Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P63017

- HSP7C_MOUSE

UniProt

P63017 - HSP7C_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Heat shock cognate 71 kDa protein

Gene

Hspa8

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. Participates in the ER-associated degradation (ERAD) quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase CHIP (By similarity).By similarity

Sites

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

Regions

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

GO - Molecular functioni

  1. ATPase activity, coupled Source: MGI
  2. ATP binding Source: UniProtKB-KW
  3. poly(A) RNA binding Source: Ensembl
  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 fibril organization Source: Ensembl
  6. negative regulation of transcription, DNA-templated Source: UniProtKB
  7. protein folding Source: MGI
  8. protein refolding Source: Ensembl
  9. regulation of cell cycle Source: MGI
  10. response to stress Source: UniProtKB-KW
  11. RNA splicing Source: UniProtKB-KW
  12. 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).By similarity

GO - Cellular componenti

  1. blood microparticle Source: Ensembl
  2. cytosol Source: MGI
  3. extracellular vesicular exosome Source: MGI
  4. intracellular Source: MGI
  5. nucleolus Source: Ensembl
  6. nucleus Source: UniProtKB
  7. plasma membrane Source: UniProtKB-KW
  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 – 11RemovedBy similarity
Chaini2 – 646645Heat shock cognate 71 kDa proteinPRO_0000078271Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei108 – 1081N6-acetyllysine1 Publication
Modified residuei153 – 1531PhosphoserineBy 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 – 3621PhosphoserineBy 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; alternateBy similarity
Modified residuei589 – 5891N6-acetyllysineBy similarity
Modified residuei597 – 5971N6-acetyllysineBy 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

BgeeiP63017.
CleanExiMM_HSPA8.
ExpressionAtlasiP63017. baseline and differential.
GenevestigatoriP63017.

Interactioni

Subunit structurei

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with PACRG. 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 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).By similarity

Binary interactionsi

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

Protein-protein interaction databases

BioGridi200428. 43 interactions.
DIPiDIP-32353N.
IntActiP63017. 34 interactions.
MINTiMINT-189032.

Structurei

Secondary structure

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

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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63017.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni186 – 377192Interaction with BAG1By 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

Belongs to the heat shock protein 70 family.Curated

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 [UniParc]FASTAAdd to Basket

« 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 LDKCNEIISW LDKNQTAEKE EFEHQQKELE
610 620 630 640
KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD
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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91I → V in BAE28187. (PubMed:16141072)Curated
Sequence conflicti35 – 351N → K in BAE30081. (PubMed:16141072)Curated
Sequence conflicti35 – 351N → K in BAE30861. (PubMed:16141072)Curated
Sequence conflicti35 – 351N → K in BAE30753. (PubMed:16141072)Curated
Sequence conflicti268 – 2681E → G in BAE31432. (PubMed:16141072)Curated
Sequence conflicti268 – 2681E → G in BAE31346. (PubMed:16141072)Curated
Sequence conflicti269 – 2691R → G in BAE31508. (PubMed:16141072)Curated
Sequence conflicti353 – 3531F → C in BAE31664. (PubMed:16141072)Curated
Sequence conflicti428 – 4281F → L in AAA37869. (PubMed:3334718)Curated
Sequence conflicti428 – 4281F → L in AAB18391. (PubMed:10095055)Curated
Sequence conflicti432 – 4321S → Y in BAE30707. (PubMed:16141072)Curated
Sequence conflicti589 – 5891K → E in AAH66191. (PubMed:15489334)Curated
Sequence conflicti645 – 6451V → M in BAE30272. (PubMed:16141072)Curated
Sequence conflicti645 – 6451V → M in BAE31427. (PubMed:16141072)Curated

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. 34 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

Bgeei P63017.
CleanExi MM_HSPA8.
ExpressionAtlasi P63017. baseline and differential.
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: October 29, 2014
This is version 112 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