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Searching in 'World-2DPAGE Repository [0054]' for entry matching: CH60_HUMAN




World-2DPAGE Repository (0054):  CH60_HUMAN


CH60_HUMAN


General information about the entry
View entry in simple text format
Entry nameCH60_HUMAN
Primary accession numberP10809
integrated into World-2DPAGE Repository (0054) on November 28, 2012 (release 1)
2D Annotations were last modified onNovember 28, 2012 (version 1)
General Annotations were last modified on October 23, 2014 (version 2)
Name and origin of the protein
DescriptionRecName: Full=60 kDa heat shock protein, mitochondrial; AltName: Full=60 kDa chaperonin; AltName: Full=Chaperonin 60; Short=CPN60; AltName: Full=Heat shock protein 60; Short=HSP-60; Short=Hsp60; AltName: Full=HuCHA60; AltName: Full=Mitochondrial matrix protein P1; AltName: Full=P60 lymphocyte protein; Flags: Precursor;.
Gene nameName=HSPD1
Synonyms=HSP60
Annotated speciesHomo sapiens (Human) [TaxID: 9606]
TaxonomyEukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
References
[1]   2D GEL CHARACTERIZATION
DOI=10.1074/mcp.M112.022947;
Vernocchi S., Battello N., Schmitz S., Revets D., Billing A.M., Turner J.D., Muller C.P.
''Membrane glucocorticoid receptor activation induces proteomic changes aligning with classical glucocorticoid-effects''
Molecular & Cellular Proteomics 12(7):1764-1779 (2013)
2D PAGE maps for identified proteins
How to interpret a protein

HSAPIENS_CCRF-CEM_3-10 {CCRF-CEM cells stimulated with Cort-BSA (internal standard)}
Homo sapiens (Human)
HSAPIENS_CCRF-CEM_3-10
  map experimental info
 
HSAPIENS_CCRF-CEM_3-10

MAP LOCATIONS:
pI=5.24; Mw=57963  [identification data]

%COV: SPOT 643: 50 [1].
SCORE: SPOT 643: 854 [1].
SEARCH ENGINE: SPOT 643: Mascot [1].
MAPPING (identification):
SPOT 643: Peptide mass fingerprinting [1]; Tandem mass spectrometry [1].

