GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

RAT:ATPB

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Rattus norvegicus (Rat). (10116)
Gene Name(s) Atp5b
Protein Name(s) ATP synthase subunit beta, mitochondrial
External Links
UniProt P10719
EMBL BC099743
M25301
M19044
M57634
PIR A28701
A30160
RefSeq NP_599191.1
UniGene Rn.92965
PDB 1MAB
2F43
PDBsum 1MAB
2F43
ProteinModelPortal P10719
SMR P10719
BioGrid 251212
IntAct P10719
MINT MINT-4587159
ChEMBL CHEMBL2176796
PhosphoSite P10719
UCD-2DPAGE P10719
World-2DPAGE 0004:P10719
PaxDb P10719
PRIDE P10719
GeneID 171374
KEGG rno:171374
UCSC RGD:621368
CTD 506
RGD 621368
eggNOG COG0055
HOGENOM HOG000009605
HOVERGEN HBG004307
InParanoid P10719
KO K02133
PhylomeDB P10719
EvolutionaryTrace P10719
NextBio 622183
PRO PR:P10719
Proteomes UP000002494
Genevestigator P10719
GO GO:0005743
GO:0005753
GO:0000275
GO:0005739
GO:0045261
GO:0005524
GO:0016887
GO:0005509
GO:0030228
GO:0046933
GO:0006172
GO:0006200
GO:0015991
GO:0046034
GO:0015986
GO:0006898
Gene3D 1.10.1140.10
3.40.50.300
HAMAP MF_01347
InterPro IPR003593
IPR020003
IPR005722
IPR000793
IPR000194
IPR004100
IPR024034
IPR027417
Pfam PF00006
PF00306
PF02874
SMART SM00382
SUPFAM SSF47917
SSF50615
SSF52540
TIGRFAMs TIGR01039
PROSITE PS00152

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:0045121

membrane raft

PMID:14499952[1]

ECO:0000314

direct assay evidence used in manual assertion

C

part_of:(CL:0002608)

Seeded From UniProt

complete

part_of

GO:0005753

mitochondrial proton-transporting ATP synthase complex

PMID:17575325[2]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:1905242

response to 3,3',5-triiodo-L-thyronine

PMID:21563808[3]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1904643

response to curcumin

PMID:26978516[4]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1901653

cellular response to peptide

PMID:14673795[5]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0046034

ATP metabolic process

PMID:10887193[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0045261

proton-transporting ATP synthase complex, catalytic core F(1)

PMID:2894844[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0045261

proton-transporting ATP synthase complex, catalytic core F(1)

PMID:1834656[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0043531

ADP binding

PMID:2902092[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0030228

lipoprotein particle receptor activity

PMID:12511957[10]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016887

ATPase activity

PMID:12511957[10]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

contributes_to

GO:0016887

ATPase activity

PMID:2894844[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0010042

response to manganese ion

PMID:15589972[11]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0009986

cell surface

PMID:19106112[12]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0009631

cold acclimation

PMID:9163327[13]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006898

receptor-mediated endocytosis

PMID:12511957[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005743

mitochondrial inner membrane

PMID:8764999[14]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005743

mitochondrial inner membrane

PMID:2894844[7]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005743

mitochondrial inner membrane

PMID:12511957[10]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

PMID:1834656[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:2902092[9]

ECO:0000353

physical interaction evidence used in manual assertion

CHEBI:50104

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:2143765[15]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:12511957[10]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0005509

calcium ion binding

PMID:8764999[14]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0001889

liver development

PMID:8420961[16]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0000275

mitochondrial proton-transporting ATP synthase complex, catalytic core F(1)

PMID:10887193[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0099132

ATP hydrolysis coupled cation transmembrane transport

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0046933

P

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000194
InterPro:IPR020003

F

Seeded From UniProt

complete

involved_in

GO:0015986

ATP synthesis coupled proton transport

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005722

P

Seeded From UniProt

complete

part_of

GO:0045261

proton-transporting ATP synthase complex, catalytic core F(1)

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005722

C

Seeded From UniProt

complete

involved_in

GO:0046034

ATP metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004100
InterPro:IPR036121

