Heat shock cognate 71 kDa protein - Rattus norvegicus (Rat)

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P63018 (HSP7C_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 84. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Heat shock cognate 71 kDa protein

Alternative name(s):
Heat shock 70 kDa protein 8

Gene names

Name:	Hspa8
Synonyms:	Hsc70, Hsc73

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	646 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone.
Subunit structure	Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with PACRG. Interacts with HSPH1/HSP105. Interacts with IRAK1BP1 and BAG1. Interacts with CITED1 (via N-terminus); the interaction suppresses the association of CITED1 to p300/CBP and Smad-mediated transcription transactivation By similarity. Interacts with DNAJC7. Ref.5
Subcellular location	Cytoplasm By similarity. Melanosome 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.
Induction	Constitutively synthesized.
Domain	The N-terminal 1-386 residues constitute the ATPase domain, while residues 387-646 form the peptide-binding domain By similarity.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR By similarity. ISGylated By similarity.
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Biological process	Stress response Transcription Transcription regulation
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone Repressor
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	chaperone mediated protein folding requiring cofactor Inferred from direct assay. Source: RGD negative regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB response to stress Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular vesicular exosome Inferred from direct assay. Source: RGD melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell neuron projection Inferred from direct assay. Source: RGD neuronal cell body Inferred from direct assay. Source: RGD protein complex Inferred from direct assay. Source: RGD ribonucleoprotein complex Inferred from sequence or structural similarity. Source: UniProtKB soluble fraction Inferred from direct assay. Source: RGD synaptic vesicle Inferred from direct assay. Source: RGD
Molecular function	ADP binding Inferred from direct assay. Source: RGD ATP binding Inferred from direct assay. Source: RGD ATPase activity, coupled Inferred from direct assay. Source: RGD receptor binding Inferred from physical interaction. Source: RGD unfolded protein binding Inferred from mutant phenotype. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 646

645

Heat shock cognate 71 kDa protein

PRO_0000078273

Regions

Region

186 – 377

192

Interaction with BAG1 By similarity

Amino acid modifications

Modified residue

N-acetylserine By similarity

Modified residue

Phosphotyrosine By similarity

Modified residue

Phosphotyrosine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

107

Phosphotyrosine By similarity

Modified residue

108

N6-acetyllysine By similarity

Modified residue

113

Phosphoserine By similarity

Modified residue

115

Phosphotyrosine By similarity

Modified residue

120

Phosphoserine By similarity

Modified residue

121

Phosphoserine By similarity

Modified residue

153

Phosphoserine By similarity

Modified residue

246

N6-acetyllysine By similarity

Modified residue

319

N6-acetyllysine By similarity

Modified residue

348

N6-acetyllysine By similarity

Modified residue

477

Phosphothreonine By similarity

Modified residue

512

N6-acetyllysine By similarity

Modified residue

524

N6-acetyllysine By similarity

Modified residue

541

Phosphoserine By similarity

Modified residue

589

N6-acetyllysine By similarity

Modified residue

597

N6-acetyllysine By similarity

Modified residue

601

N6-acetyllysine By similarity

Modified residue

637

Phosphoserine By similarity

Modified residue

638

Phosphoserine By similarity

Secondary structure

646

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P63018 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 03A27B30E6C076ED
Show »

FASTA

646

70,871

        10         20         30         40         50         60 
MSKGPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA 

        70         80         90        100        110        120 
MNPTNTVFDA KRLIGRRFDD AVVQSDMKHW PFMVVNDAGR PKVQVEYKGE TKSFYPEEVS 

       130        140        150        160        170        180 
SMVLTKMKEI AEAYLGKTVT NAVVTVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA 

       190        200        210        220        230        240 
IAYGLDKKVG AERNVLIFDL GGGTFDVSIL TIEDGIFEVK STAGDTHLGG EDFDNRMVNH 

       250        260        270        280        290        300 
FIAEFKRKHK KDISENKRAV RRLRTACERA KRTLSSSTQA SIEIDSLYEG IDFYTSITRA 

       310        320        330        340        350        360 
RFEELNADLF RGTLDPVEKA LRDAKLDKSQ IHDIVLVGGS TRIPKIQKLL QDFFNGKELN 

       370        380        390        400        410        420 
KSINPDEAVA YGAAVQAAIL SGDKSENVQD LLLLDVTPLS LGIETAGGVM TVLIKRNTTI 

       430        440        450        460        470        480 
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LTGIPPAPRG VPQIEVTFDI 

       490        500        510        520        530        540 
DANGILNVSA VDKSTGKENK ITITNDKGRL SKEDIERMVQ EAEKYKAEDE KQRDKVSSKN 

       550        560        570        580        590        600 
SLESYAFNMK ATVEDEKLQG KINDEDKQKI LDKCNEIISW LDKNQTAEKE EFEHQQKELE 

       610        620        630        640 
KVCNPIITKL YQSAGGMPGG MPGGFPGGGA PPSGGASSGP TIEEVD

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of a gene encoding hsc73, the major hsp70-like protein in unstressed rat cells." Sorger P.K., Pelham H.R.B. EMBO J. 6:993-998(1987) [PubMed: 3595567] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Constitutively expressed rat mRNA encoding a 70-kilodalton heat-shock-like protein." O'Malley K., Mauron A., Barchas J.D., Kedes L. Mol. Cell. Biol. 5:3476-3483(1985) [PubMed: 3939319] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Heart and Pituitary.
[4]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U., Lubec S. Submitted (SEP-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 4-36; 57-71; 77-108; 127-155; 160-171; 237-246; 300-319; 349-357; 424-447; 452-458; 518-526; 540-550; 584-597 AND 602-609, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain, Hippocampus and Spinal cord.
[5]	"Specific interaction of the 70-kDa heat shock cognate protein with the tetratricopeptide repeats." Liu F.H., Wu S.J., Hu S.M., Hsiao C.D., Wang C. J. Biol. Chem. 274:34425-34432(1999) [PubMed: 10567422] [Abstract] Cited for: INTERACTION WITH DNAJC7.
[6]	"High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70." Morshauser R.C., Hu W., Wang H., Pang Y., Flynn G.C., Zuiderweg E.R.P. J. Mol. Biol. 289:1387-1403(1999) [PubMed: 10373374] [Abstract] Cited for: STRUCTURE BY NMR OF 385-543.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y00054 Genomic DNA. Translation: CAA68265.1.
M11942 mRNA. Translation: AAA41354.1.
BC061547 mRNA. Translation: AAH61547.1.
BC098914 mRNA. Translation: AAH98914.1.

IPI

IPI00208205.

PIR

S07197.

RefSeq

NP_077327.1. NM_024351.2.

UniGene

Rn.120392.
Rn.201298.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CKR	NMR	-	A	385-543	[»]
1Q2G	model	-	C	385-543	[»]
1UD0	X-ray	3.45	A/B/C/D	542-646	[»]
2V7Z	X-ray	3.50	A/B	1-543	[»]
7HSC	NMR	-	A	385-543	[»]

ProteinModelPortal

P63018.

SMR

P63018. Positions 1-621.

ModBase

Search...

Protein-protein interaction databases

IntAct

P63018. 5 interactions.

MINT

MINT-2514077.

STRING

P63018.

PTM databases

PhosphoSite

P63018.

2D gel databases

World-2DPAGE

0004:P63018.

Proteomic databases

PRIDE

P63018.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

24468.

KEGG

rno:24468.

UCSC

BC061547. rat.

Organism-specific databases

CTD

3312.

RGD

621725. Hspa8.

Phylogenomic databases

eggNOG

maNOG11692.

GeneTree

ENSGT00550000074467.

HOVERGEN

HBG051845.

OrthoDB

EOG4W6NVK.

PhylomeDB

P63018.

Gene expression databases

Genevestigator

P63018.

Family and domain databases

InterPro

IPR018181. Heat_shock_70_CS.
IPR001023. Hsp70.
IPR013126. Hsp_70.
[Graphical view]

K03283.

PANTHER

PTHR19375. Hsp70. 1 hit.

Pfam

PF00012. HSP70. 1 hit.
[Graphical view]

PRINTS

PR00301. HEATSHOCK70.

PROSITE

PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

603401.

Entry information

Entry name

HSP7C_RAT

Accession

Primary (citable) accession number: P63018
Secondary accession number(s): P08109

Q62375

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	November 16, 2011
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents