CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020144
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 NEDD4 family-interacting protein 1 
Protein Synonyms/Alias
 Breast cancer-associated protein SGA-1M; NEDD4 WW domain-binding protein 5; Putative MAPK-activating protein PM13; Putative NF-kappa-B-activating protein 164; Putative NFKB and MAPK-activating protein 
Gene Name
 NDFIP1 
Gene Synonyms/Alias
 N4WBP5; PSEC0192; PSEC0223 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
63KDESGFPKPPSYNVAubiquitination[1, 2, 3, 4]
83YDEAERTKAEATIPLubiquitination[2, 3, 5, 6, 7, 8]
204INYAKVRKMPETFSNubiquitination[2, 3, 7]
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] 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] 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]
 [4] 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]
 [5] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [6] 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]
 [7] 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]
 [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
 Activates HECT domain-containing E3 ubiquitin-protein ligases, including NEDD4 and ITCH, and consequently modulates the stability of their targets. As a result, controls many cellular processes. Prevents chronic T-helper cells-mediated inflammation by activating ITCH and thus controlling JUNB degradation (By similarity). In cortical neurons, mediates the ubiquitination of SLC11A2/DMT1 by NEDD4L, leading to down-regulation of the divalent metal transporter and protection of the cells from cobalt and iron toxicity. Modulates EGFR signaling through multiple pathways. In particular, may regulate the ratio of AKT1-to-MAPK8 signaling in response to EGF, acting on AKT1 probably through PTEN destabilization and on MAPK8 through ITCH-dependent MAP2K4 inactivation. As a result, may control cell growth rate. 
Sequence Annotation
 MOTIF 40 42 PY 1.
 MOTIF 65 67 PY 2.
 MOTIF 74 76 PY 3.  
Keyword
 Alternative splicing; Complete proteome; Endosome; Golgi apparatus; Membrane; Reference proteome; Repeat; Secreted; Transmembrane; Transmembrane helix; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 221 AA 
Protein Sequence
MALALAALAA VEPACGSRYQ QLQNEEESGE PEQAAGDAPP PYSSISAESA AYFDYKDESG 60
FPKPPSYNVA TTLPSYDEAE RTKAEATIPL VPGRDEDFVG RDDFDDADQL RIGNDGIFML 120
TFFMAFLFNW IGFFLSFCLT TSAAGRYGAI SGFGLSLIKW ILIVRFSTYF PGYFDGQYWL 180
WWVFLVLGFL LFLRGFINYA KVRKMPETFS NLPRTRVLFI Y 221 
Gene Ontology
 GO:0005938; C:cell cortex; IEA:Compara.
 GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
 GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0004871; F:signal transducer activity; IMP:UniProtKB.
 GO:0006879; P:cellular iron ion homeostasis; IMP:UniProtKB.
 GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
 GO:0050728; P:negative regulation of inflammatory response; IEA:Compara.
 GO:0032713; P:negative regulation of interleukin-4 production; IEA:Compara.
 GO:0048294; P:negative regulation of isotype switching to IgE isotypes; IEA:Compara.
 GO:0051224; P:negative regulation of protein transport; IMP:UniProtKB.
 GO:0042130; P:negative regulation of T cell proliferation; IEA:Compara.
 GO:0032410; P:negative regulation of transporter activity; IMP:UniProtKB.
 GO:0002829; P:negative regulation of type 2 immune response; IEA:Compara.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IMP:UniProtKB.
 GO:0045732; P:positive regulation of protein catabolic process; IEA:Compara.
 GO:0031398; P:positive regulation of protein ubiquitination; IMP:UniProtKB.
 GO:0048302; P:regulation of isotype switching to IgG isotypes; IEA:Compara.
 GO:0045619; P:regulation of lymphocyte differentiation; IEA:Compara.
 GO:0002761; P:regulation of myeloid leukocyte differentiation; IEA:Compara.
 GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IEA:Compara. 
Interpro
 IPR019325; NEDD4/BSD2. 
Pfam
 PF10176; DUF2370 
SMART
  
PROSITE
  
PRINTS