Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Heat shock-related 70 kDa protein 2

Gene

Hspa2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release (By similarity). Plays a role in spermatogenesis (PubMed:24557841). In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells (PubMed:24557841).By similarity1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei72ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi13 – 16ATPBy similarity4
Nucleotide bindingi205 – 207ATPBy similarity3
Nucleotide bindingi271 – 278ATPBy similarity8
Nucleotide bindingi342 – 345ATPBy similarity4

GO - Molecular functioni

GO - Biological processi

  • male meiosis I Source: MGI
  • male meiotic nuclear division Source: MGI
  • negative regulation of inclusion body assembly Source: MGI
  • positive regulation of ATPase activity Source: CACAO
  • positive regulation of calcium-transporting ATPase activity Source: CACAO
  • positive regulation of G2/M transition of mitotic cell cycle Source: MGI
  • positive regulation of protein phosphorylation Source: MGI
  • protein refolding Source: MGI
  • response to cold Source: AgBase
  • response to heat Source: AgBase
  • spermatid development Source: MGI
  • spermatogenesis Source: UniProtKB
  • synaptonemal complex disassembly Source: MGI

Keywordsi

Molecular functionChaperone
Biological processDifferentiation, Spermatogenesis, Stress response
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-3371453 Regulation of HSF1-mediated heat shock response
R-MMU-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-MMU-3371568 Attenuation phase

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock-related 70 kDa protein 2
Short name:
Heat shock protein 70.2
Gene namesi
Name:Hspa2
Synonyms:Hcp70.2, Hsp70-2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:96243 Hspa2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000782591 – 633Heat shock-related 70 kDa protein 2Add BLAST633

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 vitroBy similarity1

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiP17156
MaxQBiP17156
PaxDbiP17156
PeptideAtlasiP17156
PRIDEiP17156

2D gel databases

REPRODUCTION-2DPAGEiIPI00331546
P17156
UCD-2DPAGEiP17156

PTM databases

iPTMnetiP17156
PhosphoSitePlusiP17156
SwissPalmiP17156

Expressioni

Tissue specificityi

Expressed in male germ cells (at protein level) (PubMed:24557841, PubMed:23055941, PubMed:3405224).3 Publications

Developmental stagei

Specifically expressed in prophage stage of meiosis (PubMed:3405224).1 Publication

Gene expression databases

BgeeiENSMUSG00000059970
CleanExiMM_HSPA2
GenevisibleiP17156 MM

Interactioni

Subunit structurei

Interacts with FKBP6 (By similarity). Interacts with ZNF541 (PubMed:18849567). Component of the CatSper complex (PubMed:21224844). Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2 (PubMed:23055941). Interacts with SHCBP1L; this interaction may promote the recruitment of HSPA2 to the spindle (PubMed:24557841). Interacts with MOV10L1 (PubMed:20547853).By similarity5 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi200453, 11 interactors
CORUMiP17156
DIPiDIP-42071N
ELMiP17156
IntActiP17156, 8 interactors
MINTiP17156
STRINGi10090.ENSMUSP00000079306

Structurei

3D structure databases

ProteinModelPortaliP17156
SMRiP17156
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 389Nucleotide-binding domain (NBD)By similarityAdd BLAST388
Regioni397 – 512Substrate-binding domain (SBD)By similarityAdd BLAST116

Domaini

The N-terminal nucleotide binding domain (NBD) (also known as the ATPase domain) is responsible for binding and hydrolyzing ATP. The C-terminal substrate-binding domain (SBD) (also known as peptide-binding domain) binds to the client/substrate proteins. The two domains are allosterically coupled so that, when ATP is bound to the NBD, the SBD binds relatively weakly to clients. When ADP is bound in the NBD, a conformational change enhances the affinity of the SBD for client proteins.By similarity

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiKOG0101 Eukaryota
COG0443 LUCA
GeneTreeiENSGT00910000144045
HOGENOMiHOG000228135
HOVERGENiHBG051845
InParanoidiP17156
KOiK03283
OMAiEAYLGCK
OrthoDBiEOG091G03SF
TreeFamiTF105042

Family and domain databases

Gene3Di1.20.1270.10, 1 hit
2.60.34.10, 1 hit
InterProiView protein in InterPro
IPR018181 Heat_shock_70_CS
IPR029048 HSP70_C_sf
IPR029047 HSP70_peptide-bd_sf
IPR013126 Hsp_70_fam
PANTHERiPTHR19375 PTHR19375, 1 hit
PfamiView protein in Pfam
PF00012 HSP70, 1 hit
PRINTSiPR00301 HEATSHOCK70
SUPFAMiSSF100920 SSF100920, 1 hit
SSF100934 SSF100934, 1 hit
PROSITEiView protein in PROSITE
PS00297 HSP70_1, 1 hit
PS00329 HSP70_2, 1 hit
PS01036 HSP70_3, 1 hit

Sequencei

Sequence statusi: Complete.

P17156-1 [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 EMKTFFPEEI SSMVLTKMKE IAEAYLGGKV QSAVITVPAY
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 AKNAVESYTY
560 570 580 590 600
NIKQTVEDEK LRGKISEQDK NKILDKCQEV INWLDRNQMA EKDEYEHKQK
610 620 630
ELERVCNPII SKLYQGGPGG GGSSGGPTIE EVD
Length:633
Mass (Da):69,642
Last modified:July 27, 2011 - v2
Checksum:i6F65773C7EFFA69F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti71A → R in AAA37859 (PubMed:3405224).Curated1
Sequence conflicti222V → L in AAA37859 (PubMed:3405224).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M20567 Genomic DNA Translation: AAA37859.1
CH466526 Genomic DNA Translation: EDL36460.1
BC004714 mRNA Translation: AAH04714.1
BC052350 mRNA Translation: AAH52350.1
CCDSiCCDS25993.1
PIRiS10859
RefSeqiNP_001002012.1, NM_001002012.1
NP_032327.2, NM_008301.4
XP_006515547.1, XM_006515484.3
UniGeneiMm.296181

Genome annotation databases

EnsembliENSMUST00000080449; ENSMUSP00000079306; ENSMUSG00000059970
ENSMUST00000219555; ENSMUSP00000151408; ENSMUSG00000059970
GeneIDi15512
KEGGimmu:15512
UCSCiuc007nyf.1 mouse

Similar proteinsi

Entry informationi

Entry nameiHSP72_MOUSE
AccessioniPrimary (citable) accession number: P17156
Secondary accession number(s): Q99KD7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: July 27, 2011
Last modified: July 18, 2018
This is version 159 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health