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P63017 (HSP7C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heat shock cognate 71 kDa protein
Alternative name(s):
Heat shock 70 kDa protein 8
Gene names
Name:Hspa8
Synonyms:Hsc70, Hsc73
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length646 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion By similarity.

Subunit structure

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. Ref.8 Ref.9 Ref.11

Subcellular location

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.

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

Trimethylation at Lys-561 reduces fibrillar SNCA binding By similarity.

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 processmRNA processing
mRNA splicing
Stress response
Transcription
Transcription regulation
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
Spliceosome
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
Repressor
   PTMAcetylation
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay PubMed 12588994. Source: GOC

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-templated

Inferred from sequence or structural similarity. Source: UniProtKB

protein folding

Inferred from direct assay PubMed 12588994. Source: MGI

regulation of cell cycle

Inferred from direct assay PubMed 12588994. Source: MGI

response to stress

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPrp19 complex

Inferred from sequence or structural similarity. Source: UniProtKB

cell surface

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from direct assay PubMed 16906134. Source: MGI

extracellular vesicular exosome

Inferred from direct assay PubMed 19724054. Source: MGI

intracellular

Inferred from direct assay PubMed 9122205. Source: MGI

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

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_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity, coupled

Inferred from direct assay PubMed 12588994. Source: MGI

unfolded protein binding

Inferred from physical interaction PubMed 12588994. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Klc1O884473EBI-433443,EBI-301550

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 646645Heat shock cognate 71 kDa protein
PRO_0000078271

Regions

Nucleotide binding12 – 154ATP By similarity
Nucleotide binding202 – 2043ATP By similarity
Nucleotide binding268 – 2758ATP By similarity
Nucleotide binding339 – 3424ATP By similarity
Region186 – 377192Interaction with BAG1 By similarity

Sites

Binding site711ATP By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue1081N6-acetyllysine Ref.13
Modified residue1531Phosphoserine By similarity
Modified residue2461N6-acetyllysine Ref.13
Modified residue3191N6-acetyllysine; alternate Ref.13
Modified residue3191N6-succinyllysine; alternate Ref.13
Modified residue3281N6-acetyllysine Ref.13
Modified residue3621Phosphoserine By similarity
Modified residue5121N6-acetyllysine; alternate Ref.13
Modified residue5121N6-succinyllysine; alternate Ref.13
Modified residue5241N6-acetyllysine Ref.13
Modified residue5611N6,N6,N6-trimethyllysine; alternate Ref.12
Modified residue5611N6,N6,N6-trimethyllysine; by METTL21A; alternate By similarity
Modified residue5891N6-acetyllysine By similarity
Modified residue5971N6-acetyllysine By similarity
Modified residue6011N6-acetyllysine Ref.13

Experimental info

Sequence conflict91I → V in BAE28187. Ref.4
Sequence conflict351N → K in BAE30081. Ref.4
Sequence conflict351N → K in BAE30861. Ref.4
Sequence conflict351N → K in BAE30753. Ref.4
Sequence conflict2681E → G in BAE31432. Ref.4
Sequence conflict2681E → G in BAE31346. Ref.4
Sequence conflict2691R → G in BAE31508. Ref.4
Sequence conflict3531F → C in BAE31664. Ref.4
Sequence conflict4281F → L in AAA37869. Ref.1
Sequence conflict4281F → L in AAB18391. Ref.3
Sequence conflict4321S → Y in BAE30707. Ref.4
Sequence conflict5891K → E in AAH66191. Ref.5
Sequence conflict6451V → M in BAE30272. Ref.4
Sequence conflict6451V → M in BAE31427. Ref.4

Secondary structure

.................................................................... 646
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63017 [UniParc].

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

FASTA64670,871
        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' 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. expand/collapse author list , 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]"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, 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.
+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.
PIRA45935.
JC4853.
RefSeqNP_112442.2. NM_031165.4.
UniGeneMm.290774.
Mm.336743.
Mm.351377.
Mm.412745.
Mm.485345.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3CQXX-ray2.30A/B1-381[»]
ProteinModelPortalP63017.
SMRP63017. Positions 1-621.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200428. 41 interactions.
DIPDIP-32353N.
IntActP63017. 33 interactions.
MINTMINT-189032.

2D gel databases

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

Proteomic databases

PaxDbP63017.
PRIDEP63017.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000015800; ENSMUSP00000015800; ENSMUSG00000015656.
GeneID15481.
KEGGmmu:15481.
UCSCuc009ozx.3. mouse.

Organism-specific databases

CTD3312.
MGIMGI:105384. Hspa8.

Phylogenomic databases

eggNOGCOG0443.
GeneTreeENSGT00750000117237.
HOVERGENHBG051845.
InParanoidP63017.
KOK03283.
OMAPMIVVEY.
OrthoDBEOG7PCJGF.
PhylomeDBP63017.
TreeFamTF105042.

Gene expression databases

ArrayExpressP63017.
BgeeP63017.
CleanExMM_HSPA8.
GenevestigatorP63017.

Family and domain databases

InterProIPR018181. Heat_shock_70_CS.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
PROSITEPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP63017.
NextBio288328.
PROP63017.
SOURCESearch...

Entry information

Entry nameHSP7C_MOUSE
AccessionPrimary (citable) accession number: P63017
Secondary accession number(s): P08109 expand/collapse secondary AC list , 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 16, 2014
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot