Heat shock-related 70 kDa protein 2

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P54652 (HSP72_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 124. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Heat shock-related 70 kDa protein 2
Short name=Heat shock 70 kDa protein 2

Gene names

Name:

HSPA2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	639 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Sequence similarities	Belongs to the heat shock protein 70 family.

Ontologies

Keywords
Biological process	Stress response
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	male meiosis Traceable author statement PubMed 8622925. Source: ProtInc male meiosis I Inferred from electronic annotation. Source: Compara positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G2/M Inferred from electronic annotation. Source: Compara 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: Compara
Cellular_component	CatSper complex Inferred from sequence or structural similarity. Source: UniProtKB cell surface Inferred from direct assay PubMed 12493773. Source: UniProtKB male germ cell nucleus Inferred from electronic annotation. Source: Compara mitochondrion Inferred from electronic annotation. Source: Compara synaptonemal complex Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glycolipid binding Inferred from electronic annotation. Source: Compara unfolded protein binding Traceable author statement PubMed 3037489. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HSPBP1	Q9NZL4	3	EBI-356991,EBI-356763

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 639

639

Heat shock-related 70 kDa protein 2

PRO_0000078258

Natural variations

Natural variant

191

C → S. Ref.4

VAR_032706

Natural variant

496

K → E. Ref.4

VAR_032707

Experimental info

Sequence conflict

T → P in AAH36107. Ref.5

Sequence conflict

Missing in AAC50076. Ref.6

Sequence conflict

E → G in AAH36107. Ref.5

Sequence conflict

266

L → S in AAD11466. Ref.2

Secondary structure

639

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P54652 [UniParc].

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

FASTA

639

70,021

        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' referencesShow '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]	"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].
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

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.

IPI

IPI00007702.

PIR

A55719.
I37564.

RefSeq

NP_068814.2. NM_021979.3.

UniGene

Hs.432648.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3I33	X-ray	1.30	A	6-386	[»]
4FSV	X-ray	1.80	A	2-387	[»]

ProteinModelPortal

P54652.

ModBase

Search...

Protein-protein interaction databases

IntAct

P54652. 10 interactions.

MINT

MINT-1146083.

STRING

9606.ENSP00000247207.

PTM databases

PhosphoSite

P54652.

Polymorphism databases

DMDM

1708307.

2D gel databases

REPRODUCTION-2DPAGE

IPI00007702.

Proteomic databases

PaxDb

P54652.

PeptideAtlas

P54652.

PRIDE

P54652.

Protocols and materials databases

DNASU

3306.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000247207; ENSP00000247207; ENSG00000126803.
ENST00000394709; ENSP00000378199; ENSG00000126803.

GeneID

3306.

KEGG

hsa:3306.

UCSC

uc001xhj.3. human.

Organism-specific databases

CTD

3306.

GeneCards

GC14P065002.

HGNC

HGNC:5235. HSPA2.

HPA

HPA000798.

MIM

140560. gene.

neXtProt

NX_P54652.

PharmGKB

PA29501.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0443.

HOGENOM

HOG000228135.

HOVERGEN

HBG051845.

InParanoid

P54652.

K03283.

OMA

LESYTYN.

OrthoDB

EOG4W6NVK.

PhylomeDB

P54652.

Enzyme and pathway databases

Reactome

REACT_111183. Meiosis.
REACT_115566. Cell Cycle.

Gene expression databases

Bgee

P54652.

CleanEx

HS_HSPA2.

Genevestigator

P54652.

GermOnline

ENSG00000126803. Homo sapiens.

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

ChiTaRS

HSPA2. human.

EvolutionaryTrace

P54652.

GenomeRNAi

3306.

NextBio

13115.

SOURCE

Search...

Entry information

Entry name

HSP72_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 124 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Natural variations

Experimental info

Secondary structure

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents