CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018795
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Acidic leucine-rich nuclear phosphoprotein 32 family member B 
Protein Synonyms/Alias
 Acidic protein rich in leucines; Putative HLA-DR-associated protein I-2; PHAPI2; Silver-stainable protein SSP29 
Gene Name
 ANP32B 
Gene Synonyms/Alias
 APRIL; PHAPI2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
86GLDMLAEKLPNLTHLacetylation[1]
86GLDMLAEKLPNLTHLubiquitination[2]
99HLNLSGNKLKDISTLubiquitination[3, 4]
101NLSGNKLKDISTLEPubiquitination[2, 3]
110ISTLEPLKKLECLKSubiquitination[2]
111STLEPLKKLECLKSLubiquitination[2]
116LKKLECLKSLDLFNCubiquitination[2]
Reference
 [1] 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]
 [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] 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]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965
Functional Description
 Multifunctional protein working as a cell cycle progression factor as well as a cell survival factor. Required for the progression from the G1 to the S phase. Anti-apoptotic protein which functions as a caspase-3 inhibitor. Has no phosphatase 2A (PP2A) inhibitor activity (By similarity). Exhibits histone chaperone properties, stimulating core histones to assemble into a nucleosome. 
Sequence Annotation
 REPEAT 16 40 LRR 1.
 REPEAT 43 64 LRR 2.
 REPEAT 65 84 LRR 3.
 REPEAT 89 110 LRR 4.
 DOMAIN 123 161 LRRCT.
 MOD_RES 86 86 N6-acetyllysine.
 MOD_RES 244 244 Phosphothreonine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Chaperone; Complete proteome; Cytoplasm; Leucine-rich repeat; Nucleus; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 251 AA 
Protein Sequence
MDMKRRIHLE LRNRTPAAVR ELVLDNCKSN DGKIEGLTAE FVNLEFLSLI NVGLISVSNL 60
PKLPKLKKLE LSENRIFGGL DMLAEKLPNL THLNLSGNKL KDISTLEPLK KLECLKSLDL 120
FNCEVTNLND YRESVFKLLP QLTYLDGYDR EDQEAPDSDA EVDGVDEEEE DEEGEDEEDE 180
DDEDGEEEEF DEEDDEDEDV EGDEDDDEVS EEEEEFGLDE EDEDEDEDEE EEEGGKGEKR 240
KRETDDEGED D 251 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. 
Interpro
 IPR001611; Leu-rich_rpt.
 IPR003603; U2A'_phosphoprotein32A_C. 
Pfam
  
SMART
 SM00446; LRRcap 
PROSITE
 PS51450; LRR 
PRINTS