CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024044
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Influenza virus NS1A-binding protein 
Protein Synonyms/Alias
 NS1-BP; NS1-binding protein; Aryl hydrocarbon receptor-associated protein 3 
Gene Name
 IVNS1ABP 
Gene Synonyms/Alias
 ARA3; FLARA3; KIAA0850; NS1; NS1BP; HSPC068 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
27AKLNALRKSGQFCDVubiquitination[1]
103KADKELVKDVYSAAKubiquitination[2, 3, 4]
118KLKMDRVKQVCGDYLubiquitination[1]
197SNGKLYTKVINWVQRubiquitination[1]
369GTAEMNGKLIAAGGYubiquitination[1, 5]
464GVCALNGKLYIVGGSubiquitination[1]
477GSDPYGQKGLKNCDVubiquitination[1, 2, 3]
480PYGQKGLKNCDVFDPubiquitination[1]
490DVFDPVTKLWTSCAPubiquitination[1]
Reference
 [1] 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]
 [2] 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]
 [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] 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]
 [5] 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] 
Functional Description
 Plays a role in cell division and in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats. Protects cells from cell death induced by actin destabilization; Protects neurons from dendritic spines and actin filaments damage induced by the actin-destabilizing cytochalasin B when overexpressed. Activates Erk signaling pathway when overexpressed in cultured cell lines (By similarity). May be a component of the cellular splicing machinery with a role in pre-mRNA splicing; may mediate the inhibition of splicing by NS/influenza virus NS1A protein. Functions as modifier of the AHR/Aryl hydrocarbon receptor pathway increasing the concentration of AHR available to activate transcription. 
Sequence Annotation
 DOMAIN 32 99 BTB.
 DOMAIN 134 233 BACK.
 REPEAT 369 415 Kelch 1.
 REPEAT 416 463 Kelch 2.
 REPEAT 465 512 Kelch 3.
 REPEAT 513 559 Kelch 4.
 REPEAT 560 606 Kelch 5.
 REPEAT 608 642 Kelch 6.
 REGION 164 368 Sufficient for AHR interaction and
 MOD_RES 246 246 Phosphoserine.
 MOD_RES 277 277 Phosphoserine.
 MOD_RES 322 322 Phosphoserine.
 MOD_RES 336 336 Phosphoserine.
 MOD_RES 338 338 Phosphoserine.  
Keyword
 Complete proteome; Cytoplasm; Cytoskeleton; Host-virus interaction; Kelch repeat; Nucleus; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 642 AA 
Protein Sequence
MIPNGYLMFE DENFIESSVA KLNALRKSGQ FCDVRLQVCG HEMLAHRAVL ACCSPYLFEI 60
FNSDSDPHGI SHVKFDDLNP EAVEVLLNYA YTAQLKADKE LVKDVYSAAK KLKMDRVKQV 120
CGDYLLSRMD VTSCISYRNF ASCMGDSRLL NKVDAYIQEH LLQISEEEEF LKLPRLKLEV 180
MLEDNVCLPS NGKLYTKVIN WVQRSIWENG DSLEELMEEV QTLYYSADHK LLDGNLLDGQ 240
AEVFGSDDDH IQFVQKKPPR ENGHKQISSS STGCLSSPNA TVQSPKHEWK IVASEKTSNN 300
TYLCLAVLDG IFCVIFLHGR NSPQSSPTST PKLSKSLSFE MQQDELIEKP MSPMQYARSG 360
LGTAEMNGKL IAAGGYNREE CLRTVECYNP HTDHWSFLAP MRTPRARFQM AVLMGQLYVV 420
GGSNGHSDDL SCGEMYDSNI DDWIPVPELR TNRCNAGVCA LNGKLYIVGG SDPYGQKGLK 480
NCDVFDPVTK LWTSCAPLNI RRHQSAVCEL GGYLYIIGGA ESWNCLNTVE RYNPENNTWT 540
LIAPMNVARR GAGVAVLNGK LFVCGGFDGS HAISCVEMYD PTRNEWKMMG NMTSPRSNAG 600
IATVGNTIYA VGGFDGNEFL NTVEVYNLES NEWSPYTKIF QF 642 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005681; C:spliceosomal complex; TAS:ProtInc.
 GO:0005667; C:transcription factor complex; TAS:ProtInc.
 GO:0009615; P:response to virus; TAS:ProtInc.
 GO:0008380; P:RNA splicing; TAS:ProtInc.
 GO:0006383; P:transcription from RNA polymerase III promoter; TAS:ProtInc.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR011705; BACK.
 IPR000210; BTB/POZ-like.
 IPR011333; BTB/POZ_fold.
 IPR013069; BTB_POZ.
 IPR015916; Gal_Oxidase_b-propeller.
 IPR017096; Kelch-like_gigaxonin.
 IPR006652; Kelch_1. 
Pfam
 PF07707; BACK
 PF00651; BTB
 PF01344; Kelch_1 
SMART
 SM00875; BACK
 SM00225; BTB
 SM00612; Kelch 
PROSITE
 PS50097; BTB 
PRINTS