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P54652 (HSP72_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference 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. Component of the CatSper complex By similarity. Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2 By similarity. Interacts with FKBP6. Ref.7

Sequence similarities

Belongs to the heat shock protein 70 family.

Ontologies

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

Traceable author statement PubMed 8622925. Source: ProtInc

male meiosis I

Inferred from electronic annotation. Source: Ensembl

negative regulation of inclusion body assembly

Inferred from direct assay PubMed 21231916. Source: UniProt

positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G2/M transition of mitotic cell cycle

Inferred from electronic annotation. Source: Ensembl

protein refolding

Inferred from direct assay PubMed 21231916. Source: UniProt

response to unfolded protein

Traceable author statement Ref.1. Source: ProtInc

spermatid development

Traceable author statement PubMed 8622925. Source: ProtInc

synaptonemal complex disassembly

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentCatSper complex

Inferred from sequence or structural similarity. Source: UniProtKB

blood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cell surface

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from direct assay PubMed 21231916. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

male germ cell nucleus

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

synaptonemal complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

enzyme binding

Inferred from physical interaction Ref.9. Source: BHF-UCL

glycolipid binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 16189514PubMed 16713569. Source: IntAct

unfolded protein binding

Inferred from direct assay PubMed 21231916. Source: UniProt

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSPBP1Q9NZL43EBI-356991,EBI-356763

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

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

Regions

Nucleotide binding13 – 164ATP
Nucleotide binding205 – 2073ATP
Nucleotide binding271 – 2788ATP
Nucleotide binding342 – 3454ATP

Sites

Binding site721ATP

Amino acid modifications

Modified residue4031Phosphoserine By similarity
Modified residue4081Phosphothreonine By similarity
Modified residue4141Phosphothreonine By similarity
Modified residue5641N6,N6,N6-trimethyllysine; by METTL21A; in vitro Ref.9

Natural variations

Natural variant1911C → S. Ref.4
Corresponds to variant rs45456191 [ dbSNP | Ensembl ].
VAR_032706
Natural variant4961K → E. Ref.4
VAR_032707

Experimental info

Mutagenesis5641K → A: Abolishes methylation by METTL21A. Ref.9
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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-126.
[7]"FKBP36 forms complexes with clathrin and Hsp72 in spermatocytes."
Jarczowski F., Fischer G., Edlich F.
Biochemistry 47:6946-6952(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FKBP6.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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-564, MUTAGENESIS OF LYS-564.
[10]"Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78."
Wisniewska M., Karlberg T., Lehtio L., Johansson I., Kotenyova T., Moche M., Schuler H.
PLoS ONE 5:E8625-E8625(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 6-386 IN COMPLEX WITH ADP AND PHOSPHATE.
+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.
AH006615 Genomic DNA. Translation: AAC50076.1.
CCDSCCDS9766.1.
PIRA55719.
I37564.
RefSeqNP_068814.2. NM_021979.3.
UniGeneHs.432648.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3I33X-ray1.30A6-386[»]
4FSVX-ray1.80A2-387[»]
ProteinModelPortalP54652.
SMRP54652. Positions 3-613.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109538. 38 interactions.
IntActP54652. 12 interactions.
MINTMINT-1146083.
STRING9606.ENSP00000247207.

Chemistry

ChEMBLCHEMBL2062348.

PTM databases

PhosphoSiteP54652.

Polymorphism databases

DMDM1708307.

2D gel databases

REPRODUCTION-2DPAGEIPI00007702.

Proteomic databases

MaxQBP54652.
PaxDbP54652.
PeptideAtlasP54652.
PRIDEP54652.

Protocols and materials databases

DNASU3306.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000247207; ENSP00000247207; ENSG00000126803.
ENST00000394709; ENSP00000378199; ENSG00000126803.
GeneID3306.
KEGGhsa:3306.
UCSCuc001xhj.3. human.

Organism-specific databases

CTD3306.
GeneCardsGC14P065002.
HGNCHGNC:5235. HSPA2.
HPAHPA000798.
MIM140560. gene.
neXtProtNX_P54652.
PharmGKBPA29501.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0443.
HOGENOMHOG000228135.
HOVERGENHBG051845.
InParanoidP54652.
KOK03283.
OMAEAYLGCK.
OrthoDBEOG7PCJGF.
PhylomeDBP54652.
TreeFamTF105042.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_120956. Cellular responses to stress.

Gene expression databases

BgeeP54652.
CleanExHS_HSPA2.
GenevestigatorP54652.

Family and domain databases

Gene3D1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSPR00301. HEATSHOCK70.
SUPFAMSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSHSPA2. human.
EvolutionaryTraceP54652.
GeneWikiHSPA2.
GenomeRNAi3306.
NextBio13115.
PROP54652.
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: July 9, 2014
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

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