CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023119
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Apoptotic chromatin condensation inducer in the nucleus 
Protein Synonyms/Alias
 Acinus 
Gene Name
 ACIN1 
Gene Synonyms/Alias
 ACINUS; KIAA0670 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MWRRKHPRTSGGubiquitination[1, 2]
103SALVKRLKGALMLENubiquitination[3]
143FIKQYLEKQQELLRQubiquitination[3]
302SREAPILKEFKEEGEubiquitination[3]
359LARQQQEKEMKTTSPacetylation[4]
532SAQPLPLKIEELALAsumoylation[5]
548GITEECLKQPSLEQKubiquitination[6]
654SASSNSRKSLSPGVSmethylation[7, 8]
717SQPESAEKHVTQRLQacetylation[4]
823LPKSFKRKISVVSATubiquitination[3, 6]
831ISVVSATKGVPAGNSubiquitination[3]
861STATTQKKPSISITTubiquitination[3]
1209AQEEPPAKLLDDLFRubiquitination[9]
Reference
 [1] Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry.
 Denis NJ, Vasilescu J, Lambert JP, Smith JC, Figeys D.
 Proteomics. 2007 Mar;7(6):868-74. [PMID: 17370265]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [6] 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]
 [7] Protein lysine methyltransferase G9a acts on non-histone targets.
 Rathert P, Dhayalan A, Murakami M, Zhang X, Tamas R, Jurkowska R, Komatsu Y, Shinkai Y, Cheng X, Jeltsch A.
 Nat Chem Biol. 2008 Jun;4(6):344-6. [PMID: 18438403]
 [8] Update on activities at the Universal Protein Resource (UniProt) in 2013.
 e="String">UniProt Consortium.
 Nucleic Acids Res. 2013 Jan;41(Database issue):D43-7. [PMID: 23161681]
 [9] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865] 
Functional Description
 Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Induces apoptotic chromatin condensation after activation by CASP3. Regulates cyclin A1, but not cyclin A2, expression in leukemia cells. 
Sequence Annotation
 DOMAIN 72 106 SAP.
 MOD_RES 166 166 Phosphoserine.
 MOD_RES 169 169 Phosphoserine.
 MOD_RES 208 208 Phosphoserine.
 MOD_RES 210 210 Phosphoserine.
 MOD_RES 216 216 Phosphoserine.
 MOD_RES 240 240 Phosphoserine.
 MOD_RES 243 243 Phosphoserine.
 MOD_RES 254 254 Phosphothreonine.
 MOD_RES 269 269 Phosphothreonine.
 MOD_RES 295 295 Phosphoserine.
 MOD_RES 326 326 Phosphothreonine.
 MOD_RES 328 328 Phosphoserine.
 MOD_RES 365 365 Phosphoserine.
 MOD_RES 384 384 Phosphoserine.
 MOD_RES 386 386 Phosphoserine.
 MOD_RES 388 388 Phosphoserine.
 MOD_RES 393 393 Phosphothreonine.
 MOD_RES 400 400 Phosphoserine.
 MOD_RES 410 410 Phosphoserine.
 MOD_RES 414 414 Phosphothreonine.
 MOD_RES 434 434 Phosphoserine.
 MOD_RES 453 453 Phosphoserine.
 MOD_RES 478 478 Phosphoserine.
 MOD_RES 490 490 Phosphoserine.
 MOD_RES 512 512 Phosphotyrosine.
 MOD_RES 561 561 Phosphoserine.
 MOD_RES 654 654 N6,N6,N6-trimethyllysine; by EHMT2;
 MOD_RES 654 654 N6,N6-dimethyllysine; by EHMT2;
 MOD_RES 655 655 Phosphoserine.
 MOD_RES 657 657 Phosphoserine.
 MOD_RES 682 682 Phosphothreonine.
 MOD_RES 710 710 Phosphoserine.
 MOD_RES 714 714 Phosphoserine.
 MOD_RES 717 717 N6-acetyllysine.
 MOD_RES 720 720 Phosphothreonine.
 MOD_RES 729 729 Phosphoserine.
 MOD_RES 825 825 Phosphoserine.
 MOD_RES 838 838 Phosphoserine.
 MOD_RES 840 840 Phosphothreonine (By similarity).
 MOD_RES 895 895 Phosphoserine.
 MOD_RES 898 898 Phosphoserine.
 MOD_RES 987 987 Phosphoserine.
 MOD_RES 990 990 Phosphoserine.
 MOD_RES 1004 1004 Phosphoserine.
 MOD_RES 1180 1180 Phosphoserine; by SRPK2 and PKB/AKT1.
