CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-040114
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Nuclear pore complex protein Nup153 
Protein Synonyms/Alias
  
Gene Name
 NUP153 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
15VGGGGGGKIRTRRCHubiquitination[1, 2, 3]
27RCHQGPIKPYQQGRQacetylation[3]
48SRVTESVKNIVPGWLubiquitination[1, 2, 3, 4, 5]
170FSLVKEIKDSTSQHDubiquitination[2]
194FSSRASDKDITVSKNacetylation[3]
200DKDITVSKNTSLPPLubiquitination[2, 5, 6]
227QHTATSSKKPAFNLSubiquitination[5]
250LGNSSILKTSQLGDSubiquitination[7]
263DSPFYPGKTTYGGAAubiquitination[2, 3, 4, 5, 6]
294VRRQMKAKQLSAQSYubiquitination[3, 5]
317RILQSLEKMSSPLADubiquitination[6]
353DITDFQAKREKVDSQubiquitination[2]
384TNRSVYFKPSLTPSGacetylation[3, 8]
384TNRSVYFKPSLTPSGubiquitination[2, 4]
644GSVLDILKSPGFASPubiquitination[2, 3, 6]
733TGIETPNKSGKTTLSubiquitination[5]
896ELCLVQNKADSTKCLubiquitination[7]
917PGTKSGFKGFDTSSSubiquitination[2, 5, 6]
956LTSTGNFKFGDQGGFubiquitination[5, 6]
964FGDQGGFKIGVSSDSubiquitination[5]
985SEGFKFSKPIGDFKFacetylation[8]
985SEGFKFSKPIGDFKFubiquitination[3, 4, 6]
991SKPIGDFKFGVSSESubiquitination[4]
999FGVSSESKPEEVKKDubiquitination[6]
1004ESKPEEVKKDSKNDNubiquitination[6]
1013DSKNDNFKFGLSSGLubiquitination[6]
1041SNLGQEEKKEELPKSubiquitination[5, 6]
1087NLGTIETKSASVAPFubiquitination[3, 7]
1097SVAPFTCKTSEAKKEubiquitination[2]
1102TCKTSEAKKEEMPATubiquitination[5]
1110KEEMPATKGGFSFGNubiquitination[5]
1137VLGRTEEKQQEPVTSubiquitination[6]
1151STSLVFGKKADNEEPubiquitination[4, 5, 6]
1179TKDENSSKSTFSFSMubiquitination[4, 5, 6]
1188TFSFSMTKPSEKESEubiquitination[5, 6]
1192SMTKPSEKESEQPAKubiquitination[5, 6]
1199KESEQPAKATFAFGAubiquitination[5]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1506 AA 
Protein Sequence
MASGAGGVGG GGGGKIRTRR CHQGPIKPYQ QGRQQHQGIL SRVTESVKNI VPGWLQRYFN 60
KNEDVCSCST DTSEVPRWPE NKEDHLVYAD EESSNITDGR ITPEPAVSNT EEPSTTSTAS 120
NYPDVLTRPS LHRSHLNFSM LESPALHCQP STSSAFPIGS SGFSLVKEIK DSTSQHDDDN 180
ISTTSGFSSR ASDKDITVSK NTSLPPLWSP EAERSHSLSQ HTATSSKKPA FNLSAFGTLS 240
PSLGNSSILK TSQLGDSPFY PGKTTYGGAA AAVRQSKLRN TPYQAPVRRQ MKAKQLSAQS 300
YGVTSSTARR ILQSLEKMSS PLADAKRIPS IVSSPLNSPL DRSGIDITDF QAKREKVDSQ 360
YPPVQRLMTP KPVSIATNRS VYFKPSLTPS GEFRKTNQRI DNKCSTGYEK NMTPGQNREQ 420
RESGFSYPNF SLPAANGLSS GVGGGGGKMR RERTRFVASK PLEEERQGLT VLPKLISSSC 480
AQAIIPSWPL KVLRLQEMEV PVLPKISLPI TSSSLPTFNF SSPEITTSSP SPINSSQALT 540
NKVQMTSPSS TGSPMFKFSS PIVKSTEANV LPPSSIGFTF SVPVAKTAEL SGSSSTLEPI 600
ISSSAHHVTT VNSTNCKKTP PEDCEGPFRP AEILKEGSVL DILKSPGFAS PKIDSVAAQP 660
TATSPVVYTR PAISSFSSSG IGFGESLKAG SSWQCDTCLL QNKVTDNKCI ACQAAKLSPR 720
DTAKQTGIET PNKSGKTTLS ASGTGFGDKF KPVIGTWDCD TCLVQNKPEA IKCVACETPK 780
PGTCVKRALT LTVVSESAET MTASSSSCTV TTGTLGFGDK FKRPIGSWEC SVCCVSNNAE 840
DNKCVSCMSE KPGSSVPASS SSTVPVSLPS GGSLGLEKFK KPEGSWDCEL CLVQNKADST 900
KCLACESAKP GTKSGFKGFD TSSSSSNSAA SSSFKFGVSS SSSGPSQTLT STGNFKFGDQ 960
GGFKIGVSSD SGSINPMSEG FKFSKPIGDF KFGVSSESKP EEVKKDSKND NFKFGLSSGL 1020
SNPVSLTPFQ FGVSNLGQEE KKEELPKSSS AGFSFGTGVI NSTPAPANTI VTSENKSSFN 1080
LGTIETKSAS VAPFTCKTSE AKKEEMPATK GGFSFGNVEP ASLPSASVFV LGRTEEKQQE 1140
PVTSTSLVFG KKADNEEPKC QPVFSFGNSE QTKDENSSKS TFSFSMTKPS EKESEQPAKA 1200
TFAFGAQTST TADQGAAKPV FSFLNNSSSS SSTPATSAGG GIFGSSTSSS NPPVATFVFG 1260
QSSNPVSSSA FGNTAESSTS QSLLFSQDSK LATTSSTGTA VTPFVFGPGA SSNNTTTSGF 1320
GFGATTTSSS AGSSFVFGTG PSAPSASPAF GANQTPTFGQ SQGASQPNPP GFGSISSSTA 1380
LFPTGSQPAP PTFGTVSSSS QPPVFGQQPS QSAFGSGTTP NSSSAFQFGS STTNFNFTNN 1440
SPSGVFTFGA NSSTPAASAQ PSGSGGFPFN QSPAAFTVGS NGKNVFSSSG TSFSGRKIKT 1500
AVRRRK 1506 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0031965; C:nuclear membrane; IDA:HPA.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR026054; Nucleoporin.
 IPR013913; Nucleoporin_Nup153.
 IPR018892; Retro-transposon_transp_CS.
 IPR001876; Znf_RanBP2. 
Pfam
 PF08604; Nup153
 PF10599; Nup_retrotrp_bd
 PF00641; zf-RanBP 
SMART
 SM00547; ZnF_RBZ 
PROSITE
 PS01358; ZF_RANBP2_1
 PS50199; ZF_RANBP2_2 
PRINTS