Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9UBL3

- ASH2L_HUMAN

UniProt

Q9UBL3 - ASH2L_HUMAN

Protein

Set1/Ash2 histone methyltransferase complex subunit ASH2

Gene

ASH2L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3, but not if the neighboring 'Lys-9' residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1 – 6666PHD-type; atypicalAdd
    BLAST
    Zinc fingeri117 – 15034C4-typeAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. transcription regulatory region DNA binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to DNA damage stimulus Source: MGI
    2. hemopoiesis Source: UniProtKB
    3. histone H3-K4 methylation Source: UniProtKB
    4. positive regulation of cell proliferation Source: UniProtKB
    5. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    6. regulation of transcription, DNA-templated Source: UniProtKB
    7. response to estrogen Source: UniProtKB
    8. transcription, DNA-templated Source: UniProtKB
    9. transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Molecular functioni

    Chromatin regulator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Set1/Ash2 histone methyltransferase complex subunit ASH2
    Alternative name(s):
    ASH2-like protein
    Gene namesi
    Name:ASH2L
    Synonyms:ASH2L1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:744. ASH2L.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. histone methyltransferase complex Source: UniProtKB
    2. nucleus Source: UniProtKB
    3. Set1C/COMPASS complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi296 – 2961R → K: Abolishes methylation. 1 Publication
    Mutagenesisi300 – 3001R → K: Slightly decreased methylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA25044.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 628628Set1/Ash2 histone methyltransferase complex subunit ASH2PRO_0000064697Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei101 – 1011Phosphoserine1 Publication
    Modified residuei296 – 2961Asymmetric dimethylarginine; by PRMT1 and PRMT51 Publication

    Post-translational modificationi

    Both monomethylated and dimethylated on arginine residues in the C-terminus. Arg-296 is the major site. Methylation is not required for nuclear localization, nor for MLL complex integrity or maintenance of global histone H3K4me3 levels.1 Publication

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UBL3.
    PaxDbiQ9UBL3.
    PRIDEiQ9UBL3.

    PTM databases

    PhosphoSiteiQ9UBL3.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Predominantly expressed in adult heart and testis and fetal lung and liver, with barely detectable expression in adult lung, liver, kidney, prostate, and peripheral leukocytes.1 Publication

    Gene expression databases

    ArrayExpressiQ9UBL3.
    BgeeiQ9UBL3.
    CleanExiHS_ASH2L.
    GenevestigatoriQ9UBL3.

    Organism-specific databases

    HPAiHPA042289.

    Interactioni

    Subunit structurei

    Interacts with HCFC1. Core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7. Each complex is at least composed of ASH2L, RBBP5, WDR5, DPY30, one or more specific histone methyltransferases (KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and KMT2B/MLL4), and the facultative components PAGR1, BAP18, CHD8, E2F6, HCFC1, HCFC2, HSP70, INO80C, KDM6A, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, KAT8/MOF, NCOA6, PAXIP1/PTIP, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9, TEX10 and alpha- and beta-tubulin. Interacts with DPY30 and RBBP5; the interaction is direct. Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30. Interacts with SETD1A and SETD1B.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CHD8Q9HCK82EBI-540797,EBI-1169146
    DPY30Q9C0056EBI-540797,EBI-744973
    EP300Q094725EBI-540797,EBI-447295
    HCFC1P516105EBI-540797,EBI-396176
    NCOA6Q146867EBI-540797,EBI-78670
    RBBP5Q1529113EBI-540797,EBI-592823
    TP53P046375EBI-540797,EBI-366083

    Protein-protein interaction databases

    BioGridi114528. 51 interactions.
    DIPiDIP-29222N.
    IntActiQ9UBL3. 41 interactions.
    MINTiMINT-1194078.
    STRINGi9606.ENSP00000340896.

