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USC-OGP 2-DE database

Two-dimensional polyacrylamide gel electrophoresis database


USC-OGP 2-DE database 
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Searching in 'USC-OGP 2-DE database' for entry matching: ATPB_HUMAN




USC-OGP 2-DE database:  ATPB_HUMAN


ATPB_HUMAN


General information about the entry
View entry in simple text format
Entry nameATPB_HUMAN
Primary accession numberP06576
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=ATP synthase subunit beta, mitochondrial; EC=3.6.3.14; Flags: Precursor;.
Gene nameName=ATP5B
Synonyms=ATPMB, ATPSB
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=5.00; Mw=49250



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

MAP LOCATIONS:
pI=5.02; Mw=50928

Cross-references
UniProtKB/Swiss-ProtP06576; ATPB_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 nameATPB_HUMAN
Primary accession numberP06576
Secondary accession number(s) A8K4X0 Q14283
Sequence was last modified on April 1, 1990 (version 3)
Annotations were last modified on March 15, 2017 (version 205)
Name and origin of the protein
DescriptionRecName: Full=ATP synthase subunit beta, mitochondrial; EC=3.6.3.14; Flags: Precursor;
Gene nameName=ATP5B
Synonyms=ATPMB, ATPSB
Encoded onName=ATP5B; Synonyms=ATPMB, ATPSB
KeywordsAcetylation; ATP synthesis; ATP-binding; CF(1); Complete proteome; Direct protein sequencing; Glycoprotein; Hydrogen ion transport; Hydrolase; Ion transport; Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Transit peptide; Transport.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLM27132; AAA51809.1; -; Genomic_DNA
EMBLM19483; AAA51808.1; -; Genomic_DNA
EMBLM19482; AAA51808.1; JOINED; Genomic_DNA
EMBLX03559; CAA27246.1; -; mRNA
EMBLD00022; BAA00016.1; -; mRNA
EMBLAK291085; BAF83774.1; -; mRNA
EMBLCH471054; EAW96952.1; -; Genomic_DNA
EMBLBC016512; AAH16512.1; -; mRNA
EMBLX05606; CAA29095.1; -; mRNA
CCDSCCDS8924.1; -; .
PIRA33370; A33370; .
RefSeqNP_001677.2; NM_001686.3; .
UniGeneHs.406510; -; .
ProteinModelPortalP06576; -; .
SMRP06576; -; .
BioGrid106994; 174; .
IntActP06576; 62; .
MINTMINT-5004016; -; .
STRING9606.ENSP00000262030; -; .
ChEMBLCHEMBL2062350; -; .
DrugBankDB07384; 1-ACETYL-2-CARBOXYPIPERIDINE; .
DrugBankDB07394; AUROVERTIN B; .
DrugBankDB08399; PICEATANNOL; .
DrugBankDB04216; Quercetin; .
iPTMnetP06576; -; .
PhosphoSitePlusP06576; -; .
SwissPalmP06576; -; .
BioMutaATP5B; -; .
DMDM114549; -; .
DOSAC-COBS-2DPAGEP06576; -; .
OGPP06576; -; .
REPRODUCTION-2DPAGEIPI00303476; -; .
REPRODUCTION-2DPAGEP06576; -; .
SWISS-2DPAGEP06576; -; .
UCD-2DPAGEP06576; -; .
EPDP06576; -; .
PaxDbP06576; -; .
PeptideAtlasP06576; -; .
PRIDEP06576; -; .
TopDownProteomicsP06576; -; .
DNASU506; -; .
EnsemblENST00000262030; ENSP00000262030; ENSG00000110955; .
GeneID506; -; .
KEGGhsa:506; -; .
CTD506; -; .
DisGeNET506; -; .
GeneCardsATP5B; -; .
HGNCHGNC:830; ATP5B; .
HPACAB017527; -; .
HPAHPA001520; -; .
HPAHPA001528; -; .
MIM102910; gene; .
neXtProtNX_P06576; -; .
OpenTargetsENSG00000110955; -; .
PharmGKBPA25122; -; .
eggNOGKOG1350; Eukaryota; .
eggNOGCOG0055; LUCA; .
GeneTreeENSGT00550000074800; -; .
HOGENOMHOG000009605; -; .