 MOD_RES 1329 1329 Phosphoserine (By similarity).
 MOD_RES 1331 1331 Phosphoserine (By similarity).
 MOD_RES 1332 1332 Phosphothreonine (By similarity).
 CROSSLNK 5 5 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Alternative splicing; Apoptosis; Complete proteome; Direct protein sequencing; Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1341 AA 
Protein Sequence
MWRRKHPRTS GGTRGVLSGN RGVEYGSGRG HLGTFEGRWR KLPKMPEAVG TDPSTSRKMA 60
ELEEVTLDGK PLQALRVTDL KAALEQRGLA KSGQKSALVK RLKGALMLEN LQKHSTPHAA 120
FQPNSQIGEE MSQNSFIKQY LEKQQELLRQ RLEREAREAA ELEEASAESE DEMIHPEGVA 180
SLLPPDFQSS LERPELELSR HSPRKSSSIS EEKGDSDDEK PRKGERRSSR VRQARAAKLS 240
EGSQPAEEEE DQETPSRNLR VRADRNLKTE EEEEEEEEEE EDDEEEEGDD EGQKSREAPI 300
LKEFKEEGEE IPRVKPEEMM DERPKTRSQE QEVLERGGRF TRSQEEARKS HLARQQQEKE 360
MKTTSPLEEE EREIKSSQGL KEKSKSPSPP RLTEDRKKAS LVALPEQTAS EEETPPPLLT 420
KEASSPPPHP QLHSEEEIEP MEGPAPAVLI QLSPPNTDAD TRELLVSQHT VQLVGGLSPL 480
SSPSDTKAES PAEKVPEESV LPLVQKSTLA DYSAQKDLEP ESDRSAQPLP LKIEELALAK 540
GITEECLKQP SLEQKEGRRA SHTLLPSHRL KQSADSSSSR SSSSSSSSSR SRSRSPDSSG 600
SRSHSPLRSK QRDVAQARTH ANPRGRPKMG SRSTSESRSR SRSRSRSASS NSRKSLSPGV 660
SRDSSTSYTE TKDPSSGQEV ATPPVPQLQV CEPKERTSTS SSSVQARRLS QPESAEKHVT 720
QRLQPERGSP KKCEAEEAEP PAATQPQTSE TQTSHLPESE RIHHTVEEKE EVTMDTSENR 780
PENDVPEPPM PIADQVSNDD RPEGSVEDEE KKESSLPKSF KRKISVVSAT KGVPAGNSDT 840
EGGQPGRKRR WGASTATTQK KPSISITTES LKSLIPDIKP LAGQEAVVDL HADDSRISED 900
ETERNGDDGT HDKGLKICRT VTQVVPAEGQ ENGQREEEEE EKEPEAEPPV PPQVSVEVAL 960
PPPAEHEVKK VTLGDTLTRR SISQQKSGVS ITIDDPVRTA QVPSPPRGKI SNIVHISNLV 1020
RPFTLGQLKE LLGRTGTLVE EAFWIDKIKS HCFVTYSTVE EAVATRTALH GVKWPQSNPK 1080
FLCADYAEQD ELDYHRGLLV DRPSETKTEE QGIPRPLHPP PPPPVQPPQH PRAEQREQER 1140
AVREQWAERE REMERRERTR SEREWDRDKV REGPRSRSRS RDRRRKERAK SKEKKSEKKE 1200
KAQEEPPAKL LDDLFRKTKA APCIYWLPLT DSQIVQKEAE RAERAKEREK RRKEQEEEEQ 1260
KEREKEAERE RNRQLEREKR REHSRERDRE RERERERDRG DRDRDRERDR ERGRERDRRD 1320
TKRHSRSRSR STPVRDRGGR R 1341 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0016887; F:ATPase activity; NAS:UniProtKB.
 GO:0019899; F:enzyme binding; NAS:UniProtKB.
 GO:0003676; F:nucleic acid binding; NAS:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:InterPro.
 GO:0030263; P:apoptotic chromosome condensation; IDA:UniProtKB.
 GO:0030218; P:erythrocyte differentiation; IEP:UniProtKB.
 GO:0045657; P:positive regulation of monocyte differentiation; IEP:UniProtKB. 
Interpro
 IPR012677; Nucleotide-bd_a/b_plait.
 IPR000504; RRM_dom.
 IPR003034; SAP_dom. 
Pfam
 PF02037; SAP 
SMART
 SM00360; RRM
 SM00513; SAP 
PROSITE
 PS50800; SAP 
PRINTS