CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008205
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nuclear pore complex protein Nup153 
Protein Synonyms/Alias
 153 kDa nucleoporin; Nucleoporin Nup153 
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
48SRVTESVKNIVPGWLubiquitination[1, 2]
200DKDITVSKNTSLPPLubiquitination[2, 3]
227QHTATSSKKPAFNLSubiquitination[2]
263DSPFYPGKTTYGGAAubiquitination[1, 2, 3]
294VRRQMKAKQLSAQSYubiquitination[2]
317RILQSLEKMSSPLADubiquitination[3]
384TNRSVYFKPSLTPSGacetylation[4]
384TNRSVYFKPSLTPSGubiquitination[1]
460RTRFVASKPLEEEEMacetylation[5]
460RTRFVASKPLEEEEMubiquitination[3]
613GSVLDILKSPGFASPubiquitination[3]
702TGIETPNKSGKTTLSubiquitination[2]
718SGTGFGDKFKPVIGTacetylation[4]
886PGTKSGFKGFDTSSSubiquitination[2, 3]
925LTSTGNFKFGDQGGFubiquitination[2, 3]
933FGDQGGFKIGVSSDSubiquitination[2]
954SEGFKFSKPIGDFKFacetylation[4]
954SEGFKFSKPIGDFKFubiquitination[1, 3]
960SKPIGDFKFGVSSESubiquitination[1]
968FGVSSESKPEEVKKDubiquitination[3]
973ESKPEEVKKDSKNDNubiquitination[3]
982DSKNDNFKFGLSSGLubiquitination[3]
1010SNLGQEEKKEELPKSubiquitination[2, 3]
1011NLGQEEKKEELPKSSubiquitination[3]
1071TCKTSEAKKEEMPATubiquitination[2]
1079KEEMPATKGGFSFGNubiquitination[2]
1106VLGRTEEKQQEPVTSubiquitination[3]
1120STSLVFGKKADNEEPacetylation[4]
1120STSLVFGKKADNEEPubiquitination[1, 2, 3]
1148TKDENSSKSTFSFSMubiquitination[1, 2, 3]
1157TFSFSMTKPSEKESEubiquitination[2, 3]
1161SMTKPSEKESEQPAKubiquitination[2, 3]
1168KESEQPAKATFAFGAubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [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] 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] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
Functional Description
 Component of the nuclear pore complex (NPC), a complex required for the trafficking across the nuclear envelope. Functions as a scaffolding element in the nuclear phase of the NPC essential for normal nucleocytoplasmic transport of proteins and mRNAs. Involved in the quality control and retention of unspliced mRNAs in the nucleus; in association with TPR, regulates the nuclear export of unspliced mRNA species bearing constitutive transport element (CTE) in a NXF1- and KHDRBS1-independent manner. Mediates TPR anchoring to the nuclear membrane at NPC. The repeat- containing domain may be involved in anchoring other components of the NPC to the pore membrane. Possible DNA-binding subunit of the nuclear pore complex (NPC). 
Sequence Annotation
 ZN_FING 657 687 RanBP2-type 1.
 ZN_FING 722 751 RanBP2-type 2.
 ZN_FING 793 822 RanBP2-type 3.
 ZN_FING 851 880 RanBP2-type 4.
 METAL 664 664 Zinc 1 (By similarity).
 METAL 667 667 Zinc 1 (By similarity).
 METAL 678 678 Zinc 1 (By similarity).
 METAL 681 681 Zinc 1 (By similarity).
 METAL 728 728 Zinc 2.
 METAL 731 731 Zinc 2.
 METAL 742 742 Zinc 2.
 METAL 745 745 Zinc 2.
 METAL 799 799 Zinc 3 (By similarity).
 METAL 802 802 Zinc 3 (By similarity).
 METAL 813 813 Zinc 3 (By similarity).
 METAL 816 816 Zinc 3 (By similarity).
 METAL 857 857 Zinc 4 (By similarity).
 METAL 860 860 Zinc 4 (By similarity).
 METAL 871 871 Zinc 4 (By similarity).
 METAL 874 874 Zinc 4 (By similarity).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 192 192 Phosphoserine.
 MOD_RES 209 209 Phosphoserine.
 MOD_RES 240 240 Phosphoserine.
 MOD_RES 257 257 Phosphoserine.
 MOD_RES 330 330 Phosphoserine.
 MOD_RES 334 334 Phosphoserine.
 MOD_RES 338 338 Phosphoserine.
 MOD_RES 343 343 Phosphoserine.
 MOD_RES 369 369 Phosphothreonine.
 MOD_RES 384 384 N6-acetyllysine.
 MOD_RES 500 500 Phosphoserine.
 MOD_RES 516 516 Phosphoserine.
 MOD_RES 522 522 Phosphoserine.
 MOD_RES 529 529 Phosphoserine.
 MOD_RES 588 588 Phosphothreonine.
 MOD_RES 614 614 Phosphoserine.
 MOD_RES 619 619 Phosphoserine.
 MOD_RES 633 633 Phosphoserine.
 MOD_RES 687 687 Phosphoserine.
 MOD_RES 718 718 N6-acetyllysine.
 MOD_RES 954 954 N6-acetyllysine.
 MOD_RES 1457 1457 Phosphoserine.
 MOD_RES 1463 1463 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; DNA-binding; Host-virus interaction; Membrane; Metal-binding; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Repeat; Translocation; Transport; Viral penetration into host nucleus; Virus entry into host cell; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1475 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 PLEEEEMEVP VLPKISLPIT 480
SSSLPTFNFS SPEITTSSPS PINSSQALTN KVQMTSPSST GSPMFKFSSP IVKSTEANVL 540
PPSSIGFTFS VPVAKTAELS GSSSTLEPII SSSAHHVTTV NSTNCKKTPP EDCEGPFRPA 600
EILKEGSVLD ILKSPGFASP KIDSVAAQPT ATSPVVYTRP AISSFSSSGI GFGESLKAGS 660
SWQCDTCLLQ NKVTDNKCIA CQAAKLSPRD TAKQTGIETP NKSGKTTLSA SGTGFGDKFK 720
PVIGTWDCDT CLVQNKPEAI KCVACETPKP GTCVKRALTL TVVSESAETM TASSSSCTVT 780
TGTLGFGDKF KRPIGSWECS VCCVSNNAED NKCVSCMSEK PGSSVPASSS STVPVSLPSG 840
GSLGLEKFKK PEGSWDCELC LVQNKADSTK CLACESAKPG TKSGFKGFDT SSSSSNSAAS 900
SSFKFGVSSS SSGPSQTLTS TGNFKFGDQG GFKIGVSSDS GSINPMSEGF KFSKPIGDFK 960
FGVSSESKPE EVKKDSKNDN FKFGLSSGLS NPVSLTPFQF GVSNLGQEEK KEELPKSSSA 1020
GFSFGTGVIN STPAPANTIV TSENKSSFNL GTIETKSASV APFTCKTSEA KKEEMPATKG 1080
GFSFGNVEPA SLPSASVFVL GRTEEKQQEP VTSTSLVFGK KADNEEPKCQ PVFSFGNSEQ 1140
TKDENSSKST FSFSMTKPSE KESEQPAKAT FAFGAQTSTT ADQGAAKPVF SFLNNSSSSS 1200
STPATSAGGG IFGSSTSSSN PPVATFVFGQ SSNPVSSSAF GNTAESSTSQ SLLFSQDSKL 1260
ATTSSTGTAV TPFVFGPGAS SNNTTTSGFG FGATTTSSSA GSSFVFGTGP SAPSASPAFG 1320
ANQTPTFGQS QGASQPNPPG FGSISSSTAL FPTGSQPAPP TFGTVSSSSQ PPVFGQQPSQ 1380
SAFGSGTTPN SSSAFQFGSS TTNFNFTNNS PSGVFTFGAN SSTPAASAQP SGSGGFPFNQ 1440
SPAAFTVGSN GKNVFSSSGT SFSGRKIKTA VRRRK 1475 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0042405; C:nuclear inclusion body; IDA:UniProtKB.
 GO:0031965; C:nuclear membrane; IDA:UniProtKB.
 GO:0034399; C:nuclear periphery; IDA:UniProtKB.
 GO:0044615; C:nuclear pore nuclear basket; IDA:UniProtKB.
 GO:0005730; C:nucleolus; IDA:HPA.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0005487; F:nucleocytoplasmic transporter activity; IDA:UniProtKB.
 GO:0043495; F:protein anchor; IMP:UniProtKB.
 GO:0017056; F:structural constituent of nuclear pore; IMP:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 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:0046832; P:negative regulation of RNA export from nucleus; IDA:UniProtKB.
 GO:0051292; P:nuclear pore complex assembly; IMP:UniProtKB.
 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:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
 GO:0075732; P:viral penetration into host nucleus; IEA:UniProtKB-KW.
 GO:0022415; P:viral reproductive process; TAS:Reactome. 
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