Home

USC-OGP 2-DE database

Two-dimensional polyacrylamide gel electrophoresis database


USC-OGP 2-DE database 
Search by   *
 
 
 
 
 
 
Maps   
 
 


     Select Remote Interfaces
[All Interfaces]
SWISS-2DPAGE
World-2DPAGE Portal
World-2DPAGE Repository

Exclude local DBs
has only effect if a remote
interface is selected
     
Searching in 'USC-OGP 2-DE database' for entry matching: CH60_HUMAN




USC-OGP 2-DE database:  CH60_HUMAN


CH60_HUMAN


General information about the entry
View entry in simple text format
Entry nameCH60_HUMAN
Primary accession numberP10809
integrated into USC-OGP 2-DE database on January 17, 2017 (release 1)
2D Annotations were last modified onJanuary 17, 2017 (version 1)
General Annotations were last modified on April 5, 2017 (version 2)
Name and origin of the protein
DescriptionRecName: Full=60 kDa heat shock protein, mitochondrial; EC=3.6.4.9; 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
Author 1., Author 2.
Submitted (Mar-2011) to Current
2D PAGE maps for identified proteins
How to interpret a protein

PLATELET_4-7 {PLATELET 4-7}
Homo sapiens (Human)
PLATELET_4-7
  map experimental info
 
PLATELET_4-7

MAP LOCATIONS:
pI=5.12; Mw=61844
pI=5.18; Mw=61464



PLATELET_5-6 {PLATELET 5-6}
Homo sapiens (Human)
PLATELET_5-6
  map experimental info
 
PLATELET_5-6

MAP LOCATIONS:
pI=5.20; Mw=61980
pI=5.13; Mw=61618
pI=5.17; Mw=60901
pI=5.14; Mw=59143



UVEAL_MELANOMA_3-10 {UVEAL MELANOMA 3-10}
Homo sapiens (Human)
UVEAL_MELANOMA_3-10
  map experimental info
 
