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P53396

- ACLY_HUMAN

UniProt

P53396 - ACLY_HUMAN

Protein

ATP-citrate synthase

Gene

ACLY

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine.1 Publication

    Catalytic activityi

    ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA.

    Cofactori

    Magnesium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei58 – 581ATP
    Binding sitei118 – 1181ATP
    Metal bindingi201 – 2011MagnesiumBy similarity
    Metal bindingi203 – 2031MagnesiumBy similarity
    Binding sitei346 – 3461Citrate; via amide nitrogen1 Publication
    Binding sitei348 – 3481Citrate1 Publication
    Binding sitei379 – 3791Citrate1 Publication
    Metal bindingi718 – 7181MagnesiumBy similarity
    Active sitei760 – 7601Tele-phosphohistidine intermediateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi66 – 672ATP
    Nucleotide bindingi109 – 1113ATP
    Nucleotide bindingi701 – 72121ATPBy similarityAdd
    BLAST
    Nucleotide bindingi752 – 77827ATPBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP citrate synthase activity Source: UniProtKB
    3. cofactor binding Source: InterPro
    4. metal ion binding Source: UniProtKB-KW
    5. protein binding Source: UniProtKB
    6. succinate-CoA ligase (ADP-forming) activity Source: InterPro

    GO - Biological processi

    1. ATP catabolic process Source: ProtInc
    2. cellular carbohydrate metabolic process Source: InterPro
    3. cellular lipid metabolic process Source: Reactome
    4. citrate metabolic process Source: ProtInc
    5. coenzyme A metabolic process Source: ProtInc
    6. energy reserve metabolic process Source: Reactome
    7. lipid biosynthetic process Source: UniProtKB
    8. long-chain fatty-acyl-CoA biosynthetic process Source: Reactome
    9. positive regulation of cellular metabolic process Source: Reactome
    10. small molecule metabolic process Source: Reactome
    11. triglyceride biosynthetic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS05535-MONOMER.
    ReactomeiREACT_1319. Fatty Acyl-CoA Biosynthesis.
    REACT_2122. ChREBP activates metabolic gene expression.
    SABIO-RKP53396.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-citrate synthase (EC:2.3.3.8)
    Alternative name(s):
    ATP-citrate (pro-S-)-lyase
    Short name:
    ACL
    Citrate cleavage enzyme
    Gene namesi
    Name:ACLY
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:115. ACLY.

    Subcellular locationi

    GO - Cellular componenti

    1. citrate lyase complex Source: ProtInc
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. membrane Source: UniProtKB
    6. mitochondrion Source: Ensembl
    7. nucleus Source: HPA
    8. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi540 – 5401K → R or Q: Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-546 and R,Q-554. 1 Publication
    Mutagenesisi546 – 5461K → R or Q: Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-540 and R,Q-554. 1 Publication
    Mutagenesisi554 – 5541K → R or Q: Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-540 and R,Q-546. 1 Publication

    Organism-specific databases

    PharmGKBiPA24441.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11011101ATP-citrate synthasePRO_0000102781Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei131 – 1311Phosphotyrosine1 Publication
    Modified residuei447 – 4471PhosphothreonineBy similarity
    Modified residuei451 – 4511PhosphoserineBy similarity
    Modified residuei455 – 4551Phosphoserine; by PKA and PKB/AKT1 or PKB/AKT23 Publications
    Modified residuei481 – 4811Phosphoserine8 Publications
    Modified residuei540 – 5401N6-acetyllysine; alternate1 Publication
    Cross-linki540 – 540Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
    Modified residuei546 – 5461N6-acetyllysine; alternate2 Publications
    Cross-linki546 – 546Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
    Modified residuei554 – 5541N6-acetyllysine; alternate2 Publications
    Cross-linki554 – 554Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
    Modified residuei639 – 6391Phosphothreonine1 Publication
    Modified residuei663 – 6631Phosphoserine1 Publication
    Modified residuei682 – 6821Phosphotyrosine2 Publications
    Modified residuei839 – 8391Phosphoserine1 Publication
    Modified residuei948 – 9481N6-acetyllysine1 Publication
    Modified residuei968 – 9681N6-acetyllysine1 Publication
    Modified residuei978 – 9781N6-acetyllysineBy similarity
    Modified residuei1077 – 10771N6-acetyllysine1 Publication
    Modified residuei1100 – 11001Phosphoserine2 Publications

    Post-translational modificationi

    ISGylated.1 Publication
    Acetylated at Lys-540, Lys-546 and Lys-554 by KAT2B/PCAF. Acetylation is promoted by glucose and stabilizes the protein, probably by preventing ubiquitination at the same sites. Acetylation promotes de novo lipid synthesis. Deacetylated by SIRT2.2 Publications
    Ubiquitinated at Lys-540, Lys-546 and Lys-554 by UBR4, leading to its degradation. Ubiquitination is probably inhibited by acetylation at same site Probable.2 Publications

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP53396.
    PaxDbiP53396.
    PeptideAtlasiP53396.
    PRIDEiP53396.

    PTM databases

    PhosphoSiteiP53396.

    Expressioni

    Gene expression databases

    ArrayExpressiP53396.
    BgeeiP53396.
    CleanExiHS_ACLY.
    GenevestigatoriP53396.

    Organism-specific databases

    HPAiCAB007783.
    HPA022434.
    HPA022953.
    HPA022959.
    HPA028758.

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    BioGridi106563. 40 interactions.
    IntActiP53396. 7 interactions.
    MINTiMINT-3019895.
    STRINGi9606.ENSP00000253792.

    Structurei

    Secondary structure

    1
    1101
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 64
    Helixi8 – 1811
    Beta strandi32 – 343
    Helixi40 – 467
    Helixi48 – 514
    Beta strandi55 – 595
    Turni66 – 705
    Beta strandi73 – 764
    Helixi78 – 858
    Turni86 – 905
    Beta strandi92 – 954
    Beta strandi98 – 1014
    Beta strandi105 – 1095
    Helixi115 – 1173
    Beta strandi118 – 1269
    Beta strandi129 – 1379
    Helixi140 – 1423
    Helixi145 – 1484
    Beta strandi149 – 1557
    Helixi162 – 1676
    Turni168 – 1725
    Turni175 – 1773
    Helixi178 – 19417
    Beta strandi197 – 20812
    Beta strandi211 – 2144
    Beta strandi217 – 2226
    Helixi223 – 2253
    Helixi226 – 2338
    Beta strandi242 – 2443
    Helixi248 – 25811
    Beta strandi260 – 26910
    Beta strandi274 – 2774
    Helixi282 – 29413
    Helixi298 – 3003
    Beta strandi303 – 3097
    Helixi313 – 32614
    Beta strandi336 – 3405
    Beta strandi346 – 3483
    Helixi350 – 36314
    Helixi365 – 3706
    Beta strandi373 – 3786
    Helixi384 – 39815
    Beta strandi402 – 4054
    Helixi413 – 4186
    Beta strandi499 – 5035
    Helixi506 – 51813
    Beta strandi525 – 5306
    Beta strandi536 – 5438
    Beta strandi546 – 55510
    Helixi556 – 5627
    Beta strandi568 – 5714
    Turni575 – 5773
    Helixi578 – 5858
    Beta strandi593 – 5964
    Helixi603 – 61614
    Beta strandi619 – 6213
    Beta strandi628 – 6303
    Turni631 – 6333
    Turni637 – 6404
    Helixi643 – 6486
    Turni649 – 6524
    Beta strandi656 – 6627
    Helixi664 – 67714
    Beta strandi681 – 6866
    Beta strandi689 – 6924
    Helixi697 – 7059
    Beta strandi712 – 72211
    Helixi723 – 73210
    Beta strandi740 – 7456
    Helixi768 – 7703
    Helixi772 – 78110
    Helixi790 – 7923
    Helixi793 – 80614

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3MWDX-ray2.10A1-425[»]
    B487-820[»]
    3MWEX-ray2.20A1-425[»]
    B487-821[»]
    3PFFX-ray2.30A1-817[»]
    ProteinModelPortaliP53396.
    SMRiP53396. Positions 2-425, 487-820, 911-1075.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP53396.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 265262ATP-graspAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni779 – 78911CoA-bindingSequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the succinate/malate CoA ligase beta subunit family.Curated
    In the C-terminal section; belongs to the succinate/malate CoA ligase alpha subunit family.Curated
    Contains 1 ATP-grasp domain.Curated

    Phylogenomic databases

    eggNOGiCOG0372.
    HOGENOMiHOG000151479.
    HOVERGENiHBG003318.
    InParanoidiP53396.
    KOiK01648.
    OMAiRLPKYAC.
    PhylomeDBiP53396.
    TreeFamiTF300560.

    Family and domain databases

    Gene3Di1.10.230.10. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.261. 2 hits.
    3.40.50.720. 1 hit.
    InterProiIPR014608. ATP-citrate_synthase.
    IPR013650. ATP-grasp_succ-CoA_synth-type.
    IPR013816. ATP_grasp_subdomain_2.
    IPR017440. Cit_synth/succinyl-CoA_lig_AS.
    IPR016143. Citrate_synth-like_sm_a-sub.
    IPR002020. Citrate_synthase-like.
    IPR016141. Citrate_synthase-like_core.
    IPR003781. CoA-bd.
    IPR005810. CoA_lig_alpha.
    IPR005811. CoA_ligase.
    IPR016040. NAD(P)-bd_dom.
    IPR017866. Succ-CoA_synthase_bsu_CS.
    IPR016102. Succinyl-CoA_synth-like.
    [Graphical view]
    PfamiPF08442. ATP-grasp_2. 1 hit.
    PF00285. Citrate_synt. 1 hit.
    PF02629. CoA_binding. 1 hit.
    PF00549. Ligase_CoA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036511. ATP_citrt_syn. 1 hit.
    SUPFAMiSSF48256. SSF48256. 2 hits.
    SSF52210. SSF52210. 1 hit.
    PROSITEiPS01216. SUCCINYL_COA_LIG_1. 1 hit.
    PS00399. SUCCINYL_COA_LIG_2. 1 hit.
    PS01217. SUCCINYL_COA_LIG_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P53396-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSAKAISEQT GKELLYKFIC TTSAIQNRFK YARVTPDTDW ARLLQDHPWL     50
    LSQNLVVKPD QLIKRRGKLG LVGVNLTLDG VKSWLKPRLG QEATVGKATG 100
    FLKNFLIEPF VPHSQAEEFY VCIYATREGD YVLFHHEGGV DVGDVDAKAQ 150
    KLLVGVDEKL NPEDIKKHLL VHAPEDKKEI LASFISGLFN FYEDLYFTYL 200
    EINPLVVTKD GVYVLDLAAK VDATADYICK VKWGDIEFPP PFGREAYPEE 250
    AYIADLDAKS GASLKLTLLN PKGRIWTMVA GGGASVVYSD TICDLGGVNE 300
    LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPDGKILII GGSIANFTNV 350
    AATFKGIVRA IRDYQGPLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI 400
    PIHVFGTETH MTAIVGMALG HRPIPNQPPT AAHTANFLLN ASGSTSTPAP 450
    SRTASFSESR ADEVAPAKKA KPAMPQDSVP SPRSLQGKST TLFSRHTKAI 500
    VWGMQTRAVQ GMLDFDYVCS RDEPSVAAMV YPFTGDHKQK FYWGHKEILI 550
    PVFKNMADAM RKHPEVDVLI NFASLRSAYD STMETMNYAQ IRTIAIIAEG 600
    IPEALTRKLI KKADQKGVTI IGPATVGGIK PGCFKIGNTG GMLDNILASK 650
    LYRPGSVAYV SRSGGMSNEL NNIISRTTDG VYEGVAIGGD RYPGSTFMDH 700
    VLRYQDTPGV KMIVVLGEIG GTEEYKICRG IKEGRLTKPI VCWCIGTCAT 750
    MFSSEVQFGH AGACANQASE TAVAKNQALK EAGVFVPRSF DELGEIIQSV 800
    YEDLVANGVI VPAQEVPPPT VPMDYSWARE LGLIRKPASF MTSICDERGQ 850
    ELIYAGMPIT EVFKEEMGIG GVLGLLWFQK RLPKYSCQFI EMCLMVTADH 900
    GPAVSGAHNT IICARAGKDL VSSLTSGLLT IGDRFGGALD AAAKMFSKAF 950
    DSGIIPMEFV NKMKKEGKLI MGIGHRVKSI NNPDMRVQIL KDYVRQHFPA 1000
    TPLLDYALEV EKITTSKKPN LILNVDGLIG VAFVDMLRNC GSFTREEADE 1050
    YIDIGALNGI FVLGRSMGFI GHYLDQKRLK QGLYRHPWDD ISYVLPEHMS 1100
    M 1101
    Length:1,101
    Mass (Da):120,839
    Last modified:October 17, 2006 - v3
    Checksum:i12BB4416A30DC30C
    GO
    Isoform 2 (identifier: P53396-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         476-485: Missing.

