Reviewed, UniProtKB/Swiss-Prot P39687 (AN32A_HUMAN)

Names and origin

Protein names

Recommended name:
    Acidic leucine-rich nuclear phosphoprotein 32 family member A
Alternative name(s):
    Potent heat-stable protein phosphatase 2A inhibitor I1PP2A
    Acidic nuclear phosphoprotein pp32
    Leucine-rich acidic nuclear protein
      Short name=Lanp
    Putative HLA-DR-associated protein I
      Short name=PHAPI
    Mapmodulin

Gene names

Name:	ANP32A
Synonyms:	C15orf1, LANP, MAPM, PHAP1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	249 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Ref.6 Ref.11 Ref.14 Ref.17
Subunit structure	Component of the SET complex, which also contains SET, APEX1, HMGB2 and NME1. Directly interacts with SET. Interacts with ATXN1/SCA1. Interacts with MAP1B By similarity. Interacts with ELAVL1. Part of the INHAT (inhibitor of histone acetyltransferases) complex. Interacts with E4F1.
Subcellular location	Nucleus. Cytoplasm. Note: Shuttles between nucleus and cytoplasm. Ref.6 Ref.11 Ref.15
Tissue specificity	Expressed in all tissues tested. Highly expressed in kidney and skeletal muscle, moderate levels of expression in brain, placenta and pancreas, and weakly expressed in lung. Found in all regions of the brain examined (amygdala, caudate nucleus, corpus callosum, hippocampus and thalamus), with highest levels in amygdala. Ref.6
Post-translational modification	Phosphorylated on serine residues. Ref.18 Ref.19 The N-terminus is blocked.
Sequence similarities	Belongs to the ANP32 family. Contains 4 LRR (leucine-rich) repeats.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	Leucine-rich repeat Repeat
Molecular function	Repressor
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	intracellular signaling cascade Ref.1 Traceable author statement. Source: ProtInc nucleocytoplasmic transport Ref.13 Ref.15 Inferred from direct assay. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Ref.13 Inferred from direct assay. Source: UniProtKB nucleus Ref.13 Ref.15 Inferred from direct assay. Source: UniProtKB perinuclear region of cytoplasm Ref.13 Inferred from direct assay. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AXIN1	O15169	1	EBI-359234,EBI-710484

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 249

249

Acidic leucine-rich nuclear phosphoprotein 32 family member A

PRO_0000137592

Regions

Repeat

44 – 63

20

LRR 1

Repeat

64 – 86

23

LRR 2

Repeat

87 – 111

25

LRR 3

Repeat

115 – 138

24

LRR 4

Region

150 – 174

25

Necessary for tumor-suppressive function

Region

165 – 249

85

Interaction with E4F1 By similarity

Compositional bias

168 – 249

82

Asp/Glu-rich (highly acidic)

Amino acid modifications

Modified residue

15

1

Phosphothreonine Ref.19

Modified residue

17

1

Phosphoserine Ref.19

Modified residue

158

1

Phosphoserine Ref.18

Experimental info

Sequence conflict

186

1

V → A in BAD97000. Ref.8

Secondary structure

1

.

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249

Helix Strand Turn

Details...

Helix

3 – 11

9

Helix

16 – 18

3

Beta strand

20 – 23

4

Beta strand

46 – 48

3

Beta strand

68 – 70

3

Helix

81 – 86

6

Beta strand

92 – 94

3

Helix

103 – 106

4

Helix

107 – 111

5

Beta strand

117 – 119

3

Helix

124 – 127

4

Helix

131 – 138

8

Sequences

	Sequence		Length	Mass (Da)
	P39687-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: CA2D1A756FBAEA04	FASTA	249	28,585
	10 20 30 40 50 60 MEMGRRIHLE LRNRTPSDVK ELVLDNSRSN EGKLEGLTDE FEELEFLSTI NVGLTSIANL 70 80 90 100 110 120 PKLNKLKKLE LSDNRVSGGL EVLAEKCPNL THLNLSGNKI KDLSTIEPLK KLENLKSLDL 130 140 150 160 170 180 FNCEVTNLND YRENVFKLLP QLTYLDGYDR DDKEAPDSDA EGYVEGLDDE EEDEDEEEYD 190 200 210 220 230 240 EDAQVVEDEE DEDEEEEGEE EDVSGEEEED EEGYNDGEVD DEEDEEELGE EERGQKRKRE PEDEGEDDD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purification and characterization of two putative HLA class II associated proteins: PHAPI and PHAPII." Vaesen M., Barnikol-Watanabe S., Goetz H., Adil Awni L., Cole T., Zimmermann B., Kratzin H.D., Hilschmann N. Biol. Chem. Hoppe-Seyler 375:113-126(1994) [PubMed: 8192856] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-26; 29-47; 71-97 AND 100-161. Tissue: B-cell lymphoma.
[2]	"Molecular identification of I1PP2A, a novel potent heat-stable inhibitor protein of protein phosphatase 2A." Li M., Makkinje A., Damuni Z. Biochemistry 35:6998-7002(1996) [PubMed: 8679524] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 7-12 AND 29-44. Tissue: Kidney.
[3]	"Structure of pp32, an acidic nuclear protein which inhibits oncogene-induced formation of transformed foci." Chen T.-H., Brody J.R., Romantsev F.E., Yu J.-G., Kayler A.E., Voneiff E., Kuhajda F.P., Pasternack G.R. Mol. Biol. Cell 7:2045-2056(1996) [PubMed: 8970164] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"The cerebellar leucine-rich acidic nuclear protein interacts with ataxin-1." Matilla A., Koshy B.T., Cummings C.J., Isobe T., Orr H.T., Zoghbi H.Y. Nature 389:974-978(1997) [PubMed: 9353121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Inhibitors of protein phosphatase-2A from human brain structures, immunocytological localization and activities towards dephosphorylation of the Alzheimer type hyperphosphorylated tau." Tsujio I., Zaidi T., Xu J., Kotula L., Grundke-Iqbal I., Iqbal K. FEBS Lett. 579:363-372(2005) [PubMed: 15642345] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Brain.
[7]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Synovium.
[9]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph.
[11]	"Identification of sequences required for inhibition of oncogene-mediated transformation by pp32." Brody J.R., Kadkol S.S., Mahmoud M.A., Rebel J.M., Pasternack G.R. J. Biol. Chem. 274:20053-20055(1999) [PubMed: 10400610] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[12]	"Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the Set oncoprotein." Seo S.-B., McNamara P., Heo S., Turner A., Lane W.S., Chakravarti D. Cell 104:119-130(2001) [PubMed: 11163245] [Abstract] Cited for: INTERACTION WITH THE INHAT COMPLEX, MASS SPECTROMETRY.
[13]	"Granzyme A activates an endoplasmic reticulum-associated caspase-independent nuclease to induce single-stranded DNA nicks." Beresford P.J., Zhang D., Oh D.Y., Fan Z., Greer E.L., Russo M.L., Jaju M., Lieberman J. J. Biol. Chem. 276:43285-43293(2001) [PubMed: 11555662] [Abstract] Cited for: INTERACTION WITH SET.
[14]	"Tumor suppression and potentiation by manipulation of pp32 expression." Bai J., Brody J.R., Kadkol S.S., Pasternack G.R. Oncogene 20:2153-2160(2001) [PubMed: 11360199] [Abstract] Cited for: FUNCTION.
[15]	"Delineation of mRNA export pathways by the use of cell-permeable peptides." Gallouzi I.-E., Steitz J.A. Science 294:1895-1901(2001) [PubMed: 11729309] [Abstract] Cited for: INTERACTION WITH ELAVL1, SUBCELLULAR LOCATION.
[16]	"The Anp32 family of proteins containing leucine-rich repeats." Matilla A., Radrizzani M. Cerebellum 4:7-18(2005) [PubMed: 15895553] [Abstract] Cited for: GENE FAMILY, NOMENCLATURE.
[17]	"The role of LANP and ataxin 1 in E4F-mediated transcriptional repression." Cvetanovic M., Rooney R.J., Garcia J.J., Toporovskaya N., Zoghbi H.Y., Opal P. EMBO Rep. 8:671-677(2007) [PubMed: 17557114] [Abstract] Cited for: FUNCTION, INTERACTION WITH E4F1.
[18]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-158, MASS SPECTROMETRY.
[19]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-17, MASS SPECTROMETRY.
[20]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X75090 mRNA. Translation: CAA52981.1.
U60823 mRNA. Translation: AAC50570.1.
U73477 mRNA. Translation: AAB39706.1.
AF025684 mRNA. Translation: AAB91548.1.
AY349171 mRNA. Translation: AAQ79832.1.
BT007436 mRNA. Translation: AAP36104.1.
AK223280 mRNA. Translation: BAD97000.1. Different initiation.
AK312703 mRNA. Translation: BAG35581.1.
CH471082 Genomic DNA. Translation: EAW77824.1.
BC007200 mRNA. Translation: AAH07200.1.

IPI

IPI00025849.

PIR

S36375.
S43309.

RefSeq

NP_006296.1.

UniGene

Hs.458747

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JE0	X-ray	2.40	A/B/C/D/E/F	1-149	[»]
2JE1	X-ray	2.69	A/B/C/D	1-149	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P39687. 8 interactions.

PTM databases

PhosphoSite

P39687.

2-D gel databases

SWISS-2DPAGE

P39687.

Proteomic databases

PRIDE

P39687.

Genome annotation databases

Ensembl

ENSG00000140350. Homo sapiens. [Contig view]

GeneID

8125.

KEGG

hsa:8125.

Organism-specific databases

GeneCards

GC15M066845.

HGNC

HGNC:13233. ANP32A.

HPA

CAB005231.

MIM

600832. gene.

PharmGKB

PA24811.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P39687.

HOVERGEN

P39687.

OMA

P39687. NRVSGGL.

Gene expression databases

CleanEx

HS_ANP32A.

GermOnline

ENSG00000140350. Homo sapiens.

Family and domain databases

InterPro

IPR001611. Leu-rich_rpt.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view]

Pfam

PF00560. LRR_1. 1 hit.
[Graphical view]

SMART

SM00446. LRRcap. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

30786.

PMAP-CutDB

P39687.

SOURCE

Search...

Entry information

Entry name

AN32A_HUMAN

Accession

Primary (citable) accession number: P39687
Secondary accession number(s): B2R6T4 , Q53FK4, Q5J8L8, Q7M4N6

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)