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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 - Molecular functioni

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001375931 – 247Acidic leucine-rich nuclear phosphoprotein 32 family member AAdd BLAST247

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei15PhosphothreonineBy similarity1
Modified residuei17PhosphoserineBy similarity1
Modified residuei158PhosphoserineBy similarity1

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.
PeptideAtlasiO35381.
PRIDEiO35381.

2D gel databases

REPRODUCTION-2DPAGEIPI00314736.

PTM databases

iPTMnetiO35381.
PhosphoSitePlusiO35381.
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

BgeeiENSMUSG00000032249.
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

GO - Molecular functioni

Protein-protein interaction databases

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

Structurei

Secondary structure

1247
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 11Combined sources9
Helixi16 – 18Combined sources3
Beta strandi20 – 23Combined sources4
Beta strandi30 – 32Combined sources3
Beta strandi46 – 48Combined sources3
Beta strandi68 – 70Combined sources3
Helixi80 – 82Combined sources3
Helixi83 – 86Combined sources4
Beta strandi92 – 94Combined sources3
Turni103 – 106Combined sources4
Helixi107 – 111Combined sources5
Beta strandi117 – 119Combined sources3
Helixi124 – 127Combined sources4
Helixi131 – 138Combined sources8
Beta strandi157 – 159Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO35381.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati18 – 38LRR 1Add BLAST21
Repeati43 – 64LRR 2Add BLAST22
Repeati65 – 87LRR 3Add BLAST23
Repeati89 – 110LRR 4Add BLAST22
Domaini123 – 161LRRCTAdd BLAST39

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni150 – 172Necessary for tumor-suppressive functionBy similarityAdd BLAST23
Regioni165 – 247Interaction with E4F11 PublicationAdd BLAST83

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi165 – 247Asp/Glu-rich (highly acidic)Add BLAST83

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.
OMAiNCRSYEG.
OrthoDBiEOG091G0R8Z.
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)DescriptionActionsGraphical viewLength
Sequence conflicti191D → V in AAB39707 (PubMed:8970164).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2JQDNMR-A1-164[»]
ProteinModelPortaliO35381.
SMRiO35381.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiO35381.
PhosphoSitePlusiO35381.
SwissPalmiO35381.

2D gel databases

REPRODUCTION-2DPAGEIPI00314736.

Proteomic databases

EPDiO35381.
MaxQBiO35381.
PaxDbiO35381.
PeptideAtlasiO35381.
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.
OMAiNCRSYEG.
OrthoDBiEOG091G0R8Z.
PhylomeDBiO35381.
TreeFamiTF317206.

Enzyme and pathway databases

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

Miscellaneous databases

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

Gene expression databases

BgeeiENSMUSG00000032249.
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...

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: November 2, 2016
This is version 140 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.