CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013904
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nucleoporin NUP188 homolog 
Protein Synonyms/Alias
 hNup188 
Gene Name
 NUP188 
Gene Synonyms/Alias
 KIAA0169 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
38QIEAELNKHWRRLLEacetylation[1]
38QIEAELNKHWRRLLEubiquitination[2]
51LEGLSYYKPPSPSSAubiquitination[2]
62PSSAEKVKANKDVASubiquitination[2]
65AEKVKANKDVASPLKubiquitination[2]
72KDVASPLKELGLRISubiquitination[2]
109RGTRDSVKTVLQDERubiquitination[2, 3, 4, 5, 6]
164EYADCVDKLEKELVSubiquitination[2, 6]
167DCVDKLEKELVSKYRubiquitination[2, 6]
172LEKELVSKYRQQFEEubiquitination[2]
182QQFEELYKTEAPTWEubiquitination[3]
240LVLTKMFKEQGFGSRubiquitination[2, 3, 6]
344ETSSVVRKIGGTAIQubiquitination[7, 8, 9, 10]
470KVYSFLDKMSFYNELubiquitination[2, 7, 10]
479SFYNELYKHKPHDVIubiquitination[7, 10]
481YNELYKHKPHDVISHubiquitination[2, 3, 6, 7, 9, 10]
500LWRRQTPKLLYPLGGubiquitination[2, 3, 6, 7, 9, 10, 11]
566IQHCQRVKPIIDLVHubiquitination[2, 3, 6]
628LAARNPAKVWTDLRHubiquitination[2, 3, 6, 9]
720EMLPSYHKWRYNSHGubiquitination[2, 7, 10]
812GQGQLLIKTVKLAFSubiquitination[2, 3, 6, 7, 9, 10, 11, 12]
862LAKYIYHKHDPALPRubiquitination[2, 3, 6]
876RLAIQLLKRLATVAPubiquitination[2, 3, 7, 10, 11]
908FLTRLQSKIEDMRIKubiquitination[3]
1262LGSATEDKDSMETDDubiquitination[2]
1291VLGLHLAKELCEVDEubiquitination[3]
1386QTPSASRKSLDAPSWubiquitination[2, 3]
1409SLMEQLLKTLRYNFLacetylation[13]
1409SLMEQLLKTLRYNFLubiquitination[2, 3, 9]
1496TSLLHSRKMLQHYLQubiquitination[2, 6, 11]
1505LQHYLQNKNGDGLPSubiquitination[2, 6]
1533SAAPSSSKQPAADTEubiquitination[3, 12]
1684PRDKQRMKQELSSELubiquitination[2]
1721VLPSPQGKSTSLSKAubiquitination[2, 3, 6]
1727GKSTSLSKASPESQEubiquitination[2, 4, 5, 9]
Reference
 [1] 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]
 [2] 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]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [7] 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]
 [8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [9] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [10] 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]
 [11] 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]
 [12] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [13] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 May function as a component of the nuclear pore complex (NPC). 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 1709 1709 Phosphoserine.
 MOD_RES 1717 1717 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Translocation; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1749 AA 
Protein Sequence
MAAAAGGPCV RSSRELWTIL LGRSALRELS QIEAELNKHW RRLLEGLSYY KPPSPSSAEK 60
VKANKDVASP LKELGLRISK FLGLDEEQSV QLLQCYLQED YRGTRDSVKT VLQDERQSQA 120
LILKIADYYY EERTCILRCV LHLLTYFQDE RHPYRVEYAD CVDKLEKELV SKYRQQFEEL 180
YKTEAPTWET HGNLMTERQV SRWFVQCLRE QSMLLEIIFL YYAYFEMAPS DLLVLTKMFK 240
EQGFGSRQTN RHLVDETMDP FVDRIGYFSA LILVEGMDIE SLHKCALDDR RELHQFAQDG 300
LICQDMDCLM LTFGDIPHHA PVLLAWALLR HTLNPEETSS VVRKIGGTAI QLNVFQYLTR 360
LLQSLASGGN DCTTSTACMC VYGLLSFVLT SLELHTLGNQ QDIIDTACEV LADPSLPELF 420
WGTEPTSGLG IILDSVCGMF PHLLSPLLQL LRALVSGKST AKKVYSFLDK MSFYNELYKH 480
KPHDVISHED GTLWRRQTPK LLYPLGGQTN LRIPQGTVGQ VMLDDRAYLV RWEYSYSSWT 540
LFTCEIEMLL HVVSTADVIQ HCQRVKPIID LVHKVISTDL SIADCLLPIT SRIYMLLQRL 600
TTVISPPVDV IASCVNCLTV LAARNPAKVW TDLRHTGFLP FVAHPVSSLS QMISAEGMNA 660
GGYGNLLMNS EQPQGEYGVT IAFLRLITTL VKGQLGSTQS QGLVPCVMFV LKEMLPSYHK 720
WRYNSHGVRE QIGCLILELI HAILNLCHET DLHSSHTPSL QFLCICSLAY TEAGQTVINI 780
MGIGVDTIDM VMAAQPRSDG AEGQGQGQLL IKTVKLAFSV TNNVIRLKPP SNVVSPLEQA 840
LSQHGAHGNN LIAVLAKYIY HKHDPALPRL AIQLLKRLAT VAPMSVYACL GNDAAAIRDA 900
FLTRLQSKIE DMRIKVMILE FLTVAVETQP GLIELFLNLE VKDGSDGSKE FSLGMWSCLH 960
AVLELIDSQQ QDRYWCPPLL HRAAIAFLHA LWQDRRDSAM LVLRTKPKFW ENLTSPLFGT 1020
LSPPSETSEP SILETCALIM KIICLEIYYV VKGSLDQSLK DTLKKFSIEK RFAYWSGYVK 1080
SLAVHVAETE GSSCTSLLEY QMLVSAWRML LIIATTHADI MHLTDSVVRR QLFLDVLDGT 1140
KALLLVPASV NCLRLGSMKC TLLLILLRQW KRELGSVDEI LGPLTEILEG VLQADQQLME 1200
KTKAKVFSAF ITVLQMKEMK VSDIPQYSQL VLNVCETLQE EVIALFDQTR HSLALGSATE 1260
DKDSMETDDC SRSRHRDQRD GVCVLGLHLA KELCEVDEDG DSWLQVTRRL PILPTLLTTL 1320
EVSLRMKQNL HFTEATLHLL LTLARTQQGA TAVAGAGITQ SICLPLLSVY QLSTNGTAQT 1380
PSASRKSLDA PSWPGVYRLS MSLMEQLLKT LRYNFLPEAL DFVGVHQERT LQCLNAVRTV 1440
QSLACLEEAD HTVGFILQLS NFMKEWHFHL PQLMRDIQVN LGYLCQACTS LLHSRKMLQH 1500
YLQNKNGDGL PSAVAQRVQR PPSAASAAPS SSKQPAADTE ASEQQALHTV QYGLLKILSK 1560
TLAALRHFTP DVCQILLDQS LDLAEYNFLF ALSFTTPTFD SEVAPSFGTL LATVNVALNM 1620
LGELDKKKEP LTQAVGLSTQ AEGTRTLKSL LMFTMENCFY LLISQAMRYL RDPAVHPRDK 1680
QRMKQELSSE LSTLLSSLSR YFRRGAPSSP ATGVLPSPQG KSTSLSKASP ESQEPLIQLV 1740
QAFVRHMQR 1749 
Gene Ontology
 GO:0005635; C:nuclear envelope; TAS:Reactome.
 GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
 GO:0005975; P:carbohydrate metabolic process; TAS:Reactome.
 GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
 GO:0015758; P:glucose transport; TAS:Reactome.
 GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0010827; P:regulation of glucose transport; TAS:Reactome.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0055085; P:transmembrane transport; TAS:Reactome.
 GO:0022415; P:viral reproductive process; TAS:Reactome. 
Interpro
 IPR018864; Nucleoporin_Nup188. 
Pfam
 PF10487; Nup188 
SMART
  
PROSITE
  
PRINTS