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P39687 (AN32A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acidic leucine-rich nuclear phosphoprotein 32 family member A
Alternative name(s):
Acidic nuclear phosphoprotein pp32
Leucine-rich acidic nuclear protein
Short name=LANP
Mapmodulin
Potent heat-stable protein phosphatase 2A inhibitor I1PP2A
Putative HLA-DR-associated protein I
Short name=PHAPI
Gene names
Name:ANP32A
Synonyms:C15orf1, LANP, MAPM, PHAP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Protein existenceEvidence 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.18

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. Ref.12 Ref.13 Ref.15 Ref.18

Subcellular location

Nucleus. Cytoplasm. Endoplasmic reticulum. Note: Translocates to the cytoplasm during the process of neuritogenesis By similarity. Shuttles between nucleus and cytoplasm. Ref.6 Ref.11 Ref.15 Ref.16

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.

The N-terminus is blocked.

Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group By similarity.

Sequence similarities

Belongs to the ANP32 family.

Contains 4 LRR (leucine-rich) repeats.

Contains 1 LRRCT domain.

Sequence caution

The sequence BAD97000.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AXIN1O151692EBI-359234,EBI-710484
E4F1Q66K893EBI-359234,EBI-1227043
PPP2CAP677752EBI-359234,EBI-712311
Ppp2caP633312EBI-359234,EBI-7050205From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 249249Acidic leucine-rich nuclear phosphoprotein 32 family member A
PRO_0000137592

Regions

Repeat18 – 3821LRR 1
Repeat43 – 6422LRR 2
Repeat65 – 8723LRR 3
Repeat89 – 11022LRR 4
Domain123 – 16139LRRCT
Region150 – 17425Necessary for tumor-suppressive function
Region165 – 24985Interaction with E4F1 By similarity
Compositional bias168 – 24982Asp/Glu-rich (highly acidic)

Amino acid modifications

Modified residue151Phosphothreonine Ref.19
Modified residue171Phosphoserine Ref.19

Experimental info

Sequence conflict1861V → A in BAD97000. Ref.8

Secondary structure

........................ 249
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39687 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: CA2D1A756FBAEA04

FASTA24928,585
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THE INHAT COMPLEX, IDENTIFICATION BY 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ELAVL1, SUBCELLULAR LOCATION.
[16]"Cleaving the oxidative repair protein Ape1 enhances cell death mediated by granzyme A."
Fan Z., Beresford P.J., Zhang D., Xu Z., Novina C.D., Yoshida A., Pommier Y., Lieberman J.
Nat. Immunol. 4:145-153(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[17]"The Anp32 family of proteins containing leucine-rich repeats."
Matilla A., Radrizzani M.
Cerebellum 4:7-18(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE.
[18]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH E4F1.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-17, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"The crystal structure of the tumor suppressor protein pp32 (Anp32a): structural insights into Anp32 family of proteins."
Huyton T., Wolberger C.
Protein Sci. 16:1308-1315(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-149, LEUCINE-RICH REPEATS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS36375.
S43309.
RefSeqNP_006296.1. NM_006305.3.
UniGeneHs.458747.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JE0X-ray2.40A/B/C/D/E/F1-149[»]
2JE1X-ray2.69A/B/C/D1-149[»]
ProteinModelPortalP39687.
SMRP39687. Positions 1-149.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113791. 41 interactions.
IntActP39687. 15 interactions.
MINTMINT-4999627.
STRING9606.ENSP00000417864.

PTM databases

PhosphoSiteP39687.

Polymorphism databases

DMDM730318.

2D gel databases

SWISS-2DPAGEP39687.

Proteomic databases

PaxDbP39687.
PRIDEP39687.

Protocols and materials databases

DNASU8125.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000465139; ENSP00000417864; ENSG00000140350.
GeneID8125.
KEGGhsa:8125.
UCSCuc002arl.3. human.

Organism-specific databases

CTD8125.
GeneCardsGC15M069070.
HGNCHGNC:13233. ANP32A.
HPACAB005231.
MIM600832. gene.
neXtProtNX_P39687.
PharmGKBPA24811.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG322008.
HOGENOMHOG000007361.
HOVERGENHBG053102.
InParanoidP39687.
OMANCRSYEG.
OrthoDBEOG7TJ3KH.
PhylomeDBP39687.
TreeFamTF317206.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP39687.
BgeeP39687.
CleanExHS_ANP32A.
GenevestigatorP39687.

Family and domain databases

InterProIPR001611. Leu-rich_rpt.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view]
SMARTSM00446. LRRcap. 1 hit.
[Graphical view]
PROSITEPS51450. LRR. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSANP32A. human.
EvolutionaryTraceP39687.
GenomeRNAi8125.
NextBio30786.
PMAP-CutDBP39687.
PROP39687.
SOURCESearch...

Entry information

Entry nameAN32A_HUMAN
AccessionPrimary (citable) accession number: P39687
Secondary accession number(s): B2R6T4 expand/collapse secondary AC list , Q53FK4, Q5J8L8, Q7M4N6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM