Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Acidic leucine-rich nuclear phosphoprotein 32 family member A

Gene

Anp32a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-450520. HuR (ELAVL1) binds and stabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended 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
Potent heat-stable protein phosphatase 2A inhibitor I1PP2A
Gene namesi
Name:Anp32a
Synonyms:Anp32, Lanp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:108447. Anp32a.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • nuclear matrix Source: MGI
  • nucleus Source: MGI
  • perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice are viable and fertile. They have no derangements in any of the major organ systems, including the nervous systems.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 247247Acidic leucine-rich nuclear phosphoprotein 32 family member APRO_0000137593Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151PhosphothreonineBy similarity
Modified residuei17 – 171PhosphoserineBy similarity
Modified residuei158 – 1581PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated on serine residues.By similarity
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.

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO35381.
MaxQBiO35381.
PaxDbiO35381.
PRIDEiO35381.

2D gel databases

REPRODUCTION-2DPAGEIPI00314736.

PTM databases

iPTMnetiO35381.
PhosphoSiteiO35381.
SwissPalmiO35381.

Expressioni

Tissue specificityi

Predominantly expressed in the cerebellum. Expressed also in cortex, lung, skeletal muscle, gastrointestinal tract, spleen, liver and heart.1 Publication

Gene expression databases

BgeeiO35381.
ExpressionAtlasiO35381. baseline and differential.
GenevisibleiO35381. MM.

Interactioni

Subunit structurei

Component of the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Directly interacts with SET. Interacts with ATXN1/SCA1. Interacts with MAP1B. Interacts with ELAVL1. Part of the INHAT (inhibitor of histone acetyltransferases) complex. Interacts with E4F1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
E4f1Q8CCE92EBI-643140,EBI-7450874

Protein-protein interaction databases

BioGridi198104. 2 interactions.
IntActiO35381. 9 interactions.
MINTiMINT-1566009.
STRINGi10090.ENSMUSP00000082652.

Structurei

Secondary structure

1
247
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 119Combined sources
Helixi16 – 183Combined sources
Beta strandi20 – 234Combined sources
Beta strandi30 – 323Combined sources
Beta strandi46 – 483Combined sources
Beta strandi68 – 703Combined sources
Helixi80 – 823Combined sources
Helixi83 – 864Combined sources
Beta strandi92 – 943Combined sources
Turni103 – 1064Combined sources
Helixi107 – 1115Combined sources
Beta strandi117 – 1193Combined sources
Helixi124 – 1274Combined sources
Helixi131 – 1388Combined sources
Beta strandi157 – 1593Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JQDNMR-A1-164[»]
ProteinModelPortaliO35381.
SMRiO35381. Positions 1-164.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO35381.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati18 – 3821LRR 1Add
BLAST
Repeati43 – 6422LRR 2Add
BLAST
Repeati65 – 8723LRR 3Add
BLAST
Repeati89 – 11022LRR 4Add
BLAST
Domaini123 – 16139LRRCTAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni150 – 17223Necessary for tumor-suppressive functionBy similarityAdd
BLAST
Regioni165 – 24783Interaction with E4F1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi165 – 24783Asp/Glu-rich (highly acidic)Add
BLAST

