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Sample Preparation and Post-separation Analysis

Searching in 'SWISS-2DPAGE' for entry matching: HSP71_HUMAN



General information about the entry
View entry in simple text format
Entry nameHSP71_HUMAN
Primary accession numberP08107
integrated into SWISS-2DPAGE on April 1, 2000 (release 12)
2D Annotations were last modified onMarch 31, 2004 (version 2)
General Annotations were last modified on May 19, 2011 (version 10)
Name and origin of the protein
DescriptionRecName: Full=Heat shock 70 kDa protein 1A/1B; AltName: Full=Heat shock 70 kDa protein 1/2; Short=HSP70-1/HSP70-2; Short=HSP70.1/HSP70.2;.
Gene nameName=HSPA1A
Annotated speciesHomo sapiens (Human) [TaxID: 9606]
TaxonomyEukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
MEDLINE=20529951; PubMed=11079567; [NCBI, ExPASy, EBI, Israel, Japan]
Jung E., Hoogland C., Chiappe D., Sanchez J.-C., Hochstrasser D.F.
''''''The establishment of a human liver nuclei 2-DE reference map'';'';''
Electrophoresis 21(1):3483-3487(2000)
PubMed=12429849; [NCBI, ExPASy, EBI, Israel, Japan]
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
''''''Functional proteomic analysis of human nucleolus'';'';''
Mol. Biol. Cell. 13(1):4100-4109(2002)
2D PAGE maps for identified proteins
How to interpret a protein

NUCLEI_LIVER_HUMAN {Soluble nuclear proteins and matrix from liver tissue}
Homo sapiens (Human)
Tissue: Liver
  map experimental info
  protein estimated location

pI=5.44; Mw=66230  [identification data]
pI=5.54; Mw=65877  [identification data]

MAPPING (identification):
Peptide mass fingerprinting [1].

NUCLEOLI_HELA_2D_HUMAN {2D-PAGE of nucleolar proteins from Human HeLa cells}
Homo sapiens (Human)
Tissue: Cervix carcinoma
  map experimental info
  protein estimated location

pI=5.65; Mw=68886  [identification data]

MAPPING (identification):
Peptide mass fingerprinting [2].

This SWISS-2DPAGE entry is copyright the Swiss Institute of Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified and this statement is not removed. Usage by and for commercial entities requires a license agreement (See or send email from
DOSAC-COBS 2D-PAGEP08107; P08107.
Siena-2DPAGEP08107; HSP71_HUMAN.
UniProtKB/Swiss-ProtP08107; HSP71_HUMAN.
2D PAGE maps for identified proteins
  • How to interpret a protein map
  • You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw.
  • Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly.
  • Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed.

