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Protein

Heat shock-related 70 kDa protein 2

Gene

HSPA2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells.By similarityCurated

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei72ATP1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi13 – 16ATP4
Nucleotide bindingi205 – 207ATP3
Nucleotide bindingi271 – 278ATP8
Nucleotide bindingi342 – 345ATP4

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: BHF-UCL
  • glycolipid binding Source: Ensembl
  • unfolded protein binding Source: UniProtKB

GO - Biological processi

  • male meiosis Source: ProtInc
  • male meiosis I Source: Ensembl
  • negative regulation of inclusion body assembly Source: UniProtKB
  • positive regulation of calcium-transporting ATPase activity Source: Ensembl
  • positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G2/M transition of mitotic cell cycle Source: Ensembl
  • protein refolding Source: UniProtKB
  • response to cold Source: AgBase
  • response to heat Source: AgBase
  • response to unfolded protein Source: ProtInc
  • spermatid development Source: ProtInc
  • spermatogenesis Source: UniProtKB
  • synaptonemal complex disassembly Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Differentiation, Spermatogenesis, Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000126803-MONOMER.
ReactomeiR-HSA-1221632. Meiotic synapsis.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-3371568. Attenuation phase.
SIGNORiP54652.

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock-related 70 kDa protein 2
Short name:
Heat shock 70 kDa protein 2
Gene namesi
Name:HSPA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:5235. HSPA2.

Subcellular locationi

  • Cytoplasmcytoskeletonspindle By similarity

  • Note: Colocalizes with SHCBP1L at spindle during the meiosis process.By similarity

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • CatSper complex Source: UniProtKB
  • cell surface Source: Ensembl
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • male germ cell nucleus Source: Ensembl
  • meiotic spindle Source: UniProtKB
  • membrane Source: UniProtKB
  • mitochondrion Source: Ensembl
  • myelin sheath Source: Ensembl
  • nucleus Source: UniProtKB
  • synaptonemal complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi564K → A: Abolishes methylation by METTL21A. 1 Publication1

Organism-specific databases

DisGeNETi3306.
OpenTargetsiENSG00000126803.
PharmGKBiPA29501.

Chemistry databases

ChEMBLiCHEMBL2062348.

Polymorphism and mutation databases

BioMutaiHSPA2.
DMDMi1708307.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000782581 – 639Heat shock-related 70 kDa protein 2Add BLAST639

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei403PhosphoserineBy similarity1
Modified residuei408PhosphothreonineBy similarity1
Modified residuei414PhosphothreonineBy similarity1
Modified residuei564N6,N6,N6-trimethyllysine; by METTL21A; in vitro1 Publication1

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiP54652.
MaxQBiP54652.
PaxDbiP54652.
PeptideAtlasiP54652.
PRIDEiP54652.

2D gel databases

REPRODUCTION-2DPAGEIPI00007702.

PTM databases

iPTMnetiP54652.
PhosphoSitePlusiP54652.
SwissPalmiP54652.

Expressioni

Gene expression databases

BgeeiENSG00000126803.
CleanExiHS_HSPA2.
ExpressionAtlasiP54652. baseline and differential.
GenevisibleiP54652. HS.

Organism-specific databases

HPAiHPA000798.
HPA052504.

Interactioni

Subunit structurei

Interacts with FKBP6 (PubMed:18529014). Interacts with ZNF541. Component of the CatSper complex. Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2. Interacts with SHCBP1L; this interaction may promote the recruitment of HSPA2 to the spindle (By similarity). Interacts with FKBP6 (PubMed:18529014).By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Q96BE02EBI-356991,EBI-9356686
BAG4O954294EBI-356991,EBI-2949658
HSPBP1Q9NZL46EBI-356991,EBI-356763
TRIM38O006353EBI-356991,EBI-2130415

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • unfolded protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi109538. 76 interactors.
IntActiP54652. 36 interactors.
MINTiMINT-1146083.
STRINGi9606.ENSP00000247207.

Structurei

Secondary structure

1639
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 12Combined sources5
Beta strandi14 – 23Combined sources10
Beta strandi26 – 29Combined sources4
Beta strandi37 – 40Combined sources4
Beta strandi43 – 45Combined sources3
Beta strandi50 – 52Combined sources3
Helixi54 – 58Combined sources5
Turni59 – 62Combined sources4
Helixi64 – 66Combined sources3
Helixi71 – 73Combined sources3
Turni74 – 76Combined sources3
Helixi82 – 88Combined sources7
Beta strandi92 – 98Combined sources7
Beta strandi101 – 108Combined sources8
Beta strandi111 – 115Combined sources5
Helixi117 – 136Combined sources20
Beta strandi142 – 147Combined sources6
Helixi153 – 166Combined sources14
Beta strandi169 – 175Combined sources7
Helixi176 – 183Combined sources8
Turni184 – 187Combined sources4
Beta strandi191 – 194Combined sources4
Beta strandi197 – 203Combined sources7
Beta strandi208 – 216Combined sources9
Beta strandi219 – 228Combined sources10
Helixi233 – 252Combined sources20
Helixi260 – 276Combined sources17
Turni277 – 279Combined sources3
Beta strandi280 – 291Combined sources12
Beta strandi294 – 301Combined sources8
Helixi302 – 308Combined sources7
Helixi310 – 315Combined sources6
Helixi317 – 327Combined sources11
Helixi331 – 333Combined sources3
Beta strandi336 – 341Combined sources6
Helixi342 – 345Combined sources4
Helixi347 – 356Combined sources10
Turni357 – 359Combined sources3
Turni368 – 370Combined sources3
Helixi371 – 383Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3I33X-ray1.30A6-386[»]
4FSVX-ray1.80A2-387[»]
5FPDX-ray1.97A/B4-386[»]
5FPEX-ray1.96A/B4-386[»]
5FPMX-ray1.96A/B4-386[»]
5FPNX-ray1.96A/B4-639[»]
ProteinModelPortaliP54652.
SMRiP54652.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54652.

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00820000127001.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP54652.
KOiK03283.
OMAiKENDDRG.
OrthoDBiEOG091G03SF.
PhylomeDBiP54652.
TreeFamiTF105042.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P54652-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSARGPAIGI DLGTTYSCVG VFQHGKVEII ANDQGNRTTP SYVAFTDTER
60 70 80 90 100
LIGDAAKNQV AMNPTNTIFD AKRLIGRKFE DATVQSDMKH WPFRVVSEGG
110 120 130 140 150
KPKVQVEYKG ETKTFFPEEI SSMVLTKMKE IAEAYLGGKV HSAVITVPAY
160 170 180 190 200
FNDSQRQATK DAGTITGLNV LRIINEPTAA AIAYGLDKKG CAGGEKNVLI
210 220 230 240 250
FDLGGGTFDV SILTIEDGIF EVKSTAGDTH LGGEDFDNRM VSHLAEEFKR
260 270 280 290 300
KHKKDIGPNK RAVRRLRTAC ERAKRTLSSS TQASIEIDSL YEGVDFYTSI
310 320 330 340 350
TRARFEELNA DLFRGTLEPV EKALRDAKLD KGQIQEIVLV GGSTRIPKIQ
360 370 380 390 400
KLLQDFFNGK ELNKSINPDE AVAYGAAVQA AILIGDKSEN VQDLLLLDVT
410 420 430 440 450
PLSLGIETAG GVMTPLIKRN TTIPTKQTQT FTTYSDNQSS VLVQVYEGER
460 470 480 490 500
AMTKDNNLLG KFDLTGIPPA PRGVPQIEVT FDIDANGILN VTAADKSTGK
510 520 530 540 550
ENKITITNDK GRLSKDDIDR MVQEAERYKS EDEANRDRVA AKNALESYTY
560 570 580 590 600
NIKQTVEDEK LRGKISEQDK NKILDKCQEV INWLDRNQMA EKDEYEHKQK
610 620 630
ELERVCNPII SKLYQGGPGG GSGGGGSGAS GGPTIEEVD
Length:639
Mass (Da):70,021
Last modified:October 1, 1996 - v1
Checksum:i3851755494E7B729
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14T → P in AAH36107 (PubMed:15489334).Curated1
Sequence conflicti54Missing in AAC50076 (PubMed:7849706).Curated1
Sequence conflicti80E → G in AAH36107 (PubMed:15489334).Curated1
Sequence conflicti266L → S in AAD11466 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_032706191C → S.1 PublicationCorresponds to variant rs45456191dbSNPEnsembl.1
Natural variantiVAR_032707496K → E.1 PublicationCorresponds to variant rs45447398dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9766.1.
PIRiA55719.
I37564.
RefSeqiNP_068814.2. NM_021979.3.
UniGeneiHs.432648.

Genome annotation databases

EnsembliENST00000247207; ENSP00000247207; ENSG00000126803.
ENST00000394709; ENSP00000378199; ENSG00000126803.
GeneIDi3306.
KEGGihsa:3306.
UCSCiuc001xhj.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9766.1.
PIRiA55719.
I37564.
RefSeqiNP_068814.2. NM_021979.3.
UniGeneiHs.432648.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3I33X-ray1.30A6-386[»]
4FSVX-ray1.80A2-387[»]
5FPDX-ray1.97A/B4-386[»]
5FPEX-ray1.96A/B4-386[»]
5FPMX-ray1.96A/B4-386[»]
5FPNX-ray1.96A/B4-639[»]
ProteinModelPortaliP54652.
SMRiP54652.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109538. 76 interactors.
IntActiP54652. 36 interactors.
MINTiMINT-1146083.
STRINGi9606.ENSP00000247207.

Chemistry databases

ChEMBLiCHEMBL2062348.

PTM databases

iPTMnetiP54652.
PhosphoSitePlusiP54652.
SwissPalmiP54652.

Polymorphism and mutation databases

BioMutaiHSPA2.
DMDMi1708307.

2D gel databases

REPRODUCTION-2DPAGEIPI00007702.

Proteomic databases

EPDiP54652.
MaxQBiP54652.
PaxDbiP54652.
PeptideAtlasiP54652.
PRIDEiP54652.

Protocols and materials databases

DNASUi3306.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000247207; ENSP00000247207; ENSG00000126803.
ENST00000394709; ENSP00000378199; ENSG00000126803.
GeneIDi3306.
KEGGihsa:3306.
UCSCiuc001xhj.4. human.

Organism-specific databases

CTDi3306.
DisGeNETi3306.
GeneCardsiHSPA2.
HGNCiHGNC:5235. HSPA2.
HPAiHPA000798.
HPA052504.
MIMi140560. gene.
neXtProtiNX_P54652.
OpenTargetsiENSG00000126803.
PharmGKBiPA29501.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00820000127001.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP54652.
KOiK03283.
OMAiKENDDRG.
OrthoDBiEOG091G03SF.
PhylomeDBiP54652.
TreeFamiTF105042.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000126803-MONOMER.
ReactomeiR-HSA-1221632. Meiotic synapsis.
R-HSA-3371453. Regulation of HSF1-mediated heat shock response.
R-HSA-3371568. Attenuation phase.
SIGNORiP54652.

Miscellaneous databases

ChiTaRSiHSPA2. human.
EvolutionaryTraceiP54652.
GeneWikiiHSPA2.
GenomeRNAii3306.
PROiP54652.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000126803.
CleanExiHS_HSPA2.
ExpressionAtlasiP54652. baseline and differential.
GenevisibleiP54652. HS.

Family and domain databases

Gene3Di1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProiIPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view]
PfamiPF00012. HSP70. 1 hit.
[Graphical view]
PRINTSiPR00301. HEATSHOCK70.
SUPFAMiSSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEiPS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHSP72_HUMAN
AccessioniPrimary (citable) accession number: P54652
Secondary accession number(s): Q15508, Q53XM3, Q9UE78
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.