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P59598 (ASXL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative Polycomb group protein ASXL1
Alternative name(s):
Additional sex combs-like protein 1
Gene names
Name:Asxl1
Synonyms:Kiaa0978
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1514 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable Polycomb group (PcG) protein involved in transcriptional regulation mediated by ligand-bound retinoic acid receptors (RARs) and peroxisome proliferator-activated receptor gamma (PPARG). Acts as a coactivator of RARA and RXRA through association with NCOA1. Acts as a corepressor through recruitment of KDM1A and CBX5 to target genes in a cell-type specific manner; the function seems to involve differential recruitment of methylated histone H3 to respective promoters. Acts as a corepressor for PPARG and suppresses its adipocyte differentiation-inducing activity. Non-catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Ref.2 Ref.4 Ref.5

Subunit structure

Component of the PR-DUB complex, at least composed of BAP1 and ASXL1 By similarity. Interacts with RARA, RXRA, NCOA1, KDM1A and CBX5. Interacts with PPARA, PPARG, CBX1 and CBX3. Ref.2 Ref.4 Ref.5

Subcellular location

Nucleus Ref.4.

Domain

Contains two Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs, which may be required for an association with nuclear receptors By similarity.

Sequence similarities

Belongs to the Asx family.

Contains 1 PHD-type zinc finger.

Sequence caution

The sequence BAC65695.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
Repressor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbone development

Inferred from mutant phenotype PubMed 22876197. Source: MGI

monoubiquitinated histone H2A deubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of fat cell differentiation

Inferred from direct assay Ref.5. Source: UniProtKB

negative regulation of peroxisome proliferator activated receptor signaling pathway

Inferred from direct assay Ref.5. Source: UniProtKB

negative regulation of retinoic acid receptor signaling pathway

Inferred from direct assay Ref.4. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.4. Source: UniProtKB

positive regulation of retinoic acid receptor signaling pathway

Inferred from direct assay Ref.2. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.2. Source: UniProtKB

response to retinoic acid

Inferred from direct assay Ref.2. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPR-DUB complex

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear chromatin

Inferred from direct assay Ref.4. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peroxisome proliferator activated receptor binding

Inferred from direct assay Ref.5. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.2Ref.4. Source: IntAct

retinoic acid receptor binding

Inferred from direct assay Ref.2. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.2. Source: UniProtKB

transcription corepressor activity

Inferred from direct assay Ref.4. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CBX5P459735EBI-5743705,EBI-78219From a different organism.
ESR1P033722EBI-5743705,EBI-78473From a different organism.
KDM1AO603412EBI-5743705,EBI-710124From a different organism.
NCOA1Q157882EBI-5743705,EBI-455189From a different organism.
NR3C1P041502EBI-5743705,EBI-493507From a different organism.
RARAP102764EBI-5743705,EBI-413374From a different organism.
RxraP287002EBI-5743705,EBI-346715

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15141514Putative Polycomb group protein ASXL1
PRO_0000059322

Regions

Zinc finger1476 – 151338PHD-type; atypical
Region170 – 1745Required for interaction with CBX5
Region175 – 370196Interaction with KDM1A
Region300 – 655356Interaction with NCOA1
Region1082 – 10876Required for interaction with RARA By similarity
Motif284 – 2885LXXLL motif 1
Motif409 – 4135Nuclear localization signal Potential
Motif808 – 8125LXXLL motif 2
Compositional bias199 – 20911Poly-Ser
Compositional bias284 – 2885Poly-Leu
Compositional bias639 – 67032Gly-rich
Compositional bias1430 – 14334Poly-Ser

Experimental info

Mutagenesis1701P → A: Abolishes interaction with CBX1, CBX3 and CBX5; when associated with A-172 and A-174. Ref.4
Mutagenesis1721V → A: Abolishes interaction with CBX1, CBX3 and CBX5; when associated with A-170 and A-174. Ref.4
Mutagenesis1741L → A: Abolishes interaction with CBX1, CBX3 and CBX5; when associated with A-170 and A-172. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P59598 [UniParc].

Last modified April 23, 2003. Version 1.
Checksum: 20D9FBE9D4CF9E74

FASTA1,514162,674
        10         20         30         40         50         60 
MKDKQKRKKE RTWAEAARLV LENYSDAPMT PKQILQVIEA EGLKEMRSGT SPLACLNAML 

        70         80         90        100        110        120 
HSNSRGGEGL FYKLPGRISL FTLKKDAVQW SRNAATVDGD EPEDSADVES CGSNEASTVS 

       130        140        150        160        170        180 
GENDVSLDET SSNASCSTES QSRPLSNPRD SHRASSQANK QKKRTGVMLP RVVLTPLKVN 

       190        200        210        220        230        240 
GAHVEPASGF SGRHADGESG SPSSSSSGSL ALGNSAIRGQ AEVTRDPAPL LRGFRKPATG 

       250        260        270        280        290        300 
QMKRNRGEEV DFETPGSILV NTNLRALINS RTFHALPLHF QQQLLLLLPE VDRQVGTDGL 

       310        320        330        340        350        360 
LRLSGSALNN EFFTHAAQSW RERLADGEFT HEMQVRLRQE MEKEKKVEQW KEKFFEDYYG 

       370        380        390        400        410        420 
QKLGLTKEES LQQKEVQEEA KVKSGLCVSG ESVRPQRGPN TRQRDGHFKK RSRPDLRTRS 

       430        440        450        460        470        480 
RRNIYKKQEP EQAGVAKDAS AAPDVSLSKD TKTDLAGVNS TPGPDVSSAT SGQEGPKCPS 

       490        500        510        520        530        540 
EPVASQIQAE RDNLACASAS PDRIPTLPQD TVDQETKDQK RKSFEQEASA SFPEKKPRLE 

       550        560        570        580        590        600 
DRQSFRNTIE SVHTEKPQPT KEEPKVPPIR IQLSRIKPPW VAKGRPTYQI CPRIVPITES 

       610        620        630        640        650        660 
SCRGWTGART LADIKARALQ ARGARGYHCN RETATTAIGG GGGPGGGGSG AIDEGGGRDS 

       670        680        690        700        710        720 
SSGDGSEACG HPEPRGAPST SGESASDLQR TQLLPPCPLN GEHTPAEAAM PRARREDSAS 

       730        740        750        760        770        780 
LRKEESCLLK RVPGVLTSGL EDASQPPIAP TGDQPCQALP PLSSQTPVAE MLTEQPKLLL 

       790        800        810        820        830        840 
DDRTECESSR EDQGPTIPSE SSSGRFPLGD LLGGGSDQAF DNMKEPVSMT PTFISELSLA 

       850        860        870        880        890        900 
NYLQDRPDDD GLGLGATGLL IRESSRQEAL TEAFASGSPT SWVPILSNYE VIKTSDPESR 

       910        920        930        940        950        960 
ENIPCPEPQD EKEWERAVPL IAATESVPQP ESCISHWTPP PAAVGSTGSD SEQVDLERLE 

       970        980        990       1000       1010       1020 
MNGISEAPSP HSESTDTASD SEGHLSEDSS EVDASEVTVV KGSLGGDEKQ DWDPSASLSK 

      1030       1040       1050       1060       1070       1080 
VNNDLSVLTR TGGVAASQSW VSRVCSVPHK IPDSLLLSST ECQPRSVCPL RPGSSVEVTN 

      1090       1100       1110       1120       1130       1140 
PLVMHLLHGN LPLEKVLPPG HRSSRLESSQ LPLREQSQDR GTLQGTGENN RLAARINPGS 

      1150       1160       1170       1180       1190       1200 
AQTLKESILA QSYGASAGLV RAMASKAPAM SQKIAKMVTS LDSQHPETEL TPSSGNLEEI 

      1210       1220       1230       1240       1250       1260 
DSKEHLSSFL CEEQKEGHSL SQGSDPGAAP GQCLGDHTTS KVPCFSSTNV SLSFGSEQTD 

      1270       1280       1290       1300       1310       1320 
GTLSDQNNAG GHEKKLFGPG NTVTTLQCPR SEEQTPLPAE VPPVFPSRKI EPSKNSVSGG 

      1330       1340       1350       1360       1370       1380 
VQTTRENRMP KPPPVSADSI KTEQTFLRDP IKADAENRKA AGYSSLELVG HLQGMPFVVD 

      1390       1400       1410       1420       1430       1440 
LPFWKLPREP GKGFSQPLEP SSIPSQLNIK QALYGKLSKL QLSPTSFNYS SSSATFPKGL 

      1450       1460       1470       1480       1490       1500 
AGGVVQLSHK ASFGTGHTAS LSLQMFADSS AVESISLQCA CSLKAMIMCQ GCGAFCHDDC 

      1510 
IGPSKLCVLC LVVR 

« Hide

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[2]"Additional sex comb-like 1 (ASXL1), in cooperation with SRC-1, acts as a ligand-dependent coactivator for retinoic acid receptor."
Cho Y.S., Kim E.J., Park U.H., Sin H.S., Um S.J.
J. Biol. Chem. 281:17588-17598(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH RARA AND RXRA.
[3]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[4]"ASXL1 represses retinoic acid receptor-mediated transcription through associating with HP1 and LSD1."
Lee S.W., Cho Y.S., Na J.M., Park U.H., Kang M., Kim E.J., Um S.J.
J. Biol. Chem. 285:18-29(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KDM1A; CBX1; CBX3 AND CBX5, MUTAGENESIS OF PRO-170; VAL-172 AND LEU-174.
[5]"Additional sex comb-like (ASXL) proteins 1 and 2 play opposite roles in adipogenesis via reciprocal regulation of peroxisome proliferator-activated receptor {gamma}."
Park U.H., Yoon S.K., Park T., Kim E.J., Um S.J.
J. Biol. Chem. 286:1354-1363(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PPARA AND PPARG.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK122413 mRNA. Translation: BAC65695.1. Different initiation.
CCDSCCDS38285.1.
RefSeqNP_001035028.1. NM_001039939.1.
UniGeneMm.330677.

3D structure databases

ProteinModelPortalP59598.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid230772. 3 interactions.
IntActP59598. 12 interactions.

PTM databases

PhosphoSiteP59598.

Proteomic databases

PaxDbP59598.
PRIDEP59598.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000109790; ENSMUSP00000105413; ENSMUSG00000042548.
GeneID228790.
KEGGmmu:228790.
UCSCuc008nhs.1. mouse.

Organism-specific databases

CTD171023.
MGIMGI:2684063. Asxl1.
RougeSearch...

Phylogenomic databases

eggNOGNOG81527.
HOGENOMHOG000293301.
HOVERGENHBG050598.
InParanoidP59598.
KOK11471.
OMASLKAMIM.
OrthoDBEOG7SXW2P.
PhylomeDBP59598.
TreeFamTF328464.

Gene expression databases

ArrayExpressP59598.
BgeeP59598.
CleanExMM_ASXL1.
GenevestigatorP59598.

Family and domain databases

InterProIPR026905. ASX-like_PHD.
IPR024811. ASX/ASX-like.
IPR028020. ASXH.
IPR024815. ASXL1.
IPR007759. DNA-dir_RNA_pol_delta/Asxl.
[Graphical view]
PANTHERPTHR13578. PTHR13578. 1 hit.
PTHR13578:SF19. PTHR13578:SF19. 1 hit.
PfamPF13919. ASXH. 1 hit.
PF05066. HARE-HTH. 1 hit.
PF13922. PHD_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio379148.
PROP59598.
SOURCESearch...

Entry information

Entry nameASXL1_MOUSE
AccessionPrimary (citable) accession number: P59598
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: April 23, 2003
Last modified: July 9, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot