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Protein

Heat shock-related 70 kDa protein 2

Gene

Hspa2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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. 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. Plays a role in spermatogenesis. In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells.By similarity

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

Keywordsi

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

Names & Taxonomyi

Protein namesi
Recommended name:
Heat shock-related 70 kDa protein 2
Short name:
Heat shock protein 70.2
Alternative name(s):
Testis-specific heat shock protein-related
Short name:
HST
Gene namesi
Name:Hspa2
Synonyms:Hst70
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi620664. 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_00000782601 – 633Heat shock-related 70 kDa protein 2Add BLAST633

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei403PhosphoserineCombined sources1
Modified residuei408PhosphothreonineCombined sources1
Modified residuei414PhosphothreonineCombined sources1
Modified residuei564N6,N6,N6-trimethyllysine; by METTL21A; in vitroBy similarity1

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

PaxDbiP14659.
PRIDEiP14659.

PTM databases

iPTMnetiP14659.
PhosphoSitePlusiP14659.

Expressioni

Gene expression databases

BgeeiENSRNOG00000006472.
ExpressionAtlasiP14659. baseline and differential.
GenevisibleiP14659. RN.

Interactioni

Subunit structurei

Interacts with FKBP6. 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. Interacts with MOV10L1 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi248845. 1 interactor.
ELMiP14659.
IntActiP14659. 1 interactor.
STRINGi10116.ENSRNOP00000008504.

Structurei

3D structure databases

ProteinModelPortaliP14659.
SMRiP14659.
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.
GeneTreeiENSGT00900000140908.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP14659.
KOiK03283.
OMAiEAYLGCK.
OrthoDBiEOG091G03SF.
PhylomeDBiP14659.
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.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
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.

P14659-1 [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:June 12, 2007 - v2
Checksum:i6F65773C7EFFA69F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti526 – 527ER → DG in CAA33735 (PubMed:1688714).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15705 Genomic DNA. Translation: CAA33735.1.
BC081803 mRNA. Translation: AAH81803.1.
PIRiS08211.
RefSeqiNP_068635.1. NM_021863.3.
XP_006240309.1. XM_006240247.3.
UniGeneiRn.211303.

Genome annotation databases

EnsembliENSRNOT00000008504; ENSRNOP00000008504; ENSRNOG00000006472.
GeneIDi60460.
KEGGirno:60460.
UCSCiRGD:620664. rat.

Similar proteinsi

Entry informationi

Entry nameiHSP72_RAT
AccessioniPrimary (citable) accession number: P14659
Secondary accession number(s): Q66HL1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: June 12, 2007
Last modified: October 25, 2017
This is version 138 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. SIMILARITY comments
    Index of protein domains and families