HOVERGENHBG004307; -; .
InParanoidP06576; -; .
KOK02133; -; .
OMAAEFGIYP; -; .
OrthoDBEOG091G0KVV; -; .
PhylomeDBP06576; -; .
TreeFamTF105640; -; .
ReactomeR-HSA-1268020; Mitochondrial protein import; .
ReactomeR-HSA-163210; Formation of ATP by chemiosmotic coupling; .
ReactomeR-HSA-2151201; Transcriptional activation of mitochondrial biogenesis; .
ChiTaRSATP5B; human; .
GeneWikiATP5B; -; .
GenomeRNAi506; -; .
PROPR:P06576; -; .
ProteomesUP000005640; Chromosome 12; .
BgeeENSG00000110955; -; .
CleanExHS_ATP5B; -; .
ExpressionAtlasP06576; baseline and differential; .
GenevisibleP06576; HS; .
GOGO:0009986; C:cell surface; IDA:UniProtKB; .
GOGO:0070062; C:extracellular exosome; IDA:UniProtKB; .
GOGO:0031012; C:extracellular matrix; IDA:BHF-UCL; .
GOGO:0016020; C:membrane; IDA:UniProtKB; .
GOGO:0005759; C:mitochondrial matrix; NAS:UniProtKB; .
GOGO:0031966; C:mitochondrial membrane; IDA:UniProtKB; .
GOGO:0042645; C:mitochondrial nucleoid; IDA:BHF-UCL; .
GOGO:0005753; C:mitochondrial proton-transporting ATP synthase complex; IDA:UniProtKB; .
GOGO:0005754; C:mitochondrial proton-transporting ATP synthase; catalytic core; NAS:UniProtKB
GOGO:0005739; C:mitochondrion; IDA:UniProtKB; .
GOGO:0043209; C:myelin sheath; IEA:Ensembl; .
GOGO:0005634; C:nucleus; IDA:UniProtKB; .
GOGO:0005886; C:plasma membrane; IDA:UniProtKB; .
GOGO:0005524; F:ATP binding; IEA:UniProtKB-KW; .
GOGO:0042288; F:MHC class I protein binding; IDA:UniProtKB; .
GOGO:0046933; F:proton-transporting ATP synthase activity; rotational mechanism; IEA:InterPro
GOGO:0046961; F:proton-transporting ATPase activity; rotational mechanism; IMP:UniProtKB
GOGO:0022857; F:transmembrane transporter activity; IC:UniProtKB; .
GOGO:0005215; F:transporter activity; NAS:UniProtKB; .
GOGO:0001525; P:angiogenesis; IMP:UniProtKB; .
GOGO:0006754; P:ATP biosynthetic process; IMP:UniProtKB; .
GOGO:0006091; P:generation of precursor metabolites and energy; NAS:UniProtKB; .
GOGO:0006629; P:lipid metabolic process; IEA:Ensembl; .
GOGO:0042776; P:mitochondrial ATP synthesis coupled proton transport; IC:UniProtKB; .
GOGO:0007005; P:mitochondrion organization; TAS:Reactome; .
GOGO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; IEA:Ensembl; .
GOGO:0001649; P:osteoblast differentiation; IDA:UniProtKB; .
GOGO:0015992; P:proton transport; IMP:UniProtKB; .
GOGO:0051453; P:regulation of intracellular pH; IMP:UniProtKB; .
Gene3D1.10.1140.10; -; 1; .
Gene3D3.40.50.300; -; 1; .
HAMAPMF_01347; ATP_synth_beta_bact; 1; .
InterProIPR003593; AAA+_ATPase; .
InterProIPR005722; ATP_synth_F1_bsu; .
InterProIPR020003; ATPase_a/bsu_AS; .
InterProIPR004100; ATPase_F1/V1/A1_a/bsu_N; .
InterProIPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd; .
InterProIPR024034; ATPase_F1/V1_bsu_C; .
InterProIPR027417; P-loop_NTPase; .
PfamPF00006; ATP-synt_ab; 1; .
PfamPF02874; ATP-synt_ab_N; 1; .
SMARTSM00382; AAA; 1; .
SUPFAMSSF50615; SSF50615; 1; .
SUPFAMSSF52540; SSF52540; 1; .
TIGRFAMsTIGR01039; atpD; 1; .
PROSITEPS00152; ATPASE_ALPHA_BETA; 1; .



USC-OGP 2-DE database image


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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

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