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Q9EST5

- AN32B_MOUSE

UniProt

Q9EST5 - AN32B_MOUSE

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Protein

Acidic leucine-rich nuclear phosphoprotein 32 family member B

Gene
Anp32b, Pal31
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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. Exhibits histone chaperone properties, stimulating core histones to assemble into a nucleosome By similarity.

GO - Biological processi

  1. G1/S transition of mitotic cell cycle Source: MGI
  2. inner ear development Source: MGI
  3. palate development Source: MGI
  4. vasculature development Source: MGI
  5. ventricular system development Source: MGI
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1914878. Anp32b.

Subcellular locationi

Nucleus
Note: Accumulates in the nuclei at the S phase By similarity.

GO - Cellular componenti

  1. nucleus Source: MGI
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_0000236252Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei265 – 2651Phosphothreonine By similarity

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.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9EST5.
PaxDbiQ9EST5.
PRIDEiQ9EST5.

PTM databases

PhosphoSiteiQ9EST5.

Expressioni

Gene expression databases

BgeeiQ9EST5.
CleanExiMM_ANP32B.
GenevestigatoriQ9EST5.

Interactioni

Subunit structurei

Monomer. Interacts with histones H3 and H4 By similarity.

Protein-protein interaction databases

BioGridi212319. 10 interactions.
IntActiQ9EST5. 1 interaction.
MINTiMINT-1869930.

Structurei

3D structure databases

ProteinModelPortaliQ9EST5.
SMRiQ9EST5. Positions 1-161.

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

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.
Contains 1 LRRCT domain.

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiNOG322008.
GeneTreeiENSGT00560000077130.
HOGENOMiHOG000007361.
HOVERGENiHBG053102.
OMAiDEVSGEX.
OrthoDBiEOG7TJ3KH.
PhylomeDBiQ9EST5.
TreeFamiTF317206.

Family and domain databases

InterProiIPR001611. Leu-rich_rpt.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view]
SMARTiSM00446. LRRcap. 1 hit.
[Graphical view]
PROSITEiPS51450. LRR. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9EST5-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MDMKRRIHLE LRNRTPAAVR ELVLDNCKAM DGKIEGLTDE FVNLEFLSLI    50
SVGLFSVSDL PKLPKLKKLE LSENRIFGGL DRLAEELPSL THLNLSGNNL 100
KDISTLEPLK RLDCLKSLDL FGCEVTNRSD YRETVFRLLP QLSYLDGYDR 150
EDQEAPDSDV EVDSVEEAPD SDGEVDGVDK EEEDEEGEDE EEEEDEDGEE 200
EEDEDEEDED EDEDVEGEDD EDEVSGEEEE FGHDGEVDED EEDEDEDEDE 250
EEEESGKGEK RKRETDDEGE DD 272
Length:272
Mass (Da):31,079
Last modified:March 1, 2001 - v1
Checksum:iBC22DC591AA6BC15
GO
Isoform 2 (identifier: Q9EST5-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     227-227: E → EVNTTVFFPICVKTK
     269-272: GEDD → EEEPKNSSRDIPPSSVSPLVIHHQAWGLRPNKIVNVVRFSCKTLAVS

Note: No experimental confirmation available.

Show »
Length:329
Mass (Da):37,447
Checksum:i7DDD33F69960CEE5
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei227 – 2271E → EVNTTVFFPICVKTK in isoform 2. VSP_023520
Alternative sequencei269 – 2724GEDD → EEEPKNSSRDIPPSSVSPLV IHHQAWGLRPNKIVNVVRFS CKTLAVS in isoform 2. VSP_023521

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB025582 mRNA. Translation: BAB12436.1.
AK165807 mRNA. Translation: BAE38387.1.
AL683884 Genomic DNA. Translation: CAM13790.1.
BC003489 mRNA. Translation: AAH03489.1.
BC005628 mRNA. Translation: AAH05628.1.
BC093506 mRNA. Translation: AAH93506.1.
CCDSiCCDS18151.1. [Q9EST5-1]
RefSeqiNP_570959.1. NM_130889.2. [Q9EST5-1]
UniGeneiMm.263913.

Genome annotation databases

EnsembliENSMUST00000102926; ENSMUSP00000099990; ENSMUSG00000028333. [Q9EST5-1]
GeneIDi67628.
KEGGimmu:67628.
UCSCiuc008stt.1. mouse. [Q9EST5-1]
uc012dds.1. mouse. [Q9EST5-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB025582 mRNA. Translation: BAB12436.1 .
AK165807 mRNA. Translation: BAE38387.1 .
AL683884 Genomic DNA. Translation: CAM13790.1 .
BC003489 mRNA. Translation: AAH03489.1 .
BC005628 mRNA. Translation: AAH05628.1 .
BC093506 mRNA. Translation: AAH93506.1 .
CCDSi CCDS18151.1. [Q9EST5-1 ]
RefSeqi NP_570959.1. NM_130889.2. [Q9EST5-1 ]
UniGenei Mm.263913.

3D structure databases

ProteinModelPortali Q9EST5.
SMRi Q9EST5. Positions 1-161.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 212319. 10 interactions.
IntActi Q9EST5. 1 interaction.
MINTi MINT-1869930.

PTM databases

PhosphoSitei Q9EST5.

Proteomic databases

MaxQBi Q9EST5.
PaxDbi Q9EST5.
PRIDEi Q9EST5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000102926 ; ENSMUSP00000099990 ; ENSMUSG00000028333 . [Q9EST5-1 ]
GeneIDi 67628.
KEGGi mmu:67628.
UCSCi uc008stt.1. mouse. [Q9EST5-1 ]
uc012dds.1. mouse. [Q9EST5-2 ]

Organism-specific databases

CTDi 10541.
MGIi MGI:1914878. Anp32b.

Phylogenomic databases

eggNOGi NOG322008.
GeneTreei ENSGT00560000077130.
HOGENOMi HOG000007361.
HOVERGENi HBG053102.
OMAi DEVSGEX.
OrthoDBi EOG7TJ3KH.
PhylomeDBi Q9EST5.
TreeFami TF317206.

Miscellaneous databases

NextBioi 325077.
PROi Q9EST5.
SOURCEi Search...

Gene expression databases

Bgeei Q9EST5.
CleanExi MM_ANP32B.
Genevestigatori Q9EST5.

Family and domain databases

InterProi IPR001611. Leu-rich_rpt.
IPR003603. U2A'_phosphoprotein32A_C.
[Graphical view ]
SMARTi SM00446. LRRcap. 1 hit.
[Graphical view ]
PROSITEi PS51450. LRR. 3 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: BALB/c.
    Tissue: Brain.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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] (ISOFORMS 1 AND 2).
    Strain: FVB/N and NMRI.
    Tissue: Mammary tumor.
  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. "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.

Entry informationi

Entry nameiAN32B_MOUSE
AccessioniPrimary (citable) accession number: Q9EST5
Secondary accession number(s): B1AVH9, Q566J4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 103 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

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi