name:Hspa8
Synonyms:Hsc70, Hsc73
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:105384. Hspa8.

Subcellular locationi

Cytoplasm By similarity. Melanosome By similarity. Nucleusnucleolus By similarity. Cell membrane By similarity
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 By similarity.

GO - Cellular componenti

  1. cytosol Source: MGI
  2. extracellular vesicular exosome Source: MGI
  3. intracellular Source: MGI
  4. melanosome Source: UniProtKB-SubCell
  5. nucleolus Source: UniProtKB
  6. nucleus Source: UniProtKB
  7. plasma membrane Source: UniProtKB-SubCell
  8. Prp19 complex Source: UniProtKB
  9. ribonucleoprotein complex Source: UniProtKB
  10. spliceosomal complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 646645Heat shock cognate 71 kDa proteinPRO_0000078271Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine By similarity
Modified residuei108 – 1081N6-acetyllysine1 Publication
Modified residuei153 – 1531Phosphoserine By similarity
Modified residuei246 – 2461N6-acetyllysine1 Publication
Modified residuei319 – 3191N6-acetyllysine; alternate1 Publication
Modified residuei319 – 3191N6-succinyllysine; alternate1 Publication
Modified residuei328 – 3281N6-acetyllysine1 Publication
Modified residuei362 – 3621Phosphoserine By similarity
Modified residuei512 – 5121N6-acetyllysine; alternate1 Publication
Modified residuei512 – 5121N6-succinyllysine; alternate1 Publication
Modified residuei524 – 5241N6-acetyllysine1 Publication
Modified residuei561 – 5611N6,N6,N6-trimethyllysine; alternate1 Publication
Modified residuei561 – 5611N6,N6,N6-trimethyllysine; by METTL21A; alternate By similarity
Modified residuei589 – 5891N6-acetyllysine By similarity
Modified residuei597 – 5971N6-acetyllysine By similarity
Modified residuei601 – 6011N6-acetyllysine1 Publication

Post-translational modificationi

Acetylated By similarity.
ISGylated.1 Publication
Trimethylation at Lys-561 reduces fibrillar SNCA binding By similarity.

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP63017.
PaxDbiP63017.
PRIDEiP63017.

2D gel databases

COMPLUYEAST-2DPAGEP63017.
REPRODUCTION-2DPAGEIPI00323357.
P63017.
Q6NZD0.
SWISS-2DPAGEP63017.
UCD-2DPAGEP63017.

Expressioni

Tissue specificityi

Ubiquitous.

Inductioni

Constitutively synthesized.

Gene expression databases

ArrayExpressiP63017.
BgeeiP63017.
CleanExiMM_HSPA8.
GenevestigatoriP63017.

Interactioni

Subunit structurei

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with PACRG. Interacts with BAG1. Interacts with DNAJC7. 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 IRAK1BP1 and HSPH1/HSP105. Interacts with TRIM5. Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity By similarity. Following LPS binding, may form a complex with CXCR4, GDF5 and HSP90AA1 By similarity. Interacts with PARK2 By similarity.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Klc1O884473EBI-433443,EBI-301550

Protein-protein interaction databases

BioGridi200428. 43 interactions.
DIPiDIP-32353N.
IntActiP63017. 33 interactions.
MINTiMINT-189032.

Structurei

Secondary structure

1
646
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115
Beta strandi13 – 2210
Beta strandi25 – 284
Beta strandi36 – 394
Beta strandi42 – 443
Beta strandi49 – 513
Helixi53 – 575
Turni58 – 614
Helixi63 – 653
Helixi70 – 723
Turni73 – 753
Helixi81 – 866
Turni87 – 893
Beta strandi91 – 977
Beta strandi100 – 1078
Beta strandi110 – 1145
Helixi116 – 13520
Beta strandi141 – 1466
Helixi152 – 16413
Beta strandi168 – 1747
Helixi175 – 1828
Turni183 – 1864
Beta strandi187 – 20014
Beta strandi205 – 2139
Beta strandi216 – 22510
Helixi230 – 24920
Helixi257 – 27317
Turni274 – 2763
Beta strandi278 – 28811
Beta strandi291 – 2988
Helixi299 – 31214
Helixi314 – 32411
Helixi328 – 3303
Beta strandi333 – 3386
Helixi339 – 3424
Helixi344 – 35310
Turni354 – 3563
Turni365 – 3673
Helixi368 – 38013

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CQXX-ray2.30A/B1-381[»]
ProteinModelPortaliP63017.
SMRiP63017. Positions 1-621.

Miscellaneous databases

EvolutionaryTraceiP63017.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni186 – 377192Interaction with BAG1 By similarityAdd
BLAST

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0443.
GeneTreeiENSGT00750000117237.
HOVERGENiHBG051845.
InParanoidiP63017.
KOiK03283.
OMAiGENKIFT.
OrthoDBiEOG7PCJGF.
PhylomeDBiP63017.
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]

Sequencei

Sequence statusi: Complete.

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

P63017-1 [UniParc]FASTAAdd to Basket

« Hide

MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL    50
IGDAAKNQVA MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR 100
PKVQVEYKGE TKSFYPEEVS SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF 150
NDSQRQATKD AGTIAGLNVL RIINEPTAAA IAYGLDKKVG AERNVLIFDL 200
GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH FIAEFKRKHK 250
KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA 300
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL 350
QDFFNGKELN KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS 400
LGIETAGGVM TVLIKRNTTI PTKQTQTFTT YSDNQPGVLI QVYEGERAMT 450
KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI DANGILNVSA VDKSTGKENK 500
ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN SLESYAFNMK 550
ATVEDEKLQG KINDEDKQKI LDKCNEIISW LDKNQTAEKE EFEHQQKELE 600
KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD 646
Length:646
Mass (Da):70,871
Last modified:August 1, 1988 - v1
Checksum:i03A27B30E6C076ED
GO

Sequence cautioni

The sequence BAE31508.1 differs from that shown. Reason: Frameshift at positions 256 and 269.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91I → V in BAE28187. 1 Publication
Sequence conflicti35 – 351N → K in BAE30081. 1 Publication
Sequence conflicti35 – 351N → K in BAE30861. 1 Publication
Sequence conflicti35 – 351N → K in BAE30753. 1 Publication
Sequence conflicti268 – 2681E → G in BAE31432. 1 Publication
Sequence conflicti268 – 2681E → G in BAE31346. 1 Publication
Sequence conflicti269 – 2691R → G in BAE31508. 1 Publication
Sequence conflicti353 – 3531F → C in BAE31664. 1 Publication
Sequence conflicti428 – 4281F → L in AAA37869. 1 Publication
Sequence conflicti428 – 4281F → L in AAB18391. 1 Publication
Sequence conflicti432 – 4321S → Y in BAE30707. 1 Publication
Sequence conflicti589 – 5891K → E in AAH66191. 1 Publication
Sequence conflicti645 – 6451V → M in BAE30272. 1 Publication
Sequence conflicti645 – 6451V → M in BAE31427. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19141 mRNA. Translation: AAA37869.1.
U27129 mRNA. Translation: AAC52836.1.
U73744 Genomic DNA. Translation: AAB18391.1.
AK035286 mRNA. Translation: BAC29016.1.
AK075935 mRNA. Translation: BAC36065.1.
AK145579 mRNA. Translation: BAE26523.1.
AK146708 mRNA. Translation: BAE27374.1.
AK146985 mRNA. Translation: BAE27588.1.
AK147864 mRNA. Translation: BAE28187.1.
AK150474 mRNA. Translation: BAE29591.1.
AK150498 mRNA. Translation: BAE29612.1.
AK150701 mRNA. Translation: BAE29780.1.
AK150958 mRNA. Translation: BAE29990.1.
AK151065 mRNA. Translation: BAE30081.1.
AK151127 mRNA. Translation: BAE30135.1.
AK151287 mRNA. Translation: BAE30272.1.
AK151435 mRNA. Translation: BAE30398.1.
AK151516 mRNA. Translation: BAE30465.1.
AK151537 mRNA. Translation: BAE30484.1.
AK151775 mRNA. Translation: BAE30681.1.
AK151808 mRNA. Translation: BAE30707.1.
AK151865 mRNA. Translation: BAE30753.1.
AK151892 mRNA. Translation: BAE30776.1.
AK151948 mRNA. Translation: BAE30822.1.
AK151997 mRNA. Translation: BAE30861.1.
AK152598 mRNA. Translation: BAE31346.1.
AK152697 mRNA. Translation: BAE31427.1.
AK152703 mRNA. Translation: BAE31432.1.
AK152803 mRNA. Translation: BAE31508.1. Frameshift.
AK153032 mRNA. Translation: BAE31664.1.
AK153834 mRNA. Translation: BAE32204.1.
AK159479 mRNA. Translation: BAE35116.1.
AK164000 mRNA. Translation: BAE37581.1.
AK166643 mRNA. Translation: BAE38912.1.
AK166721 mRNA. Translation: BAE38970.1.
AK166767 mRNA. Translation: BAE39005.1.
AK166776 mRNA. Translation: BAE39012.1.
AK166808 mRNA. Translation: BAE39036.1.
AK166830 mRNA. Translation: BAE39053.1.
AK166846 mRNA. Translation: BAE39065.1.
AK166861 mRNA. Translation: BAE39076.1.
AK166873 mRNA. Translation: BAE39084.1.
AK166908 mRNA. Translation: BAE39109.1.
AK166910 mRNA. Translation: BAE39111.1.
AK166913 mRNA. Translation: BAE39113.1.
AK166933 mRNA. Translation: BAE39127.1.
AK167043 mRNA. Translation: BAE39211.1.
AK167121 mRNA. Translation: BAE39269.1.
AK167122 mRNA. Translation: BAE39270.1.
AK167134 mRNA. Translation: BAE39280.1.
AK167163 mRNA. Translation: BAE39304.1.
AK167218 mRNA. Translation: BAE39344.1.
AK167229 mRNA. Translation: BAE39353.1.
AK167845 mRNA. Translation: BAE39865.1.
AK167910 mRNA. Translation: BAE39917.1.
AK168492 mRNA. Translation: BAE40379.1.
AK168519 mRNA. Translation: BAE40398.1.
AK168542 mRNA. Translation: BAE40419.1.
AK168711 mRNA. Translation: BAE40553.1.
AK168750 mRNA. Translation: BAE40590.1.
AK168776 mRNA. Translation: BAE40612.1.
AK168887 mRNA. Translation: BAE40704.1.
AK168934 mRNA. Translation: BAE40745.1.
AK169093 mRNA. Translation: BAE40876.1.
AK169179 mRNA. Translation: BAE40957.1.
AK169236 mRNA. Translation: BAE41004.1.
AK169293 mRNA. Translation: BAE41049.1.
BC006722 mRNA. Translation: AAH06722.1.
BC066191 mRNA. Translation: AAH66191.1.
BC085486 mRNA. Translation: AAH85486.1.
BC089322 mRNA. Translation: AAH89322.1.
BC089457 mRNA. Translation: AAH89457.1.
BC106193 mRNA. Translation: AAI06194.1.
X54401 Genomic DNA. Translation: CAA38267.1.
X54402 Genomic DNA. Translation: CAA38268.1.
X54403 Genomic DNA. Translation: CAA38269.1.
CCDSiCCDS23083.1.
PIRiA45935.
JC4853.
RefSeqiNP_112442.2. NM_031165.4.
UniGeneiMm.290774.
Mm.336743.
Mm.351377.
Mm.412745.
Mm.485345.

Genome annotation databases

EnsembliENSMUST00000015800; ENSMUSP00000015800; ENSMUSG00000015656.
GeneIDi15481.
KEGGimmu:15481.
UCSCiuc009ozx.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M19141 mRNA. Translation: AAA37869.1 .
U27129 mRNA. Translation: AAC52836.1 .
U73744 Genomic DNA. Translation: AAB18391.1 .
AK035286 mRNA. Translation: BAC29016.1 .
AK075935 mRNA. Translation: BAC36065.1 .
AK145579 mRNA. Translation: BAE26523.1 .
AK146708 mRNA. Translation: BAE27374.1 .
AK146985 mRNA. Translation: BAE27588.1 .
AK147864 mRNA. Translation: BAE28187.1 .
AK150474 mRNA. Translation: BAE29591.1 .
AK150498 mRNA. Translation: BAE29612.1 .
AK150701 mRNA. Translation: BAE29780.1 .
AK150958 mRNA. Translation: BAE29990.1 .
AK151065 mRNA. Translation: BAE30081.1 .
AK151127 mRNA. Translation: BAE30135.1 .
AK151287 mRNA. Translation: BAE30272.1 .
AK151435 mRNA. Translation: BAE30398.1 .
AK151516 mRNA. Translation: BAE30465.1 .
AK151537 mRNA. Translation: BAE30484.1 .
AK151775 mRNA. Translation: BAE30681.1 .
AK151808 mRNA. Translation: BAE30707.1 .
AK151865 mRNA. Translation: BAE30753.1 .
AK151892 mRNA. Translation: BAE30776.1 .
AK151948 mRNA. Translation: BAE30822.1 .
AK151997 mRNA. Translation: BAE30861.1 .
AK152598 mRNA. Translation: BAE31346.1 .
AK152697 mRNA. Translation: BAE31427.1 .
AK152703 mRNA. Translation: BAE31432.1 .
AK152803 mRNA. Translation: BAE31508.1 . Frameshift.
AK153032 mRNA. Translation: BAE31664.1 .
AK153834 mRNA. Translation: BAE32204.1 .
AK159479 mRNA. Translation: BAE35116.1 .
AK164000 mRNA. Translation: BAE37581.1 .
AK166643 mRNA. Translation: BAE38912.1 .
AK166721 mRNA. Translation: BAE38970.1 .
AK166767 mRNA. Translation: BAE39005.1 .
AK166776 mRNA. Translation: BAE39012.1 .
AK166808 mRNA. Translation: BAE39036.1 .
AK166830 mRNA. Translation: BAE39053.1 .
AK166846 mRNA. Translation: BAE39065.1 .
AK166861 mRNA. Translation: BAE39076.1 .
AK166873 mRNA. Translation: BAE39084.1 .
AK166908 mRNA. Translation: BAE39109.1 .
AK166910 mRNA. Translation: BAE39111.1 .
AK166913 mRNA. Translation: BAE39113.1 .
AK166933 mRNA. Translation: BAE39127.1 .
AK167043 mRNA. Translation: BAE39211.1 .
AK167121 mRNA. Translation: BAE39269.1 .
AK167122 mRNA. Translation: BAE39270.1 .
AK167134 mRNA. Translation: BAE39280.1 .
AK167163 mRNA. Translation: BAE39304.1 .
AK167218 mRNA. Translation: BAE39344.1 .
AK167229 mRNA. Translation: BAE39353.1 .
AK167845 mRNA. Translation: BAE39865.1 .
AK167910 mRNA. Translation: BAE39917.1 .
AK168492 mRNA. Translation: BAE40379.1 .
AK168519 mRNA. Translation: BAE40398.1 .
AK168542 mRNA. Translation: BAE40419.1 .
AK168711 mRNA. Translation: BAE40553.1 .
AK168750 mRNA. Translation: BAE40590.1 .
AK168776 mRNA. Translation: BAE40612.1 .
AK168887 mRNA. Translation: BAE40704.1 .
AK168934 mRNA. Translation: BAE40745.1 .
AK169093 mRNA. Translation: BAE40876.1 .
AK169179 mRNA. Translation: BAE40957.1 .
AK169236 mRNA. Translation: BAE41004.1 .
AK169293 mRNA. Translation: BAE41049.1 .
BC006722 mRNA. Translation: AAH06722.1 .
BC066191 mRNA. Translation: AAH66191.1 .
BC085486 mRNA. Translation: AAH85486.1 .
BC089322 mRNA. Translation: AAH89322.1 .
BC089457 mRNA. Translation: AAH89457.1 .
BC106193 mRNA. Translation: AAI06194.1 .
X54401 Genomic DNA. Translation: CAA38267.1 .
X54402 Genomic DNA. Translation: CAA38268.1 .
X54403 Genomic DNA. Translation: CAA38269.1 .
CCDSi CCDS23083.1.
PIRi A45935.
JC4853.
RefSeqi NP_112442.2. NM_031165.4.
UniGenei Mm.290774.
Mm.336743.
Mm.351377.
Mm.412745.
Mm.485345.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3CQX X-ray 2.30 A/B 1-381 [» ]
ProteinModelPortali P63017.
SMRi P63017. Positions 1-621.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 200428. 43 interactions.
DIPi DIP-32353N.
IntActi P63017. 33 interactions.
MINTi MINT-189032.