    Structurei

    Secondary structure

    1
    628
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi114 – 1163
    Turni118 – 1203
    Beta strandi123 – 1253
    Helixi126 – 1294
    Beta strandi142 – 1465
    Turni148 – 1503
    Beta strandi157 – 1604
    Helixi165 – 18319
    Turni193 – 1964
    Helixi197 – 2037
    Helixi205 – 2073
    Helixi219 – 2213
    Helixi223 – 2286
    Turni231 – 2333
    Beta strandi234 – 2396
    Helixi248 – 2503
    Beta strandi252 – 2576
    Helixi261 – 2633
    Helixi371 – 3733
    Beta strandi376 – 3783
    Beta strandi383 – 3886
    Beta strandi392 – 3943
    Beta strandi398 – 4025
    Beta strandi408 – 4136
    Beta strandi416 – 42914
    Beta strandi435 – 4417
    Beta strandi457 – 4615
    Turni462 – 4654
    Beta strandi467 – 4693
    Beta strandi472 – 4743
    Beta strandi485 – 4928
    Beta strandi540 – 5456
    Beta strandi548 – 5569
    Beta strandi562 – 57110
    Beta strandi573 – 5775
    Beta strandi579 – 5813
    Helixi594 – 5985
    Beta strandi599 – 6024

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3RSNX-ray2.10A96-271[»]
    3S32X-ray2.45A95-280[»]
    3TOJX-ray2.07A/B370-496[»]
    A/B539-617[»]
    ProteinModelPortaliQ9UBL3.
    SMRiQ9UBL3. Positions 105-269, 370-605.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini360 – 583224B30.2/SPRYPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni67 – 177111DNA-bindingAdd
    BLAST

    Sequence similaritiesi

    Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
    Contains 1 PHD-type zinc finger.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1 – 6666PHD-type; atypicalAdd
    BLAST
    Zinc fingeri117 – 15034C4-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG249281.
    HOGENOMiHOG000013137.
    HOVERGENiHBG050592.
    InParanoidiQ9UBL3.
    KOiK14964.
    OMAiRQEFDES.
    OrthoDBiEOG70KGP3.
    PhylomeDBiQ9UBL3.
    TreeFamiTF314785.

    Family and domain databases

    InterProiIPR001870. B30.2/SPRY.
    IPR008985. ConA-like_lec_gl_sf.
    IPR018355. SPla/RYanodine_receptor_subgr.
    IPR003877. SPRY_rcpt.
    [Graphical view]
    PfamiPF00622. SPRY. 1 hit.
    [Graphical view]
    SMARTiSM00449. SPRY. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 2 hits.
    PROSITEiPS50188. B302_SPRY. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UBL3-1) [UniParc]FASTAAdd to Basket

    Also known as: ASH2L1

    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

    MAAAGAGPGQ EAGAGPGPGA VANATGAEEG EMKPVAAGAA APPGEGISAA    50
    PTVEPSSGEA EGGEANLVDV SGGLETESSN GKDTLEGAGD TSEVMDTQAG 100
    SVDEENGRQL GEVELQCGIC TKWFTADTFG IDTSSCLPFM TNYSFHCNVC 150
    HHSGNTYFLR KQANLKEMCL SALANLTWQS RTQDEHPKTM FSKDKDIIPF 200
    IDKYWECMTT RQRPGKMTWP NNIVKTMSKE RDVFLVKEHP DPGSKDPEED 250
    YPKFGLLDQD LSNIGPAYDN QKQSSAVSTS GNLNGGIAAG SSGKGRGAKR 300
    KQQDGGTTGT TKKARSDPLF SAQRLPPHGY PLEHPFNKDG YRYILAEPDP 350
    HAPDPEKLEL DCWAGKPIPG DLYRACLYER VLLALHDRAP QLKISDDRLT 400
    VVGEKGYSMV RASHGVRKGA WYFEITVDEM PPDTAARLGW SQPLGNLQAP 450
    LGYDKFSYSW RSKKGTKFHQ SIGKHYSSGY GQGDVLGFYI NLPEDTETAK 500
    SLPDTYKDKA LIKFKSYLYF EEKDFVDKAE KSLKQTPHSE IIFYKNGVNQ 550
    GVAYKDIFEG VYFPAISLYK SCTVSINFGP CFKYPPKDLT YRPMSDMGWG 600
    AVVEHTLADV LYHVETEVDG RRSPPWEP 628
    Length:628
    Mass (Da):68,723
    Last modified:May 1, 2000 - v1
    Checksum:i8F5F007430D4B863
    GO
    Isoform 2 (identifier: Q9UBL3-2) [UniParc]FASTAAdd to Basket

