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: 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 (PubMed:24557841). In association with SHCBP1L may participate in the maintenance of spindle integrity during meiosis in male germ cells (PubMed:24557841).Curated1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei72 – 721ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 164ATPBy similarity
Nucleotide bindingi205 – 2073ATPBy similarity
Nucleotide bindingi271 – 2788ATPBy similarity
Nucleotide bindingi342 – 3454ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • enzyme binding Source: MGI
  • glycolipid binding Source: MGI
  • unfolded protein binding Source: MGI

GO - Biological processi

  • male meiosis Source: MGI
  • male meiosis I 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 cyclin-dependent protein serine/threonine kinase activity involved in 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
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Differentiation, Spermatogenesis, Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:96243. Hspa2.

Subcellular locationi

  • Cytoplasmcytoskeletonspindle 1 Publication

  • Note: Colocalizes with SHCBP1L at spindle during the meiosis process (PubMed:24557841).1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 633633Heat shock-related 70 kDa protein 2PRO_0000078259Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei403 – 4031PhosphoserineBy similarity
Modified residuei408 – 4081PhosphothreonineBy similarity
Modified residuei414 – 4141PhosphothreonineBy similarity
Modified residuei564 – 5641N6,N6,N6-trimethyllysine; by METTL21A; in vitroBy similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiP17156.
MaxQBiP17156.
PaxDbiP17156.
PRIDEiP17156.

2D gel databases

REPRODUCTION-2DPAGEIPI00331546.
P17156.
UCD-2DPAGEP17156.

PTM databases

iPTMnetiP17156.
PhosphoSiteiP17156.
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

BgeeiP17156.
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. 10 interactions.
DIPiDIP-42071N.
IntActiP17156. 5 interactions.
MINTiMINT-1207820.
STRINGi10090.ENSMUSP00000079306.

Structurei

3D structure databases

ProteinModelPortaliP17156.
SMRiP17156. Positions 3-616.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00820000127001.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP17156.
KOiK03283.
OMAiKTQIHDI.
OrthoDBiEOG7PCJGF.
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711A → R in AAA37859 (PubMed:3405224).Curated
Sequence conflicti222 – 2221V → L in AAA37859 (PubMed:3405224).Curated

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_006515484.2.
UniGeneiMm.296181.

Genome annotation databases

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

Cross-referencesi

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_006515484.2.
UniGeneiMm.296181.

3D structure databases

ProteinModelPortaliP17156.
SMRiP17156. Positions 3-616.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200453. 10 interactions.
DIPiDIP-42071N.
IntActiP17156. 5 interactions.
MINTiMINT-1207820.
STRINGi10090.ENSMUSP00000079306.

PTM databases

iPTMnetiP17156.
PhosphoSiteiP17156.
SwissPalmiP17156.

2D gel databases

REPRODUCTION-2DPAGEIPI00331546.
P17156.
UCD-2DPAGEP17156.

Proteomic databases

EPDiP17156.
MaxQBiP17156.
PaxDbiP17156.
PRIDEiP17156.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3306.
MGIiMGI:96243. Hspa2.

Phylogenomic databases

eggNOGiKOG0101. Eukaryota.
COG0443. LUCA.
GeneTreeiENSGT00820000127001.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP17156.
KOiK03283.
OMAiKTQIHDI.
OrthoDBiEOG7PCJGF.
TreeFamiTF105042.

Enzyme and pathway databases

ReactomeiR-MMU-1221632. Meiotic synapsis.
R-MMU-1221633. Meiotic Synapsis.

Miscellaneous databases

PROiP17156.
SOURCEiSearch...

Gene expression databases

BgeeiP17156.
CleanExiMM_HSPA2.
GenevisibleiP17156. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and sequence analysis of a new member of the mouse HSP70 gene family and characterization of its unique cellular and developmental pattern of expression in the male germ line."
    Zakeri Z.F., Wolgemuth D.J., Hunt C.R.
    Mol. Cell. Biol. 8:2925-2932(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor and Testis.
  4. "A novel germ cell-specific protein, SHIP1, forms a complex with chromatin remodeling activity during spermatogenesis."
    Choi E., Han C., Park I., Lee B., Jin S., Choi H., Kim do H., Park Z.Y., Eddy E.M., Cho C.
    J. Biol. Chem. 283:35283-35294(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ZNF541.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Lung, Spleen and Testis.
  6. "MOV10L1 is necessary for protection of spermatocytes against retrotransposons by Piwi-interacting RNAs."
    Frost R.J., Hamra F.K., Richardson J.A., Qi X., Bassel-Duby R., Olson E.N.
    Proc. Natl. Acad. Sci. U.S.A. 107:11847-11852(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MOV10L1.
  7. "A novel gene required for male fertility and functional CATSPER channel formation in spermatozoa."
    Chung J.J., Navarro B., Krapivinsky G., Krapivinsky L., Clapham D.E.
    Nat. Commun. 2:153-153(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CATSPER COMPLEX.
    Strain: C57BL/6J.
  8. "RAB-like 2 has an essential role in male fertility, sperm intra-flagellar transport, and tail assembly."
    Lo J.C., Jamsai D., O'Connor A.E., Borg C., Clark B.J., Whisstock J.C., Field M.C., Adams V., Ishikawa T., Aitken R.J., Whittle B., Goodnow C.C., Ormandy C.J., O'Bryan M.K.
    PLoS Genet. 8:E1002969-E1002969(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RABL2, TISSUE SPECIFICITY.
  9. "SHCBP1L, a conserved protein in mammals, is predominantly expressed in male germ cells and maintains spindle stability during meiosis in testis."
    Liu M., Shi X., Bi Y., Qi L., Guo X., Wang L., Zhou Z., Sha J.
    Mol. Hum. Reprod. 20:463-475(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SHCBP1L, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiHSP72_MOUSE
AccessioniPrimary (citable) accession number: P17156
Secondary accession number(s): Q99KD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 141 of the entry and version 2 of the sequence. [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

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.