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Protein

Acidic leucine-rich nuclear phosphoprotein 32 family member E

Gene

Anp32e

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Histone chaperone that specifically mediates the genome-wide removal of histone H2A.Z/H2AFZ from the nucleosome: removes H2A.Z/H2AFZ from its normal sites of deposition, especially from enhancer and insulator regions. Not involved in deposition of H2A.Z/H2AFZ in the nucleosome. May stabilize the evicted H2A.Z/H2AFZ-H2B dimer, thus shifting the equilibrium towards dissociation and the off-chromatin state. Inhibits activity of protein phosphatase 2A (PP2A). Does not inhibit protein phosphatase 1. May play a role in cerebellar development and synaptogenesis (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionChaperone, Chromatin regulator

Names & Taxonomyi

Protein namesi
Recommended name:
Acidic leucine-rich nuclear phosphoprotein 32 family member E
Gene namesi
Name:Anp32e
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 2

Organism-specific databases

RGDi1310611. Anp32e.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002362511 – 258Acidic leucine-rich nuclear phosphoprotein 32 family member EAdd BLAST258

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Cross-linki68Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Post-translational modificationi

Phosphorylated. The phosphorylation is nuclear localization signal (NLS)-dependent (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ5XIE0.
PRIDEiQ5XIE0.

PTM databases

iPTMnetiQ5XIE0.
PhosphoSitePlusiQ5XIE0.

Expressioni

Gene expression databases

BgeeiENSRNOG00000021168.
GenevisibleiQ5XIE0. RN.

Interactioni

Subunit structurei

Component of a SWR1-like complex, composed of EP400, KAT5/TIP60, TRRAP, BRD8, RUVBL1, RUVBL2, ING3 and ANP32E; the complex does not contain SRCAP. Interacts with H2A.Z/H2AFZ. Interacts with the importin alpha KPNA1 and KPNA2 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi263117. 2 interactors.
STRINGi10116.ENSRNOP00000028744.

Structurei

3D structure databases

ProteinModelPortaliQ5XIE0.
SMRiQ5XIE0.
ModBaseiSearch...
MobiDBiSearch...

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
Regioni205 – 258ZID domainBy similarityAdd BLAST54

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi151 – 258Asp/Glu-rich (highly acidic)Add BLAST108

Domaini

The H2A.Z-interacting domain (ZID) mediates a direct interaction with H2A.Z/H2AFZ.By similarity

Sequence similaritiesi

Belongs to the ANP32 family.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG2739. Eukaryota.
ENOG4111HZT. LUCA.
GeneTreeiENSGT00560000077130.
HOGENOMiHOG000007361.
HOVERGENiHBG053102.
InParanoidiQ5XIE0.
KOiK18648.
OMAiRCPNLTY.
OrthoDBiEOG091G0R8Z.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiView protein in InterPro
IPR001611. Leu-rich_rpt.
IPR032675. LRR_dom_sf.
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiView protein in PROSITE
PS51450. LRR. 4 hits.

Sequencei

Sequence statusi: Complete.

Q5XIE0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEMKKKINME LKNRAPEEVT ELVLDNCLCV NGEIEGLNDT FKELEFLSMA
60 70 80 90 100
NVELSSLARL PSLNKLRKLE LSDNIISGGL EVLAEKCPNL TYLNLSGNKI
110 120 130 140 150
KDLSTVEALQ NLKNLKSLDL FNCEITNLED YRESIFELLQ QITYLDGFDQ
160 170 180 190 200
EDNEAPDSEE EEEDEDGDED EEDEEEDEAG PPEGYEDEDE DEDEAGSEVG
210 220 230 240 250
EGEEEVGLSY LMKEEIQDEE DDDDYVDEGE EEEEEEEEGP RGEKRKRDAE

DDGEEDDD
Length:258
Mass (Da):29,418
Last modified:November 23, 2004 - v1
Checksum:i2312700EA7157B37
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083744 mRNA. Translation: AAH83744.1.
RefSeqiNP_001013218.1. NM_001013200.1.
UniGeneiRn.4268.

Genome annotation databases

EnsembliENSRNOT00000028744; ENSRNOP00000028744; ENSRNOG00000021168.
GeneIDi361999.
KEGGirno:361999.
UCSCiRGD:1310611. rat.

Similar proteinsi

Entry informationi

Entry nameiAN32E_RAT
AccessioniPrimary (citable) accession number: Q5XIE0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: November 23, 2004
Last modified: November 22, 2017
This is version 99 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families