CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037411
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Nuclear pore complex protein Nup155 
Protein Synonyms/Alias
  
Gene Name
 NUP155 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
231GRIFLAGKDGCLYEVubiquitination[1]
297ILYTRSEKGVIQVYDubiquitination[1, 2, 3, 4]
404SASSTVEKPSKVHRAubiquitination[3]
407STVEKPSKVHRALYSubiquitination[3]
540EEIERFFKLHQEDQAubiquitination[1, 3]
740GNPNTTAKVQQRLIGubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
766MQQELQRKFHEAQLSubiquitination[1, 2, 3, 8]
775HEAQLSEKISLQAIQubiquitination[1]
838RMLRESLKEYQKISNubiquitination[1, 3, 8]
842ESLKEYQKISNQVDLubiquitination[1, 3]
875LSLTAAEKKDPQGLGubiquitination[1]
876SLTAAEKKDPQGLGLubiquitination[3, 8]
887GLGLHFYKHGEPEEDubiquitination[1, 3]
909QERLNSYKCITDTLQubiquitination[1, 3, 4, 7]
923QELVNQSKAAPQSPSubiquitination[1, 3, 4, 8]
934QSPSVPKKPGPPVLSubiquitination[2]
961HHFEQMLKLSQRSKDubiquitination[1, 3]
1005PHLVRMAKVDQNRVRubiquitination[4]
1062ARAILSAKSSTAISSubiquitination[1, 2, 3, 6]
1083FLHELEEKMEVARIQubiquitination[1, 2, 3, 4, 8]
1133GEFADPFKLAECKLAubiquitination[1, 3, 4, 8]
1244EVYDQLFKSRDPFWNubiquitination[2, 3, 4, 5]
1322NFKSLQAKLERLH**ubiquitination[3, 8]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1327 AA 
Protein Sequence
MPSSLLGAAM PASTSAAALQ EALENAGRLI DRQLQEDRMY PDLSELLMVS APNNPTVSGM 60
SDMDYPLQGP GLLSVPNLPE ISSIRRVPLP PELVEQFGHM QCNCMMGVFP PISRAWLTID 120
SDIFMWNYED GGDLAYFDGL SETILAVGLV KPKAGIFQPH VRHLLVLATP VDIVILGLSY 180
ANLQTGSGVL NDSLSGGMQL LPDPLYSLPT DNTYLLTITS TDNGRIFLAG KDGCLYEVAY 240
QAEAGWFSQR CRKINHSKSS LSFLVPSLLQ FTFSEDDPIL QIAIDNSRNI LYTRSEKGVI 300
QVYDLGQDGQ GMSRVASVSQ NAIVSAAGNI ARTIDRSVFK PIVQIAVIEN SESLDCQLLA 360
VTHAGVRLYF STCPFRQPLA RPNTLTLVHV RLPPGFSASS TVEKPSKVHR ALYSKGILLM 420
AASENEDNDI LWCVNHDTFP FQKPMMETQM TAGVDGHSWA LSAIDELKVD KIITPLNKDH 480
IPITDSPVVV QQHMLPPKKF VLLSAQGSLM FHKLRPVDQL RHLLVSNVGG DGEEIERFFK 540
LHQEDQACAT CLILACSTAA CDREVSAWAT RAFFRYGGEA QMRFPTTLPP PSNVGPILGS 600
PVYSSSPVPS GSPYPNPSFL GTPSHGIQPP AMSTPVCALG NPATQATNMS CVTGPEIVYS 660
GKHNGICIYF SRIMGNIWDA SLVVERIFKS GNREITAIES SVPCQLLESV LQELKGLQEF 720
LDRNSQFAGG PLGNPNTTAK VQQRLIGFMR PENGNPQQMQ QELQRKFHEA QLSEKISLQA 780
IQQLVRKSYQ ALALWKLLCE HQFTIIVAEL QKANELLQRS RQVQNKTEKE RMLRESLKEY 840
QKISNQVDLS NVCAQYRQVR FYEGVVELSL TAAEKKDPQG LGLHFYKHGE PEEDIVGLQA 900
FQERLNSYKC ITDTLQELVN QSKAAPQSPS VPKKPGPPVL SSDPNMLSNE EAGHHFEQML 960
KLSQRSKDEL FSIALYNWLI QVDLADKLLQ VASPFLEPHL VRMAKVDQNR VRYMDLLWRY 1020
YEKNRSFSNA ARVLSRLADM HSTEISLQQR LEYIARAILS AKSSTAISSI AADGEFLHEL 1080
EEKMEVARIQ LQIQETLQRQ YSHHSSVQDA VSQLDSELMD ITKLYGEFAD PFKLAECKLA 1140
IIHCAGYSDP ILVQTLWQDI IEKELSDSVT LSSSDRMHAL SLKIVLLGKI YAGTPRFFPL 1200
DFIVQFLEQQ VCTLNWDVGF VIQTMNEIGV PLPRLLEVYD QLFKSRDPFW NRMKKPLHLL 1260
DCIHVLLIRY VENPSQVLNC ERRRFTNLCL DAVCGYLVEL QSMSSSVAVQ AITGNFKSLQ 1320
AKLERLH 1327 
Gene Ontology
 GO:0005643; C:nuclear pore; IEA:InterPro.
 GO:0017056; F:structural constituent of nuclear pore; IEA:InterPro.
 GO:0006913; P:nucleocytoplasmic transport; IEA:InterPro. 
Interpro
 IPR007187; Nucleoporin_Nup133/Nup155_C.
 IPR014908; Nucleoporin_Nup133/Nup155_N.
 IPR004870; Nucleoporin_Nup155. 
Pfam
 PF03177; Nucleoporin_C
 PF08801; Nucleoporin_N 
SMART
  
PROSITE
  
PRINTS