CPLM-007166

Genbank Nucleotide ID

Acidic leucine-rich nuclear phosphoprotein 32 family member A

Protein Synonyms/Alias

Acidic nuclear phosphoprotein pp32; Leucine-rich acidic nuclear protein; LANP; Mapmodulin; Potent heat-stable protein phosphatase 2A inhibitor I1PP2A; Putative HLA-DR-associated protein I; PHAPI

C15orf1; LANP; MAPM; PHAP1

Homo sapiens (Human)

Position	Peptide	Type	References
20	NRTPSDVKELVLDNS	ubiquitination	[1, 2, 3, 4, 5]
99	HLNLSGNKIKDLSTI	ubiquitination	[1, 3]
110	LSTIEPLKKLENLKS	ubiquitination	[1]
116	LKKLENLKSLDLFNC	ubiquitination	[4]
137	DYRENVFKLLPQLTY	ubiquitination	[3]

[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] 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]
[4] 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]
[5] 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]

Functional Description

Implicated in a number of cellular processes, including proliferation, differentiation, caspase-dependent and caspase- independent apoptosis, suppression of transformation (tumor suppressor), inhibition of protein phosphatase 2A, regulation of mRNA trafficking and stability in association with ELAVL1, and inhibition of acetyltransferases as part of the INHAT (inhibitor of histone acetyltransferases) complex. Plays a role in E4F1- mediated transcriptional repression.

REPEAT 18 38 LRR 1.
REPEAT 43 64 LRR 2.
REPEAT 65 87 LRR 3.
REPEAT 89 110 LRR 4.
DOMAIN 123 161 LRRCT.
REGION 150 174 Necessary for tumor-suppressive function.
REGION 165 249 Interaction with E4F1 (By similarity).
MOD_RES 15 15 Phosphothreonine.
MOD_RES 17 17 Phosphoserine.

3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Endoplasmic reticulum; Leucine-rich repeat; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO:0005654; C:nucleoplasm; TAS:Reactome.
GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO:0010467; P:gene expression; TAS:Reactome.
GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
GO:0016071; P:mRNA metabolic process; TAS:Reactome.
GO:0006913; P:nucleocytoplasmic transport; IDA:UniProtKB.
GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.

IPR001611; Leu-rich_rpt.
IPR025875; Leu-rich_rpt_4.
IPR003603; U2A'_phosphoprotein32A_C.