    Also known as: ASH2L2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-94: Missing.
         541-573: Missing.

    Show »
    Length:501
    Mass (Da):56,477
    Checksum:iBD76059C4DE39703
    GO
    Isoform 3 (identifier: Q9UBL3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-94: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:534
    Mass (Da):60,208
    Checksum:i4317F1206E97C897
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti212 – 2121Q → H in AAC13564. (PubMed:11466562)Curated
    Sequence conflicti217 – 2171M → T in AAC13564. (PubMed:11466562)Curated
    Sequence conflicti292 – 2921S → T in AAC13563. (PubMed:11466562)Curated
    Sequence conflicti351 – 3511H → Q in AAC13564. (PubMed:11466562)Curated
    Sequence conflicti360 – 3601L → I in AAC13564. (PubMed:11466562)Curated
    Sequence conflicti369 – 3691P → S in AAC13564. (PubMed:11466562)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti478 – 4781S → F.
    Corresponds to variant rs34167006 [ dbSNP | Ensembl ].
    VAR_050679

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9494Missing in isoform 2 and isoform 3. 3 PublicationsVSP_007577Add
    BLAST
    Alternative sequencei541 – 57333Missing in isoform 2. 1 PublicationVSP_007578Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF056718 mRNA. Translation: AAC13564.1.
    AF056717 mRNA. Translation: AAC13563.1.
    AB022785 Genomic DNA. Translation: BAA74520.1.
    AB020982 mRNA. Translation: BAA35127.1.
    AK291938 mRNA. Translation: BAF84627.1.
    CH471080 Genomic DNA. Translation: EAW63337.1.
    CH471080 Genomic DNA. Translation: EAW63336.1.
    CH471080 Genomic DNA. Translation: EAW63340.1.
    BC015936 mRNA. Translation: AAH15936.1.
    CCDSiCCDS47840.1. [Q9UBL3-3]
    CCDS59100.1. [Q9UBL3-2]
    CCDS6101.1. [Q9UBL3-1]
    RefSeqiNP_001098684.1. NM_001105214.2. [Q9UBL3-3]
    NP_001248761.1. NM_001261832.1. [Q9UBL3-2]
    NP_004665.2. NM_004674.4. [Q9UBL3-1]
    UniGeneiHs.521530.

    Genome annotation databases

    EnsembliENST00000343823; ENSP00000340896; ENSG00000129691. [Q9UBL3-1]
    ENST00000428278; ENSP00000395310; ENSG00000129691. [Q9UBL3-3]
    ENST00000521652; ENSP00000430259; ENSG00000129691. [Q9UBL3-2]
    GeneIDi9070.
    KEGGihsa:9070.
    UCSCiuc003xkt.5. human. [Q9UBL3-1]
    uc010lwa.4. human. [Q9UBL3-2]

