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Q9NR48

- ASH1L_HUMAN

UniProt

Q9NR48 - ASH1L_HUMAN

Protein

Histone-lysine N-methyltransferase ASH1L

Gene

ASH1L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 113 (01 Oct 2014)
      Sequence version 2 (31 Oct 2006)
      Previous versions | rss
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    Functioni

    Histone methyltransferase specifically methylating 'Lys-36' of histone H3 (H3K36me).1 Publication

    Catalytic activityi

    S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi887 – 89913A.T hook 1Add
    BLAST
    DNA bindingi1347 – 135913A.T hook 2Add
    BLAST
    DNA bindingi1847 – 185913A.T hook 3Add
    BLAST
    Zinc fingeri2585 – 263147PHD-typeAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: InterPro
    2. DNA binding Source: InterPro
    3. histone-lysine N-methyltransferase activity Source: UniProtKB-EC
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell-cell signaling Source: ProtInc
    2. DNA packaging Source: ProtInc
    3. regulation of transcription, DNA-templated Source: UniProtKB-KW
    4. transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Methyltransferase, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, S-adenosyl-L-methionine, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone-lysine N-methyltransferase ASH1L (EC:2.1.1.43)
    Alternative name(s):
    ASH1-like protein
    Short name:
    huASH1
    Absent small and homeotic disks protein 1 homolog
    Lysine N-methyltransferase 2H
    Gene namesi
    Name:ASH1L
    Synonyms:KIAA1420, KMT2H
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:19088. ASH1L.

    Subcellular locationi

    Nucleus 1 Publication. Cell junctiontight junction 1 Publication. Chromosome 1 Publication
    Note: The relevance of tight junction localization is however unclear.

    GO - Cellular componenti

    1. chromosome Source: UniProtKB-SubCell
    2. cytoplasm Source: HPA
    3. extracellular vesicular exosome Source: UniProt
    4. Golgi apparatus Source: HPA
    5. nucleus Source: HPA
    6. tight junction Source: ProtInc

    Keywords - Cellular componenti

    Cell junction, Chromosome, Nucleus, Tight junction

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134891064.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 29692969Histone-lysine N-methyltransferase ASH1LPRO_0000259516Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei22 – 221Phosphoserine1 Publication
    Modified residuei375 – 3751N6-acetyllysine1 Publication
    Cross-linki402 – 402Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Cross-linki406 – 406Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei2317 – 23171N6-acetyllysineBy similarity
    Modified residuei2319 – 23191N6-acetyllysineBy similarity
    Modified residuei2323 – 23231N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9NR48.
    PaxDbiQ9NR48.
    PRIDEiQ9NR48.

    PTM databases

    PhosphoSiteiQ9NR48.

    Expressioni

    Tissue specificityi

    Widely expressed, with highest level in brain, heart and kidney.1 Publication

    Gene expression databases

    ArrayExpressiQ9NR48.
    BgeeiQ9NR48.
    CleanExiHS_ASH1L.
    GenevestigatoriQ9NR48.

    Organism-specific databases

    HPAiHPA004806.

    Interactioni

    Protein-protein interaction databases

    BioGridi120969. 6 interactions.
    IntActiQ9NR48. 2 interactions.
    MINTiMINT-1183184.
    STRINGi9606.ENSP00000376204.

    Structurei

    Secondary structure

    1
    2969
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2104 – 21063
    Helixi2116 – 21183
    Turni2124 – 21263
    Turni2128 – 21314
    Turni2137 – 21415
    Beta strandi2148 – 21514
    Beta strandi2155 – 21606
    Beta strandi2170 – 21734
    Beta strandi2176 – 21794
    Helixi2181 – 219010
    Beta strandi2200 – 22045
    Beta strandi2207 – 22104
    Beta strandi2212 – 22154
    Helixi2217 – 22204
    Beta strandi2228 – 22369
    Beta strandi2239 – 224810
    Beta strandi2262 – 22643
    Helixi2438 – 245821
    Helixi2469 – 24713
    Helixi2477 – 24793
    Helixi2483 – 24864
    Helixi2493 – 25019
    Helixi2508 – 252619
    Helixi2531 – 255828

