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Reviewed, UniProtKB/Swiss-Prot P54652 (HSP72_HUMAN)

Last modified March 2, 2010. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
Heat shock-related 70 kDa protein 2

Short name=Heat shock 70 kDa protein 2
Gene names
Name:HSPA2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length639 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

In cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation and mediate the folding of newly translated polypeptides in the cytosol as well as within organelles. These chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins. They bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation and membrane translocation, or following stress-induced damage.

Subunit structure

Interacts with ZNF541 By similarity.

Sequence similarities

Belongs to the heat shock protein 70 family.

Ontologies

Keywords
   Biological processStress response
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processmale meiosis

Traceable author statement. Source: ProtInc

response to unfolded protein Ref.1

Traceable author statement. Source: ProtInc

spermatid development

Traceable author statement. Source: ProtInc

   Cellular componentcell surface

Inferred from direct assay. Source: UniProtKB

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

unfolded protein binding

Traceable author statement. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 639639Heat shock-related 70 kDa protein 2
PRO_0000078258

Amino acid modifications

Modified residue421Phosphotyrosine Ref.7
Modified residue1081Phosphotyrosine Ref.7

Natural variations

Natural variant1911C → S
VAR_032706
Natural variant4961K → E
VAR_032707

Experimental info

Sequence conflict141T → P in AAH36107. Ref.5
Sequence conflict541Missing in AAC50076. Ref.6
Sequence conflict801E → G in AAH36107. Ref.5
Sequence conflict2661L → S in AAD11466. Ref.2

Secondary structure

........................................................ 639
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P54652-1 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 3851755494E7B729

FASTA63970,021
        10         20         30         40         50         60 
MSARGPAIGI DLGTTYSCVG VFQHGKVEII ANDQGNRTTP SYVAFTDTER LIGDAAKNQV 

        70         80         90        100        110        120 
AMNPTNTIFD AKRLIGRKFE DATVQSDMKH WPFRVVSEGG KPKVQVEYKG ETKTFFPEEI 

       130        140        150        160        170        180 
SSMVLTKMKE IAEAYLGGKV HSAVITVPAY FNDSQRQATK DAGTITGLNV LRIINEPTAA 

       190        200        210        220        230        240 
AIAYGLDKKG CAGGEKNVLI FDLGGGTFDV SILTIEDGIF EVKSTAGDTH LGGEDFDNRM 

       250        260        270        280        290        300 
VSHLAEEFKR KHKKDIGPNK RAVRRLRTAC ERAKRTLSSS TQASIEIDSL YEGVDFYTSI 

       310        320        330        340        350        360 
TRARFEELNA DLFRGTLEPV EKALRDAKLD KGQIQEIVLV GGSTRIPKIQ KLLQDFFNGK 

       370        380        390        400        410        420 
ELNKSINPDE AVAYGAAVQA AILIGDKSEN VQDLLLLDVT PLSLGIETAG GVMTPLIKRN 

       430        440        450        460        470        480 
TTIPTKQTQT FTTYSDNQSS VLVQVYEGER AMTKDNNLLG KFDLTGIPPA PRGVPQIEVT 

       490        500        510        520        530        540 
FDIDANGILN VTAADKSTGK ENKITITNDK GRLSKDDIDR MVQEAERYKS EDEANRDRVA 

       550        560        570        580        590        600 
AKNALESYTY NIKQTVEDEK LRGKISEQDK NKILDKCQEV INWLDRNQMA EKDEYEHKQK 

       610        620        630 
ELERVCNPII SKLYQGGPGG GSGGGGSGAS GGPTIEEVD 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing, and mapping of the human chromosome 14 heat shock protein gene (HSPA2)."
Bonnycastle L.L.C., Yu C.-E., Hunt C.R., Trask B.J., Clancy K.P., Weber J.L., Patterson D., Schellenberg G.D.
Genomics 23:85-93(1994) [PubMed: 7829106] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Goralski T.J., Krensky A.M.
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]NIEHS SNPs program
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-191 AND GLU-496.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Eye.
[6]"A heat shock gene at 14q22: mapping and expression."
Roux A.-F., Nguyen V.T.T., Squire J.A., Cox D.W.
Hum. Mol. Genet. 3:1819-1822(1994) [PubMed: 7849706] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-126.
[7]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-42 AND TYR-108, MASS SPECTROMETRY.
Tissue: Lung.
[8]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L26336 Genomic DNA. Translation: AAA52698.1.
U56725 mRNA. Translation: AAD11466.1.
BT009815 mRNA. Translation: AAP88817.1.
DQ489378 Genomic DNA. Translation: ABE96830.1.
BC001752 mRNA. Translation: AAH01752.1.
BC036107 mRNA. Translation: AAH36107.1.
U10149 Genomic DNA. Translation: AAC50076.1.
IPIIPI00007702.
PIRA55719.
I37564.
RefSeqNP_068814.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3I33X-ray1.30A6-386[»]
SMRP54652. Positions 3-557, 545-620.
ModBaseSearch...

Protein-protein interaction databases

IntActP54652. 8 interactions.
STRINGP54652.

PTM databases

PhosphoSiteP54652.

2-D gel databases

REPRODUCTION-2DPAGEIPI00007702.

Proteomic databases

PeptideAtlasP54652.
PRIDEP54652.

Genome annotation databases

EnsemblENST00000247207; ENSP00000247207; ENSG00000126803; Homo sapiens. [Genome view]
ENST00000394709; ENSP00000378199; ENSG00000126803; Homo sapiens. [Genome view]
GeneID3306.
KEGGhsa:3306.
UCSCuc001xhj.2. human.

Organism-specific databases

CTD3306.
GeneCardsGC14P064072.
H-InvDBHIX0011736.
HGNCHGNC:5235. HSPA2.
HPAHPA000798.
MIM140560. gene.
PharmGKBPA29501.
GenAtlasSearch...

Phylogenomic databases

eggNOGmaNOG09073.
HOGENOMHBG334976.
HOVERGENHBG051845.
InParanoidP54652.
OMALESYTYN.
OrthoDBEOG9TQPV5.
PhylomeDBP54652.

Gene expression databases

ArrayExpressP54652.
BgeeP54652.
CleanExHS_HSPA2.
GenevestigatorP54652.
GermOnlineENSG00000126803. Homo sapiens.

Family and domain databases

InterProIPR018181. Heat_shock_70_CS.
IPR001023. Hsp70.
IPR013126. Hsp_70.
[Graphical view]
PANTHERPTHR19375. Hsp70. 1 hit.
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 Resources

NextBio13115.
SOURCESearch...

Entry information

Entry nameHSP72_HUMAN
AccessionPrimary (citable) accession number: P54652
Secondary accession number(s): Q15508, Q53XM3, Q9UE78
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 2, 2010
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents