CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-025614
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ACLY variant protein 
Protein Synonyms/Alias
  
Gene Name
 ACLY variant protein 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
40LSAAMSAKAISEQTGubiquitination[1]
48AISEQTGKELLYKFIubiquitination[1, 2]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965
Functional Description
  
Sequence Annotation
  
Keyword
  
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1137 AA 
Protein Sequence
LPAAGVLRIL RGSSGLWKKR RARTSAETGR AGLSAAMSAK AISEQTGKEL LYKFICTTSA 60
IQNRFKYARV TPDTDWARLL QDHPWLLSQN LVVKPDQLIK RRGKLGLVGV NLTLDGVKSW 120
LKPRLGQEAT VGKATGFLKN FLIEPFVPHS QAEEFYVCIY ATREGDYVLF HHEGGVDVGD 180
VDAKAQKLLV GVDEKLNPED IKKHLLVHAP EDKKEILASF ISGLFNFYED LYFTYLEINP 240
LVVTKDGVYV LDLAAKVDAT ADYICKVKWG DIEFPPPFGR EAYPEEAYIA DLDAKSGASL 300
KLTLLNPKGR IWTMVAGGGA SVVYSDTICD LGGVNELANY GEYSGAPSEQ QTYDYAKTIL 360
SLMTREKHPD GKILIIGGSI ANFTNVAATF KGIVRAIRDY QGPLKEHEVT IFVRRGGPNY 420
QEGLRVMGEV GKTTGIPIHV FGTETHMTAI VGMALGHRPI PNQPPTAAHT ANFLLNASGS 480
TSTPAPSRTA SFSESRADEV APAKKAKPAM PQDSVPSPRS LQGKSTTLFS RHTKAIVWGM 540
QTRAVQGMLD FDYVCSRDEP SVAAMVYPFT GDHKQKFYWG HKEILIPVFK NMADAMRKHP 600
EVDVLINFAS LRSAYDSTME TMNYAQIRTI AIIAEGIPEA LTRKLIKKAD QKGVTIIGPA 660
TVGGIKPGCF KIGNTGGMLD NILASKLYRP GSVAYVSRSG GMSNELNNII SRTTDGVYEG 720
VAIGGDRYPG STFMDHVLRY QDTPGVKMIV VLGEIGGTEE YKICRGIKEG RLTKPIVCWC 780
IGTCATMFSS EVQFGHAGAC ANQASETAVA KNQALKEAGV FVPRSFDELG EIIQSVYEDL 840
VANGVIVPAQ EVPPPTVPMD YSWARELGLI RKPASFMTSI CDERGQELIY AGMPITEVFK 900
EEMGIGGVLG LLWFQKRLPK YSCQFIEMCL MVTADHGPAV SGAHNTIICA RAGKDLVSSL 960
TSGLLTIGDR FGGALDAAAK MFSKAFDSGI IPMEFVNKMK KEGKLIMGIG HRVKSINNPD 1020
MRVQILKDYV RQHFPATPLL DYALEVEKIT TSKKPNLILN VDGLIGVAFV DMLRNCGSFT 1080
REEADEYIDI GALNGIFVLG RSMGFIGHYL DQKRLKQGLY RHPWDDISYV LPEHMSM 1137 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0003878; F:ATP citrate synthase activity; IEA:InterPro.
 GO:0048037; F:cofactor binding; IEA:InterPro.
 GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:InterPro.
 GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro. 
Interpro
 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. 
Pfam
 PF08442; ATP-grasp_2
 PF00285; Citrate_synt
 PF02629; CoA_binding
 PF00549; Ligase_CoA 
SMART
  
PROSITE
 PS01216; SUCCINYL_COA_LIG_1
 PS00399; SUCCINYL_COA_LIG_2
 PS01217; SUCCINYL_COA_LIG_3 
PRINTS