P

Seeded From UniProt

complete

enables

GO:0046933

proton-transporting ATP synthase activity, rotational mechanism

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005722

F

Seeded From UniProt

complete

involved_in

GO:1902600

proton transmembrane transport

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004100
InterPro:IPR036121

P

Seeded From UniProt

complete

part_of

GO:0045261

proton-transporting ATP synthase complex, catalytic core F(1)

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0139

C

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

involved_in

GO:0006754

ATP biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0066

P

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0496

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0472

C

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

part_of

GO:0005743

mitochondrial inner membrane

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0999
UniProtKB-SubCell:SL-0168

C

Seeded From UniProt

complete

involved_in

GO:0006811

ion transport

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0406

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Ledesma, MD et al. (2003) Proteomic characterisation of neuronal sphingolipid-cholesterol microdomains: role in plasminogen activation. Brain Res. 987 107-16 PubMed GONUTS page
  2. Meyer, B et al. (2007) Identification of two proteins associated with mammalian ATP synthase. Mol. Cell Proteomics 6 1690-9 PubMed GONUTS page
  3. Severino, V et al. (2011) Proteomic characterization of early changes induced by triiodothyronine in rat liver. J. Proteome Res. 10 3212-24 PubMed GONUTS page
  4. Qiu, P et al. (2016) Overdose Intake of Curcumin Initiates the Unbalanced State of Bodies. J. Agric. Food Chem. 64 2765-71 PubMed GONUTS page
  5. Yu, JH et al. (2003) Proteome analysis of rat pancreatic acinar cells: implication for cerulein-induced acute pancreatitis. Proteomics 3 2446-53 PubMed GONUTS page
  6. 6.0 6.1 Ko, YH et al. (2000) Mitochondrial F(0)F(1) ATP synthase. Subunit regions on the F1 motor shielded by F(0), Functional significance, and evidence for an involvement of the unique F(0) subunit F(6). J. Biol. Chem. 275 32931-9 PubMed GONUTS page
  7. 7.0 7.1 7.2 Pedersen, PL et al. (1987) Mitochondrial ATP synthase: dramatic Mg2+-induced alterations in the structure and function of the F1-ATPase moiety. Biochemistry 26 8631-7 PubMed GONUTS page
  8. 8.0 8.1 Bianchet, M et al. (1991) Mitochondrial ATP synthase. Quaternary structure of the F1 moiety at 3.6 A determined by x-ray diffraction analysis. J. Biol. Chem. 266 21197-201 PubMed GONUTS page
  9. 9.0 9.1 Garboczi, DN et al. (1988) Mitochondrial ATP synthase. Overexpression in Escherichia coli of a rat liver beta subunit peptide and its interaction with adenine nucleotides. J. Biol. Chem. 263 15694-8 PubMed GONUTS page
  10. 10.0 10.1 10.2 10.3 10.4 Martinez, LO et al. (2003) Ectopic beta-chain of ATP synthase is an apolipoprotein A-I receptor in hepatic HDL endocytosis. Nature 421 75-9 PubMed GONUTS page
  11. Zhang, S et al. (2005) Changes in the brain mitochondrial proteome of male Sprague-Dawley rats treated with manganese chloride. Toxicol. Appl. Pharmacol. 202 13-7 PubMed GONUTS page
  12. Osanai, T et al. (2009) Coupling factor 6 enhances Src-mediated responsiveness to angiotensin II in resistance arterioles and cells. Cardiovasc. Res. 81 780-7 PubMed GONUTS page
  13. Andersson, U et al. (1997) ATP synthase subunit c expression: physiological regulation of the P1 and P2 genes. Biochem. J. 323 ( Pt 2) 379-85 PubMed GONUTS page
  14. 14.0 14.1 Hubbard, MJ & McHugh, NJ (1996) Mitochondrial ATP synthase F1-beta-subunit is a calcium-binding protein. FEBS Lett. 391 323-9 PubMed GONUTS page
  15. Garboczi, DN et al. (1990) Rat liver mitochondrial ATP synthase. Effects of mutations in the glycine-rich region of a beta subunit peptide on its interaction with adenine nucleotides. J. Biol. Chem. 265 14632-7 PubMed GONUTS page
  16. Luis, AM et al. (1993) Translational regulation of mitochondrial differentiation in neonatal rat liver. Specific increase in the translational efficiency of the nuclear-encoded mitochondrial beta-F1-ATPase mRNA. J. Biol. Chem. 268 1868-75 PubMed GONUTS page