2D gel databases

COMPLUYEAST-2DPAGE P63017.
REPRODUCTION-2DPAGE IPI00323357.
P63017.
Q6NZD0.
SWISS-2DPAGE P63017.
UCD-2DPAGE P63017.

Proteomic databases

MaxQBi P63017.
PaxDbi P63017.
PRIDEi P63017.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000015800 ; ENSMUSP00000015800 ; ENSMUSG00000015656 .
GeneIDi 15481.
KEGGi mmu:15481.
UCSCi uc009ozx.3. mouse.

Organism-specific databases

CTDi 3312.
MGIi MGI:105384. Hspa8.

Phylogenomic databases

eggNOGi COG0443.
GeneTreei ENSGT00750000117237.
HOVERGENi HBG051845.
InParanoidi P63017.
KOi K03283.
OMAi GENKIFT.
OrthoDBi EOG7PCJGF.
PhylomeDBi P63017.
TreeFami TF105042.

Enzyme and pathway databases

Reactomei REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_213550. HSF1-dependent transactivation.
REACT_222185. Regulation of HSF1-mediated heat shock response.
REACT_223784. Attenuation phase.

Miscellaneous databases

EvolutionaryTracei P63017.
NextBioi 288328.
PROi P63017.
SOURCEi Search...

Gene expression databases

ArrayExpressi P63017.
Bgeei P63017.
CleanExi MM_HSPA8.
Genevestigatori P63017.

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. "Developmental regulation of a constitutively expressed mouse mRNA encoding a 72-kDa heat shock-like protein."
    Giebel L.B., Dworniczak B.P., Bautz E.K.F.
    Dev. Biol. 125:200-207(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Developmental regulation of murine integrin beta 1 subunit- and Hsc73-encoding genes in mammary gland: sequence of a new mouse Hsc73 cDNA."
    Soulier S., Vilotte J.-L., L'Huillier P.J., Mercier J.-C.
    Gene 172:285-289(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129.
    Tissue: Mammary gland.
  3. "Characterization and expression of the mouse Hsc70 gene."
    Hunt C.R., Parsian A.J., Goswami P.C., Kozak C.A.
    Biochim. Biophys. Acta 1444:315-325(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and DBA/2.
    Tissue: Amnion, Bone marrow, Heart, Kidney, Liver, Stomach, Thymus and Urinary bladder.
  5. "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].
    Strain: C57BL/6 and FVB/N.
    Tissue: Brain, Embryo, Embryonic germ cell, Eye and Mammary gland.
  6. Lubec G., Kang S.U., Klug S., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 4-49; 57-71; 77-102; 113-155; 160-188; 221-246; 300-319; 326-342; 349-357; 362-384; 424-447; 540-550 AND 584-597, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  7. "Mouse U14 snRNA is encoded in an intron of the mouse cognate hsc70 heat shock gene."
    Liu J., Maxwell E.S.
    Nucleic Acids Res. 18:6565-6571(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 333-383; 438-452 AND 580-587.
  8. "Association of HSP105 with HSC70 in high molecular mass complexes in mouse FM3A cells."
    Hatayama T., Yasuda K., Yasuda K.
    Biochem. Biophys. Res. Commun. 248:395-401(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSPH1.
  9. "Hsp105alpha suppresses Hsc70 chaperone activity by inhibiting Hsc70 ATPase activity."
    Yamagishi N., Ishihara K., Hatayama T.
    J. Biol. Chem. 279:41727-41733(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSPH1.
  10. Cited for: ISGYLATION.
  11. "The disordered amino-terminus of SIMPL interacts with members of the 70-kDa heat-shock protein family."
    Haag Breese E., Uversky V.N., Georgiadis M.M., Harrington M.A.
    DNA Cell Biol. 25:704-714(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IRAK1BP1, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "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.
  13. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-108; LYS-246; LYS-319; LYS-328; LYS-512; LYS-524 AND LYS-601, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-319 AND LYS-512, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.

Entry informationi

Entry nameiHSP7C_MOUSE
AccessioniPrimary (citable) accession number: P63017
Secondary accession number(s): P08109
, P12225, Q3U6R0, Q3U764, Q3U7D7, Q3U7E2, Q3U9B4, Q3U9G0, Q3UGM0, Q5FWJ6, Q62373, Q62374, Q62375, Q6NZD0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: September 3, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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