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Protein

ATP-citrate synthase

Gene

ACLY

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

Functioni

ATP-citrate synthase 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

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)DescriptionActionsGraphical viewLength
Binding sitei58ATP1
Binding sitei118ATP1
Metal bindingi201MagnesiumBy similarity1
Metal bindingi203MagnesiumBy similarity1
Binding sitei346Citrate; via amide nitrogen1 Publication1
Binding sitei348Citrate1 Publication1
Binding sitei379Citrate1 Publication1
Metal bindingi718MagnesiumBy similarity1
Active sitei760Tele-phosphohistidine intermediateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi66 – 67ATP2
Nucleotide bindingi109 – 111ATP3
Nucleotide bindingi701 – 721ATPBy similarityAdd BLAST21
Nucleotide bindingi752 – 778ATPBy similarityAdd BLAST27

GO - Molecular functioni

  • ATP binding Source: BHF-UCL
  • ATP citrate synthase activity Source: UniProtKB
  • cofactor binding Source: InterPro
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • acetyl-CoA biosynthetic process Source: BHF-UCL
  • cholesterol biosynthetic process Source: BHF-UCL
  • citrate metabolic process Source: BHF-UCL
  • fatty acid biosynthetic process Source: GO_Central
  • lipid biosynthetic process Source: UniProtKB
  • long-chain fatty-acyl-CoA biosynthetic process Source: Reactome
  • oxaloacetate metabolic process Source: BHF-UCL
  • positive regulation of cellular metabolic 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.
ZFISH:HS05535-MONOMER.
BRENDAi2.3.3.8. 2681.
ReactomeiR-HSA-163765. ChREBP activates metabolic gene expression.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-75105. Fatty Acyl-CoA Biosynthesis.
SABIO-RKP53396.
SIGNORiP53396.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:115. ACLY.

Subcellular locationi

GO - Cellular componenti

  • citrate lyase complex Source: GO_Central
  • cytoplasm Source: HPA
  • cytosol Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi540K → R or Q: Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-546 and R,Q-554. 1 Publication1
Mutagenesisi546K → R or Q: Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-540 and R,Q-554. 1 Publication1
Mutagenesisi554K → R or Q: Decreased acetylation and increased de novo lipid synthesis; when associated with R,Q-540 and R,Q-546. 1 Publication1

Organism-specific databases

DisGeNETi47.
OpenTargetsiENSG00000131473.
PharmGKBiPA24441.

Chemistry databases

ChEMBLiCHEMBL3720.

Polymorphism and mutation databases

BioMutaiACLY.
DMDMi116241237.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001027811 – 1101ATP-citrate synthaseAdd BLAST1101

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei131PhosphotyrosineCombined sources1
Modified residuei263PhosphoserineBy similarity1
Modified residuei447PhosphothreonineBy similarity1
Modified residuei451PhosphoserineBy similarity1
Modified residuei455Phosphoserine; by PKA and PKB/AKT1 or PKB/AKT2Combined sources1
Modified residuei459PhosphoserineCombined sources1
Modified residuei481PhosphoserineCombined sources1
Modified residuei540N6-acetyllysine; alternate1 Publication1
Cross-linki540Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei546N6-acetyllysine; alternateCombined sources1 Publication1
Cross-linki546Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei554N6-acetyllysine; alternateCombined sources1 Publication1
Cross-linki554Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei639PhosphothreonineCombined sources1
Modified residuei663PhosphoserineCombined sources1
Modified residuei682PhosphotyrosineCombined sources1
Modified residuei839PhosphoserineCombined sources1
Modified residuei948N6-acetyllysineCombined sources1
Modified residuei968N6-acetyllysineCombined sources1
Modified residuei978N6-acetyllysineBy similarity1
Modified residuei1077N6-acetyllysineCombined sources1
Modified residuei1100PhosphoserineCombined sources1

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 SIRT2.1 Publication
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).1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP53396.
MaxQBiP53396.
PaxDbiP53396.
PeptideAtlasiP53396.
PRIDEiP53396.

PTM databases

iPTMnetiP53396.
PhosphoSitePlusiP53396.
SwissPalmiP53396.

Expressioni

Gene expression databases

BgeeiENSG00000131473.
CleanExiHS_ACLY.
ExpressionAtlasiP53396. baseline and differential.
GenevisibleiP53396. HS.

Organism-specific databases

HPAiCAB007783.
HPA022434.
HPA022953.
HPA022959.
HPA028758.

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

BioGridi106563. 60 interactors.
IntActiP53396. 13 interactors.
MINTiMINT-3019895.
STRINGi9606.ENSP00000253792.

Chemistry databases

BindingDBiP53396.

Structurei

Secondary structure

11101
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 6Combined sources4
Helixi8 – 18Combined sources11
Beta strandi32 – 34Combined sources3
Helixi40 – 46Combined sources7
Helixi48 – 51Combined sources4
Beta strandi55 – 59Combined sources5
Turni66 – 70Combined sources5
Beta strandi73 – 76Combined sources4
Helixi78 – 85Combined sources8
Turni86 – 90Combined sources5
Beta strandi92 – 95Combined sources4
Beta strandi98 – 101Combined sources4
Beta strandi105 – 109Combined sources5
Helixi115 – 117Combined sources3
Beta strandi118 – 126Combined sources9
Beta strandi129 – 137Combined sources9
Helixi140 – 142Combined sources3
Helixi145 – 148Combined sources4
Beta strandi149 – 155Combined sources7
Helixi162 – 167Combined sources6
Turni168 – 172Combined sources5
Turni175 – 177Combined sources3
Helixi178 – 194Combined sources17
Beta strandi197 – 208Combined sources12
Beta strandi211 – 214Combined sources4
Beta strandi217 – 222Combined sources6
Helixi223 – 225Combined sources3
Helixi226 – 233Combined sources8
Beta strandi242 – 244Combined sources3
Helixi248 – 258Combined sources11
Beta strandi260 – 269Combined sources10
Beta strandi274 – 277Combined sources4
Helixi282 – 294Combined sources13
Helixi298 – 300Combined sources3
Beta strandi303 – 309Combined sources7
Helixi313 – 326Combined sources14
Beta strandi336 – 340Combined sources5
Beta strandi346 – 348Combined sources3
Helixi350 – 363Combined sources14
Helixi365 – 370Combined sources6
Beta strandi373 – 378Combined sources6
Helixi384 – 398Combined sources15
Beta strandi402 – 405Combined sources4
Helixi413 – 418Combined sources6
Beta strandi499 – 503Combined sources5
Helixi506 – 518Combined sources13
Beta strandi525 – 530Combined sources6
Beta strandi536 – 543Combined sources8
Beta strandi546 – 555Combined sources10
Helixi556 – 562Combined sources7
Beta strandi568 – 571Combined sources4
Turni575 – 577Combined sources3
Helixi578 – 585Combined sources8
Beta strandi593 – 596Combined sources4
Helixi603 – 616Combined sources14
Beta strandi619 – 621Combined sources3
Beta strandi628 – 630Combined sources3
Turni631 – 633Combined sources3
Turni637 – 640Combined sources4
Helixi643 – 648Combined sources6
Turni649 – 652Combined sources4
Beta strandi656 – 662Combined sources7
Helixi664 – 677Combined sources14
Beta strandi681 – 686Combined sources6
Beta strandi689 – 692Combined sources4
Helixi697 – 705Combined sources9
Beta strandi712 – 722Combined sources11
Helixi723 – 732Combined sources10
Beta strandi740 – 745Combined sources6
Helixi768 – 770Combined sources3
Helixi772 – 781Combined sources10
Helixi790 – 792Combined sources3
Helixi793 – 806Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MWDX-ray2.10A1-425[»]
B487-820[»]
3MWEX-ray2.20A1-425[»]
B487-821[»]
3PFFX-ray2.30A1-817[»]
ProteinModelPortaliP53396.
SMRiP53396.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53396.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 265ATP-graspAdd BLAST262

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni779 – 789CoA-bindingSequence analysisAdd BLAST11

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

eggNOGiKOG1254. Eukaryota.
COG0045. LUCA.
COG0074. LUCA.
COG0372. LUCA.
GeneTreeiENSGT00530000063275.
HOGENOMiHOG000151479.
HOVERGENiHBG003318.
InParanoidiP53396.
KOiK01648.
OMAiEGRVWTM.
OrthoDBiEOG091G0OYH.
PhylomeDBiP53396.
TreeFamiTF300560.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 2 hits.
3.40.50.720. 1 hit.
InterProiIPR014608. ATP-citrate_synthase.
IPR013816. ATP_grasp_subdomain_2.
IPR017440. Cit_synth/succinyl-CoA_lig_AS.
IPR032263. Citrate-bd.
IPR016142. Citrate_synth-like_lrg_a-sub.
IPR016143. Citrate_synth-like_sm_a-sub.
IPR002020. Citrate_synthase.
IPR033847. Citrt_syn/SCS-alpha_CS.
IPR003781. CoA-bd.
IPR005811. CoA_ligase.
IPR016040. NAD(P)-bd_dom.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PfamiPF16114. Citrate_bind. 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.
SMARTiSM00881. CoA_binding. 1 hit.
[Graphical view]
SUPFAMiSSF48256. SSF48256. 2 hits.
SSF51735. SSF51735. 1 hit.
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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

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
Isoform 3 (identifier: P53396-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     95-355: Missing.
     476-485: Missing.

Note: No experimental confirmation available.
Show »
Length:830
Mass (Da):91,099
Checksum:i1F3758EEAACA3730
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti75N → D in CAA45614 (PubMed:1371749).Curated1
Sequence conflicti111V → A in CAA45614 (PubMed:1371749).Curated1
Sequence conflicti245E → V in CAA45614 (PubMed:1371749).Curated1
Sequence conflicti419 – 423LGHRP → WAPA in CAA45614 (PubMed:1371749).Curated5
Sequence conflicti442 – 444SGS → QRE in CAA45614 (PubMed:1371749).Curated3
Sequence conflicti457 – 459SES → YESMVDEV in CAA45614 (PubMed:1371749).Curated3
Sequence conflicti653 – 656RPGS → PQAA in CAA45614 (PubMed:1371749).Curated4
Sequence conflicti728C → S in CAA45614 (PubMed:1371749).Curated1
Sequence conflicti872V → A in CAA45614 (PubMed:1371749).Curated1
Sequence conflicti916 – 919AGKD → TAVE in CAA45614 (PubMed:1371749).Curated4

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_028230175E → D.3 PublicationsCorresponds to variant rs2304497dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_05723095 – 355Missing in isoform 3. 1 PublicationAdd BLAST261
Alternative sequenceiVSP_042201476 – 485Missing in isoform 2 and isoform 3. 1 Publication10

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64330 mRNA. Translation: CAA45614.1.
U18197 mRNA. Translation: AAB60340.1.
AK295675 mRNA. Translation: BAG58532.1.
AK304802 mRNA. Translation: BAG65552.1.
AC091172 Genomic DNA. No translation available.
AC125257 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_001290203.1. NM_001303274.1.
NP_001290204.1. NM_001303275.1.
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]
ENST00000537919; ENSP00000445349; ENSG00000131473. [P53396-3]
ENST00000590151; ENSP00000466259; ENSG00000131473. [P53396-1]
GeneIDi47.
KEGGihsa:47.
UCSCiuc002hyg.4. human. [P53396-1]

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:
EMBLi
GenBanki
DDBJi
Links Updated
X64330 mRNA. Translation: CAA45614.1.
U18197 mRNA. Translation: AAB60340.1.
AK295675 mRNA. Translation: BAG58532.1.
AK304802 mRNA. Translation: BAG65552.1.
AC091172 Genomic DNA. No translation available.
AC125257 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_001290203.1. NM_001303274.1.
NP_001290204.1. NM_001303275.1.
NP_942127.1. NM_198830.1. [P53396-2]
XP_005257452.1. XM_005257395.1. [P53396-1]
UniGeneiHs.387567.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MWDX-ray2.10A1-425[»]
B487-820[»]
3MWEX-ray2.20A1-425[»]
B487-821[»]
3PFFX-ray2.30A1-817[»]
ProteinModelPortaliP53396.
SMRiP53396.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106563. 60 interactors.
IntActiP53396. 13 interactors.
MINTiMINT-3019895.
STRINGi9606.ENSP00000253792.

Chemistry databases

BindingDBiP53396.
ChEMBLiCHEMBL3720.

PTM databases

iPTMnetiP53396.
PhosphoSitePlusiP53396.
SwissPalmiP53396.

Polymorphism and mutation databases

BioMutaiACLY.
DMDMi116241237.

Proteomic databases

EPDiP53396.
MaxQBiP53396.
PaxDbiP53396.
PeptideAtlasiP53396.
PRIDEiP53396.

Protocols and materials databases

DNASUi47.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000352035; ENSP00000253792; ENSG00000131473. [P53396-1]
ENST00000353196; ENSP00000345398; ENSG00000131473. [P53396-2]
ENST00000393896; ENSP00000377474; ENSG00000131473. [P53396-2]
ENST00000537919; ENSP00000445349; ENSG00000131473. [P53396-3]
ENST00000590151; ENSP00000466259; ENSG00000131473. [P53396-1]
GeneIDi47.
KEGGihsa:47.
UCSCiuc002hyg.4. human. [P53396-1]

Organism-specific databases

CTDi47.
DisGeNETi47.
GeneCardsiACLY.
HGNCiHGNC:115. ACLY.
HPAiCAB007783.
HPA022434.
HPA022953.
HPA022959.
HPA028758.
MIMi108728. gene.
neXtProtiNX_P53396.
OpenTargetsiENSG00000131473.
PharmGKBiPA24441.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1254. Eukaryota.
COG0045. LUCA.
COG0074. LUCA.
COG0372. LUCA.
GeneTreeiENSGT00530000063275.
HOGENOMiHOG000151479.
HOVERGENiHBG003318.
InParanoidiP53396.
KOiK01648.
OMAiEGRVWTM.
OrthoDBiEOG091G0OYH.
PhylomeDBiP53396.
TreeFamiTF300560.

Enzyme and pathway databases

BioCyciMetaCyc:HS05535-MONOMER.
ZFISH:HS05535-MONOMER.
BRENDAi2.3.3.8. 2681.
ReactomeiR-HSA-163765. ChREBP activates metabolic gene expression.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-75105. Fatty Acyl-CoA Biosynthesis.
SABIO-RKP53396.
SIGNORiP53396.

Miscellaneous databases

ChiTaRSiACLY. human.
EvolutionaryTraceiP53396.
GenomeRNAii47.
PROiP53396.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000131473.
CleanExiHS_ACLY.
ExpressionAtlasiP53396. baseline and differential.
GenevisibleiP53396. HS.

Family and domain databases

Gene3Di1.10.230.10. 1 hit.
1.10.580.10. 1 hit.
3.30.470.20. 1 hit.
3.40.50.261. 2 hits.
3.40.50.720. 1 hit.
InterProiIPR014608. ATP-citrate_synthase.
IPR013816. ATP_grasp_subdomain_2.
IPR017440. Cit_synth/succinyl-CoA_lig_AS.
IPR032263. Citrate-bd.
IPR016142. Citrate_synth-like_lrg_a-sub.
IPR016143. Citrate_synth-like_sm_a-sub.
IPR002020. Citrate_synthase.
IPR033847. Citrt_syn/SCS-alpha_CS.
IPR003781. CoA-bd.
IPR005811. CoA_ligase.
IPR016040. NAD(P)-bd_dom.
IPR017866. Succ-CoA_synthase_bsu_CS.
IPR016102. Succinyl-CoA_synth-like.
[Graphical view]
PfamiPF16114. Citrate_bind. 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.
SMARTiSM00881. CoA_binding. 1 hit.
[Graphical view]
SUPFAMiSSF48256. SSF48256. 2 hits.
SSF51735. SSF51735. 1 hit.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiACLY_HUMAN
AccessioniPrimary (citable) accession number: P53396
Secondary accession number(s): B4DIM0
, B4E3P0, Q13037, Q9BRL0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 17, 2006
Last modified: November 30, 2016
This is version 181 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

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 one 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.