    Polymorphism databases

    DMDMi32141382.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF056718 mRNA. Translation: AAC13564.1 .
    AF056717 mRNA. Translation: AAC13563.1 .
    AB022785 Genomic DNA. Translation: BAA74520.1 .
    AB020982 mRNA. Translation: BAA35127.1 .
    AK291938 mRNA. Translation: BAF84627.1 .
    CH471080 Genomic DNA. Translation: EAW63337.1 .
    CH471080 Genomic DNA. Translation: EAW63336.1 .
    CH471080 Genomic DNA. Translation: EAW63340.1 .
    BC015936 mRNA. Translation: AAH15936.1 .
    CCDSi CCDS47840.1. [Q9UBL3-3 ]
    CCDS59100.1. [Q9UBL3-2 ]
    CCDS6101.1. [Q9UBL3-1 ]
    RefSeqi NP_001098684.1. NM_001105214.2. [Q9UBL3-3 ]
    NP_001248761.1. NM_001261832.1. [Q9UBL3-2 ]
    NP_004665.2. NM_004674.4. [Q9UBL3-1 ]
    UniGenei Hs.521530.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3RSN X-ray 2.10 A 96-271 [» ]
    3S32 X-ray 2.45 A 95-280 [» ]
    3TOJ X-ray 2.07 A/B 370-496 [» ]
    A/B 539-617 [» ]
    ProteinModelPortali Q9UBL3.
    SMRi Q9UBL3. Positions 105-269, 370-605.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114528. 51 interactions.
    DIPi DIP-29222N.
    IntActi Q9UBL3. 41 interactions.
    MINTi MINT-1194078.
    STRINGi 9606.ENSP00000340896.

    PTM databases

    PhosphoSitei Q9UBL3.

    Polymorphism databases

    DMDMi 32141382.

    Proteomic databases

    MaxQBi Q9UBL3.
    PaxDbi Q9UBL3.
    PRIDEi Q9UBL3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000343823 ; ENSP00000340896 ; ENSG00000129691 . [Q9UBL3-1 ]
    ENST00000428278 ; ENSP00000395310 ; ENSG00000129691 . [Q9UBL3-3 ]
    ENST00000521652 ; ENSP00000430259 ; ENSG00000129691 . [Q9UBL3-2 ]
    GeneIDi 9070.
    KEGGi hsa:9070.
    UCSCi uc003xkt.5. human. [Q9UBL3-1 ]
    uc010lwa.4. human. [Q9UBL3-2 ]

    Organism-specific databases

    CTDi 9070.
    GeneCardsi GC08P037963.
    H-InvDB HIX0007454.
    HGNCi HGNC:744. ASH2L.
    HPAi HPA042289.
    MIMi 604782. gene.
    neXtProti NX_Q9UBL3.
    PharmGKBi PA25044.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG249281.
    HOGENOMi HOG000013137.
    HOVERGENi HBG050592.
    InParanoidi Q9UBL3.
    KOi K14964.
    OMAi RQEFDES.
    OrthoDBi EOG70KGP3.
    PhylomeDBi Q9UBL3.
    TreeFami TF314785.

    Enzyme and pathway databases

    Reactomei REACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_200753. formation of the beta-catenin:TCF transactivating complex.

    Miscellaneous databases

    ChiTaRSi ASH2L. human.
    GeneWikii ASH2L.
    GenomeRNAii 9070.
    NextBioi 33985.
    PROi Q9UBL3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBL3.
    Bgeei Q9UBL3.
    CleanExi HS_ASH2L.
    Genevestigatori Q9UBL3.

    Family and domain databases

    InterProi IPR001870. B30.2/SPRY.
    IPR008985. ConA-like_lec_gl_sf.
    IPR018355. SPla/RYanodine_receptor_subgr.
    IPR003877. SPRY_rcpt.
    [Graphical view ]
    Pfami PF00622. SPRY. 1 hit.
    [Graphical view ]
    SMARTi SM00449. SPRY. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 2 hits.
    PROSITEi PS50188. B302_SPRY. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "ASH2L: alternative splicing and downregulation during induced megakaryocytic differentiation of multipotential leukemia cell lines."
      Wang J., Zhou Y., Yin B., Du G., Huang X., Li G., Shen Y., Yuan J., Qiang B.
      J. Mol. Med. 79:399-405(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Fetal brain.
    2. "Cloning and characterization of ASH2L and ash2l, human and mouse homologs of the Drosophila ash2 gene."
      Ikegawa S., Isomura M., Koshizuka Y., Nakamura Y.
      Cytogenet. Cell Genet. 84:167-172(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY.
    3. "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] (ISOFORM 3).
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 3).
      Tissue: Skin.
    6. "Human Sin3 deacetylase and trithorax-related Set1/Ash2 histone H3-K4 methyltransferase are tethered together selectively by the cell-proliferation factor HCF-1."
      Wysocka J., Myers M.P., Laherty C.D., Eisenman R.N., Herr W.
      Genes Dev. 17:896-911(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HCFC1.
    7. Cited for: IDENTIFICATION IN THE MEN1-ASSOCIATED HISTONE METHYLTRANSFERASE COMPLEX.
    8. "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression."
      Yokoyama A., Wang Z., Wysocka J., Sanyal M., Aufiero D.J., Kitabayashi I., Herr W., Cleary M.L.
      Mol. Cell. Biol. 24:5639-5649(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL-LIKE COMPLEX.
    9. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
      Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
      Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
    10. "CpG-binding protein (CXXC finger protein 1) is a component of the mammalian Set1 histone H3-Lys4 methyltransferase complex, the analogue of the yeast Set1/COMPASS complex."
      Lee J.-H., Skalnik D.G.
      J. Biol. Chem. 280:41725-41731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE SET1 COMPLEX.
    11. "Identification and characterization of the human Set1B histone H3-Lys4 methyltransferase complex."
      Lee J.-H., Tate C.M., You J.-S., Skalnik D.G.
      J. Biol. Chem. 282:13419-13428(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, IDENTIFICATION IN THE SET1 COMPLEX.
    12. "PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex."
      Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T., Dressler G.R., Copeland T.D., Kalkum M., Ge K.
      J. Biol. Chem. 282:20395-20406(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MLL2/3 COMPLEX.
    13. "Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A Histone H3-Lys4 methyltransferase complex to transcription start sites of transcribed human genes."
      Lee J.H., Skalnik D.G.
      Mol. Cell. Biol. 28:609-618(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN SET1 COMPLEX, INTERACTION WITH SETD1A AND SETD1B.
    14. "Molecular regulation of H3K4 trimethylation by Wdr82, a component of human Set1/COMPASS."
      Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M., Shilatifard A.
      Mol. Cell. Biol. 28:7337-7344(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN SET1 COMPLEX.
    15. "On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex."
      Patel A., Dharmarajan V., Vought V.E., Cosgrove M.S.
      J. Biol. Chem. 284:24242-24256(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CHARACTERIZATION OF THE MLL1/MLL COMPLEX, INTERACTION WITH DPY30 AND RBBP5.
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Protein-arginine methyltransferase 1 (PRMT1) methylates Ash2L, a shared component of mammalian histone H3K4 methyltransferase complexes."
      Butler J.S., Zurita-Lopez C.I., Clarke S.G., Bedford M.T., Dent S.Y.
      J. Biol. Chem. 286:12234-12244(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: METHYLATION AT ARG-296 BY PRMT1 AND PRMT5, MUTAGENESIS OF ARG-296 AND ARG-300.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Crystal structure of the N-terminal region of human Ash2L shows a winged-helix motif involved in DNA binding."
      Chen Y., Wan B., Wang K.C., Cao F., Yang Y., Protacio A., Dou Y., Chang H.Y., Lei M.
      EMBO Rep. 12:797-803(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 96-271, DOMAIN PHD, DNA-BINDING REGION.

    Entry informationi

    Entry nameiASH2L_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBL3
    Secondary accession number(s): A8K7C3
    , D3DSW9, O60659, O60660, Q96B62
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 16, 2003
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 130 of the entry and version 1 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 8
      Human chromosome 8: 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