Copyright
Data from Dr. Claude P. Muller, Centre de Recherche Public de la Sante / National Public Health Laboratory, Luxembourg
Cross-references
UniProtKB/Swiss-ProtP10809; CH60_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: 0.0
Entry nameCH60_HUMAN
Primary accession numberP10809
Secondary accession number(s) B2R5M6 B7Z712 Q38L19 Q9UCR6
Sequence was last modified on August 1, 1990 (version 2)
Annotations were last modified on October 1, 2014 (version 181)
Name and origin of the protein
DescriptionRecName: Full=60 kDa heat shock protein, mitochondrial; AltName: Full=60 kDa chaperonin; AltName: Full=Chaperonin 60; Short=CPN60; AltName: Full=Heat shock protein 60; Short=HSP-60; Short=Hsp60; AltName: Full=HuCHA60; AltName: Full=Mitochondrial matrix protein P1; AltName: Full=P60 lymphocyte protein; Flags: Precursor;
Gene nameName=HSPD1
Synonyms=HSP60
Encoded onName=HSPD1; Synonyms=HSP60
KeywordsAcetylation; Alternative splicing; ATP-binding; Chaperone; Complete proteome; Direct protein sequencing; Disease mutation; Hereditary spastic paraplegia; Host-virus interaction; Leukodystrophy; Mitochondrion; Neurodegeneration; Nucleotide-binding; Phosphoprotein; Reference proteome; Transit peptide.
Copyright
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLM22382; AAA60127.1; -; mRNA
EMBLM34664; AAA36022.1; -; mRNA
EMBLAJ250915; CAB75426.1; -; Genomic_DNA
EMBLDQ217936; ABB01006.1; -; Genomic_DNA
EMBLAK301276; BAH13448.1; -; mRNA
EMBLAK312240; BAG35173.1; -; mRNA
EMBLAC010746; -; NOT_ANNOTATED_CDS; Genomic_DNA
EMBLAC020550; -; NOT_ANNOTATED_CDS; Genomic_DNA
EMBLAC114809; -; NOT_ANNOTATED_CDS; Genomic_DNA
EMBLBC002676; AAH02676.1; -; mRNA
EMBLBC003030; AAH03030.1; -; mRNA
EMBLBC067082; AAH67082.1; -; mRNA
EMBLBC073746; AAH73746.1; -; mRNA
CCDSCCDS33357.1; -; .
PIRA32800; A32800; .
RefSeqNP_002147.2; NM_002156.4; .
RefSeqNP_955472.1; NM_199440.1; .
RefSeqXP_005246575.1; XM_005246518.1; .
UniGeneHs.595053; -; .
UniGeneHs.727543; -; .
ProteinModelPortalP10809; -; .
SMRP10809; 27-551; .
BioGrid109561; 127; .
DIPDIP-58N; -; .
IntActP10809; 67; .
MINTMINT-1162735; -; .
STRING9606.ENSP00000340019; -; .
ChEMBLCHEMBL4721; -; .
PhosphoSiteP10809; -; .
DMDM129379; -; .
DOSAC-COBS-2DPAGEP10809; -; .
OGPP10809; -; .
REPRODUCTION-2DPAGEIPI00784154; -; .
REPRODUCTION-2DPAGEP10809; -; .
SWISS-2DPAGEP10809; -; .
UCD-2DPAGEP10809; -; .
MaxQBP10809; -; .
PaxDbP10809; -; .
PRIDEP10809; -; .
DNASU3329; -; .
EnsemblENST00000345042; ENSP00000340019; ENSG00000144381; .
EnsemblENST00000388968; ENSP00000373620; ENSG00000144381; .
EnsemblENST00000544407; ENSP00000441296; ENSG00000144381; .
GeneID3329; -; .
KEGGhsa:3329; -; .
UCSCuc002uui.3; human; .
CTD3329; -; .
GeneCardsGC02M198315; -; .
HGNCHGNC:5261; HSPD1; .
HPACAB002775; -; .
HPAHPA001523; -; .
HPAHPA050025; -; .
MIM118190; gene; .
MIM605280; phenotype; .
MIM612233; phenotype; .
neXtProtNX_P10809; -; .
Orphanet100994; Autosomal dominant spastic paraplegia type 13; .
Orphanet280288; Pelizaeus-Merzbacher-like due to HSPD1 mutation; .
PharmGKBPA29527; -; .
eggNOGCOG0459; -; .
HOGENOMHOG000076290; -; .
HOVERGENHBG001982; -; .
InParanoidP10809; -; .
KOK04077; -; .
OMANYKAANE; -; .
OrthoDBEOG7HTHGJ; -; .
PhylomeDBP10809; -; .
TreeFamTF300475; -; .
ReactomeREACT_118595; Mitochondrial protein import; .
ChiTaRSHSPD1; human; .
GeneWikiGroEL; -; .
GenomeRNAi3329; -; .
NextBio13188; -; .
PROPR:P10809; -; .
ArrayExpressP10809; -; .
BgeeP10809; -; .
CleanExHS_HSPD1; -; .
GenevestigatorP10809; -; .
GOGO:0009986; C:cell surface; IDA:UniProtKB; .
GOGO:0005905; C:coated pit; IDA:BHF-UCL; .
GOGO:0030135; C:coated vesicle; IDA:BHF-UCL; .
GOGO:0005737; C:cytoplasm; IDA:UniProtKB; .
GOGO:0005829; C:cytosol; IDA:UniProtKB; .
GOGO:0005769; C:early endosome; IDA:BHF-UCL; .
GOGO:0005615; C:extracellular space; IDA:BHF-UCL; .
GOGO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB; .
GOGO:0046696; C:lipopolysaccharide receptor complex; IDA:BHF-UCL; .
GOGO:0016020; C:membrane; IDA:UniProtKB; .
GOGO:0005743; C:mitochondrial inner membrane; ISS:BHF-UCL; .
GOGO:0005759; C:mitochondrial matrix; TAS:BHF-UCL; .
GOGO:0005739; C:mitochondrion; IDA:UniProtKB; .
GOGO:0005886; C:plasma membrane; IEA:Ensembl; .
GOGO:0043234; C:protein complex; IDA:UniProtKB; .
GOGO:0030141; C:secretory granule; ISS:BHF-UCL; .
GOGO:0005524; F:ATP binding; IEA:UniProtKB-KW; .
GOGO:0016887; F:ATPase activity; ISS:BHF-UCL; .
GOGO:0051087; F:chaperone binding; IPI:UniProtKB; .
GOGO:0003688; F:DNA replication origin binding; ISS:BHF-UCL; .
GOGO:0003725; F:double-stranded RNA binding; IDA:MGI; .
GOGO:0001530; F:lipopolysaccharide binding; IDA:BHF-UCL; .
GOGO:0002039; F:p53 binding; IPI:UniProtKB; .
GOGO:0044822; F:poly(A) RNA binding; IDA:UniProtKB; .
GOGO:0005515; F:protein binding; IPI:UniProtKB; .
GOGO:0003697; F:single-stranded DNA binding; ISS:BHF-UCL; .
GOGO:0051082; F:unfolded protein binding; IC:UniProtKB; .
GOGO:0006458; P:'de novo' protein folding; ISS:BHF-UCL; .
GOGO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:BHF-UCL; .
GOGO:0006200; P:ATP catabolic process; ISS:GOC; .
GOGO:0042113; P:B cell activation; IDA:BHF-UCL; .
GOGO:0002368; P:B cell cytokine production; IDA:BHF-UCL; .
GOGO:0042100; P:B cell proliferation; IDA:BHF-UCL; .
GOGO:0051131; P:chaperone-mediated protein complex assembly; ISS:BHF-UCL; .
GOGO:0048291; P:isotype switching to IgG isotypes; IDA:BHF-UCL; .
GOGO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; IDA:BHF-UCL; .
GOGO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB; .
GOGO:0043065; P:positive regulation of apoptotic process; IMP:BHF-UCL; .
GOGO:0032727; P:positive regulation of interferon-alpha production; IDA:BHF-UCL; .
GOGO:0032729; P:positive regulation of interferon-gamma production; IDA:BHF-UCL; .
GOGO:0032733; P:positive regulation of interleukin-10 production; IDA:BHF-UCL; .
GOGO:0032735; P:positive regulation of interleukin-12 production; IDA:BHF-UCL; .
GOGO:0032755; P:positive regulation of interleukin-6 production; IDA:BHF-UCL; .
GOGO:0043032; P:positive regulation of macrophage activation; IDA:BHF-UCL; .
GOGO:0050870; P:positive regulation of T cell activation; IDA:BHF-UCL; .
GOGO:0002842; P:positive regulation of T cell mediated immune response to tumor cell; IDA:BHF-UCL; .
GOGO:0051604; P:protein maturation; ISS:BHF-UCL; .
GOGO:0042026; P:protein refolding; IDA:UniProtKB; .
GOGO:0050821; P:protein stabilization; IMP:UniProtKB; .
GOGO:0006986; P:response to unfolded protein; IDA:BHF-UCL; .
GOGO:0042110; P:T cell activation; IDA:MGI; .
GOGO:0016032; P:viral process; IEA:UniProtKB-KW; .
Gene3D1.10.560.10; -; 2; .
Gene3D3.50.7.10; -; 1; .
HAMAPMF_00600; CH60; 1; .
InterProIPR018370; Chaperonin_Cpn60_CS; .
InterProIPR001844; Chaprnin_Cpn60; .
InterProIPR002423; Cpn60/TCP-1; .
InterProIPR027409; GroEL-like_apical_dom; .
InterProIPR027413; GROEL-like_equatorial; .
PANTHERPTHR11353; PTHR11353; 1; .
PfamPF00118; Cpn60_TCP1; 1; .
PRINTSPR00298; CHAPERONIN60; .
SUPFAMSSF48592; SSF48592; 2; .
SUPFAMSSF52029; SSF52029; 1; .
TIGRFAMsTIGR02348; GroEL; 1; .
PROSITEPS00296; CHAPERONINS_CPN60; 1; .



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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