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3MQMX-ray2.54A/B2438-2561[»]
    3OPEX-ray2.90A/B2074-2293[»]
    ProteinModelPortaliQ9NR48.
    SMRiQ9NR48. Positions 1981-2285, 2436-2561, 2584-2636, 2704-2806.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NR48.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2091 – 214252AWSPROSITE-ProRule annotationAdd
    BLAST
    Domaini2145 – 2261117SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini2269 – 228517Post-SETPROSITE-ProRule annotationAdd
    BLAST
    Domaini2463 – 253371BromoPROSITE-ProRule annotationAdd
    BLAST
    Domaini2661 – 2798138BAHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2069 – 2288220Catalytic domainAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1380 – 142445Pro-richAdd
    BLAST
    Compositional biasi1580 – 1791212Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily.PROSITE-ProRule annotation
    Contains 3 A.T hook DNA-binding domains.Curated
    Contains 1 AWS domain.PROSITE-ProRule annotation
    Contains 1 BAH domain.PROSITE-ProRule annotation
    Contains 1 bromo domain.PROSITE-ProRule annotation
    Contains 1 PHD-type zinc finger.Curated
    Contains 1 post-SET domain.PROSITE-ProRule annotation
    Contains 1 SET domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri2585 – 263147PHD-typeAdd
    BLAST

    Keywords - Domaini

    Bromodomain, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG2940.
    HOGENOMiHOG000034094.
    HOVERGENiHBG080871.
    InParanoidiQ9NR48.
    KOiK06101.
    OMAiPENSFRK.
    OrthoDBiEOG7ZPNJ4.
    PhylomeDBiQ9NR48.
    TreeFamiTF106416.

    Family and domain databases

    Gene3Di1.20.920.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProiIPR017956. AT_hook_DNA-bd_motif.
    IPR006560. AWS.
    IPR001025. BAH_dom.
    IPR001487. Bromodomain.
    IPR003616. Post-SET_dom.
    IPR001214. SET_dom.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF01426. BAH. 1 hit.
    PF00439. Bromodomain. 1 hit.
    PF00628. PHD. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view]
    SMARTiSM00384. AT_hook. 4 hits.
    SM00570. AWS. 1 hit.
    SM00439. BAH. 1 hit.
    SM00297. BROMO. 1 hit.
    SM00249. PHD. 1 hit.
    SM00508. PostSET. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view]
    SUPFAMiSSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEiPS51215. AWS. 1 hit.
    PS51038. BAH. 1 hit.
    PS50014. BROMODOMAIN_2. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS50280. SET. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NR48-1) [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

    MDPRNTAMLG LGSDSEGFSR KSPSAISTGT LVSKREVELE KNTKEEEDLR     50
    KRNRERNIEA GKDDGLTDAQ QQFSVKETNF SEGNLKLKIG LQAKRTKKPP 100
    KNLENYVCRP AIKTTIKHPR KALKSGKMTD EKNEHCPSKR DPSKLYKKAD 150
    DVAAIECQSE EVIRLHSQGE NNPLSKKLSP VHSEMADYIN ATPSTLLGSR 200
    DPDLKDRALL NGGTSVTEKL AQLIATCPPS KSSKTKPKKL GTGTTAGLVS 250
    KDLIRKAGVG SVAGIIHKDL IKKPTISTAV GLVTKDPGKK PVFNAAVGLV 300
    NKDSVKKLGT GTTAVFINKN LGKKPGTITT VGLLSKDSGK KLGIGIVPGL 350
    VHKESGKKLG LGTVVGLVNK DLGKKLGSTV GLVAKDCAKK IVASSAMGLV 400
    NKDIGKKLMS CPLAGLISKD AINLKAEALL PTQEPLKASC STNINNQESQ 450
    ELSESLKDSA TSKTFEKNVV RQNKESILEK FSVRKEIINL EKEMFNEGTC 500
    IQQDSFSSSE KGSYETSKHE KQPPVYCTSP DFKMGGASDV STAKSPFSAV 550
    GESNLPSPSP TVSVNPLTRS PPETSSQLAP NPLLLSSTTE LIEEISESVG 600
    KNQFTSESTH LNVGHRSVGH SISIECKGID KEVNDSKTTH IDIPRISSSL 650
    GKKPSLTSES SIHTITPSVV NFTSLFSNKP FLKLGAVSAS DKHCQVAESL 700
    STSLQSKPLK KRKGRKPRWT KVVARSTCRS PKGLELERSE LFKNVSCSSL 750
    SNSNSEPAKF MKNIGPPSFV DHDFLKRRLP KLSKSTAPSL ALLADSEKPS 800
    HKSFATHKLS SSMCVSSDLL SDIYKPKRGR PKSKEMPQLE GPPKRTLKIP 850
    ASKVFSLQSK EEQEPPILQP EIEIPSFKQG LSVSPFPKKR GRPKRQMRSP 900
    VKMKPPVLSV APFVATESPS KLESESDNHR SSSDFFESED QLQDPDDLDD 950
    SHRPSVCSMS DLEMEPDKKI TKRNNGQLMK TIIRKINKMK TLKRKKLLNQ 1000
    ILSSSVESSN KGKVQSKLHN TVSSLAATFG SKLGQQINVS KKGTIYIGKR 1050
    RGRKPKTVLN GILSGSPTSL AVLEQTAQQA AGSALGQILP PLLPSSASSS 1100
    EILPSPICSQ SSGTSGGQSP VSSDAGFVEP SSVPYLHLHS RQGSMIQTLA 1150
    MKKASKGRRR LSPPTLLPNS PSHLSELTSL KEATPSPISE SHSDETIPSD 1200
    SGIGTDNNST SDRAEKFCGQ KKRRHSFEHV SLIPPETSTV LSSLKEKHKH 1250
    KCKRRNHDYL SYDKMKRQKR KRKKKYPQLR NRQDPDFIAE LEELISRLSE 1300
    IRITHRSHHF IPRDLLPTIF RINFNSFYTH PSFPLDPLHY IRKPDLKKKR 1350
    GRPPKMREAM AEMPFMHSLS FPLSSTGFYP SYGMPYSPSP LTAAPIGLGY 1400
    YGRYPPTLYP PPPSPSFTTP LPPPSYMHAG HLLLNPAKYH KKKHKLLRQE 1450
    AFLTTSRTPL LSMSTYPSVP PEMAYGWMVE HKHRHRHKHR EHRSSEQPQV 1500
    SMDTGSSRSV LESLKRYRFG KDAVGERYKH KEKHRCHMSC PHLSPSKSLI 1550
    NREEQWVHRE PSESSPLALG LQTPLQIDCS ESSPSLSLGG FTPNSEPASS 1600
    DEHTNLFTSA IGSCRVSNPN SSGRKKLTDS PGLFSAQDTS LNRLHRKESL 1650
    PSNERAVQTL AGSQPTSDKP SQRPSESTNC SPTRKRSSSE STSSTVNGVP 1700
    SRSPRLVASG DDSVDSLLQR MVQNEDQEPM EKSIDAVIAT ASAPPSSSPG 1750
    RSHSKDRTLG KPDSLLVPAV TSDSCNNSIS LLSEKLTSSC SPHHIKRSVV 1800
    EAMQRQARKM CNYDKILATK KNLDHVNKIL KAKKLQRQAR TGNNFVKRRP 1850
    GRPRKCPLQA VVSMQAFQAA QFVNPELNRD EEGAALHLSP DTVTDVIEAV 1900
    VQSVNLNPEH KKGLKRKGWL LEEQTRKKQK PLPEEEEQEN NKSFNEAPVE 1950
    IPSPSETPAK PSEPESTLQP VLSLIPREKK PPRPPKKKYQ KAGLYSDVYK 2000
    TTDPKSRLIQ LKKEKLEYTP GEHEYGLFPA PIHVVFFVSG KYLRQKRIDF 2050
    QLPYDILWQW KHNQLYKKPD VPLYKKIRSN VYVDVKPLSG YEATTCNCKK 2100
    PDDDTRKGCV DDCLNRMIFA ECSPNTCPCG EQCCNQRIQR HEWVQCLERF 2150
    RAEEKGWGIR TKEPLKAGQF IIEYLGEVVS EQEFRNRMIE QYHNHSDHYC 2200
    LNLDSGMVID SYRMGNEARF INHSCDPNCE MQKWSVNGVY RIGLYALKDM 2250
    PAGTELTYDY NFHSFNVEKQ QLCKCGFEKC RGIIGGKSQR VNGLTSSKNS 2300
    QPMATHKKSG RSKEKRKSKH KLKKRRGHLS EEPSENINTP TRLTPQLQMK 2350
    PMSNRERNFV LKHHVFLVRN WEKIRQKQEE VKHTSDNIHS ASLYTRWNGI 2400
    CRDDGNIKSD VFMTQFSALQ TARSVRTRRL AAAEENIEVA RAARLAQIFK 2450
    EICDGIISYK DSSRQALAAP LLNLPPKKKN ADYYEKISDP LDLITIEKQI 2500
    LTGYYKTVEA FDADMLKVFR NAEKYYGRKS PVGRDVCRLR KAYYNARHEA 2550
    SAQIDEIVGE TASEADSSET SVSEKENGHE KDDDVIRCIC GLYKDEGLMI 2600
    QCDKCMVWQH CDCMGVNSDV EHYLCEQCDP RPVDREVPMI PRPHYAQPGC 2650
    VYFICLLRDD LLLRQGDCVY LMRDSRRTPD GHPVRQSYRL LSHINRDKLD 2700
    IFRIEKLWKN EKEERFAFGH HYFRPHETHH SPSRRFYHNE LFRVPLYEII 2750
    PLEAVVGTCC VLDLYTYCKG RPKGVKEQDV YICDYRLDKS AHLFYKIHRN 2800
    RYPVCTKPYA FDHFPKKLTP KKDFSPHYVP DNYKRNGGRS SWKSERSKPP 2850
    LKDLGQEDDA LPLIEEVLAS QEQAANEIPS LEEPEREGAT ANVSEGEKKT 2900
    EESSQEPQST CTPEERRHNQ RERLNQILLN LLEKIPGKNA IDVTYLLEEG 2950
    SGRKLRRRTL FIPENSFRK 2969
    Length:2,969
    Mass (Da):332,790
    Last modified:October 31, 2006 - v2
    Checksum:iDA0135C72A2E2065
    GO
    Isoform 2 (identifier: Q9NR48-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2035-2039: Missing.

    Show »
    Length:2,964
    Mass (Da):332,211
    Checksum:i4D6E14A56BB20329
    GO

    Sequence cautioni

    The sequence BAA92658.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2594 – 25941K → N in AAF68983. (PubMed:10860993)Curated
    Sequence conflicti2697 – 26971D → H in AAF68983. (PubMed:10860993)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti277 – 2771S → G.1 Publication
    VAR_069405
    Natural varianti724 – 7241A → S Found in a patient with mental retardation, no speech and facial dysmorphisms. 1 Publication
    VAR_069406
    Natural varianti972 – 9721K → R.1 Publication
    VAR_069407
    Natural varianti1276 – 12761Y → H.1 Publication
    VAR_069408
    Natural varianti1416 – 14161S → P.
    Corresponds to variant rs13373934 [ dbSNP | Ensembl ].
    VAR_055905
    Natural varianti1771 – 17711T → A.1 Publication
    Corresponds to variant rs4971053 [ dbSNP | Ensembl ].
    VAR_028949
    Natural varianti1775 – 17751C → W.1 Publication
    VAR_069409
    Natural varianti2853 – 28531D → G.1 Publication
    VAR_069410

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2035 – 20395Missing in isoform 2. 1 PublicationVSP_039421

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF257305 mRNA. Translation: AAF68983.1.
    AL139410, AL353807 Genomic DNA. Translation: CAI12716.2.
    AL139410, AL353807 Genomic DNA. Translation: CAI12722.1.
    AL353807, AL139410 Genomic DNA. Translation: CAI13211.2.
    AL353807, AL139410 Genomic DNA. Translation: CAI13212.1.
    AB037841 mRNA. Translation: BAA92658.1. Different initiation.
    AB209068 mRNA. Translation: BAD92305.1.
    DB282357 mRNA. No translation available.
    CCDSiCCDS1113.2. [Q9NR48-2]
    RefSeqiNP_060959.2. NM_018489.2. [Q9NR48-2]
    XP_006711513.1. XM_006711450.1. [Q9NR48-2]
    XP_006711514.1. XM_006711451.1. [Q9NR48-2]
    UniGeneiHs.491060.

    Genome annotation databases

    EnsembliENST00000368346; ENSP00000357330; ENSG00000116539. [Q9NR48-1]
    ENST00000392403; ENSP00000376204; ENSG00000116539. [Q9NR48-2]
    GeneIDi55870.
    KEGGihsa:55870.
    UCSCiuc001fkt.3. human. [Q9NR48-2]
    uc009wqq.3. human. [Q9NR48-1]

    Polymorphism databases

    DMDMi117949323.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF257305 mRNA. Translation: AAF68983.1 .
    AL139410 , AL353807 Genomic DNA. Translation: CAI12716.2 .
    AL139410 , AL353807 Genomic DNA. Translation: CAI12722.1 .
    AL353807 , AL139410 Genomic DNA. Translation: CAI13211.2 .
    AL353807 , AL139410 Genomic DNA. Translation: CAI13212.1 .
    AB037841 mRNA. Translation: BAA92658.1 . Different initiation.
    AB209068 mRNA. Translation: BAD92305.1 .
    DB282357 mRNA. No translation available.
    CCDSi CCDS1113.2. [Q9NR48-2 ]
    RefSeqi NP_060959.2. NM_018489.2. [Q9NR48-2 ]
    XP_006711513.1. XM_006711450.1. [Q9NR48-2 ]
    XP_006711514.1. XM_006711451.1. [Q9NR48-2 ]
    UniGenei Hs.491060.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3MQM X-ray 2.54 A/B 2438-2561 [» ]
    3OPE X-ray 2.90 A/B 2074-2293 [» ]
    ProteinModelPortali Q9NR48.
    SMRi Q9NR48. Positions 1981-2285, 2436-2561, 2584-2636, 2704-2806.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120969. 6 interactions.
    IntActi Q9NR48. 2 interactions.
    MINTi MINT-1183184.
    STRINGi 9606.ENSP00000376204.

    PTM databases

    PhosphoSitei Q9NR48.

    Polymorphism databases

    DMDMi 117949323.

