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P53396

- ACLY_HUMAN

UniProt

P53396 - ACLY_HUMAN

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Protein

ATP-citrate synthase

Gene

ACLY

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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.

Enzyme regulationi

Phosphorylation results in a 6-fold increase in V(max) and the conversion of citrate dependence from sigmoidal to hyperbolic. Fructose 6-phosphate (F6P) is also a potent activator.1 Publication

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. 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
Complete GO annotation...

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: UniProtKB
  5. membrane Source: UniProtKB
  6. mitochondrion Source: Ensembl
  7. nucleus Source: HPA
  8. plasma membrane Source: HPA
Complete GO annotation...

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

BgeeiP53396.
CleanExiHS_ACLY.
ExpressionAtlasiP53396. baseline and differential.
GenevestigatoriP53396.

Organism-specific databases

HPAiCAB007783.
HPA022434.
HPA022953.
HPA022959.
HPA028758.

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

BioGridi106563. 43 interactions.
IntActiP53396. 8 interactions.
MINTiMINT-3019895.
STRINGi9606.ENSP00000253792.

Structurei

Secondary structure

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

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.
GeneTreeiENSGT00530000063275.
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

        10         20         30         40         50
MSAKAISEQT GKELLYKFIC TTSAIQNRFK YARVTPDTDW ARLLQDHPWL
60 70 80 90 100
LSQNLVVKPD QLIKRRGKLG LVGVNLTLDG VKSWLKPRLG QEATVGKATG
110 120 130 140 150
FLKNFLIEPF VPHSQAEEFY VCIYATREGD YVLFHHEGGV DVGDVDAKAQ
160 170 180 190 200
KLLVGVDEKL NPEDIKKHLL VHAPEDKKEI LASFISGLFN FYEDLYFTYL
210 220 230 240 250
EINPLVVTKD GVYVLDLAAK VDATADYICK VKWGDIEFPP PFGREAYPEE
260 270 280 290 300
AYIADLDAKS GASLKLTLLN PKGRIWTMVA GGGASVVYSD TICDLGGVNE
310 320 330 340 350
LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPDGKILII GGSIANFTNV
360 370 380 390 400
AATFKGIVRA IRDYQGPLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI
410 420 430 440 450
PIHVFGTETH MTAIVGMALG HRPIPNQPPT AAHTANFLLN ASGSTSTPAP
460 470 480 490 500
SRTASFSESR ADEVAPAKKA KPAMPQDSVP SPRSLQGKST TLFSRHTKAI
510 520 530 540 550
VWGMQTRAVQ GMLDFDYVCS RDEPSVAAMV YPFTGDHKQK FYWGHKEILI
560 570 580 590 600
PVFKNMADAM RKHPEVDVLI NFASLRSAYD STMETMNYAQ IRTIAIIAEG
610 620 630 640 650
IPEALTRKLI KKADQKGVTI IGPATVGGIK PGCFKIGNTG GMLDNILASK
660 670 680 690 700
LYRPGSVAYV SRSGGMSNEL NNIISRTTDG VYEGVAIGGD RYPGSTFMDH
710 720 730 740 750
VLRYQDTPGV KMIVVLGEIG GTEEYKICRG IKEGRLTKPI VCWCIGTCAT
760 770 780 790 800
MFSSEVQFGH AGACANQASE TAVAKNQALK EAGVFVPRSF DELGEIIQSV
810 820 830 840 850
YEDLVANGVI VPAQEVPPPT VPMDYSWARE LGLIRKPASF MTSICDERGQ
860 870 880 890 900
ELIYAGMPIT EVFKEEMGIG GVLGLLWFQK RLPKYSCQFI EMCLMVTADH
910 920 930 940 950
GPAVSGAHNT IICARAGKDL VSSLTSGLLT IGDRFGGALD AAAKMFSKAF
960 970 980 990 1000
DSGIIPMEFV NKMKKEGKLI MGIGHRVKSI NNPDMRVQIL KDYVRQHFPA
1010 1020 1030 1040 1050
TPLLDYALEV EKITTSKKPN LILNVDGLIG VAFVDMLRNC GSFTREEADE
1060 1070 1080 1090 1100
YIDIGALNGI FVLGRSMGFI GHYLDQKRLK QGLYRHPWDD ISYVLPEHMS

M
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. 43 interactions.
IntActi P53396. 8 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.
GeneTreei ENSGT00530000063275.
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

Bgeei P53396.
CleanExi HS_ACLY.
ExpressionAtlasi P53396. baseline and differential.
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

« Hide 'large scale' publications
  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. "Phosphorylation of recombinant human ATP:citrate lyase by cAMP-dependent protein kinase abolishes homotropic allosteric regulation of the enzyme by citrate and increases the enzyme activity. Allosteric activation of ATP:citrate lyase by phosphorylated sugars."
    Potapova I.A., El-Maghrabi M.R., Doronin S.V., Benjamin W.B.
    Biochemistry 39:1169-1179(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, PHOSPHORYLATION.
  7. Cited for: ISGYLATION.
  8. "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].
  9. "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.
  10. "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.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  12. "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.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455; SER-481 AND SER-1100, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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].
  15. 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].
  16. "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.
  17. "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].
  18. "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.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "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].
  21. "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.
  22. "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.
  23. "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 29, 2014
This is version 157 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