Sequence similaritiesi

Belongs to the ANP32 family.Curated
Contains 4 LRR (leucine-rich) repeats.Curated
Contains 1 LRRCT domain.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG2739. Eukaryota.
ENOG4111HZT. LUCA.
GeneTreeiENSGT00560000077130.
HOGENOMiHOG000007361.
HOVERGENiHBG053102.
InParanoidiO35381.
KOiK18646.
OMAiEDDANGY.
OrthoDBiEOG7TJ3KH.
PhylomeDBiO35381.
TreeFamiTF317206.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35381-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEMDKRIYLE LRNRTPSDVK ELVLDNCKSI EGKIEGLTDE FEELEFLSTI
60 70 80 90 100
NVGLTSISNL PKLNKLKKLE LSENRISGDL EVLAEKCPNL KHLNLSGNKI
110 120 130 140 150
KDLSTIEPLK KLENLKSLDL FNCEVTNLNA YRENVFKLLP QVMYLDGYDR
160 170 180 190 200
DNKEAPDSDV EGYVEDDDEE DEDEEEYDEY AQLVEDEEEE DEEEEGEEED
210 220 230 240
VSGEEEEDEE GYNDGEVDDE EDEEEAGEEE GSQKRKREPD DEGEEDD
Length:247
Mass (Da):28,538
Last modified:January 1, 1998 - v1
Checksum:i82EEDCF72ECC2918
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1911D → V in AAB39707 (PubMed:8970164).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73478 mRNA. Translation: AAB39707.1.
AF022957 mRNA. Translation: AAB91546.1.
BC062899 mRNA. Translation: AAH62899.1.
CCDSiCCDS40663.1.
RefSeqiNP_033802.2. NM_009672.3.
UniGeneiMm.269088.

Genome annotation databases

EnsembliENSMUST00000085519; ENSMUSP00000082652; ENSMUSG00000032249.
GeneIDi11737.
KEGGimmu:11737.
UCSCiuc009qah.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73478 mRNA. Translation: AAB39707.1.
AF022957 mRNA. Translation: AAB91546.1.
BC062899 mRNA. Translation: AAH62899.1.
CCDSiCCDS40663.1.
RefSeqiNP_033802.2. NM_009672.3.
UniGeneiMm.269088.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JQDNMR-A1-164[»]
ProteinModelPortaliO35381.
SMRiO35381. Positions 1-164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198104. 2 interactions.
IntActiO35381. 9 interactions.
MINTiMINT-1566009.
STRINGi10090.ENSMUSP00000082652.

PTM databases

iPTMnetiO35381.
PhosphoSiteiO35381.
SwissPalmiO35381.

2D gel databases

REPRODUCTION-2DPAGEIPI00314736.

Proteomic databases

EPDiO35381.
MaxQBiO35381.
PaxDbiO35381.
PRIDEiO35381.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000085519; ENSMUSP00000082652; ENSMUSG00000032249.
GeneIDi11737.
KEGGimmu:11737.
UCSCiuc009qah.3. mouse.

Organism-specific databases

CTDi8125.
MGIiMGI:108447. Anp32a.

Phylogenomic databases

eggNOGiKOG2739. Eukaryota.
ENOG4111HZT. LUCA.
GeneTreeiENSGT00560000077130.
HOGENOMiHOG000007361.
HOVERGENiHBG053102.
InParanoidiO35381.
KOiK18646.
OMAiEDDANGY.
OrthoDBiEOG7TJ3KH.
PhylomeDBiO35381.
TreeFamiTF317206.

Enzyme and pathway databases

ReactomeiR-MMU-450520. HuR (ELAVL1) binds and stabilizes mRNA.

Miscellaneous databases

ChiTaRSiAnp32a. mouse.
EvolutionaryTraceiO35381.
NextBioi279459.
PROiO35381.
SOURCEiSearch...

Gene expression databases

BgeeiO35381.
ExpressionAtlasiO35381. baseline and differential.
GenevisibleiO35381. MM.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 4 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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].
  2. "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], INTERACTION WITH SCA1.
    Tissue: Cerebellum.
  3. "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].
    Strain: C57BL/6J.
    Tissue: Brain.
  4. "Mapmodulin/leucine-rich acidic nuclear protein binds the light chain of microtubule-associated protein 1B and modulates neuritogenesis."
    Opal P., Garcia J.J., Propst F., Matilla A., Orr H.T., Zoghbi H.Y.
    J. Biol. Chem. 278:34691-34699(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MAP1B.
  5. Cited for: DISRUPTION PHENOTYPE.
  6. "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, TISSUE SPECIFICITY.
  7. "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.
  8. "Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation."
    Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.
    Cell 137:1076-1087(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCYLATION.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiAN32A_MOUSE
AccessioniPrimary (citable) accession number: O35381
Secondary accession number(s): P97437
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.