Details for: ACLY
Associated with
Other Information
Genular Protein ID: 632920189
Symbol: ACLY_HUMAN
Name: ATP-citrate synthase
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 1371749
Title: Cloning and expression of a human ATP-citrate lyase cDNA.
PubMed ID: 1371749
PubMed ID: 9116495
Title: Variant cDNA sequences of human ATP:citrate lyase: cloning, expression, and purification from baculovirus-infected insect cells.
PubMed ID: 9116495
PubMed ID: 14702039
Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.
PubMed ID: 14702039
DOI: 10.1038/ng1285
PubMed ID: 16625196
Title: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.
PubMed ID: 16625196
DOI: 10.1038/nature04689
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 10653665
Title: 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.
PubMed ID: 10653665
DOI: 10.1021/bi992159y
PubMed ID: 16139798
Title: Proteomic identification of proteins conjugated to ISG15 in mouse and human cells.
PubMed ID: 16139798
PubMed ID: 15592455
Title: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.
PubMed ID: 15592455
DOI: 10.1038/nbt1046
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 17924679
Title: 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.
PubMed ID: 17924679
DOI: 10.1021/pr070152u
PubMed ID: 18088087
PubMed ID: 18691976
Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
PubMed ID: 18691976
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19286649
Title: A novel direct homogeneous assay for ATP citrate lyase.
PubMed ID: 19286649
PubMed ID: 19369195
Title: Large-scale proteomics analysis of the human kinome.
PubMed ID: 19369195
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 23932781
Title: Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth.
PubMed ID: 23932781
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 27664236
Title: Cullin3-KLHL25 ubiquitin ligase targets ACLY for degradation to inhibit lipid synthesis and tumor progression.
PubMed ID: 27664236
PubMed ID: 29779826
Title: The BCKDH Kinase and Phosphatase Integrate BCAA and Lipid Metabolism via Regulation of ATP-Citrate Lyase.
PubMed ID: 29779826
PubMed ID: 34491895
Title: ACLY ubiquitination by CUL3-KLHL25 induces the reprogramming of fatty acid metabolism to facilitate iTreg differentiation.
PubMed ID: 34491895
DOI: 10.7554/elife.62394
PubMed ID: 20558738
Title: Identification of the citrate-binding site of human ATP-citrate lyase using X-ray crystallography.
PubMed ID: 20558738
PubMed ID: 22102020
Title: ADP-Mg2+ bound to the ATP-grasp domain of ATP-citrate lyase.
PubMed ID: 22102020
Sequence Information:
- Length: 1101
- Mass: 120839
- Checksum: 12BB4416A30DC30C
- Sequence:
MSAKAISEQT GKELLYKFIC TTSAIQNRFK YARVTPDTDW ARLLQDHPWL LSQNLVVKPD QLIKRRGKLG LVGVNLTLDG VKSWLKPRLG QEATVGKATG FLKNFLIEPF VPHSQAEEFY VCIYATREGD YVLFHHEGGV DVGDVDAKAQ KLLVGVDEKL NPEDIKKHLL VHAPEDKKEI LASFISGLFN FYEDLYFTYL EINPLVVTKD GVYVLDLAAK VDATADYICK VKWGDIEFPP PFGREAYPEE AYIADLDAKS GASLKLTLLN PKGRIWTMVA GGGASVVYSD TICDLGGVNE LANYGEYSGA PSEQQTYDYA KTILSLMTRE KHPDGKILII GGSIANFTNV AATFKGIVRA IRDYQGPLKE HEVTIFVRRG GPNYQEGLRV MGEVGKTTGI PIHVFGTETH MTAIVGMALG HRPIPNQPPT AAHTANFLLN ASGSTSTPAP SRTASFSESR ADEVAPAKKA KPAMPQDSVP SPRSLQGKST TLFSRHTKAI VWGMQTRAVQ GMLDFDYVCS RDEPSVAAMV YPFTGDHKQK FYWGHKEILI PVFKNMADAM RKHPEVDVLI NFASLRSAYD STMETMNYAQ IRTIAIIAEG IPEALTRKLI KKADQKGVTI IGPATVGGIK PGCFKIGNTG GMLDNILASK LYRPGSVAYV SRSGGMSNEL NNIISRTTDG VYEGVAIGGD RYPGSTFMDH VLRYQDTPGV KMIVVLGEIG GTEEYKICRG IKEGRLTKPI VCWCIGTCAT MFSSEVQFGH AGACANQASE TAVAKNQALK EAGVFVPRSF DELGEIIQSV YEDLVANGVI VPAQEVPPPT VPMDYSWARE LGLIRKPASF MTSICDERGQ ELIYAGMPIT EVFKEEMGIG GVLGLLWFQK RLPKYSCQFI EMCLMVTADH GPAVSGAHNT IICARAGKDL VSSLTSGLLT IGDRFGGALD AAAKMFSKAF DSGIIPMEFV NKMKKEGKLI MGIGHRVKSI NNPDMRVQIL KDYVRQHFPA TPLLDYALEV EKITTSKKPN LILNVDGLIG VAFVDMLRNC GSFTREEADE YIDIGALNGI FVLGRSMGFI GHYLDQKRLK QGLYRHPWDD ISYVLPEHMS M
Genular Protein ID: 267288009
Symbol: Q4LE36_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Sequence Information:
- Length: 1137
- Mass: 124557
- Checksum: E634EE8F9AEDB882
- Sequence:
LPAAGVLRIL RGSSGLWKKR RARTSAETGR AGLSAAMSAK AISEQTGKEL LYKFICTTSA IQNRFKYARV TPDTDWARLL QDHPWLLSQN LVVKPDQLIK RRGKLGLVGV NLTLDGVKSW LKPRLGQEAT VGKATGFLKN FLIEPFVPHS QAEEFYVCIY ATREGDYVLF HHEGGVDVGD VDAKAQKLLV GVDEKLNPED IKKHLLVHAP EDKKEILASF ISGLFNFYED LYFTYLEINP LVVTKDGVYV LDLAAKVDAT ADYICKVKWG DIEFPPPFGR EAYPEEAYIA DLDAKSGASL KLTLLNPKGR IWTMVAGGGA SVVYSDTICD LGGVNELANY GEYSGAPSEQ QTYDYAKTIL SLMTREKHPD GKILIIGGSI ANFTNVAATF KGIVRAIRDY QGPLKEHEVT IFVRRGGPNY QEGLRVMGEV GKTTGIPIHV FGTETHMTAI VGMALGHRPI PNQPPTAAHT ANFLLNASGS TSTPAPSRTA SFSESRADEV APAKKAKPAM PQDSVPSPRS LQGKSTTLFS RHTKAIVWGM QTRAVQGMLD FDYVCSRDEP SVAAMVYPFT GDHKQKFYWG HKEILIPVFK NMADAMRKHP EVDVLINFAS LRSAYDSTME TMNYAQIRTI AIIAEGIPEA LTRKLIKKAD QKGVTIIGPA TVGGIKPGCF KIGNTGGMLD NILASKLYRP GSVAYVSRSG GMSNELNNII SRTTDGVYEG VAIGGDRYPG STFMDHVLRY QDTPGVKMIV VLGEIGGTEE YKICRGIKEG RLTKPIVCWC IGTCATMFSS EVQFGHAGAC ANQASETAVA KNQALKEAGV FVPRSFDELG EIIQSVYEDL VANGVIVPAQ EVPPPTVPMD YSWARELGLI RKPASFMTSI CDERGQELIY AGMPITEVFK EEMGIGGVLG LLWFQKRLPK YSCQFIEMCL MVTADHGPAV SGAHNTIICA RAGKDLVSSL TSGLLTIGDR FGGALDAAAK MFSKAFDSGI IPMEFVNKMK KEGKLIMGIG HRVKSINNPD MRVQILKDYV RQHFPATPLL DYALEVEKIT TSKKPNLILN VDGLIGVAFV DMLRNCGSFT REEADEYIDI GALNGIFVLG RSMGFIGHYL DQKRLKQGLY RHPWDDISYV LPEHMSM
Database document:
This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.