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Searching in 'World-2DPAGE Repository [0054]' for entry matching: P25705




World-2DPAGE Repository (0054):  P25705


P25705


General information about the entry
View entry in simple text format
Entry nameATPA_HUMAN
Primary accession numberP25705
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=ATP synthase subunit alpha, mitochondrial; Flags: Precursor;.
Gene nameName=ATP5A1
Synonyms=ATP5A, ATP5AL2, ATPM
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=8.28; Mw=55209  [identification data]

%COV: SPOT 711: 56 [1].
SCORE: SPOT 711: 858 [1].
SEARCH ENGINE: SPOT 711: Mascot [1].
MAPPING (identification):
SPOT 711: 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-ProtP25705; ATPA_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 nameATPA_HUMAN
Primary accession numberP25705
Secondary accession number(s) A8K092 B4DY56 K7ENP3 Q53XX6 Q8IXV2 Q96FB4 Q96HW2 Q96IR6 Q9BTV8
Sequence was last modified on May 1, 1992 (version 1)
Annotations were last modified on October 1, 2014 (version 176)
Name and origin of the protein
DescriptionRecName: Full=ATP synthase subunit alpha, mitochondrial; Flags: Precursor;
Gene nameName=ATP5A1
Synonyms=ATP5A, ATP5AL2, ATPM
Encoded onName=ATP5A1; Synonyms=ATP5A, ATP5AL2, ATPM
KeywordsAcetylation; Alternative splicing; ATP synthesis; ATP-binding; Cell membrane; CF(1); Complete proteome; Direct protein sequencing; Disease mutation; Glycoprotein; Hydrogen ion transport; Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Pyrrolidone carboxylic acid; Reference proteome; Transit peptide; Transport.
Copyright
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLX59066; CAA41789.1; -; mRNA
EMBLX65460; CAA46452.1; -; mRNA
EMBLD14710; BAA03531.1; -; mRNA
EMBLD28126; BAA05672.1; -; Genomic_DNA
EMBLBT007209; AAP35873.1; -; mRNA
EMBLAK092735; BAG52604.1; -; mRNA
EMBLAK289457; BAF82146.1; -; mRNA
EMBLAK302272; BAG63618.1; -; mRNA
EMBLAC012569; -; NOT_ANNOTATED_CDS; Genomic_DNA
EMBLBC003119; AAH03119.1; -; mRNA
EMBLBC007299; AAH07299.1; -; mRNA
EMBLBC008028; AAH08028.2; -; mRNA
EMBLBC011384; AAH11384.1; -; mRNA
EMBLBC016046; AAH16046.1; -; mRNA
EMBLBC019310; AAH19310.1; -; mRNA
EMBLBC039135; AAH39135.2; -; mRNA
EMBLBC064562; AAH64562.1; -; mRNA
EMBLBC067385; AAH67385.1; -; mRNA
CCDSCCDS11927.1; -. [P25705-1]; .
CCDSCCDS58620.1; -. [P25705-2]; .
CCDSCCDS59315.1; -. [P25705-3]; .
PIRS17193; PWHUA; .
RefSeqNP_001001935.1; NM_001001935.2. [P25705-2]; .
RefSeqNP_001001937.1; NM_001001937.1. [P25705-1]; .
RefSeqNP_001244263.1; NM_001257334.1. [P25705-3]; .
RefSeqNP_001244264.1; NM_001257335.1. [P25705-2]; .
RefSeqNP_004037.1; NM_004046.5. [P25705-1]; .
UniGeneHs.298280; -; .
ProteinModelPortalP25705; -; .
SMRP25705; 56-553; .
BioGrid106987; 76; .
DIPDIP-32871N; -; .
IntActP25705; 34; .
MINTMINT-1163289; -; .
STRING9606.ENSP00000282050; -; .
ChEMBLCHEMBL2062351; -; .
PhosphoSiteP25705; -; .
DMDM114517; -; .
OGPP25705; -; .
REPRODUCTION-2DPAGEP25705; -; .
UCD-2DPAGEP25705; -; .
MaxQBP25705; -; .
PaxDbP25705; -; .
PRIDEP25705; -; .
DNASU498; -; .
EnsemblENST00000282050; ENSP00000282050; ENSG00000152234. [P25705-1]; .
EnsemblENST00000398752; ENSP00000381736; ENSG00000152234. [P25705-1]; .
EnsemblENST00000590665; ENSP00000467037; ENSG00000152234. [P25705-3]; .
EnsemblENST00000593152; ENSP00000465477; ENSG00000152234. [P25705-2]; .
GeneID498; -; .
KEGGhsa:498; -; .
UCSCuc002lbr.2; human. [P25705-1]; .
CTD498; -; .
GeneCardsGC18M043664; -; .
HGNCHGNC:823; ATP5A1; .
HPACAB013067; -; .
MIM164360; gene; .
MIM615228; phenotype; .
neXtProtNX_P25705; -; .
Orphanet254913; Isolated ATP synthase deficiency; .
PharmGKBPA25115; -; .
eggNOGCOG0056; -; .
HOVERGENHBG001536; -; .
InParanoidP25705; -; .
KOK02132; -; .
OMAKEPMLTG; -; .
OrthoDBEOG773XFP; -; .
PhylomeDBP25705; -; .
TreeFamTF300321; -; .
ReactomeREACT_118595; Mitochondrial protein import; .
ReactomeREACT_6759; Formation of ATP by chemiosmotic coupling; .
ChiTaRSATP5A1; human; .
GenomeRNAi498; -; .
NextBio2089; -; .
PMAP-CutDBP25705; -; .
PROPR:P25705; -; .
ArrayExpressP25705; -; .
BgeeP25705; -; .
CleanExHS_ATP5A1; -; .
GenevestigatorP25705; -; .
GOGO:0070062; C:extracellular vesicular exosome; IDA:UniProt; .
GOGO:0016020; C:membrane; IDA:UniProtKB; .
GOGO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB; .
GOGO:0005759; C:mitochondrial matrix; TAS:Reactome; .
GOGO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB; .
GOGO:0005739; C:mitochondrion; NAS:UniProtKB; .
GOGO:0005886; C:plasma membrane; IDA:UniProtKB; .
GOGO:0045261; C:proton-transporting ATP synthase complex; catalytic core F(1); IEA:UniProtKB-KW
GOGO:0005524; F:ATP binding; ISS:UniProtKB; .
GOGO:0042288; F:MHC class I protein binding; IDA:UniProtKB; .
GOGO:0044822; F:poly(A) RNA binding; IDA:UniProtKB; .
GOGO:0005515; F:protein binding; IPI:UniProtKB; .
GOGO:0046933; F:proton-transporting ATP synthase activity; rotational mechanism; ISS:UniProtKB
GOGO:0046961; F:proton-transporting ATPase activity; rotational mechanism; IEA:InterPro
GOGO:0022857; F:transmembrane transporter activity; IC:UniProtKB; .
GOGO:0006754; P:ATP biosynthetic process; NAS:UniProtKB; .
GOGO:0006200; P:ATP catabolic process; IDA:GOC; .
GOGO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro; .
GOGO:0044237; P:cellular metabolic process; TAS:Reactome; .
GOGO:0009790; P:embryo development; ISS:UniProtKB; .
GOGO:0006629; P:lipid metabolic process; ISS:UniProtKB; .
GOGO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IC:UniProtKB; .
GOGO:0001937; P:negative regulation of endothelial cell proliferation; IMP:UniProtKB; .
GOGO:0022904; P:respiratory electron transport chain; TAS:Reactome; .
GOGO:0044281; P:small molecule metabolic process; TAS:Reactome; .
Gene3D2.40.30.20; -; 1; .
Gene3D3.40.50.300; -; 1; .
HAMAPMF_01346; ATP_synth_alpha_bact; 1; .
InterProIPR020003; ATPase_a/bsu_AS; .
InterProIPR023366; ATPase_asu-like; .
InterProIPR005294; ATPase_F1-cplx_asu; .
InterProIPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C; .
InterProIPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd; .
InterProIPR004100; ATPase_F1_a/bsu_N; .
InterProIPR027417; P-loop_NTPase; .
PfamPF00006; ATP-synt_ab; 1; .
PfamPF00306; ATP-synt_ab_C; 1; .
PfamPF02874; ATP-synt_ab_N; 1; .
SUPFAMSSF47917; SSF47917; 1; .
SUPFAMSSF50615; SSF50615; 1; .
SUPFAMSSF52540; SSF52540; 1; .
TIGRFAMsTIGR00962; atpA; 1; .
PROSITEPS00152; ATPASE_ALPHA_BETA; 1; .



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World-2DPAGE Repository (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