UVEAL_MELANOMA_3-10

MAP LOCATIONS:
pI=5.33; Mw=66847
pI=5.37; Mw=64830

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 March 15, 2017 (version 209)
Name and origin of the protein
DescriptionRecName: Full=60 kDa heat shock protein, mitochondrial; EC=3.6.4.9; 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
Keywords3D-structure; Acetylation; Alternative splicing; ATP-binding; Chaperone; Complete proteome; Direct protein sequencing; Disease mutation; Hereditary spastic paraplegia; Host-virus interaction; Hydrolase; Leukodystrophy; Mitochondrion; Neurodegeneration; Nucleotide-binding; Phosphoprotein; Reference proteome; Transit peptide.
Copyright
Copyrighted by the UniProt Consortium, see http://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; -. [P10809-1]; .
PIRA32800; A32800; .
RefSeqNP_002147.2; NM_002156.4. [P10809-1]; .
RefSeqNP_955472.1; NM_199440.1. [P10809-1]; .
UniGeneHs.595053; -; .
UniGeneHs.727543; -; .
PDB4PJ1; X-ray; 3.15 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=27-556
PDBsum4PJ1; -; .
ProteinModelPortalP10809; -; .
SMRP10809; -; .
BioGrid109561; 277; .
DIPDIP-58N; -; .
IntActP10809; 117; .
MINTMINT-1162735; -; .
STRING9606.ENSP00000340019; -; .
ChEMBLCHEMBL4721; -; .
iPTMnetP10809; -; .
PhosphoSitePlusP10809; -; .
SwissPalmP10809; -; .
BioMutaHSPD1; -; .
DMDM129379; -; .
DOSAC-COBS-2DPAGEP10809; -; .
OGPP10809; -; .
REPRODUCTION-2DPAGEIPI00784154; -; .
REPRODUCTION-2DPAGEP10809; -; .
SWISS-2DPAGEP10809; -; .
UCD-2DPAGEP10809; -; .
EPDP10809; -; .
MaxQBP10809; -; .
PaxDbP10809; -; .
PeptideAtlasP10809; -; .
PRIDEP10809; -; .
TopDownProteomicsP10809-1; -. [P10809-1]; .
DNASU3329; -; .
EnsemblENST00000345042; ENSP00000340019; ENSG00000144381. [P10809-1]; .
EnsemblENST00000388968; ENSP00000373620; ENSG00000144381. [P10809-1]; .
GeneID3329; -; .
KEGGhsa:3329; -; .
UCSCuc002uui.4; human. [P10809-1]; .
CTD3329; -; .
DisGeNET3329; -; .
GeneCardsHSPD1; -; .
HGNCHGNC:5261; HSPD1; .
HPACAB002775; -; .
HPACAB072816; -; .
HPAHPA001523; -; .
HPAHPA050025; -; .
MalaCardsHSPD1; -; .
MIM118190; gene; .
MIM605280; phenotype; .
MIM612233; phenotype; .
neXtProtNX_P10809; -; .
OpenTargetsENSG00000144381; -; .
Orphanet100994; Autosomal dominant spastic paraplegia type 13; .
Orphanet280288; Pelizaeus-Merzbacher-like disease due to HSPD1 mutation; .
PharmGKBPA29527; -; .
eggNOGKOG0356; Eukaryota; .
eggNOGCOG0459; LUCA; .
GeneTreeENSGT00390000005727; -; .
HOGENOMHOG000076290; -; .
HOVERGENHBG001982; -; .
InParanoidP10809; -; .
KOK04077; -; .
OMAKDPAMGG; -; .
OrthoDBEOG091G04JM; -; .
PhylomeDBP10809; -; .
TreeFamTF300475; -; .
ReactomeR-HSA-1268020; Mitochondrial protein import; .
ReactomeR-HSA-8869496; TFAP2A acts as a transcriptional repressor during retinoic acid induced cell differentiation; .
ChiTaRSHSPD1; human; .
GeneWikiGroEL; -; .
GenomeRNAi3329; -; .
PROPR:P10809; -; .
ProteomesUP000005640; Chromosome 2; .
BgeeENSG00000144381; -; .
CleanExHS_HSPD1; -; .
ExpressionAtlasP10809; baseline and differential; .
GenevisibleP10809; HS; .
GOGO:0009986; C:cell surface; IDA:UniProtKB; .
GOGO:0005905; C:clathrin-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:0070062; C:extracellular exosome; IDA:UniProtKB; .
GOGO:0031012; C:extracellular matrix; IDA:BHF-UCL; .
GOGO:0005615; C:extracellular space; IDA:BHF-UCL; .
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:0043209; C:myelin sheath; IEA:Ensembl; .
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:0044183; F:protein binding involved in protein folding; IBA:GO_Central; .
GOGO:0003723; F:RNA binding; IDA:UniProtKB; .
GOGO:0003697; F:single-stranded DNA binding; ISS:BHF-UCL; .
GOGO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-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:0008637; P:apoptotic mitochondrial changes; IBA:GO_Central; .
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:0061077; P:chaperone-mediated protein folding; IBA:GO_Central; .
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:0045041; P:protein import into mitochondrial intermembrane space; IBA:GO_Central; .
GOGO:0051604; P:protein maturation; ISS:BHF-UCL; .
GOGO:0042026; P:protein refolding; IDA:UniProtKB; .
GOGO:0050821; P:protein stabilization; IMP:UniProtKB; .
GOGO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:Reactome; .
GOGO:0009409; P:response to cold; ISS:AgBase; .
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; .
PfamPF00118; Cpn60_TCP1; 1; .
PRINTSPR00298; CHAPERONIN60; .
SUPFAMSSF52029; SSF52029; 1; .
TIGRFAMsTIGR02348; GroEL; 1; .
PROSITEPS00296; CHAPERONINS_CPN60; 1; .



USC-OGP 2-DE database image


Gateways to other related servers


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

[Home]