P53396 (ACLY_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

ACLY

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1101 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Catalytic activity	ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Post-translational modification	ISGylated. Ref.7
Sequence similarities	In the N-terminal section; belongs to the succinate/malate CoA ligase beta subunit family. In the C-terminal section; belongs to the succinate/malate CoA ligase alpha subunit family.

Ontologies

Keywords
Biological process	Lipid synthesis
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Transferase
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	ATP catabolic process Traceable author statement. Source: ProtInc cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro citrate metabolic process Traceable author statement. Source: ProtInc coenzyme A metabolic process Traceable author statement. Source: ProtInc energy reserve metabolic process Traceable author statement. Source: Reactome long-chain fatty-acyl-CoA biosynthetic process Traceable author statement. Source: Reactome positive regulation of cellular metabolic process Traceable author statement. Source: Reactome triglyceride biosynthetic process Traceable author statement. Source: Reactome
Cellular component	citrate lyase complex Traceable author statement. Source: ProtInc cytosol Traceable author statement. Source: Reactome nucleus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP citrate synthase activity Traceable author statement. Source: ProtInc citrate (pro-3S)-lyase activity Traceable author statement. Source: Reactome metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW succinate-CoA ligase (ADP-forming) activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P53396-1)

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.

Isoform 2 (identifier: P53396-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1101

1101

ATP-citrate synthase

PRO_0000102781

Regions

Nucleotide binding

701 – 721

21

ATP By similarity

Nucleotide binding

752 – 778

27

ATP By similarity

Region

779 – 789

11

CoA-binding Potential

Sites

Active site

760

1

Tele-phosphohistidine intermediate By similarity

Metal binding

718

1

Magnesium By similarity

Binding site

346

1

Citrate; via amide nitrogen

Binding site

348

1

Citrate

Binding site

379

1

Citrate

Amino acid modifications

Modified residue

86

1

N6-acetyllysine Ref.17

Modified residue

131

1

Phosphotyrosine Ref.8

Modified residue

260

1

Phosphoserine Ref.15

Modified residue

442

1

Phosphoserine Ref.15

Modified residue

445

1

Phosphothreonine Ref.15

Modified residue

447

1

Phosphothreonine Ref.15

Modified residue

453

1

Phosphothreonine Ref.15

Modified residue

455

1

Phosphoserine; by PKA and PKB/AKT1 or PKB/AKT2 Ref.6 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15

Modified residue

478

1

Phosphoserine Ref.15

Modified residue

481

1

Phosphoserine Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16

Modified residue

546

1

N6-acetyllysine Ref.17

Modified residue

554

1

N6-acetyllysine Ref.17

Modified residue

639

1

Phosphothreonine Ref.15

Modified residue

663

1

Phosphoserine Ref.15

Modified residue

682

1

Phosphotyrosine Ref.8 Ref.15 Ref.16

Modified residue

839

1

Phosphoserine Ref.15

Modified residue

922

1

Phosphoserine Ref.15

Modified residue

948

1

N6-acetyllysine Ref.17

Modified residue

962

1

N6-acetyllysine Ref.17

Modified residue

968

1

N6-acetyllysine Ref.17

Modified residue

978

1

N6-acetyllysine Ref.17

Modified residue

979

1

Phosphoserine Ref.15

Modified residue

1077

1

N6-acetyllysine Ref.17

Modified residue

1100

1

Phosphoserine Ref.14 Ref.15

Natural variations

Alternative sequence

476 – 485

10

Missing in isoform 2.

VSP_042201

Natural variant

175

1

E → D. Ref.1 Ref.2
Corresponds to variant rs2304497 [ dbSNP | Ensembl ].

VAR_028230

Experimental info

Sequence conflict

75

1

N → D in CAA45614. Ref.1

Sequence conflict

111

1

V → A in CAA45614. Ref.1

Sequence conflict

245

1

E → V in CAA45614. Ref.1

Sequence conflict

419 – 423

5

LGHRP → WAPA in CAA45614. Ref.1

Sequence conflict

442 – 444

3

SGS → QRE in CAA45614. Ref.1

Sequence conflict

457 – 459

3

SES → YESMVDEV in CAA45614. Ref.1

Sequence conflict

653 – 656

4

RPGS → PQAA in CAA45614. Ref.1

Sequence conflict

728

1

C → S in CAA45614. Ref.1

Sequence conflict

872

1

V → A in CAA45614. Ref.1

Sequence conflict

916 – 919

4

AGKD → TAVE in CAA45614. Ref.1

Secondary structure

1

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1101

Helix Strand Turn

Details...

Beta strand

3 – 6

4

Helix

13 – 18

6

Beta strand

32 – 34

3

Helix

40 – 46

7

Helix

48 – 51

4

Beta strand

55 – 59

5

Helix

82 – 85

4

Turn

86 – 88

3

Beta strand

105 – 109

5

Helix

115 – 117

3

Beta strand

118 – 124

7

Beta strand

131 – 135

5

Helix

145 – 148

4

Beta strand

149 – 153

5

Helix

162 – 167

6

Turn

168 – 172

5

Turn

175 – 177

3

Helix

178 – 185

8

Helix

189 – 194

6

Beta strand

197 – 206

10

Beta strand

217 – 222

6

Helix

223 – 225

3

Helix

226 – 229

4

Turn

230 – 232

3

Helix

248 – 258

11

Beta strand

263 – 269

7

Beta strand

275 – 277

3

Helix

285 – 294

10

Beta strand

306 – 308

3

Helix

313 – 326

14

Beta strand

337 – 340

4

Beta strand

346 – 348

3

Helix

350 – 354

5

Helix

358 – 363

6

Turn

368 – 372

5

Beta strand

374 – 378

5

Beta strand

402 – 405

4

Helix

411 – 414

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 17, 2006. Version 3. Checksum: 12BB4416A30DC30C	FASTA	1,101	120,839
	10 20 30 40 50 60 MSAKAISEQT GKELLYKFIC TTSAIQNRFK YARVTPDTDW ARLLQDHPWL LSQNLVVKPD 70 80 90 100 110 120 QLIKRRGKLG LVGVNLTLDG VKSWLKPRLG QEATVGKATG FLKNFLIEPF VPHSQAEEFY 130 140 150 160 170 180 VCIYATREGD YVLFHHEGGV DVGDVDAKAQ KLLVGVDEKL NPEDIKKHLL VHAPEDKKEI 190 200 210 220 230 240 LASFISGLFN FYEDLYFTYL EINPLVVTKD GVYVLDLAAK VDATADYICK VKWGDIEFPP 250 260 270 280 290 300 PFGREAYPEE AYIADLDAKS GASLKLTLLN PKGRIWTMVA GGGASVVYSD TICDLGGVNE 310 320 330 340 350 360 LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPDGKILII GGSIANFTNV AATFKGIVRA 370 380 390 400 410 420 IRDYQGPLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI PIHVFGTETH MTAIVGMALG 430 440 450 460 470 480 HRPIPNQPPT AAHTANFLLN ASGSTSTPAP SRTASFSESR ADEVAPAKKA KPAMPQDSVP 490 500 510 520 530 540 SPRSLQGKST TLFSRHTKAI VWGMQTRAVQ GMLDFDYVCS RDEPSVAAMV YPFTGDHKQK 550 560 570 580 590 600 FYWGHKEILI PVFKNMADAM RKHPEVDVLI NFASLRSAYD STMETMNYAQ IRTIAIIAEG 610 620 630 640 650 660 IPEALTRKLI KKADQKGVTI IGPATVGGIK PGCFKIGNTG GMLDNILASK LYRPGSVAYV 670 680 690 700 710 720 SRSGGMSNEL NNIISRTTDG VYEGVAIGGD RYPGSTFMDH VLRYQDTPGV KMIVVLGEIG 730 740 750 760 770 780 GTEEYKICRG IKEGRLTKPI VCWCIGTCAT MFSSEVQFGH AGACANQASE TAVAKNQALK 790 800 810 820 830 840 EAGVFVPRSF DELGEIIQSV YEDLVANGVI VPAQEVPPPT VPMDYSWARE LGLIRKPASF 850 860 870 880 890 900 MTSICDERGQ ELIYAGMPIT EVFKEEMGIG GVLGLLWFQK RLPKYSCQFI EMCLMVTADH 910 920 930 940 950 960 GPAVSGAHNT IICARAGKDL VSSLTSGLLT IGDRFGGALD AAAKMFSKAF DSGIIPMEFV 970 980 990 1000 1010 1020 NKMKKEGKLI MGIGHRVKSI NNPDMRVQIL KDYVRQHFPA TPLLDYALEV EKITTSKKPN 1030 1040 1050 1060 1070 1080 LILNVDGLIG VAFVDMLRNC GSFTREEADE YIDIGALNGI FVLGRSMGFI GHYLDQKRLK 1090 1100 QGLYRHPWDD ISYVLPEHMS M
	Isoform 2 [UniParc]. Checksum: 04EB8D05059409E5	FASTA	1,091	119,772
	10 20 30 40 50 60 MSAKAISEQT GKELLYKFIC TTSAIQNRFK YARVTPDTDW ARLLQDHPWL LSQNLVVKPD 70 80 90 100 110 120 QLIKRRGKLG LVGVNLTLDG VKSWLKPRLG QEATVGKATG FLKNFLIEPF VPHSQAEEFY 130 140 150 160 170 180 VCIYATREGD YVLFHHEGGV DVGDVDAKAQ KLLVGVDEKL NPEDIKKHLL VHAPEDKKEI 190 200 210 220 230 240 LASFISGLFN FYEDLYFTYL EINPLVVTKD GVYVLDLAAK VDATADYICK VKWGDIEFPP 250 260 270 280 290 300 PFGREAYPEE AYIADLDAKS GASLKLTLLN PKGRIWTMVA GGGASVVYSD TICDLGGVNE 310 320 330 340 350 360 LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPDGKILII GGSIANFTNV AATFKGIVRA 370 380 390 400 410 420 IRDYQGPLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI PIHVFGTETH MTAIVGMALG 430 440 450 460 470 480 HRPIPNQPPT AAHTANFLLN ASGSTSTPAP SRTASFSESR ADEVAPAKKA KPAMPQGKST 490 500 510 520 530 540 TLFSRHTKAI VWGMQTRAVQ GMLDFDYVCS RDEPSVAAMV YPFTGDHKQK FYWGHKEILI 550 560 570 580 590 600 PVFKNMADAM RKHPEVDVLI NFASLRSAYD STMETMNYAQ IRTIAIIAEG IPEALTRKLI 610 620 630 640 650 660 KKADQKGVTI IGPATVGGIK PGCFKIGNTG GMLDNILASK LYRPGSVAYV SRSGGMSNEL 670 680 690 700 710 720 NNIISRTTDG VYEGVAIGGD RYPGSTFMDH VLRYQDTPGV KMIVVLGEIG GTEEYKICRG 730 740 750 760 770 780 IKEGRLTKPI VCWCIGTCAT MFSSEVQFGH AGACANQASE TAVAKNQALK EAGVFVPRSF 790 800 810 820 830 840 DELGEIIQSV YEDLVANGVI VPAQEVPPPT VPMDYSWARE LGLIRKPASF MTSICDERGQ 850 860 870 880 890 900 ELIYAGMPIT EVFKEEMGIG GVLGLLWFQK RLPKYSCQFI EMCLMVTADH GPAVSGAHNT 910 920 930 940 950 960 IICARAGKDL VSSLTSGLLT IGDRFGGALD AAAKMFSKAF DSGIIPMEFV NKMKKEGKLI 970 980 990 1000 1010 1020 MGIGHRVKSI NNPDMRVQIL KDYVRQHFPA TPLLDYALEV EKITTSKKPN LILNVDGLIG 1030 1040 1050 1060 1070 1080 VAFVDMLRNC GSFTREEADE YIDIGALNGI FVLGRSMGFI GHYLDQKRLK QGLYRHPWDD 1090 ISYVLPEHMS M

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of a human ATP-citrate lyase cDNA." Elshourbagy N.A., Near J.C., Kmetz P.J., Wells T.N.C., Groot P.H.E., Saxty B.A., Hughes S.A., Franklin M., Gloger I.S. Eur. J. Biochem. 204:491-499(1992) [PubMed: 1371749] [Abstract] 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: 9116495] [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: 14702039] [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: 16625196] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Lymph.
[6]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells." Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E. Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed: 16139798] [Abstract] 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: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-131 AND TYR-682, MASS SPECTROMETRY.
[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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455 AND SER-481, MASS SPECTROMETRY. 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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455 AND SER-481, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, MASS SPECTROMETRY. Tissue: Platelet.
[13]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455 AND SER-481, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455; SER-481 AND SER-1100, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260; SER-442; THR-445; THR-447; THR-453; SER-455; SER-478; SER-481; THR-639; SER-663; TYR-682; SER-839; SER-922; SER-979 AND SER-1100, MASS SPECTROMETRY.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481 AND TYR-682, MASS SPECTROMETRY. 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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-86; LYS-546; LYS-554; LYS-948; LYS-962; LYS-968; LYS-978 AND LYS-1077, MASS SPECTROMETRY.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"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: 20558738] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-425 AND 487-820 IN COMPLEX WITH CITRATE, CITRATE-BINDING SITES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00021290.
IPI00394838.

PIR

S21173.

RefSeq

NP_001087.2. NM_001096.2.
NP_942127.1. NM_198830.1.

UniGene

Hs.387567.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P53396.

SMR

P53396. Positions 2-425, 487-820, 875-1085.

ModBase

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Protein-protein interaction databases

IntAct

P53396. 3 interactions.

MINT

MINT-3019895.

STRING

P53396.

PTM databases

PhosphoSite

P53396.

Polymorphism databases

DMDM

116241237.

Proteomic databases

PeptideAtlas

P53396.

PRIDE

P53396.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000352035; ENSP00000253792; ENSG00000131473.

GeneID

47.

KEGG

hsa:47.

UCSC

uc002hyg.1. human.

Organism-specific databases

CTD

47.

GeneCards

GC17M040023.

H-InvDB

HIX0013825.

HGNC

HGNC:115. ACLY.

HPA

CAB007783.
HPA022434.
HPA022953.
HPA022959.
HPA028758.

MIM

108728. gene.

neXtProt

NX_P53396.

PharmGKB

PA24441.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG06313.

GeneTree

ENSGT00530000063275.

HOVERGEN

HBG003318.

InParanoid

P53396.

OrthoDB

EOG40ZQWS.

PhylomeDB

P53396.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.
REACT_22258. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

P53396.

Bgee

P53396.

CleanEx

HS_ACLY.

Genevestigator

P53396.

GermOnline

ENSG00000131473. Homo sapiens.

Family and domain databases

InterPro

IPR014608. ATP-citrate_synthase.
IPR013650. ATP-grasp_succ-CoA_synth-type.
IPR013816. ATP_grasp_subdomain_2.
IPR017440. Cit_synth/succinyl-CoA_lig_AS.
IPR016142. Citrate_synth-like_lrg_a-sub.
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]

Gene3D

G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
G3DSA:1.10.580.10. Citrate_synthase_lrg_a-sub. 1 hit.
G3DSA:1.10.230.10. Citrate_synthase_sm_a-sub. 1 hit.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
G3DSA:3.40.50.261. Succinyl-CoA_synth-like. 2 hits.

KO

K01648.

Pfam

PF08442. ATP-grasp_2. 1 hit.
PF00285. Citrate_synt. 1 hit.
PF02629. CoA_binding. 1 hit.
PF00549. Ligase_CoA. 1 hit.
[Graphical view]

PIRSF

PIRSF036511. ATP_citrt_syn. 1 hit.

SUPFAM

SSF48256. Citrate_synthase_core. 1 hit.
SSF52210. CoA_ligase. 1 hit.

PROSITE

PS01216. SUCCINYL_COA_LIG_1. 1 hit.
PS00399. SUCCINYL_COA_LIG_2. 1 hit.
PS01217. SUCCINYL_COA_LIG_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

181.

SOURCE

Search...

Entry information

Entry name

ACLY_HUMAN

Accession

Primary (citable) accession number: P53396
Secondary accession number(s): B4DIM0, Q13037, Q9BRL0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 128 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.