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Q8IXJ9 (ASXL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1541 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 nuclear hormone receptors, such as retinoic acid receptors (RARs) and peroxisome proliferator-activated receptor gamma (PPARG). Acts as coactivator of RARA and RXRA through association with NCOA1. Acts as 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 corepressor for PPARG and suppresses its adipocyte differentiation-inducing activity By similarity. Non-catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). Ref.7 Ref.13

Subunit structure

Component of the PR-DUB complex, at least composed of BAP1 and ASXL1. Interacts with RARA, RXRA, NCOA1, KDM1A and CBX5. Interacts with PPARA, PPARG, CBX1 and CBX3 By similarity. Ref.7 Ref.11 Ref.13

Subcellular location

Nucleus By similarity.

Tissue specificity

Widely expressed at low level. Expressed in heart, brain, skeletal muscle, placenta, pancreas, spleen, prostate, small intestine, colon, peripheral blood, leukocytes, bone marrow and fetal liver. Highly expressed in testes. Ref.1 Ref.4

Domain

Contains one Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, which may be required for an association with nuclear receptors.

Involvement in disease

Bohring-Opitz syndrome (BOPS) [MIM:605039]: A syndrome characterized by severe intrauterine growth retardation, poor feeding, profound mental retardation, trigonocephaly, prominent metopic suture, exophthalmos, nevus flammeus of the face, upslanting palpebral fissures, hirsutism, and flexion of the elbows and wrists with deviation of the wrists and metacarpophalangeal joints.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14

Myelodysplastic syndrome (MDS) [MIM:614286]: A heterogeneous group of closely related clonal hematopoietic disorders. All are characterized by a hypercellular or hypocellular bone marrow with impaired morphology and maturation, dysplasia of the myeloid, megakaryocytic and/or erythroid lineages, and peripheral blood cytopenias resulting from ineffective blood cell production. Included diseases are: refractory anemia (RA), refractory anemia with ringed sideroblasts (RARS), refractory anemia with excess blasts (RAEB), refractory cytopenia with multilineage dysplasia and ringed sideroblasts (RCMD-RS); chronic myelomonocytic leukemia (CMML) is a myelodysplastic/myeloproliferative disease. MDS is considered a premalignant condition in a subgroup of patients that often progresses to acute myeloid leukemia (AML).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.12

Sequence similarities

Belongs to the Asx family.

Contains 1 PHD-type zinc finger.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Ubl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCraniosynostosis
   DomainZinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChromatin regulator
Repressor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbone development

Inferred from electronic annotation. Source: Ensembl

monoubiquitinated histone H2A deubiquitination

Inferred from direct assay Ref.13. Source: UniProtKB

negative regulation of fat cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of peroxisome proliferator activated receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of retinoic acid receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of retinoic acid receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

response to retinoic acid

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPR-DUB complex

Inferred from direct assay Ref.13. Source: UniProtKB

nuclear chromatin

Inferred from sequence or structural similarity. 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 sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7PubMed 18624398PubMed 19615732Ref.11PubMed 22897849. Source: IntAct

retinoic acid receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription corepressor activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8IXJ9-1)

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.
Isoform 2 (identifier: Q8IXJ9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     433-479: AGVAKDAKSV...SSAAPDLEGP → SKLWCEPQCI...VPRLRCVLSR
     480-1541: Missing.
Note: Derived from EST data. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15411541Putative Polycomb group protein ASXL1
PRO_0000059321

Regions

Zinc finger1503 – 154038PHD-type; atypical
Region170 – 1745Required for interaction with CBX5 By similarity
Region175 – 370196Interaction with KDM1A By similarity
Region300 – 658359Interaction with NCOA1 By similarity
Region1107 – 11126Required for interaction with RARA
Motif160 – 1645Nuclear localization signal 1 Potential
Motif284 – 2885LXXLL motif
Motif409 – 4135Nuclear localization signal 2 Potential
Compositional bias2 – 98Poly-Lys
Compositional bias199 – 20911Poly-Ser
Compositional bias641 – 68444Gly-rich
Compositional bias1457 – 14604Poly-Ser

Natural variations

Alternative sequence433 – 47947AGVAK…DLEGP → SKLWCEPQCITFLANVHQQH GGKHLAPVCVQPESHDHVPR LRCVLSR in isoform 2.
VSP_007219
Alternative sequence480 – 15411062Missing in isoform 2.
VSP_007220
Natural variant7511V → I.
Corresponds to variant rs6058693 [ dbSNP | Ensembl ].
VAR_051602
Natural variant8151L → P. Ref.1 Ref.3 Ref.4 Ref.6
Corresponds to variant rs6058694 [ dbSNP | Ensembl ].
VAR_028157
Natural variant9831L → R.
Corresponds to variant rs34359205 [ dbSNP | Ensembl ].
VAR_051603
Natural variant13251L → F.
Corresponds to variant rs6057581 [ dbSNP | Ensembl ].
VAR_028158

Experimental info

Mutagenesis11081V → A: Abolishes interaction with RARA. Ref.7
Mutagenesis11111L → A: Abolishes interaction with RARA. Ref.7
Sequence conflict4541A → T in CAD27708. Ref.1
Sequence conflict880 – 8823TRQ → ASE in CAB56029. Ref.6
Sequence conflict11021E → D in CAB55975. Ref.6
Sequence conflict14661G → A in AAH33284. Ref.3
Sequence conflict14701S → C in AAH33284. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: B4EE3FACEBFD6865

FASTA1,541165,448
        10         20         30         40         50         60 
MKDKQKKKKE RTWAEAARLV LENYSDAPMT PKQILQVIEA EGLKEMRSGT SPLACLNAML 

        70         80         90        100        110        120 
HSNSRGGEGL FYKLPGRISL FTLKKDALQW SRHPATVEGE EPEDTADVES CGSNEASTVS 

       130        140        150        160        170        180 
GENDVSLDET SSNASCSTES QSRPLSNPRD SYRASSQANK QKKKTGVMLP RVVLTPLKVN 

       190        200        210        220        230        240 
GAHVESASGF SGCHADGESG SPSSSSSGSL ALGSAAIRGQ AEVTQDPAPL LRGFRKPATG 

       250        260        270        280        290        300 
QMKRNRGEEI DFETPGSILV NTNLRALINS RTFHALPSHF QQQLLFLLPE VDRQVGTDGL 

       310        320        330        340        350        360 
LRLSSSALNN EFFTHAAQSW RERLADGEFT HEMQVRIRQE MEKEKKVEQW KEKFFEDYYG 

       370        380        390        400        410        420 
QKLGLTKEES LQQNVGQEEA EIKSGLCVPG ESVRIQRGPA TRQRDGHFKK RSRPDLRTRA 

       430        440        450        460        470        480 
RRNLYKKQES EQAGVAKDAK SVASDVPLYK DGEAKTDPAG LSSPHLPGTS SAAPDLEGPE 

       490        500        510        520        530        540 
FPVESVASRI QAEPDNLARA SASPDRIPSL PQETVDQEPK DQKRKSFEQA ASASFPEKKP 

       550        560        570        580        590        600 
RLEDRQSFRN TIESVHTEKP QPTKEEPKVP PIRIQLSRIK PPWVVKGQPT YQICPRIIPT 

       610        620        630        640        650        660 
TESSCRGWTG ARTLADIKAR ALQVRGARGH HCHREAATTA IGGGGGPGGG GGGATDEGGG 

       670        680        690        700        710        720 
RGSSSGDGGE ACGHPEPRGG PSTPGKCTSD LQRTQLLPPY PLNGEHTQAG TAMSRARRED 

       730        740        750        760        770        780 
LPSLRKEESC LLQRATVGLT DGLGDASQLP VAPTGDQPCQ ALPLLSSQTS VAERLVEQPQ 

       790        800        810        820        830        840 
LHPDVRTECE SGTTSWESDD EEQGPTVPAD NGPILSLVGD DTLEKGTGQA LDSHPTMKDP 

       850        860        870        880        890        900 
VNVTPSSTPE SSPTDCLQNR AFDDELGLGG SCPPMRESDT RQENLKTKAL VSNSSLHWIP 

       910        920        930        940        950        960 
IPSNDEVVKQ PKPESREHIP SVEPQVGEEW EKAAPTPPAL PGDLTAEEGL DPLDSLTSLW 

       970        980        990       1000       1010       1020 
TVPSRGGSDS NGSYCQQVDI EKLKINGDSE ALSPHGESTD TASDFEGHLT EDSSEADTRE 

      1030       1040       1050       1060       1070       1080 
AAVTKGSSVD KDEKPNWNQS APLSKVNGDM RLVTRTDGMV APQSWVSRVC AVRQKIPDSL 

      1090       1100       1110       1120       1130       1140 
LLASTEYQPR AVCLSMPGSS VEATNPLVMQ LLQGSLPLEK VLPPAHDDSM SESPQVPLTK 

      1150       1160       1170       1180       1190       1200 
DQSHGSLRMG SLHGLGKNSG MVDGSSPSSL RALKEPLLPD SCETGTGLAR IEATQAPGAP 

      1210       1220       1230       1240       1250       1260 
QKNCKAVPSF DSLHPVTNPI TSSRKLEEMD SKEQFSSFSC EDQKEVRAMS QDSNSNAAPG 

      1270       1280       1290       1300       1310       1320 
KSPGDLTTSR TPRFSSPNVI SFGPEQTGRA LGDQSNVTGQ GKKLFGSGNV AATLQRPRPA 

      1330       1340       1350       1360       1370       1380 
DPMPLPAEIP PVFPSGKLGP STNSMSGGVQ TPREDWAPKP HAFVGSVKNE KTFVGGPLKA 

      1390       1400       1410       1420       1430       1440 
NAENRKATGH SPLELVGHLE GMPFVMDLPF WKLPREPGKG LSEPLEPSSL PSQLSIKQAF 

      1450       1460       1470       1480       1490       1500 
YGKLSKLQLS STSFNYSSSS PTFPKGLAGS VVQLSHKANF GASHSASLSL QMFTDSSTVE 

      1510       1520       1530       1540 
SISLQCACSL KAMIMCQGCG AFCHDDCIGP SKLCVLCLVV R 

« Hide

Isoform 2 [UniParc].

Checksum: 4A0734FEC5B6B35F
Show »

FASTA47953,374

References

« Hide 'large scale' references
[1]"A human homolog of Additional sex combs, additional sex combs-like 1, maps to chromosome 20q11."
Fisher C.L., Berger J., Randazzo F., Brock H.W.
Gene 306:115-126(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, VARIANT PRO-815.
[2]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] (ISOFORM 1), VARIANT PRO-815.
Tissue: Prostate.
[4]"Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 174-1541, TISSUE SPECIFICITY, VARIANT PRO-815.
Tissue: Brain.
[5]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-1541 (ISOFORM 1), VARIANT PRO-815.
Tissue: Testis.
[7]"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; RXRA AND NCOA1, MUTAGENESIS OF VAL-1108 AND LEU-1111.
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Mutations of polycomb-associated gene ASXL1 in myelodysplastic syndromes and chronic myelomonocytic leukaemia."
Gelsi-Boyer V., Trouplin V., Adelaide J., Bonansea J., Cervera N., Carbuccia N., Lagarde A., Prebet T., Nezri M., Sainty D., Olschwang S., Xerri L., Chaffanet M., Mozziconacci M.J., Vey N., Birnbaum D.
Br. J. Haematol. 145:788-800(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MDS.
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"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: INTERACTION WITH KDM1A AND CBX5.
[12]"Frequent mutation of the polycomb-associated gene ASXL1 in the myelodysplastic syndromes and in acute myeloid leukemia."
Boultwood J., Perry J., Pellagatti A., Fernandez-Mercado M., Fernandez-Santamaria C., Calasanz M.J., Larrayoz M.J., Garcia-Delgado M., Giagounidis A., Malcovati L., Della Porta M.G., Jadersten M., Killick S., Hellstrom-Lindberg E., Cazzola M., Wainscoat J.S.
Leukemia 24:1062-1065(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MDS.
[13]"Histone H2A deubiquitinase activity of the Polycomb repressive complex PR-DUB."
Scheuermann J.C., de Ayala Alonso A.G., Oktaba K., Ly-Hartig N., McGinty R.K., Fraterman S., Wilm M., Muir T.W., Muller J.
Nature 465:243-247(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE PR-DUB COMPLEX, INTERACTION WITH BAP1.
[14]"De novo nonsense mutations in ASXL1 cause Bohring-Opitz syndrome."
Hoischen A., van Bon B.W., Rodriguez-Santiago B., Gilissen C., Vissers L.E., de Vries P., Janssen I., van Lier B., Hastings R., Smithson S.F., Newbury-Ecob R., Kjaergaard S., Goodship J., McGowan R., Bartholdi D., Rauch A., Peippo M., Cobben J.M. expand/collapse author list , Wieczorek D., Gillessen-Kaesbach G., Veltman J.A., Brunner H.G., de Vries B.B.
Nat. Genet. 43:729-731(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN BOPS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ438952 mRNA. Translation: CAD27708.1.
AL121583, AL034550 Genomic DNA. Translation: CAI40414.1.
AL034550, AL121583 Genomic DNA. Translation: CAI42259.1.
BC033284 mRNA. Translation: AAH33284.1.
BC137278 mRNA. Translation: AAI37279.1.
BC137280 mRNA. Translation: AAI37281.1.
AB023195 mRNA. Translation: BAA76822.2.
AL117518 mRNA. Translation: CAB55975.1.
AL117647 mRNA. Translation: CAB56029.2.
CCDSCCDS13201.1. [Q8IXJ9-1]
PIRT17285.
T17339.
RefSeqNP_056153.2. NM_015338.5.
UniGeneHs.374043.

3D structure databases

ProteinModelPortalQ8IXJ9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid128104. 13 interactions.
DIPDIP-46910N.
IntActQ8IXJ9. 23 interactions.
MINTMINT-7034503.

PTM databases

PhosphoSiteQ8IXJ9.

Polymorphism databases

DMDM317373477.

Proteomic databases

MaxQBQ8IXJ9.
PaxDbQ8IXJ9.
PRIDEQ8IXJ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000375687; ENSP00000364839; ENSG00000171456. [Q8IXJ9-1]
GeneID171023.
KEGGhsa:171023.
UCSCuc002wxs.3. human. [Q8IXJ9-1]

Organism-specific databases

CTD171023.
GeneCardsGC20P030946.
HGNCHGNC:18318. ASXL1.
MIM605039. phenotype.
612990. gene.
614286. phenotype.
neXtProtNX_Q8IXJ9.
Orphanet97297. Bohring-Opitz syndrome.
PharmGKBPA25078.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG81527.
HOVERGENHBG050598.
InParanoidQ8IXJ9.
KOK11471.
OMASLKAMIM.
PhylomeDBQ8IXJ9.
TreeFamTF328464.

Gene expression databases

ArrayExpressQ8IXJ9.
BgeeQ8IXJ9.
CleanExHS_ASXL1.
GenevestigatorQ8IXJ9.

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

GeneWikiASXL1.
GenomeRNAi171023.
NextBio89192.
PROQ8IXJ9.
SOURCESearch...

Entry information

Entry nameASXL1_HUMAN
AccessionPrimary (citable) accession number: Q8IXJ9
Secondary accession number(s): B2RP59 expand/collapse secondary AC list , Q5JWS9, Q8IYY7, Q9H466, Q9NQF8, Q9UFJ0, Q9UFP8, Q9Y2I4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM