Q8IXJ9 (ASXL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative Polycomb group protein ASXL1

Alternative name(s):
Additional sex combs-like protein 1

Gene names

Name:	ASXL1
Synonyms:	KIAA0978

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1541 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Transcription Transcription regulation Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Craniosynostosis
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PR-DUB complex Inferred from direct assay Ref.13. Source: UniProtKB nuclear chromatin Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	DNA 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 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AKT1	P31749	2	EBI-1646500,EBI-296087
BAP1	Q92560	4	EBI-1646500,EBI-1791447
CBX5	P45973	2	EBI-1646500,EBI-78219
EED	O75530	5	EBI-1646500,EBI-923794
ESR1	P03372	2	EBI-1646500,EBI-78473
EZH2	Q15910	6	EBI-1646500,EBI-530054
KDM1A	O60341	2	EBI-1646500,EBI-710124
RARA	P10276	3	EBI-1646500,EBI-413374
Rxra	P28700	2	EBI-1646500,EBI-346715	From a different organism.
THRB	P68306	2	EBI-1646500,EBI-5743841	From a different organism.

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1541	1541	Putative Polycomb group protein ASXL1		PRO_0000059321
Regions
	Zinc finger	1503 – 1540	38	PHD-type; atypical
	Region	170 – 174	5	Required for interaction with CBX5 By similarity
	Region	175 – 370	196	Interaction with KDM1A By similarity
	Region	300 – 658	359	Interaction with NCOA1 By similarity
	Region	1107 – 1112	6	Required for interaction with RARA
	Motif	160 – 164	5	Nuclear localization signal 1 Potential
	Motif	284 – 288	5	LXXLL motif
	Motif	409 – 413	5	Nuclear localization signal 2 Potential
	Compositional bias	2 – 9	8	Poly-Lys
	Compositional bias	199 – 209	11	Poly-Ser
	Compositional bias	641 – 684	44	Gly-rich
	Compositional bias	1457 – 1460	4	Poly-Ser
Amino acid modifications
	Modified residue	503	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	433 – 479	47	AGVAK…DLEGP → SKLWCEPQCITFLANVHQQH GGKHLAPVCVQPESHDHVPR LRCVLSR in isoform 2.		VSP_007219
	Alternative sequence	480 – 1541	1062	Missing in isoform 2.		VSP_007220
	Natural variant	751	1	V → I. Corresponds to variant rs6058693 [ dbSNP | Ensembl ].		VAR_051602
	Natural variant	815	1	L → P. Ref.1 Ref.3 Ref.4 Ref.6 Corresponds to variant rs6058694 [ dbSNP | Ensembl ].		VAR_028157
	Natural variant	983	1	L → R. Corresponds to variant rs34359205 [ dbSNP | Ensembl ].		VAR_051603
	Natural variant	1325	1	L → F. Corresponds to variant rs6057581 [ dbSNP | Ensembl ].		VAR_028158
Experimental info
	Mutagenesis	1108	1	V → A: Abolishes interaction with RARA. Ref.7
	Mutagenesis	1111	1	L → A: Abolishes interaction with RARA. Ref.7
	Sequence conflict	454	1	A → T in CAD27708. Ref.1
	Sequence conflict	880 – 882	3	TRQ → ASE in CAB56029. Ref.6
	Sequence conflict	1102	1	E → D in CAB55975. Ref.6
	Sequence conflict	1466	1	G → A in AAH33284. Ref.3
	Sequence conflict	1470	1	S → C in AAH33284. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 11, 2011. Version 3. Checksum: B4EE3FACEBFD6865	FASTA	1,541	165,448
	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
	Isoform 2 [UniParc]. Checksum: 4A0734FEC5B6B35F	FASTA	479	53,374
	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 RRNLYKKQES EQSKLWCEPQ CITFLANVHQ QHGGKHLAPV CVQPESHDHV PRLRCVLSR

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00217537. IPI00234299.
PIR	T17285. T17339.
RefSeq	NP_056153.2. NM_015338.5.
UniGene	Hs.374043.
3D structure databases
ProteinModelPortal	Q8IXJ9.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-46910N.
IntAct	Q8IXJ9. 20 interactions.
MINT	MINT-7034503.
PTM databases
PhosphoSite	Q8IXJ9.
Polymorphism databases
DMDM	30172872.
Proteomic databases
PaxDb	Q8IXJ9.
PRIDE	Q8IXJ9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000375687; ENSP00000364839; ENSG00000171456.
GeneID	171023.
KEGG	hsa:171023.
UCSC	uc002wxs.3. human.
Organism-specific databases
CTD	171023.
GeneCards	GC20P030946.
HGNC	HGNC:18318. ASXL1.
MIM	605039. phenotype. 612990. gene. 614286. phenotype.
neXtProt	NX_Q8IXJ9.
Orphanet	97297. Bohring-Opitz syndrome.
PharmGKB	PA25078.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG81527.
HOVERGEN	HBG050598.
InParanoid	Q8IXJ9.
KO	K11471.
OMA	SKLCVLC.
OrthoDB	EOG4GQQ44.
PhylomeDB	Q8IXJ9.
Gene expression databases
ArrayExpress	Q8IXJ9.
Bgee	Q8IXJ9.
CleanEx	HS_ASXL1.
Genevestigator	Q8IXJ9.
GermOnline	ENSG00000171456. Homo sapiens.
Family and domain databases
InterPro	IPR026905. ASX-like_PHD. IPR024811. ASX/ASX-like. IPR024815. ASXL1. [Graphical view]
PANTHER	PTHR13578. PTHR13578. 1 hit. PTHR13578:SF11. PTHR13578:SF11. 1 hit.
Pfam	PF13922. PHD_3. 1 hit. [Graphical view]
PROSITE	PS01359. ZF_PHD_1. False negative. PS50016. ZF_PHD_2. False negative. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	171023.
NextBio	89192.
SOURCE	Search...

Entry information

Entry name

ASXL1_HUMAN

Accession

Primary (citable) accession number: Q8IXJ9
Secondary accession number(s): B2RP59 , 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:	May 1, 2013
This is version 99 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.