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Q03265 - ATPA_MOUSE

UniProt

Q03265 - ATPA_MOUSE

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Protein

ATP synthase subunit alpha, mitochondrial

Gene

Atp5a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 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. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei413 – 4131Required for activityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi212 – 2198ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: MGI
  2. MHC class I protein binding Source: MGI
  3. poly(A) RNA binding Source: MGI
  4. proton-transporting ATPase activity, rotational mechanism Source: InterPro
  5. proton-transporting ATP synthase activity, rotational mechanism Source: MGI

GO - Biological processi

  1. ATP catabolic process Source: MGI
  2. ATP hydrolysis coupled proton transport Source: InterPro
  3. ATP synthesis coupled proton transport Source: InterPro
  4. lipid metabolic process Source: MGI
  5. negative regulation of endothelial cell proliferation Source: MGI
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_245290. Formation of ATP by chemiosmotic coupling.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit alpha, mitochondrial
Gene namesi
Name:Atp5a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:88115. Atp5a1.

Subcellular locationi

Mitochondrion inner membrane By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity; Extracellular side By similarity
Note: Colocalizes with HRG on the cell surface of T-cells.By similarity

GO - Cellular componenti

  1. COP9 signalosome Source: Ensembl
  2. extracellular vesicular exosome Source: MGI
  3. membrane Source: MGI
  4. mitochondrial inner membrane Source: MGI
  5. mitochondrial proton-transporting ATP synthase complex Source: UniProtKB
  6. mitochondrion Source: MGI
  7. myelin sheath Source: UniProtKB
  8. plasma membrane Source: MGI
  9. proton-transporting ATP synthase complex, catalytic core F(1) Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4343MitochondrionBy similarityAdd
BLAST
Chaini44 – 553510ATP synthase subunit alpha, mitochondrialPRO_0000002425Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441Pyrrolidone carboxylic acidBy similarity
Modified residuei76 – 761Phosphoserine1 Publication
Glycosylationi76 – 761O-linked (GlcNAc)By similarity
Modified residuei123 – 1231N6-acetyllysine1 Publication
Modified residuei126 – 1261N6-acetyllysine1 Publication
Modified residuei132 – 1321N6-acetyllysine1 Publication
Modified residuei161 – 1611N6-acetyllysine; alternate1 Publication
Modified residuei161 – 1611N6-succinyllysine; alternate1 Publication
Modified residuei166 – 1661PhosphoserineBy similarity
Modified residuei167 – 1671N6-acetyllysine; alternate1 Publication
Modified residuei167 – 1671N6-succinyllysine; alternate1 Publication
Modified residuei230 – 2301N6-acetyllysine; alternate1 Publication
Modified residuei230 – 2301N6-succinyllysine; alternate1 Publication
Modified residuei239 – 2391N6-acetyllysine; alternate1 Publication
Modified residuei239 – 2391N6-succinyllysine; alternate1 Publication
Modified residuei240 – 2401N6-acetyllysine1 Publication
Modified residuei261 – 2611N6-acetyllysine; alternate1 Publication
Modified residuei261 – 2611N6-succinyllysine; alternate1 Publication
Modified residuei305 – 3051N6-acetyllysine; alternate1 Publication
Modified residuei305 – 3051N6-succinyllysine; alternate1 Publication
Modified residuei427 – 4271N6-acetyllysine; alternate1 Publication
Modified residuei427 – 4271N6-succinyllysine; alternate1 Publication
Modified residuei434 – 4341N6-acetyllysine1 Publication
Modified residuei498 – 4981N6-acetyllysine; alternate2 Publications
Modified residuei498 – 4981N6-succinyllysine; alternate1 Publication
Modified residuei506 – 5061N6-acetyllysine; alternate1 Publication
Modified residuei506 – 5061N6-succinyllysine; alternate1 Publication
Modified residuei531 – 5311N6-acetyllysine; alternate2 Publications
Modified residuei531 – 5311N6-succinyllysine; alternate1 Publication
Modified residuei539 – 5391N6-acetyllysine; alternate2 Publications
Modified residuei539 – 5391N6-succinyllysine; alternate1 Publication
Modified residuei541 – 5411N6-acetyllysine1 Publication

Post-translational modificationi

Acetylation of Lys-132, Lys-230 and Lys-498 is observed in liver mitochondria from fasted mice but not from fed mice.2 Publications
Acetylated on lysine residues. BLOC1S1 is required for acetylation (By similarity).By similarity

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiQ03265.
PaxDbiQ03265.
PRIDEiQ03265.

2D gel databases

REPRODUCTION-2DPAGEIPI00130280.
Q03265.
SWISS-2DPAGEQ03265.
UCD-2DPAGEQ03265.

PTM databases

PhosphoSiteiQ03265.

Expressioni

Gene expression databases

BgeeiQ03265.
ExpressionAtlasiQ03265. baseline and differential.
GenevestigatoriQ03265.

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has three main subunits: a, b and c. Interacts with ATPAF2. Interacts with HRG; the interaction occurs on the surface of T-cells and alters the cell morphology when associated with concanavalin (in vitro). Interacts with PLG (angiostatin peptide); the interaction inhibits most of the angiogenic properties of angiostatin. 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. Interacts with BLOC1S1. Interacts with BCL2L1 isoform BCL-X(L); the interaction mediates the association of BCL2L1 isoform BCL-X(L) with the mitochondrial membrane F1F0 ATP synthase and enhances neurons metabolic efficency (By similarity).By similarity

Protein-protein interaction databases

BioGridi198253. 14 interactions.
IntActiQ03265. 18 interactions.
MINTiMINT-1859704.

Structurei

3D structure databases

ProteinModelPortaliQ03265.
SMRiQ03265. Positions 56-552.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0056.
GeneTreeiENSGT00550000074846.
HOVERGENiHBG001536.
InParanoidiQ03265.
KOiK02132.
OMAiATRNLHS.
OrthoDBiEOG773XFP.
PhylomeDBiQ03265.
TreeFamiTF300321.

Family and domain databases

Gene3Di2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01346. ATP_synth_alpha_bact.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR023366. ATPase_asu-like.
IPR005294. ATPase_F1-cplx_asu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00962. atpA. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q03265-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLSVRVAAAV ARALPRRAGL VSKNALGSSF VGARNLHASN TRLQKTGTAE 
        60         70         80         90        100
MSSILEERIL GADTSVDLEE TGRVLSIGDG IARVHGLRNV QAEEMVEFSS 
       110        120        130        140        150
GLKGMSLNLE PDNVGVVVFG NDKLIKEGDV VKRTGAIVDV PVGEELLGRV 
       160        170        180        190        200
VDALGNAIDG KGPIGSKTRR RVGLKAPGII PRISVREPMQ TGIKAVDSLV 
       210        220        230        240        250
PIGRGQRELI IGDRQTGKTS IAIDTIINQK RFNDGTDEKK KLYCIYVAIG 
       260        270        280        290        300
QKRSTVAQLV KRLTDADAMK YTIVVSATAS DAAPLQYLAP YSGCSMGEYF 
       310        320        330        340        350
RDNGKHALII YDDLSKQAVA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE 
       360        370        380        390        400
RAAKMNDSFG GGSLTALPVI ETQAGDVSAY IPTNVISITD GQIFLETELF 
       410        420        430        440        450
YKGIRPAINV GLSVSRVGSA AQTRAMKQVA GTMKLELAQY REVAAFAQFG 
       460        470        480        490        500
SDLDAATQQL LSRGVRLTEL LKQGQYSPMA IEEQVAVIYA GVRGYLDKLE 
       510        520        530        540        550
PSKITKFENA FLSHVISQHQ SLLGNIRSDG KISEQSDAKL KEIVTNFLAG 