    Show »
    Length:1,091
    Mass (Da):119,772
    Checksum:i04EB8D05059409E5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti75 – 751N → D in CAA45614. (PubMed:1371749)Curated
    Sequence conflicti111 – 1111V → A in CAA45614. (PubMed:1371749)Curated
    Sequence conflicti245 – 2451E → V in CAA45614. (PubMed:1371749)Curated
    Sequence conflicti419 – 4235LGHRP → WAPA in CAA45614. (PubMed:1371749)Curated
    Sequence conflicti442 – 4443SGS → QRE in CAA45614. (PubMed:1371749)Curated
    Sequence conflicti457 – 4593SES → YESMVDEV in CAA45614. (PubMed:1371749)Curated
    Sequence conflicti653 – 6564RPGS → PQAA in CAA45614. (PubMed:1371749)Curated
    Sequence conflicti728 – 7281C → S in CAA45614. (PubMed:1371749)Curated
    Sequence conflicti872 – 8721V → A in CAA45614. (PubMed:1371749)Curated
    Sequence conflicti916 – 9194AGKD → TAVE in CAA45614. (PubMed:1371749)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti175 – 1751E → D.3 Publications
    Corresponds to variant rs2304497 [ dbSNP | Ensembl ].
    VAR_028230

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei476 – 48510Missing in isoform 2. 1 PublicationVSP_042201

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64330 mRNA. Translation: CAA45614.1.
    U18197 mRNA. Translation: AAB60340.1.
    AK295675 mRNA. Translation: BAG58532.1.
    AC091172 Genomic DNA. No translation available.
    BC006195 mRNA. Translation: AAH06195.1.
    CCDSiCCDS11412.1. [P53396-1]
    CCDS11413.1. [P53396-2]
    PIRiS21173.
    RefSeqiNP_001087.2. NM_001096.2. [P53396-1]
    NP_942127.1. NM_198830.1. [P53396-2]
    XP_005257452.1. XM_005257395.1. [P53396-1]
    UniGeneiHs.387567.

    Genome annotation databases

    EnsembliENST00000352035; ENSP00000253792; ENSG00000131473. [P53396-1]
    ENST00000353196; ENSP00000345398; ENSG00000131473. [P53396-2]
    ENST00000393896; ENSP00000377474; ENSG00000131473. [P53396-2]
    ENST00000590151; ENSP00000466259; ENSG00000131473. [P53396-1]
    GeneIDi47.
    KEGGihsa:47.
    UCSCiuc002hyg.3. human. [P53396-1]
    uc002hyh.3. human. [P53396-2]

    Polymorphism databases

    DMDMi116241237.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64330 mRNA. Translation: CAA45614.1 .
    U18197 mRNA. Translation: AAB60340.1 .
    AK295675 mRNA. Translation: BAG58532.1 .
    AC091172 Genomic DNA. No translation available.
    BC006195 mRNA. Translation: AAH06195.1 .
    CCDSi CCDS11412.1. [P53396-1 ]
    CCDS11413.1. [P53396-2 ]
    PIRi S21173.
    RefSeqi NP_001087.2. NM_001096.2. [P53396-1 ]
    NP_942127.1. NM_198830.1. [P53396-2 ]
    XP_005257452.1. XM_005257395.1. [P53396-1 ]
    UniGenei Hs.387567.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3MWD X-ray 2.10 A 1-425 [» ]
    B 487-820 [» ]
    3MWE X-ray 2.20 A 1-425 [» ]
    B 487-821 [» ]
    3PFF X-ray 2.30 A 1-817 [» ]
    ProteinModelPortali P53396.
    SMRi P53396. Positions 2-425, 487-820, 911-1075.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106563. 40 interactions.
    IntActi P53396. 7 interactions.
    MINTi MINT-3019895.
    STRINGi 9606.ENSP00000253792.

    Chemistry

    BindingDBi P53396.
    ChEMBLi CHEMBL3720.

    PTM databases

    PhosphoSitei P53396.

    Polymorphism databases

    DMDMi 116241237.

    Proteomic databases

    MaxQBi P53396.
    PaxDbi P53396.
    PeptideAtlasi P53396.
    PRIDEi P53396.

    Protocols and materials databases

    DNASUi 47.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000352035 ; ENSP00000253792 ; ENSG00000131473 . [P53396-1 ]
    ENST00000353196 ; ENSP00000345398 ; ENSG00000131473 . [P53396-2 ]
    ENST00000393896 ; ENSP00000377474 ; ENSG00000131473 . [P53396-2 ]
    ENST00000590151 ; ENSP00000466259 ; ENSG00000131473 . [P53396-1 ]
    GeneIDi 47.
    KEGGi hsa:47.
    UCSCi uc002hyg.3. human. [P53396-1 ]
    uc002hyh.3. human. [P53396-2 ]

    Organism-specific databases

    CTDi 47.
    GeneCardsi GC17M040023.
    HGNCi HGNC:115. ACLY.
    HPAi CAB007783.
    HPA022434.
    HPA022953.
    HPA022959.
    HPA028758.
    MIMi 108728. gene.
    neXtProti NX_P53396.
    PharmGKBi PA24441.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0372.
    HOGENOMi HOG000151479.
    HOVERGENi HBG003318.
    InParanoidi P53396.
    KOi K01648.
    OMAi RLPKYAC.
    PhylomeDBi P53396.
    TreeFami TF300560.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS05535-MONOMER.
    Reactomei REACT_1319. Fatty Acyl-CoA Biosynthesis.
    REACT_2122. ChREBP activates metabolic gene expression.
    SABIO-RK P53396.

    Miscellaneous databases

    ChiTaRSi ACLY. human.
    EvolutionaryTracei P53396.
    GenomeRNAii 47.
    NextBioi 181.
    PROi P53396.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P53396.
    Bgeei P53396.
    CleanExi HS_ACLY.
    Genevestigatori P53396.

    Family and domain databases

    Gene3Di 1.10.230.10. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.261. 2 hits.
    3.40.50.720. 1 hit.
    InterProi IPR014608. ATP-citrate_synthase.
    IPR013650. ATP-grasp_succ-CoA_synth-type.
    IPR013816. ATP_grasp_subdomain_2.
    IPR017440. Cit_synth/succinyl-CoA_lig_AS.
    IPR016143. Citrate_synth-like_sm_a-sub.
    IPR002020. Citrate_synthase-like.
    IPR016141. Citrate_synthase-like_core.
    IPR003781. CoA-bd.
    IPR005810. CoA_lig_alpha.
    IPR005811. CoA_ligase.
    IPR016040. NAD(P)-bd_dom.
    IPR017866. Succ-CoA_synthase_bsu_CS.
    IPR016102. Succinyl-CoA_synth-like.
    [Graphical view ]
    Pfami PF08442. ATP-grasp_2. 1 hit.
    PF00285. Citrate_synt. 1 hit.
    PF02629. CoA_binding. 1 hit.
    PF00549. Ligase_CoA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036511. ATP_citrt_syn. 1 hit.
    SUPFAMi SSF48256. SSF48256. 2 hits.
    SSF52210. SSF52210. 1 hit.
    PROSITEi PS01216. SUCCINYL_COA_LIG_1. 1 hit.
    PS00399. SUCCINYL_COA_LIG_2. 1 hit.
    PS01217. SUCCINYL_COA_LIG_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-175.
      Tissue: Liver.
    2. "Variant cDNA sequences of human ATP:citrate lyase: cloning, expression, and purification from baculovirus-infected insect cells."
      Lord K.A., Wang X.M., Simmons S.J., Bruckner R.C., Loscig J., O'Connor B., Bentley R., Smallwood A., Chadwick C.C., Stevis P.E., Ciccarelli R.B.
      Protein Expr. Purif. 9:133-141(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASP-175.
      Tissue: Liver.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ASP-175.
      Tissue: Hippocampus.
    4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Lymph.
    6. Cited for: ISGYLATION.
    7. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-131 AND TYR-682, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455; SER-481 AND SER-1100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481; THR-639; SER-663; TYR-682; SER-839 AND SER-1100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-546; LYS-554; LYS-948; LYS-968 AND LYS-1077, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455 AND SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455 AND SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth."
      Lin R., Tao R., Gao X., Li T., Zhou X., Guan K.L., Xiong Y., Lei Q.Y.
      Mol. Cell 51:506-518(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ACETYLATION AT LYS-540; LYS-546 AND LYS-554, UBIQUITINATION AT LYS-540; LYS-546 AND LYS-554, MUTAGENESIS OF LYS-540; LYS-546 AND LYS-554.
    21. "Identification of the citrate-binding site of human ATP-citrate lyase using X-ray crystallography."
      Sun T., Hayakawa K., Bateman K.S., Fraser M.E.
      J. Biol. Chem. 285:27418-27428(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-425 AND 487-820 IN COMPLEX WITH CITRATE, CITRATE-BINDING SITES.
    22. "ADP-Mg2+ bound to the ATP-grasp domain of ATP-citrate lyase."
      Sun T., Hayakawa K., Fraser M.E.
      Acta Crystallogr. F 67:1168-1172(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-817 IN COMPLEX WITH ADP.

    Entry informationi

    Entry nameiACLY_HUMAN
    AccessioniPrimary (citable) accession number: P53396
    Secondary accession number(s): B4DIM0, Q13037, Q9BRL0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 156 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3