    Proteomic databases

    MaxQBi Q9NR48.
    PaxDbi Q9NR48.
    PRIDEi Q9NR48.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368346 ; ENSP00000357330 ; ENSG00000116539 . [Q9NR48-1 ]
    ENST00000392403 ; ENSP00000376204 ; ENSG00000116539 . [Q9NR48-2 ]
    GeneIDi 55870.
    KEGGi hsa:55870.
    UCSCi uc001fkt.3. human. [Q9NR48-2 ]
    uc009wqq.3. human. [Q9NR48-1 ]

    Organism-specific databases

    CTDi 55870.
    GeneCardsi GC01M155305.
    HGNCi HGNC:19088. ASH1L.
    HPAi HPA004806.
    MIMi 607999. gene.
    neXtProti NX_Q9NR48.
    PharmGKBi PA134891064.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2940.
    HOGENOMi HOG000034094.
    HOVERGENi HBG080871.
    InParanoidi Q9NR48.
    KOi K06101.
    OMAi PENSFRK.
    OrthoDBi EOG7ZPNJ4.
    PhylomeDBi Q9NR48.
    TreeFami TF106416.

    Miscellaneous databases

    ChiTaRSi ASH1L. human.
    EvolutionaryTracei Q9NR48.
    GeneWikii ASH1L.
    GenomeRNAii 55870.
    NextBioi 61186.
    PROi Q9NR48.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NR48.
    Bgeei Q9NR48.
    CleanExi HS_ASH1L.
    Genevestigatori Q9NR48.

    Family and domain databases

    Gene3Di 1.20.920.10. 1 hit.
    3.30.40.10. 1 hit.
    InterProi IPR017956. AT_hook_DNA-bd_motif.
    IPR006560. AWS.
    IPR001025. BAH_dom.
    IPR001487. Bromodomain.
    IPR003616. Post-SET_dom.
    IPR001214. SET_dom.
    IPR019786. Zinc_finger_PHD-type_CS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF01426. BAH. 1 hit.
    PF00439. Bromodomain. 1 hit.
    PF00628. PHD. 1 hit.
    PF00856. SET. 1 hit.
    [Graphical view ]
    SMARTi SM00384. AT_hook. 4 hits.
    SM00570. AWS. 1 hit.
    SM00439. BAH. 1 hit.
    SM00297. BROMO. 1 hit.
    SM00249. PHD. 1 hit.
    SM00508. PostSET. 1 hit.
    SM00317. SET. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47370. SSF47370. 1 hit.
    SSF57903. SSF57903. 1 hit.
    PROSITEi PS51215. AWS. 1 hit.
    PS51038. BAH. 1 hit.
    PS50014. BROMODOMAIN_2. 1 hit.
    PS50868. POST_SET. 1 hit.
    PS50280. SET. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "huASH1 protein, a putative transcription factor encoded by a human homologue of the Drosophila ash1 gene, localizes to both nuclei and cell-cell tight junctions."
      Nakamura T., Blechman J., Tada S., Rozovskaia T., Itoyama T., Bullrich F., Mazo A., Croce C.M., Geiger B., Canaani E.
      Proc. Natl. Acad. Sci. U.S.A. 97:7284-7289(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT ALA-1771.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1345.
      Tissue: Brain.
    4. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 710-1345.
      Tissue: Brain.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2000-2183 (ISOFORM 2).
    6. "The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells."
      Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., Haines D.S., Figeys D.
      J. Proteome Res. 6:298-305(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-402 AND LYS-406.
      Tissue: Lung adenocarcinoma.
    7. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-375, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Crystal structure of the human histone methyltransferase ASH1L catalytic domain and its implications for the regulatory mechanism."
      An S., Yeo K.J., Jeon Y.H., Song J.J.
      J. Biol. Chem. 286:8369-8374(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 2074-2293 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE, FUNCTION, CATALYTIC ACTIVITY.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 2438-2561.
    12. Cited for: VARIANTS GLY-277; SER-724; ARG-972; HIS-1276; TRP-1775 AND GLY-2853.

    Entry informationi

    Entry nameiASH1L_HUMAN
    AccessioniPrimary (citable) accession number: Q9NR48
    Secondary accession number(s): Q59GP1
    , Q5T714, Q5T715, Q9P2C7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 31, 2006
    Last sequence update: October 31, 2006
    Last modified: October 1, 2014
    This is version 113 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3