FEP
Length:553
Mass (Da):59,753
Last modified:October 1, 1993 - v1
Checksum:iCF35B4FBA7ED431D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31S → T in BAE37632. (PubMed:16141072)Curated
Sequence conflicti63 – 631D → Y in BAE34114. (PubMed:16141072)Curated
Sequence conflicti119 – 1191F → L in BAE34114. (PubMed:16141072)Curated
Sequence conflicti126 – 1261K → N in BAE34114. (PubMed:16141072)Curated
Sequence conflicti315 – 3151S → Y in BAE34114. (PubMed:16141072)Curated
Sequence conflicti321 – 3211Y → C in BAE40868. (PubMed:16141072)Curated
Sequence conflicti422 – 45635Missing in BAE27439. (PubMed:16141072)CuratedAdd
BLAST
Sequence conflicti486 – 4861A → T in BAE40158. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01062 mRNA. Translation: AAA37271.1.
AK043976 mRNA. Translation: BAC31722.1.
AK076572 mRNA. Translation: BAC36399.1.
AK146797 mRNA. Translation: BAE27439.1.
AK150426 mRNA. Translation: BAE29549.1.
AK150843 mRNA. Translation: BAE29901.1.
AK151004 mRNA. Translation: BAE30027.1.
AK151128 mRNA. Translation: BAE30136.1.
AK151224 mRNA. Translation: BAE30216.1.
AK151920 mRNA. Translation: BAE30798.1.
AK152054 mRNA. Translation: BAE30910.1.
AK152890 mRNA. Translation: BAE31573.1.
AK157529 mRNA. Translation: BAE34114.1.
AK159540 mRNA. Translation: BAE35167.1.
AK159491 mRNA. Translation: BAE35125.1.
AK159758 mRNA. Translation: BAE35349.1.
AK160043 mRNA. Translation: BAE35585.1.
AK164110 mRNA. Translation: BAE37632.1.
AK164193 mRNA. Translation: BAE37675.1.
AK166709 mRNA. Translation: BAE38962.1.
AK166812 mRNA. Translation: BAE39039.1.
AK167159 mRNA. Translation: BAE39300.1.
AK167863 mRNA. Translation: BAE39881.1.
AK168198 mRNA. Translation: BAE40158.1.
AK168617 mRNA. Translation: BAE40482.1.
AK168879 mRNA. Translation: BAE40697.1.
AK168890 mRNA. Translation: BAE40707.1.
AK168932 mRNA. Translation: BAE40744.1.
AK169080 mRNA. Translation: BAE40864.1.
AK169084 mRNA. Translation: BAE40868.1.
AK169105 mRNA. Translation: BAE40887.1.
AK169142 mRNA. Translation: BAE40921.1.
AK169300 mRNA. Translation: BAE41056.1.
AK169308 mRNA. Translation: BAE41063.1.
AK169414 mRNA. Translation: BAE41160.1.
BC014854 mRNA. Translation: AAH14854.1.
CCDSiCCDS29358.1.
PIRiJC1473.
RefSeqiNP_031531.1. NM_007505.2.
UniGeneiMm.276137.

Genome annotation databases

EnsembliENSMUST00000026495; ENSMUSP00000026495; ENSMUSG00000025428.
GeneIDi11946.
KEGGimmu:11946.
UCSCiuc008fru.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01062 mRNA. Translation: AAA37271.1.
AK043976 mRNA. Translation: BAC31722.1.
AK076572 mRNA. Translation: BAC36399.1.
AK146797 mRNA. Translation: BAE27439.1.
AK150426 mRNA. Translation: BAE29549.1.
AK150843 mRNA. Translation: BAE29901.1.
AK151004 mRNA. Translation: BAE30027.1.
AK151128 mRNA. Translation: BAE30136.1.
AK151224 mRNA. Translation: BAE30216.1.
AK151920 mRNA. Translation: BAE30798.1.
AK152054 mRNA. Translation: BAE30910.1.
AK152890 mRNA. Translation: BAE31573.1.
AK157529 mRNA. Translation: BAE34114.1.
AK159540 mRNA. Translation: BAE35167.1.
AK159491 mRNA. Translation: BAE35125.1.
AK159758 mRNA. Translation: BAE35349.1.
AK160043 mRNA. Translation: BAE35585.1.
AK164110 mRNA. Translation: BAE37632.1.
AK164193 mRNA. Translation: BAE37675.1.
AK166709 mRNA. Translation: BAE38962.1.
AK166812 mRNA. Translation: BAE39039.1.
AK167159 mRNA. Translation: BAE39300.1.
AK167863 mRNA. Translation: BAE39881.1.
AK168198 mRNA. Translation: BAE40158.1.
AK168617 mRNA. Translation: BAE40482.1.
AK168879 mRNA. Translation: BAE40697.1.
AK168890 mRNA. Translation: BAE40707.1.
AK168932 mRNA. Translation: BAE40744.1.
AK169080 mRNA. Translation: BAE40864.1.
AK169084 mRNA. Translation: BAE40868.1.
AK169105 mRNA. Translation: BAE40887.1.
AK169142 mRNA. Translation: BAE40921.1.
AK169300 mRNA. Translation: BAE41056.1.
AK169308 mRNA. Translation: BAE41063.1.
AK169414 mRNA. Translation: BAE41160.1.
BC014854 mRNA. Translation: AAH14854.1.
CCDSiCCDS29358.1.
PIRiJC1473.
RefSeqiNP_031531.1. NM_007505.2.
UniGeneiMm.276137.

3D structure databases

ProteinModelPortaliQ03265.
SMRiQ03265. Positions 56-552.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198253. 14 interactions.
IntActiQ03265. 18 interactions.
MINTiMINT-1859704.

PTM databases

PhosphoSiteiQ03265.

2D gel databases

REPRODUCTION-2DPAGEIPI00130280.
Q03265.
SWISS-2DPAGEQ03265.
UCD-2DPAGEQ03265.

Proteomic databases

MaxQBiQ03265.
PaxDbiQ03265.
PRIDEiQ03265.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026495; ENSMUSP00000026495; ENSMUSG00000025428.
GeneIDi11946.
KEGGimmu:11946.
UCSCiuc008fru.1. mouse.

Organism-specific databases

CTDi498.
MGIiMGI:88115. Atp5a1.

Phylogenomic databases

eggNOGiCOG0056.
GeneTreeiENSGT00550000074846.
HOVERGENiHBG001536.
InParanoidiQ03265.
KOiK02132.
OMAiATRNLHS.
OrthoDBiEOG773XFP.
PhylomeDBiQ03265.
TreeFamiTF300321.

Enzyme and pathway databases

ReactomeiREACT_245290. Formation of ATP by chemiosmotic coupling.

Miscellaneous databases

ChiTaRSiAtp5a1. mouse.
NextBioi280057.
PROiQ03265.
SOURCEiSearch...

Gene expression databases

BgeeiQ03265.
ExpressionAtlasiQ03265. baseline and differential.
GenevestigatoriQ03265.

Family and domain databases

Gene3Di2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01346. ATP_synth_alpha_bact.
InterProiIPR020003. ATPase_a/bsu_AS.
IPR023366. ATPase_asu-like.
IPR005294. ATPase_F1-cplx_asu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00962. atpA. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and functional expression analysis of the alpha subunit of mouse ATP synthase."
    Yotov W.V., St Arnaud R.
    Biochem. Biophys. Res. Commun. 191:142-148(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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: BALB/c, C57BL/6J and NOD.
    Tissue: Heart, Hippocampus, Liver, Spinal cord and Spleen.
  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].
    Tissue: Eye.
  4. Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 24-42; 46-83; 89-123; 133-161; 176-182; 195-204; 208-214; 219-230; 241-252; 254-261; 263-270; 306-316; 323-329; 335-347; 403-416; 435-463; 467-503; 507-527 AND 540-553.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  5. "Quantitative analysis of both protein expression and serine / threonine post-translational modifications through stable isotope labeling with dithiothreitol."
    Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L., Hart G.W., Burlingame A.L.
    Proteomics 5:388-398(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-498; LYS-531 AND LYS-539, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-167; LYS-230; LYS-239; LYS-261; LYS-305; LYS-427; LYS-498; LYS-506; LYS-531 AND LYS-539, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  7. "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-123; LYS-126; LYS-132; LYS-161; LYS-167; LYS-230; LYS-239; LYS-240; LYS-261; LYS-305; LYS-427; LYS-434; LYS-498; LYS-506; LYS-531; LYS-539 AND LYS-541, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
+Additional computationally mapped references.

Entry informationi

Entry nameiATPA_MOUSE
AccessioniPrimary (citable) accession number: Q03265
Secondary accession number(s): Q3TFN0
, Q3THN8, Q3TPR0, Q3TPV3, Q3TZU3, Q3UIR7, Q543Y6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: February 4, 2015
This is version 154 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.