External data extracted from UniProtKB/Swiss-Prot
Extracted from UniProtKB/Swiss-Prot, release: 2011_10
Entry nameHSP71_HUMAN
Primary accession numberP08107
Secondary accession number(s) P19790 Q5JQI4 Q5SP17 Q9UQL9 Q9UQM0
Sequence was last modified on May 15, 2007 (version 5)
Annotations were last modified on October 19, 2011 (version 150)
Name and origin of the protein
DescriptionRecName: Full=Heat shock 70 kDa protein 1A/1B; AltName: Full=Heat shock 70 kDa protein 1/2; Short=HSP70-1/HSP70-2; Short=HSP70.1/HSP70.2;
Gene nameName=HSPA1A
Encoded onName=HSPA1A; Synonyms=HSPA1; and Name=HSPA1B
Keywords3D-structure; Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Host cell receptor for virus entry; Nucleotide-binding; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Stress response.
Copyrighted by the UniProt Consortium, see Distributed under the Creative Commons Attribution-NoDerivs License
EMBLM59828; AAA63226.1; -; Genomic_DNA
EMBLM59830; AAA63227.1; -; Genomic_DNA
EMBLM11717; AAA52697.1; -; Genomic_DNA
EMBLAF134726; AAD21815.1; -; Genomic_DNA
EMBLAF134726; AAD21816.1; -; Genomic_DNA
EMBLBA000025; BAB63299.1; -; Genomic_DNA
EMBLBA000025; BAB63300.1; -; Genomic_DNA
EMBLDQ388429; ABD48956.1; -; Genomic_DNA
EMBLDQ451402; ABD96830.1; -; Genomic_DNA
EMBLAL662834; CAI17737.1; -; Genomic_DNA
EMBLAL662834; CAI17738.1; -; Genomic_DNA
EMBLAL671762; CAI18216.1; -; Genomic_DNA
EMBLAL671762; CAI18217.1; -; Genomic_DNA
EMBLAL929592; CAI18464.1; -; Genomic_DNA
EMBLAL929592; CAI18466.1; -; Genomic_DNA
EMBLBC002453; AAH02453.1; -; mRNA
EMBLBC009322; AAH09322.1; -; mRNA
EMBLBC018740; AAH18740.1; -; mRNA
EMBLBC057397; AAH57397.1; -; mRNA
EMBLBC063507; AAH63507.1; -; mRNA
EMBLM24743; AAA59844.1; -; Genomic_DNA
EMBLM24744; AAA59845.1; -; Genomic_DNA
EMBLX04676; CAA28381.1; -; Genomic_DNA
EMBLX04677; CAA28382.1; -; Genomic_DNA
IPIIPI00304925; -; .
PIRA29160; A29160; .
PIRA45871; A45871; .
PIRI59139; I59139; .
PIRI79540; I79540; .
RefSeqNP_005336.3; NM_005345.5; .
RefSeqNP_005337.2; NM_005346.4; .
UniGeneHs.274402; -; .
UniGeneHs.719966; -; .
UniGeneHs.728810; -; .
PDB1HJO; X-ray; 2.30 A; A=3-382
PDB1S3X; X-ray; 1.84 A; A=1-382
PDB1XQS; X-ray; 2.90 A; C/D=184-371
PDB2E88; X-ray; 1.80 A; A=1-388
PDB2E8A; X-ray; 1.77 A; A=1-388
PDB3A8Y; X-ray; 2.30 A; A/B=1-388
PDB3D2E; X-ray; 2.35 A; B/D=1-382
PDB3D2F; X-ray; 2.30 A; B/D=1-382
PDB3JXU; X-ray; 2.14 A; A=1-387
PDB3LOF; X-ray; 2.40 A; A/B/C/D/E/F=534-641
PDBsum1HJO; -; .
PDBsum1S3X; -; .
PDBsum1XQS; -; .
PDBsum2E88; -; .
PDBsum2E8A; -; .
PDBsum3A8Y; -; .
PDBsum3D2E; -; .
PDBsum3D2F; -; .
PDBsum3JXU; -; .
PDBsum3LOF; -; .
ProteinModelPortalP08107; -; .
SMRP08107; 1-613; .
DIPDIP-211N; -; .
IntActP08107; 52; .
MINTMINT-96699; -; .
STRINGP08107; -; .
TCDB1.A.33.1.3; cation channel-forming heat shock protein-70 (Hsp70) family; .
PhosphoSiteP08107; -; .
SWISS-2DPAGEP08107; -; .
Cornea-2DPAGEP08107; -; .
OGPP08107; -; .
UCD-2DPAGEP08107; -; .
PRIDEP08107; -; .
EnsemblENST00000375650; ENSP00000364801; ENSG00000204388; .
EnsemblENST00000375651; ENSP00000364802; ENSG00000204389; .
EnsemblENST00000391548; ENSP00000375391; ENSG00000224501; .
EnsemblENST00000391555; ENSP00000375399; ENSG00000212866; .
EnsemblENST00000430065; ENSP00000404524; ENSG00000235941; .
EnsemblENST00000433487; ENSP00000408907; ENSG00000234475; .
EnsemblENST00000441618; ENSP00000406359; ENSG00000237724; .
EnsemblENST00000445736; ENSP00000403530; ENSG00000231555; .
EnsemblENST00000450744; ENSP00000393087; ENSG00000232804; .
GeneID3303; -; .
GeneID3304; -; .
KEGGhsa:3303; -; .
KEGGhsa:3304; -; .
UCSCuc003nxk.2; human; .
CTD3303; -; .
CTD3304; -; .
GeneCardsGC06P031553; -; .
GeneCardsGC06P031797; -; .
H-InvDBHIX0005734; -; .
H-InvDBHIX0057751; -; .
H-InvDBHIX0058169; -; .
HPACAB008640; -; .
HPACAB032815; -; .
MIM140550; gene; .
MIM603012; gene; .
neXtProtNX_P08107; -; .
eggNOGmaNOG16200; -; .
HOGENOMHBG334976; -; .
HOVERGENHBG051845; -; .
InParanoidP08107; -; .
OrthoDBEOG4W6NVK; -; .
PhylomeDBP08107; -; .
Pathway_Interaction_DBfoxm1pathway; FOXM1 transcription factor network; .
ReactomeREACT_21257; Metabolism of RNA; .
NextBio13107; -; .
BgeeP08107; -; .
CleanExHS_HSPA1A; -; .
GenevestigatorP08107; -; .
GermOnlineENSG00000204388; Homo sapiens; .
GermOnlineENSG00000204389; Homo sapiens; .
GOGO:0005829; C:cytosol; TAS:Reactome; .
GOGO:0005783; C:endoplasmic reticulum; TAS:UniProtKB; .
GOGO:0016234; C:inclusion body; IDA:BHF-UCL; .
GOGO:0005739; C:mitochondrion; TAS:UniProtKB; .
GOGO:0016607; C:nuclear speck; IDA:UniProtKB; .
GOGO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB; .
GOGO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB; .
GOGO:0005524; F:ATP binding; IEA:UniProtKB-KW; .
GOGO:0044183; F:protein binding involved in protein folding; IDA:BHF-UCL; .
GOGO:0047485; F:protein N-terminus binding; IPI:UniProtKB; .
GOGO:0004872; F:receptor activity; IEA:UniProtKB-KW; .
GOGO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL; .
GOGO:0051082; F:unfolded protein binding; TAS:UniProtKB; .
GOGO:0006916; P:anti-apoptosis; TAS:UniProtKB; .
GOGO:0006402; P:mRNA catabolic process; IDA:UniProtKB; .
GOGO:0030308; P:negative regulation of cell growth; IMP:UniProtKB; .
GOGO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB; .
GOGO:0090084; P:negative regulation of inclusion body assembly; IDA:BHF-UCL; .
GOGO:0042026; P:protein refolding; IDA:BHF-UCL; .
GOGO:0006986; P:response to unfolded protein; IDA:UniProtKB; .
InterProIPR018181; Heat_shock_70_CS; .
InterProIPR001023; Hsp70; .
InterProIPR013126; Hsp_70; .
PANTHERPTHR19375; Hsp70; 1; .
PfamPF00012; HSP70; 1; .
PROSITEPS00297; HSP70_1; 1; .
PROSITEPS00329; HSP70_2; 1; .
PROSITEPS01036; HSP70_3; 1; .


SWISS-2DPAGE (search AC)

Database constructed and maintained by SIB, using the Make2D-DB II package (ver. 3.10.2) from the World-2DPAGE Constellation of the ExPASy web server