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Protein

Acidic leucine-rich nuclear phosphoprotein 32 family member B

Gene

Anp32b

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

Functioni

Exhibits histone chaperone properties, stimulating core histones to assemble into a nucleosome (By similarity). Multifunctional protein working as a cell cycle progression factor as well as a cell survival factor. Required for the progression from the G1 to the S phase. Anti-apoptotic protein which functions as a caspase-3 inhibitor. Has no phosphatase 2A (PP2A) inhibitor activity.By similarity2 Publications

GO - Biological processi

  • negative regulation of apoptotic process Source: RGD
  • positive regulation of cell proliferation Source: RGD
  • positive regulation of G1/S transition of mitotic cell cycle Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Names & Taxonomyi

Protein namesi
Recommended name:
Acidic leucine-rich nuclear phosphoprotein 32 family member B
Alternative name(s):
Proliferation-related acidic leucine-rich protein PAL31
Gene namesi
Name:Anp32b
Synonyms:Pal31
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621285. Anp32b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 272272Acidic leucine-rich nuclear phosphoprotein 32 family member BPRO_0000236253Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei164 – 1641PhosphoserineCombined sources
Modified residuei171 – 1711PhosphoserineCombined sources
Modified residuei265 – 2651PhosphothreonineCombined sources

Post-translational modificationi

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).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9EST6.
PRIDEiQ9EST6.

PTM databases

iPTMnetiQ9EST6.
PhosphoSiteiQ9EST6.

Expressioni

Tissue specificityi

Predominantly expressed in brain. Expressed in the entire embryonic brain, whereas in the adult brain its expression is restricted to the subventricular zone where there are neural progenitor cells.1 Publication

Inductioni

Expressed specifically during the late G1 and S phases.

Interactioni

Subunit structurei

Monomer. Interacts with histones H3 and H4 (By similarity).By similarity

Protein-protein interaction databases

BioGridi250983. 1 interaction.
IntActiQ9EST6. 1 interaction.
STRINGi10116.ENSRNOP00000012478.

Structurei

3D structure databases

ProteinModelPortaliQ9EST6.
SMRiQ9EST6. Positions 1-161.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati16 – 4025LRR 1Add
BLAST
Repeati43 – 6422LRR 2Add
BLAST
Repeati65 – 8420LRR 3Add
BLAST
Repeati89 – 11022LRR 4Add
BLAST
Domaini123 – 16139LRRCTAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi146 – 272127Asp/Glu-rich (highly acidic)Add
BLAST

Domaini

Histone binding is mediated by the concave surface of the LRR region.By similarity

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.
HOGENOMiHOG000007361.
HOVERGENiHBG053102.
InParanoidiQ9EST6.
KOiK18647.
PhylomeDBiQ9EST6.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view]
SMARTiSM00446. LRRcap. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9EST6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDMKRRIHLE LRNRTPAAVQ ELVLDNCKAN DGKIEGLTDE FVNLEFLSLI
60 70 80 90 100
NVGLFSVSDL PKLPKLKKLE LSENRIFGGL DRLAEELPSL THLNLSGNNL
110 120 130 140 150
KDISTLEPLK RLDCLKSLDL FGCEVTNRSD YRETVFRLLP QLSYLDGYDR
160 170 180 190 200
EDQEAPDSDV EVDSVEEAPD SDGEVDGVDK EEEDEEGEDE EEEEDEDGEE
210 220 230 240 250
EEDEDEEDED EDEDVEGEDD EDEVSGEEEE FGHDGEVDED EEDEDEDEDE
260 270
EEEESGKGEK RKRETDDEGE DD
Length:272
Mass (Da):31,061
Last modified:March 1, 2001 - v1
Checksum:i556AC9B169E9D996
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025581 mRNA. Translation: BAB12435.1.
BC086508 mRNA. Translation: AAH86508.1.
PIRiJC7357.
RefSeqiNP_571986.1. NM_131911.2.
UniGeneiRn.20465.

Genome annotation databases

GeneIDi170724.
KEGGirno:170724.
UCSCiRGD:621285. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB025581 mRNA. Translation: BAB12435.1.
BC086508 mRNA. Translation: AAH86508.1.
PIRiJC7357.
RefSeqiNP_571986.1. NM_131911.2.
UniGeneiRn.20465.

3D structure databases

ProteinModelPortaliQ9EST6.
SMRiQ9EST6. Positions 1-161.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250983. 1 interaction.
IntActiQ9EST6. 1 interaction.
STRINGi10116.ENSRNOP00000012478.

PTM databases

iPTMnetiQ9EST6.
PhosphoSiteiQ9EST6.

Proteomic databases

PaxDbiQ9EST6.
PRIDEiQ9EST6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi170724.
KEGGirno:170724.
UCSCiRGD:621285. rat.

Organism-specific databases

CTDi10541.
RGDi621285. Anp32b.

Phylogenomic databases

eggNOGiKOG2739. Eukaryota.
ENOG4111HZT. LUCA.
HOGENOMiHOG000007361.
HOVERGENiHBG053102.
InParanoidiQ9EST6.
KOiK18647.
PhylomeDBiQ9EST6.

Miscellaneous databases

PROiQ9EST6.

Family and domain databases

Gene3Di3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view]
SMARTiSM00446. LRRcap. 1 hit.
[Graphical view]
SUPFAMiSSF52058. SSF52058. 1 hit.
PROSITEiPS51450. LRR. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PAL31, a novel nuclear protein, expressed in the developing brain."
    Mutai H., Toyoshima Y., Sun W., Hattori N., Tanaka S., Shiota K.
    Biochem. Biophys. Res. Commun. 274:427-433(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: Wistar Imamichi.
    Tissue: Brain.
  2. "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: Heart.
  3. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  4. "Proliferation related acidic leucine-rich protein PAL31 functions as a caspase-3 inhibitor."
    Sun W., Kimura H., Hattori N., Tanaka S., Matsuyama S., Shiota K.
    Biochem. Biophys. Res. Commun. 342:817-823(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "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.
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164; SER-171 AND THR-265, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAN32B_RAT
AccessioniPrimary (citable) accession number: Q9EST6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Suppression of the expression of this gene by RNAi induces apoptosis.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.