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P56135

- ATPK_MOUSE

UniProt

P56135 - ATPK_MOUSE

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Protein

ATP synthase subunit f, mitochondrial

Gene
Atp5j2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F0 domain. Minor subunit located with subunit a in the membrane.

GO - Molecular functioni

  1. ATPase activity Source: Ensembl

GO - Biological processi

  1. ATP biosynthetic process Source: UniProtKB-KW
  2. proton transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit f, mitochondrial
Gene namesi
Name:Atp5j2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1927558. Atp5j2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei57 – 7620Helical; Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. mitochondrial inner membrane Source: MGI
  3. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  4. mitochondrion Source: MGI
  5. proton-transporting ATP synthase complex, coupling factor F(o) Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

CF(0), Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 8887ATP synthase subunit f, mitochondrialPRO_0000194825Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity
Modified residuei16 – 161N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP56135.
PRIDEiP56135.

PTM databases

PhosphoSiteiP56135.

Expressioni

Gene expression databases

ArrayExpressiP56135.
BgeeiP56135.
GenevestigatoriP56135.

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF0 seems to have nine subunits: a, b, c, d, e, f, g, F6 and 8 (or A6L). Component of an ATP synthase complex composed of ATP5F1, ATP5G1, ATP5E, ATP5H, ATP5I, ATP5J, ATP5J2, MT-ATP6, MT-ATP8, ATP5A1, ATP5B, ATP5D, ATP5C1, ATP5O, ATP5L, USMG5 and MP68 By similarity.

Protein-protein interaction databases

BioGridi208283. 1 interaction.
IntActiP56135. 2 interactions.
MINTiMINT-1843047.

Structurei

3D structure databases

ProteinModelPortaliP56135.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase F chain family.

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG292892.
GeneTreeiENSGT00510000046986.
HOGENOMiHOG000034215.
HOVERGENiHBG002418.
InParanoidiP56135.
KOiK02130.
OMAiYLWEYDH.
OrthoDBiEOG73JKZ1.
PhylomeDBiP56135.
TreeFamiTF342865.

Family and domain databases

InterProiIPR019344. F1F0-ATPsyn_F_prd.
[Graphical view]
PANTHERiPTHR13080. PTHR13080. 1 hit.
PfamiPF10206. WRW. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P56135-1 [UniParc]FASTAAdd to Basket

« Hide

MASLVPLKEK KLMEVKLGEL PSWIMMRDFT PSGIAGAFRR GYDRYYNKYI   50
NVRKGSISGI SMVLAAYVVF SYCISYKELK HERRRKYH 88
Length:88
Mass (Da):10,344
Last modified:January 23, 2007 - v3
Checksum:i89526C72EC436E48
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB030192 mRNA. Translation: BAA92756.1.
AK002519 mRNA. Translation: BAB22157.1.
AK003235 mRNA. Translation: BAB22660.1.
AK003817 mRNA. Translation: BAB23014.1.
AK013130 mRNA. Translation: BAB28667.1.
AK151737 mRNA. Translation: BAE30651.1.
AK168095 mRNA. Translation: BAE40067.1.
BC029226 mRNA. Translation: AAH29226.1.
CCDSiCCDS39385.1.
RefSeqiNP_065607.1. NM_020582.2.
UniGeneiMm.133551.

Genome annotation databases

EnsembliENSMUST00000161741; ENSMUSP00000125504; ENSMUSG00000038690.
GeneIDi57423.
KEGGimmu:57423.
UCSCiuc009amk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB030192 mRNA. Translation: BAA92756.1 .
AK002519 mRNA. Translation: BAB22157.1 .
AK003235 mRNA. Translation: BAB22660.1 .
AK003817 mRNA. Translation: BAB23014.1 .
AK013130 mRNA. Translation: BAB28667.1 .
AK151737 mRNA. Translation: BAE30651.1 .
AK168095 mRNA. Translation: BAE40067.1 .
BC029226 mRNA. Translation: AAH29226.1 .
CCDSi CCDS39385.1.
RefSeqi NP_065607.1. NM_020582.2.
UniGenei Mm.133551.

3D structure databases

ProteinModelPortali P56135.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 208283. 1 interaction.
IntActi P56135. 2 interactions.
MINTi MINT-1843047.

PTM databases

PhosphoSitei P56135.

Proteomic databases

PaxDbi P56135.
PRIDEi P56135.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000161741 ; ENSMUSP00000125504 ; ENSMUSG00000038690 .
GeneIDi 57423.
KEGGi mmu:57423.
UCSCi uc009amk.1. mouse.

Organism-specific databases

CTDi 9551.
MGIi MGI:1927558. Atp5j2.

Phylogenomic databases

eggNOGi NOG292892.
GeneTreei ENSGT00510000046986.
HOGENOMi HOG000034215.
HOVERGENi HBG002418.
InParanoidi P56135.
KOi K02130.
OMAi YLWEYDH.
OrthoDBi EOG73JKZ1.
PhylomeDBi P56135.
TreeFami TF342865.

Miscellaneous databases

ChiTaRSi ATP5J2. mouse.
NextBioi 313776.
PROi P56135.
SOURCEi Search...

Gene expression databases

ArrayExpressi P56135.
Bgeei P56135.
Genevestigatori P56135.

Family and domain databases

InterProi IPR019344. F1F0-ATPsyn_F_prd.
[Graphical view ]
PANTHERi PTHR13080. PTHR13080. 1 hit.
Pfami PF10206. WRW. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Growth suppression of Escherichia coli by induction of expression of mammalian genes with transmembrane or ATPase domains."
    Inoue S., Sano H., Ohta M.
    Biochem. Biophys. Res. Commun. 268:553-561(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and DBA/2.
    Tissue: Bone marrow, Embryo and Kidney.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary gland.
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 17-39, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiATPK_MOUSE
AccessioniPrimary (citable) accession number: P56135
Secondary accession number(s): Q3THX9, Q9JMF4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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