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Q76MZ3

- 2AAA_MOUSE

UniProt

Q76MZ3 - 2AAA_MOUSE

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Protein

Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

Gene

Ppp2r1a

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

Functioni

The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Required for proper chromosome segregation and for centromeric localization of SGOL1 in mitosis (By similarity).By similarity

GO - Molecular functioni

  1. antigen binding Source: Ensembl
  2. protein serine/threonine phosphatase activity Source: MGI

GO - Biological processi

  1. chromosome segregation Source: UniProtKB
  2. peptidyl-serine dephosphorylation Source: MGI
  3. positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
Complete GO annotation...

Keywords - Biological processi

Chromosome partition

Enzyme and pathway databases

ReactomeiREACT_196577. MASTL Facilitates Mitotic Progression.
REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_198526. Spry regulation of FGF signaling.
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_203336. Degradation of beta-catenin by the destruction complex.
REACT_203795. DARPP-32 events.
REACT_206803. Cyclin A/B1 associated events during G2/M transition.
REACT_207679. Separation of Sister Chromatids.
REACT_208887. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_210064. ERKs are inactivated.
REACT_210180. Initiation of Nuclear Envelope Reformation.
REACT_215063. ERK/MAPK targets.
REACT_216784. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_217323. Integration of energy metabolism.
REACT_218396. Beta-catenin phosphorylation cascade.
REACT_230286. APC truncation mutants have impaired AXIN binding.
REACT_232322. Glycolysis.
REACT_234076. S37 mutants of beta-catenin aren't phosphorylated.
REACT_243078. Loss of Nlp from mitotic centrosomes.
REACT_244487. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_245720. Recruitment of mitotic centrosome proteins and complexes.
REACT_245985. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_248000. S45 mutants of beta-catenin aren't phosphorylated.
REACT_250714. truncations of AMER1 destabilize the destruction complex.
REACT_252458. AXIN missense mutants destabilize the destruction complex.
REACT_256756. Mitotic Prometaphase.
REACT_258573. Cyclin D associated events in G1.
REACT_258576. T41 mutants of beta-catenin aren't phosphorylated.
REACT_260752. S33 mutants of beta-catenin aren't phosphorylated.
REACT_261276. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_261568. CTLA4 inhibitory signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
Alternative name(s):
PP2A subunit A isoform PR65-alpha
PP2A subunit A isoform R1-alpha
Gene namesi
Name:Ppp2r1a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:1926334. Ppp2r1a.

Subcellular locationi

Cytoplasm By similarity. Chromosomecentromere By similarity
Note: Centromeric localization requires the presence of BUB1.By similarity

GO - Cellular componenti

  1. chromosome, centromeric region Source: UniProtKB
  2. cytosol Source: MGI
  3. protein phosphatase type 2A complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 589588Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoformPRO_0000071401Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei280 – 2801N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ76MZ3.
PaxDbiQ76MZ3.
PRIDEiQ76MZ3.

2D gel databases

REPRODUCTION-2DPAGEQ76MZ3.

PTM databases

PhosphoSiteiQ76MZ3.

Expressioni

Gene expression databases

BgeeiQ76MZ3.
ExpressionAtlasiQ76MZ3. baseline and differential.
GenevestigatoriQ76MZ3.

Interactioni

Subunit structurei

PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with IPO9. Interacts with TP53 and SGOL1. Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD (By similarity). Interacts with PLA2G16; this interaction might decrease PP2A activity (By similarity). Interacts with FOXO1; the interaction dephosphorylates FOXO1 on AKT-mediated phosphoylation sites. Interacts with CTTNBP2NL (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
P030812EBI-400413,EBI-1266256From a different organism.
Ppp2caP633303EBI-400413,EBI-397144

Protein-protein interaction databases

BioGridi206176. 27 interactions.
DIPiDIP-29429N.
IntActiQ76MZ3. 46 interactions.
MINTiMINT-135926.
STRINGi10090.ENSMUSP00000007708.

Structurei

Secondary structure

1
589
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2111Combined sources
Helixi25 – 339Combined sources
Helixi35 – 417Combined sources
Helixi44 – 496Combined sources
Helixi51 – 566Combined sources
Helixi63 – 7311Combined sources
Turni77 – 815Combined sources
Helixi83 – 853Combined sources
Helixi86 – 894Combined sources
Helixi90 – 989Combined sources
Helixi102 – 11615Combined sources
Helixi121 – 1266Combined sources
Helixi128 – 1369Combined sources
Helixi141 – 1477Combined sources
Turni148 – 1503Combined sources
Helixi151 – 1544Combined sources
Helixi155 – 1573Combined sources
Helixi160 – 17415Combined sources
Helixi179 – 1879Combined sources
Helixi189 – 1935Combined sources
Helixi198 – 21316Combined sources
Helixi218 – 23215Combined sources
Helixi237 – 2426Combined sources
Helixi244 – 2518Combined sources
Helixi257 – 2659Combined sources
Helixi267 – 2748Combined sources
Helixi276 – 29116Combined sources
Helixi296 – 3038Combined sources
Helixi306 – 3116Combined sources
Turni315 – 3173Combined sources
Helixi318 – 3247Combined sources
Helixi327 – 3348Combined sources
Helixi339 – 3468Combined sources
Helixi349 – 3524Combined sources
Helixi353 – 37321Combined sources
Helixi378 – 3858Combined sources
Helixi386 – 3883Combined sources
Helixi389 – 3946Combined sources
Helixi397 – 4037Combined sources
Helixi405 – 4117Combined sources
Helixi417 – 4248Combined sources
Helixi427 – 4348Combined sources
Helixi436 – 4427Combined sources
Helixi444 – 4518Combined sources
Helixi456 – 47318Combined sources
Helixi475 – 4817Combined sources
Helixi483 – 4886Combined sources
Helixi489 – 4913Combined sources
Helixi495 – 52026Combined sources
Helixi522 – 5287Combined sources
Helixi534 – 54714Combined sources
Helixi548 – 5503Combined sources
Helixi553 – 5586Combined sources
Helixi560 – 5689Combined sources
Beta strandi569 – 5713Combined sources
Helixi573 – 58513Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IAEX-ray3.50A/D1-589[»]
2PF4X-ray3.10A/B/C/D1-589[»]
3FGAX-ray2.70A2-589[»]
ProteinModelPortaliQ76MZ3.
SMRiQ76MZ3. Positions 2-589.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ76MZ3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati8 – 4639HEAT 1Add
BLAST
Repeati47 – 8438HEAT 2Add
BLAST
Repeati85 – 12339HEAT 3Add
BLAST
Repeati124 – 16138HEAT 4Add
BLAST
Repeati162 – 20039HEAT 5Add
BLAST
Repeati201 – 23939HEAT 6Add
BLAST
Repeati240 – 27839HEAT 7Add
BLAST
Repeati279 – 32143HEAT 8Add
BLAST
Repeati322 – 36039HEAT 9Add
BLAST
Repeati361 – 39939HEAT 10Add
BLAST
Repeati400 – 43839HEAT 11Add
BLAST
Repeati439 – 47739HEAT 12Add
BLAST
Repeati478 – 51639HEAT 13Add
BLAST
Repeati517 – 55539HEAT 14Add
BLAST
Repeati556 – 58934HEAT 15Add
BLAST

Domaini

Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure.

Sequence similaritiesi

Contains 15 HEAT repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG247268.
GeneTreeiENSGT00730000110944.
HOGENOMiHOG000078539.
HOVERGENiHBG000011.
InParanoidiQ76MZ3.
KOiK03456.
OMAiRNLCQDD.
OrthoDBiEOG764722.
PhylomeDBiQ76MZ3.
TreeFamiTF105552.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
[Graphical view]
PfamiPF02985. HEAT. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50077. HEAT_REPEAT. 11 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q76MZ3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAADGDDSL YPIAVLIDEL RNEDVQLRLN SIKKLSTIAL ALGVERTRSE
60 70 80 90 100
LLPFLTDTIY DEDEVLLALA EQLGTFTTLV GGPEYVHCLL PPLESLATVE
110 120 130 140 150
ETVVRDKAVE SLRAISHEHS PSDLEAHFVP LVKRLAGGDW FTSRTSACGL
160 170 180 190 200
FSVCYPRVSS AVKAELRQYF RNLCSDDTPM VRRAAASKLG EFAKVLELDN
210 220 230 240 250
VKSEIIPMFS NLASDEQDSV RLLAVEACVN IAQLLPQEDL EALVMPTLRQ
260 270 280 290 300
AAEDKSWRVR YMVADKFTEL QKAVGPEITK TDLVPAFQNL MKDCEAEVRA
310 320 330 340 350
AASHKVKEFC ENLSADCREN VIMTQILPCI KELVSDANQH VKSALASVIM
360 370 380 390 400
GLSPILGKDN TIEHLLPLFL AQLKDECPEV RLNIISNLDC VNEVIGIRQL
410 420 430 440 450
SQSLLPAIVE LAEDAKWRVR LAIIEYMPLL AGQLGVEFFD EKLNSLCMAW
460 470 480 490 500
LVDHVYAIRE AATSNLKKLV EKFGKEWAHA TIIPKVLAMS GDPNYLHRMT
510 520 530 540 550
TLFCINVLSE VCGQDITTKH MLPTVLRMAG DPVANVRFNV AKSLQKIGPI
560 570 580
LDNSTLQSEV KPILEKLTQD QDVDVKYFAQ EALTVLSLA
Length:589
Mass (Da):65,323
Last modified:January 23, 2007 - v3
Checksum:i5175409E4D50A366
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021743 mRNA. Translation: BAA75478.1.
AK054239 mRNA. Translation: BAC35700.1.
AK078135 mRNA. Translation: BAC37143.1.
BC006606 mRNA. Translation: AAH06606.1.
CCDSiCCDS28432.1.
RefSeqiNP_058587.1. NM_016891.3.
UniGeneiMm.294138.

Genome annotation databases

EnsembliENSMUST00000007708; ENSMUSP00000007708; ENSMUSG00000007564.
GeneIDi51792.
KEGGimmu:51792.
UCSCiuc008aqi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021743 mRNA. Translation: BAA75478.1 .
AK054239 mRNA. Translation: BAC35700.1 .
AK078135 mRNA. Translation: BAC37143.1 .
BC006606 mRNA. Translation: AAH06606.1 .
CCDSi CCDS28432.1.
RefSeqi NP_058587.1. NM_016891.3.
UniGenei Mm.294138.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2IAE X-ray 3.50 A/D 1-589 [» ]
2PF4 X-ray 3.10 A/B/C/D 1-589 [» ]
3FGA X-ray 2.70 A 2-589 [» ]
ProteinModelPortali Q76MZ3.
SMRi Q76MZ3. Positions 2-589.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 206176. 27 interactions.
DIPi DIP-29429N.
IntActi Q76MZ3. 46 interactions.
MINTi MINT-135926.
STRINGi 10090.ENSMUSP00000007708.

Chemistry

BindingDBi Q76MZ3.
ChEMBLi CHEMBL3557.

PTM databases

PhosphoSitei Q76MZ3.

2D gel databases

REPRODUCTION-2DPAGE Q76MZ3.

Proteomic databases

MaxQBi Q76MZ3.
PaxDbi Q76MZ3.
PRIDEi Q76MZ3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000007708 ; ENSMUSP00000007708 ; ENSMUSG00000007564 .
GeneIDi 51792.
KEGGi mmu:51792.
UCSCi uc008aqi.1. mouse.

Organism-specific databases

CTDi 5518.
MGIi MGI:1926334. Ppp2r1a.

Phylogenomic databases

eggNOGi NOG247268.
GeneTreei ENSGT00730000110944.
HOGENOMi HOG000078539.
HOVERGENi HBG000011.
InParanoidi Q76MZ3.
KOi K03456.
OMAi RNLCQDD.
OrthoDBi EOG764722.
PhylomeDBi Q76MZ3.
TreeFami TF105552.

Enzyme and pathway databases

Reactomei REACT_196577. MASTL Facilitates Mitotic Progression.
REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_198526. Spry regulation of FGF signaling.
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_198961. Resolution of Sister Chromatid Cohesion.
REACT_203336. Degradation of beta-catenin by the destruction complex.
REACT_203795. DARPP-32 events.
REACT_206803. Cyclin A/B1 associated events during G2/M transition.
REACT_207679. Separation of Sister Chromatids.
REACT_208887. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_210064. ERKs are inactivated.
REACT_210180. Initiation of Nuclear Envelope Reformation.
REACT_215063. ERK/MAPK targets.
REACT_216784. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_217323. Integration of energy metabolism.
REACT_218396. Beta-catenin phosphorylation cascade.
REACT_230286. APC truncation mutants have impaired AXIN binding.
REACT_232322. Glycolysis.
REACT_234076. S37 mutants of beta-catenin aren't phosphorylated.
REACT_243078. Loss of Nlp from mitotic centrosomes.
REACT_244487. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_245720. Recruitment of mitotic centrosome proteins and complexes.
REACT_245985. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_248000. S45 mutants of beta-catenin aren't phosphorylated.
REACT_250714. truncations of AMER1 destabilize the destruction complex.
REACT_252458. AXIN missense mutants destabilize the destruction complex.
REACT_256756. Mitotic Prometaphase.
REACT_258573. Cyclin D associated events in G1.
REACT_258576. T41 mutants of beta-catenin aren't phosphorylated.
REACT_260752. S33 mutants of beta-catenin aren't phosphorylated.
REACT_261276. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_261568. CTLA4 inhibitory signaling.

Miscellaneous databases

ChiTaRSi Ppp2r1a. mouse.
EvolutionaryTracei Q76MZ3.
NextBioi 308024.
PROi Q76MZ3.
SOURCEi Search...

Gene expression databases

Bgeei Q76MZ3.
ExpressionAtlasi Q76MZ3. baseline and differential.
Genevestigatori Q76MZ3.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
[Graphical view ]
Pfami PF02985. HEAT. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
PROSITEi PS50077. HEAT_REPEAT. 11 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Alpha4 protein as a common regulator of type 2A-related serine/threonine protein phosphatases."
    Nanahoshi M., Tsujishita Y., Tokunaga C., Inui S., Sakaguchi N., Hara K., Yonezawa K.
    FEBS Lett. 446:108-112(1999) [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: C57BL/6J.
    Tissue: Medulla oblongata and Oviduct.
  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: FVB/N.
    Tissue: Mammary tumor.
  4. "The B55alpha-containing PP2A holoenzyme dephosphorylates FOXO1 in islet beta-cells under oxidative stress."
    Yan L., Guo S., Brault M., Harmon J., Robertson R.P., Hamid R., Stein R., Yang E.
    Biochem. J. 444:239-247(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH FOXO1.
  5. "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-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry namei2AAA_MOUSE
AccessioniPrimary (citable) accession number: Q76MZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 96 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

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3