P19120 (HSP7C_BOVIN) Reviewed, UniProtKB/Swiss-Prot

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

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	650 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 By similarity.
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 DNAJC7. Interacts with CITED1 (via N-terminus); the interaction suppresses the association of CITED1 to p300/CBP and Smad-mediated transcription transactivation By similarity.
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.
Tissue specificity	Ubiquitous.
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 Reference proteome
Gene Ontology (GO)
Biological process	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	melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell ribonucleoprotein complex Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 650

649

Heat shock cognate 71 kDa protein

PRO_0000078268

Regions

Region

186 – 377

192

Interaction with BAG1 By similarity

Amino acid modifications

Modified residue

2

1

N-acetylserine By similarity

Modified residue

15

1

Phosphotyrosine By similarity

Modified residue

41

1

Phosphotyrosine By similarity

Modified residue

88

1

N6-acetyllysine By similarity

Modified residue

107

1

Phosphotyrosine By similarity

Modified residue

108

1

N6-acetyllysine By similarity

Modified residue

113

1

Phosphoserine By similarity

Modified residue

115

1

Phosphotyrosine By similarity

Modified residue

120

1

Phosphoserine By similarity

Modified residue

121

1

Phosphoserine By similarity

Modified residue

153

1

Phosphoserine By similarity

Modified residue

246

1

N6-acetyllysine By similarity

Modified residue

319

1

N6-acetyllysine By similarity

Modified residue

348

1

N6-acetyllysine By similarity

Modified residue

477

1

Phosphothreonine By similarity

Modified residue

512

1

N6-acetyllysine By similarity

Modified residue

524

1

N6-acetyllysine By similarity

Modified residue

541

1

Phosphoserine By similarity

Modified residue

589

1

N6-acetyllysine By similarity

Modified residue

597

1

N6-acetyllysine By similarity

Modified residue

601

1

N6-acetyllysine By similarity

Modified residue

641

1

Phosphoserine By similarity

Modified residue

642

1

Phosphoserine By similarity

Experimental info

Sequence conflict

180

1

A → T in AAI05183. Ref.3

Sequence conflict

543

1

E → K in CAA37422. Ref.1

Sequence conflict

543

1

E → K in CAA37823. Ref.1

Secondary structure

1

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650

Helix Strand Turn

Details...

Beta strand

7 – 10

4

Beta strand

13 – 22

10

Beta strand

25 – 28

4

Beta strand

36 – 39

4

Beta strand

42 – 44

3

Beta strand

49 – 51

3

Helix

53 – 56

4

Turn

57 – 61

5

Turn

63 – 65

3

Helix

70 – 73

4

Helix

81 – 87

7

Beta strand

91 – 97

7

Beta strand

100 – 107

8

Beta strand

110 – 114

5

Helix

116 – 135

20

Beta strand

141 – 146

6

Helix

152 – 164

13

Beta strand

168 – 174

7

Helix

175 – 182

8

Turn

183 – 186

4

Beta strand

193 – 200

8

Beta strand

205 – 213

9

Beta strand

216 – 225

10

Helix

230 – 249

20

Helix

257 – 273

17

Turn

274 – 276

3

Beta strand

278 – 288

11

Beta strand

291 – 298

8

Helix

299 – 305

7

Helix

307 – 312

6

Helix

314 – 324

11

Helix

328 – 330

3

Beta strand

333 – 338

6

Helix

339 – 342

4

Helix

344 – 353

10

Turn

354 – 356

3

Turn

365 – 367

3

Helix

368 – 381

14

Beta strand

401 – 405

5

Turn

406 – 408

3

Beta strand

409 – 414

6

Beta strand

419 – 432

14

Beta strand

436 – 449

14

Helix

450 – 452

3

Beta strand

453 – 462

10

Beta strand

474 – 480

7

Beta strand

486 – 492

7

Turn

493 – 495

3

Beta strand

498 – 503

6

Helix

512 – 524

13

Turn

525 – 527

3

Helix

528 – 532

5

Sequences

	Sequence		Length	Mass (Da)
	P19120 [UniParc]. Last modified May 29, 2007. Version 2. Checksum: FBE109C14A28B925	FASTA	650	71,241
	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 LDKCNEIINW LDKNQTAEKE EFEHQQKELE 610 620 630 640 650 KVCNPIITKL YQSAGGMPGG MPGGMPGGFP GGGAPPSGGA SSGPTIEEVD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the cDNA of a bovine 70 kilodalton heat shock cognate protein." Deluca-Flaherty C., McKay D.B. Nucleic Acids Res. 18:5569-5569(1990) [PubMed: 2216746] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain cortex.
[2]	"Characterization of 954 bovine full-CDS cDNA sequences." Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L. BMC Genomics 6:166-166(2005) [PubMed: 16305752] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	NIH - Mammalian Gene Collection (MGC) project Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Crossbred X Angus. Tissue: Ileum.
[4]	"Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein." Flaherty K.M., de Luca-Flaherty C., McKay D.B. Nature 346:623-628(1990) [PubMed: 2143562] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-385.
[5]	"Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment." Flaherty K.M., Wilbanks S.M., Deluca-Flaherty C., McKay D.B. J. Biol. Chem. 269:12899-12907(1994) [PubMed: 8175707] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-385.
[6]	"Structural replacement of active site monovalent cations by the epsilon-amino group of lysine in the ATPase fragment of bovine Hsc70." Wilbanks S.M., McKay D.B. Biochemistry 37:7456-7462(1998) [PubMed: 9585559] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-385.
[7]	"The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change." Sousa M.C., McKay D.B. Biochemistry 37:15392-15399(1998) [PubMed: 9799500] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-381.
[8]	"Mapping the role of active site residues for transducing an ATP-induced conformational change in the bovine 70-kDa heat shock cognate protein." Johnson E.R., McKay D.B. Biochemistry 38:10823-10830(1999) [PubMed: 10451379] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-381 OF MUTANTS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X53827 mRNA. Translation: CAA37823.1.
X53335 mRNA. Translation: CAA37422.1.
BT030487 mRNA. Translation: ABQ12927.1.
BC105182 mRNA. Translation: AAI05183.1.

IPI

IPI00708526.

PIR

S11456.

RefSeq

NP_776770.2. NM_174345.3.

UniGene

Bt.12309.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ATR	X-ray	2.34	A	1-386	[»]
1ATS	X-ray	2.43	A	1-386	[»]
1BA0	X-ray	1.90	A	1-386	[»]
1BA1	X-ray	1.70	A	1-386	[»]
1BUP	X-ray	1.70	A	1-386	[»]
1HPM	X-ray	1.70	A	1-386	[»]
1HX1	X-ray	1.90	A	4-381	[»]
1KAX	X-ray	1.70	A	1-381	[»]
1KAY	X-ray	1.70	A	1-381	[»]
1KAZ	X-ray	1.70	A	1-381	[»]
1NGA	X-ray	2.18	A	1-386	[»]
1NGB	X-ray	2.18	A	1-386	[»]
1NGC	X-ray	2.20	A	1-386	[»]
1NGD	X-ray	2.18	A	1-386	[»]
1NGE	X-ray	2.05	A	1-386	[»]
1NGF	X-ray	2.17	A	1-386	[»]
1NGG	X-ray	2.19	A	1-386	[»]
1NGH	X-ray	2.23	A	1-386	[»]
1NGI	X-ray	2.15	A	1-386	[»]
1NGJ	X-ray	2.10	A	1-386	[»]
1Q2G	model	-	B	4-381	[»]
1QQM	X-ray	1.90	A	4-381	[»]
1QQN	X-ray	1.90	A	4-381	[»]
1QQO	X-ray	1.90	A	4-381	[»]
1YUW	X-ray	2.60	A	1-554	[»]
2BUP	X-ray	1.70	A	1-381	[»]
2QW9	X-ray	1.85	A/B	1-394	[»]
2QWL	X-ray	1.75	A/B	1-394	[»]
2QWM	X-ray	1.86	A/B	1-394	[»]
2QWN	X-ray	2.40	A	1-394	[»]
2QWO	X-ray	1.70	A	1-394	[»]
2QWP	X-ray	1.75	A	1-394	[»]
2QWQ	X-ray	2.21	A	1-394	[»]
2QWR	X-ray	2.21	A	1-394	[»]
3C7N	X-ray	3.12	B	1-554	[»]
3HSC	X-ray	1.93	A	1-386	[»]

ProteinModelPortal

P19120.

SMR

P19120. Positions 1-621.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35481N.

IntAct

P19120. 2 interactions.

MINT

MINT-157582.

STRING

P19120.

Proteomic databases

PRIDE

P19120.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000017497; ENSBTAP00000017497; ENSBTAG00000013162.

GeneID

281831.

KEGG

bta:281831.

Organism-specific databases

CTD

3312.

Phylogenomic databases

eggNOG

maNOG11692.

HOVERGEN

HBG051845.

InParanoid

P19120.

OMA

HQQKDLE.

OrthoDB

EOG4W6NVK.

PhylomeDB

P19120.

Family and domain databases

InterPro

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

KO

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...

Entry information

Entry name

HSP7C_BOVIN

Accession

Primary (citable) accession number: P19120
Secondary accession number(s): A5D968, Q3MHM4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	May 29, 2007
Last modified:	November 16, 2011
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program