P63017 (HSP7C_MOUSE) 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, Hsc73

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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. 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.
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 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 By similarity. Interacts with IRAK1BP1 and HSPH1/HSP105. Interacts with TRIM5 By similarity. Ref.8 Ref.9 Ref.11
Subcellular location	Cytoplasm By similarity. Melanosome By similarity. Nucleus › nucleolus 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	Acetylated By similarity. ISGylated. Ref.10
Sequence similarities	Belongs to the heat shock protein 70 family.
Sequence caution	The sequence BAE31508.1 differs from that shown. Reason: Frameshift at positions 256 and 269.

Ontologies

Keywords
Biological process	Stress response Transcription Transcription regulation mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
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	RNA splicing Inferred from electronic annotation. Source: UniProtKB-KW chaperone mediated protein folding requiring cofactor Inferred from genetic interaction PubMed 14644449. Source: MGI mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of transcription, DNA-dependent Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell cycle Inferred from direct assay PubMed 12588994. Source: MGI response to stress Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Prp19 complex Inferred from sequence or structural similarity. Source: UniProtKB cell surface Inferred from electronic annotation. Source: Compara cytosol Inferred from direct assay PubMed 16906134. Source: MGI extracellular vesicular exosome Inferred from direct assay PubMed 19724054. Source: MGI melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from sequence or structural similarity. Source: UniProtKB ribonucleoprotein complex Inferred from sequence or structural similarity. Source: UniProtKB spliceosomal complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATPase activity, coupled Inferred from direct assay PubMed 12588994. Source: MGI
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 – 646

645

Heat shock cognate 71 kDa protein

PRO_0000078271

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 Ref.12

Modified residue

41

1

Phosphotyrosine Ref.12

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

362

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

Experimental info

Sequence conflict

9

1

I → V in BAE28187. Ref.4

Sequence conflict

35

1

N → K in BAE30081. Ref.4

Sequence conflict

35

1

N → K in BAE30861. Ref.4

Sequence conflict

35

1

N → K in BAE30753. Ref.4

Sequence conflict

268

1

E → G in BAE31432. Ref.4

Sequence conflict

268

1

E → G in BAE31346. Ref.4

Sequence conflict

269

1

R → G in BAE31508. Ref.4

Sequence conflict

353

1

F → C in BAE31664. Ref.4

Sequence conflict

428

1

F → L in AAA37869. Ref.1

Sequence conflict

428

1

F → L in AAB18391. Ref.3

Sequence conflict

432

1

S → Y in BAE30707. Ref.4

Sequence conflict

589

1

K → E in AAH66191. Ref.5

Sequence conflict

645

1

V → M in BAE30272. Ref.4

Sequence conflict

645

1

V → M in BAE31427. Ref.4

Secondary structure

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646

Helix Strand Turn

Details...

Beta strand

7 – 11

5

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 – 57

5

Turn

58 – 61

4

Helix

63 – 65

3

Helix

70 – 72

3

Turn

73 – 75

3

Helix

81 – 86

6

Turn

87 – 89

3

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

187 – 200

14

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 – 312

14

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 – 380

13

Sequences

	Sequence		Length	Mass (Da)
	P63017 [UniParc]. Last modified August 1, 1988. Version 1. Checksum: 03A27B30E6C076ED	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, 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]	"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells." Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E. Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY.
[12]	"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-15 AND TYR-41, MASS SPECTROMETRY. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00323357.

PIR

A45935.
JC4853.

RefSeq

NP_112442.2. NM_031165.4.

UniGene

Mm.290774.
Mm.336743.
Mm.351377.
Mm.412745.
Mm.485345.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CQX	X-ray	2.30	A/B	1-381	[»]

ProteinModelPortal

P63017.

SMR

P63017. Positions 1-621.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32353N.

IntAct

P63017. 23 interactions.

MINT

MINT-189032.

2D gel databases

COMPLUYEAST-2DPAGE

P63017.

REPRODUCTION-2DPAGE

IPI00323357.
P63017.
Q6NZD0.

SWISS-2DPAGE

P63017.

UCD-2DPAGE

P63017.

Proteomic databases

PaxDb

P63017.

PRIDE

P63017.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000015800; ENSMUSP00000015800; ENSMUSG00000015656.

GeneID

15481.

KEGG

mmu:15481.

UCSC

uc009ozx.2. mouse.

Organism-specific databases

CTD

3312.

MGI

MGI:105384. Hspa8.

Phylogenomic databases

eggNOG

COG0443.

GeneTree

ENSGT00550000074467.

HOVERGEN

HBG051845.

InParanoid

P63017.

KO

K03283.

OMA

FNVINDN.

OrthoDB

EOG4W6NVK.

Gene expression databases

ArrayExpress

P63017.

Bgee

P63017.

CleanEx

MM_HSPA8.

Genevestigator

P63017.

GermOnline

ENSMUSG00000015656. Mus musculus.

Family and domain databases

InterPro

IPR018181. Heat_shock_70_CS.
IPR013126. Hsp_70_fam.
[Graphical view]

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

EvolutionaryTrace

P63017.

NextBio

288328.

SOURCE

Search...

Entry information

Entry name

HSP7C_MOUSE

Accession

Primary (citable) accession number: P63017
Secondary accession number(s): P08109 , P12225, Q3U6R0, Q3U764, Q3U7D7, Q3U7E2, Q3U9B4, Q3U9G0, Q3UGM0, Q5FWJ6, Q62373, Q62374, Q62375, Q6NZD0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 1, 1988
Last modified:	April 3, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program