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P54652

- HSP72_HUMAN

UniProt

P54652 - HSP72_HUMAN

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Protein

Heat shock-related 70 kDa protein 2

Gene

HSPA2

Organism
Homo sapiens (Human)
Status
Reviewed - 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.

Sites

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

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. enzyme binding Source: BHF-UCL
  3. glycolipid binding Source: Ensembl
  4. unfolded protein binding Source: UniProt

GO - Biological processi

  1. male meiosis Source: ProtInc
  2. male meiosis I Source: Ensembl
  3. negative regulation of inclusion body assembly Source: UniProt
  4. positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G2/M transition of mitotic cell cycle Source: Ensembl
  5. protein refolding Source: UniProt
  6. response to unfolded protein Source: ProtInc
  7. spermatid development Source: ProtInc
  8. synaptonemal complex disassembly Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_200624. Attenuation phase.
REACT_200780. Regulation of HSF1-mediated heat shock response.
REACT_75792. Meiotic synapsis.

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
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:5235. HSPA2.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. CatSper complex Source: UniProtKB
  3. cell surface Source: Ensembl
  4. cytosol Source: UniProt
  5. extracellular vesicular exosome Source: UniProt
  6. male germ cell nucleus Source: Ensembl
  7. membrane Source: UniProtKB
  8. mitochondrion Source: Ensembl
  9. nucleus Source: UniProt
  10. synaptonemal complex Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi564 – 5641K → A: Abolishes methylation by METTL21A. 1 Publication

Organism-specific databases

PharmGKBiPA29501.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 639639Heat shock-related 70 kDa protein 2PRO_0000078258Add
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 vitro1 Publication

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiP54652.
PaxDbiP54652.
PeptideAtlasiP54652.
PRIDEiP54652.

2D gel databases

REPRODUCTION-2DPAGEIPI00007702.

PTM databases

PhosphoSiteiP54652.

Expressioni

Gene expression databases

BgeeiP54652.
CleanExiHS_HSPA2.
GenevestigatoriP54652.

Organism-specific databases

HPAiHPA000798.

Interactioni

Subunit structurei

Interacts with ZNF541. Component of the CatSper complex (By similarity). Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2 (By similarity). Interacts with FKBP6.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q96BE02EBI-356991,EBI-9356686
BAG4O954292EBI-356991,EBI-2949658
HSPBP1Q9NZL43EBI-356991,EBI-356763

Protein-protein interaction databases

BioGridi109538. 45 interactions.
IntActiP54652. 25 interactions.
MINTiMINT-1146083.
STRINGi9606.ENSP00000247207.

Structurei

Secondary structure

1
639
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 125Combined sources
Beta strandi14 – 2310Combined sources
Beta strandi26 – 294Combined sources
Beta strandi37 – 404Combined sources
Beta strandi43 – 453Combined sources
Beta strandi50 – 523Combined sources
Helixi54 – 585Combined sources
Turni59 – 624Combined sources
Helixi64 – 663Combined sources
Helixi71 – 733Combined sources
Turni74 – 763Combined sources
Helixi82 – 887Combined sources
Beta strandi92 – 987Combined sources
Beta strandi101 – 1088Combined sources
Beta strandi111 – 1155Combined sources
Helixi117 – 13620Combined sources
Beta strandi142 – 1476Combined sources
Helixi153 – 16614Combined sources
Beta strandi169 – 1757Combined sources
Helixi176 – 1838Combined sources
Turni184 – 1874Combined sources
Beta strandi191 – 1944Combined sources
Beta strandi197 – 2037Combined sources
Beta strandi208 – 2169Combined sources
Beta strandi219 – 22810Combined sources
Helixi233 – 25220Combined sources
Helixi260 – 27617Combined sources
Turni277 – 2793Combined sources
Beta strandi280 – 29112Combined sources
Beta strandi294 – 3018Combined sources
Helixi302 – 3087Combined sources
Helixi310 – 3156Combined sources
Helixi317 – 32711Combined sources
Helixi331 – 3333Combined sources
Beta strandi336 – 3416Combined sources
Helixi342 – 3454Combined sources
Helixi347 – 35610Combined sources
Turni357 – 3593Combined sources
Turni368 – 3703Combined sources
Helixi371 – 38313Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3I33X-ray1.30A6-386[»]
4FSVX-ray1.80A2-387[»]
ProteinModelPortaliP54652.
SMRiP54652. Positions 3-613.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54652.

Family & Domainsi

Sequence similaritiesi

Belongs to the heat shock protein 70 family.Curated

Phylogenomic databases

eggNOGiCOG0443.
GeneTreeiENSGT00750000117237.
HOGENOMiHOG000228135.
HOVERGENiHBG051845.
InParanoidiP54652.
KOiK03283.
OMAiEAYLGCK.
OrthoDBiEOG7PCJGF.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141T → P in AAH36107. (PubMed:15489334)Curated
Sequence conflicti54 – 541Missing in AAC50076. (PubMed:7849706)Curated
Sequence conflicti80 – 801E → G in AAH36107. (PubMed:15489334)Curated
Sequence conflicti266 – 2661L → S in AAD11466. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti191 – 1911C → S.1 Publication
Corresponds to variant rs45456191 [ dbSNP | Ensembl ].
VAR_032706
Natural varianti496 – 4961K → E.1 Publication
VAR_032707

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human.

Polymorphism databases

DMDMi1708307.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS9766.1.
PIRi A55719.
I37564.
RefSeqi NP_068814.2. NM_021979.3.
UniGenei Hs.432648.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3I33 X-ray 1.30 A 6-386 [» ]
4FSV X-ray 1.80 A 2-387 [» ]
ProteinModelPortali P54652.
SMRi P54652. Positions 3-613.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109538. 45 interactions.
IntActi P54652. 25 interactions.
MINTi MINT-1146083.
STRINGi 9606.ENSP00000247207.

Chemistry

ChEMBLi CHEMBL2062348.

PTM databases

PhosphoSitei P54652.

Polymorphism databases

DMDMi 1708307.

2D gel databases

REPRODUCTION-2DPAGE IPI00007702.

Proteomic databases

MaxQBi P54652.
PaxDbi P54652.
PeptideAtlasi P54652.
PRIDEi P54652.

Protocols and materials databases

DNASUi 3306.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000247207 ; ENSP00000247207 ; ENSG00000126803 .
ENST00000394709 ; ENSP00000378199 ; ENSG00000126803 .
GeneIDi 3306.
KEGGi hsa:3306.
UCSCi uc001xhj.3. human.

Organism-specific databases

CTDi 3306.
GeneCardsi GC14P065002.
HGNCi HGNC:5235. HSPA2.
HPAi HPA000798.
MIMi 140560. gene.
neXtProti NX_P54652.
PharmGKBi PA29501.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0443.
GeneTreei ENSGT00750000117237.
HOGENOMi HOG000228135.
HOVERGENi HBG051845.
InParanoidi P54652.
KOi K03283.
OMAi EAYLGCK.
OrthoDBi EOG7PCJGF.
PhylomeDBi P54652.
TreeFami TF105042.

Enzyme and pathway databases

Reactomei REACT_200624. Attenuation phase.
REACT_200780. Regulation of HSF1-mediated heat shock response.
REACT_75792. Meiotic synapsis.

Miscellaneous databases

ChiTaRSi HSPA2. human.
EvolutionaryTracei P54652.
GeneWikii HSPA2.
GenomeRNAii 3306.
NextBioi 13115.
PROi P54652.
SOURCEi Search...

Gene expression databases

Bgeei P54652.
CleanExi HS_HSPA2.
Genevestigatori P54652.

Family and domain databases

Gene3Di 1.20.1270.10. 1 hit.
2.60.34.10. 1 hit.
InterProi IPR018181. Heat_shock_70_CS.
IPR029048. HSP70_C.
IPR029047. HSP70_peptide-bd.
IPR013126. Hsp_70_fam.
[Graphical view ]
Pfami PF00012. HSP70. 1 hit.
[Graphical view ]
PRINTSi PR00301. HEATSHOCK70.
SUPFAMi SSF100920. SSF100920. 1 hit.
SSF100934. SSF100934. 1 hit.
PROSITEi PS00297. HSP70_1. 1 hit.
PS00329. HSP70_2. 1 hit.
PS01036. HSP70_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. "FKBP36 forms complexes with clathrin and Hsp72 in spermatocytes."
    Jarczowski F., Fischer G., Edlich F.
    Biochemistry 47:6946-6952(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FKBP6.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Identification and characterization of a novel human methyltransferase modulating Hsp70 function through lysine methylation."
    Jakobsson M.E., Moen A., Bousset L., Egge-Jacobsen W., Kernstock S., Melki R., Falnes P.O.
    J. Biol. Chem. 288:27752-27763(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-564, MUTAGENESIS OF LYS-564.
  10. "Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78."
    Wisniewska M., Karlberg T., Lehtio L., Johansson I., Kotenyova T., Moche M., Schuler H.
    PLoS ONE 5:E8625-E8625(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 6-386 IN COMPLEX WITH ADP AND PHOSPHATE.

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: October 29, 2014
This is version 139 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

External Data

Dasty 3