CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006721
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nuclear pore glycoprotein p62 
Protein Synonyms/Alias
 62 kDa nucleoporin; Nucleoporin Nup62 
Gene Name
 NUP62 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
371TLIENGEKITSLHREubiquitination[1, 2, 3]
435EEREKTYKLAENIDAubiquitination[1, 3]
445ENIDAQLKRMAQDLKubiquitination[2, 4]
504RKVEEVTKVCEGRRKubiquitination[2, 5]
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] 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] 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]
 [4] 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]
 [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] 
Functional Description
 Essential component of the nuclear pore complex. The N- terminal is probably involved in nucleocytoplasmic transport. The C-terminal is probably involved in protein-protein interaction via coiled-coil formation and may function in anchorage of p62 to the pore complex. 
Sequence Annotation
 REPEAT 1 9 1.
 REPEAT 13 21 2.
 REPEAT 29 37 3.
 REPEAT 39 47 4.
 REPEAT 57 65 5.
 REPEAT 71 79 6.
 REPEAT 85 93 7.
 REPEAT 111 119 8.
 REPEAT 137 145 9.
 REPEAT 155 163 10.
 REPEAT 168 176 11.
 REPEAT 185 193 12.
 REPEAT 234 242 13.
 REPEAT 253 261 14.
 REPEAT 287 295 15.
 REGION 2 295 15 X 9 AA approximate repeats.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 408 408 Phosphoserine.
 CARBOHYD 373 373 O-linked (GlcNAc) (By similarity).
 CARBOHYD 468 468 O-linked (GlcNAc) (By similarity).  
Keyword
 3D-structure; Acetylation; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Disease mutation; Glycoprotein; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein; Polymorphism; Protein transport; Reference proteome; Repeat; Translocation; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 522 AA 
Protein Sequence
MSGFNFGGTG APTGGFTFGT AKTATTTPAT GFSFSTSGTG GFNFGAPFQP ATSTPSTGLF 60
SLATQTPATQ TTGFTFGTAT LASGGTGFSL GIGASKLNLS NTAATPAMAN PSGFGLGSSN 120
LTNAISSTVT SSQGTAPTGF VFGPSTTSVA PATTSGGFSF TGGSTAQPSG FNIGSAGNSA 180
QPTAPATLPF TPATPAATTA GATQPAAPTP TATITSTGPS LFASIATAPT SSATTGLSLC 240
TPVTTAGAPT AGTQGFSLKA PGAASGTSTT TSTAATATAT TTSSSSTTGF ALNLKPLAPA 300
GIPSNTAAAV TAPPGPGAAA GAAASSAMTY AQLESLINKW SLELEDQERH FLQQATQVNA 360
WDRTLIENGE KITSLHREVE KVKLDQKRLD QELDFILSQQ KELEDLLSPL EELVKEQSGT 420
IYLQHADEER EKTYKLAENI DAQLKRMAQD LKDIIEHLNT SGAPADTSDP LQQICKILNA 480
HMDSLQWIDQ NSALLQRKVE EVTKVCEGRR KEQERSFRIT FD 522 
Gene Ontology
 GO:0005737; C:cytoplasm; NAS:UniProtKB.
 GO:0031965; C:nuclear membrane; IDA:HPA.
 GO:0005643; C:nuclear pore; IDA:UniProtKB.
 GO:0031074; C:nucleocytoplasmic shuttling complex; NAS:UniProtKB.
 GO:0030529; C:ribonucleoprotein complex; IDA:MGI.
 GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
 GO:0003682; F:chromatin binding; NAS:UniProtKB.
 GO:0030159; F:receptor signaling complex scaffold activity; IDA:UniProtKB.
 GO:0042169; F:SH2 domain binding; IDA:UniProtKB.
 GO:0017056; F:structural constituent of nuclear pore; IEA:InterPro.
 GO:0046966; F:thyroid hormone receptor binding; ISS:UniProtKB.
 GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
 GO:0005975; P:carbohydrate metabolic process; TAS:Reactome.
 GO:0008219; P:cell death; IMP:UniProtKB.
 GO:0019221; P:cytokine-mediated signaling pathway; TAS:Reactome.
 GO:0015758; P:glucose transport; TAS:Reactome.
 GO:0009755; P:hormone-mediated signaling pathway; NAS:UniProtKB.
 GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
 GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
 GO:0006913; P:nucleocytoplasmic transport; NAS:GOC.
 GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; NAS:UniProtKB.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IDA:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0015031; P:protein transport; IEA:UniProtKB-KW.
 GO:0010827; P:regulation of glucose transport; TAS:Reactome.
 GO:0046578; P:regulation of Ras protein signal transduction; NAS:UniProtKB.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0006351; P:transcription, DNA-dependent; IDA:UniProtKB.
 GO:0055085; P:transmembrane transport; TAS:Reactome.
 GO:0022415; P:viral reproductive process; TAS:Reactome. 
Interpro
 IPR026010; NSP1/NUP62.
 IPR007758; Nucleoporin_NSP1_C. 
Pfam
 PF05064; Nsp1_C 
SMART
  
PROSITE
  
PRINTS