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Q9UBL3

- ASH2L_HUMAN

UniProt

Q9UBL3 - ASH2L_HUMAN

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Protein

Set1/Ash2 histone methyltransferase complex subunit ASH2

Gene
ASH2L, ASH2L1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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 Inferred 1 Publication

GO - Cellular componenti

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

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. 50 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini360 – 583224B30.2/SPRYAdd
BLAST

Region

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

Sequence similaritiesi

Contains 1 B30.2/SPRY domain.

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

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. VSP_007577Add
BLAST
Alternative sequencei541 – 57333Missing in isoform 2. VSP_007578Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti212 – 2121Q → H in AAC13564. 1 Publication
Sequence conflicti217 – 2171M → T in AAC13564. 1 Publication
Sequence conflicti292 – 2921S → T in AAC13563. 1 Publication
Sequence conflicti351 – 3511H → Q in AAC13564. 1 Publication
Sequence conflicti360 – 3601L → I in AAC13564. 1 Publication
Sequence conflicti369 – 3691P → S in AAC13564. 1 Publication

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

EnsembliENST00000250635; ENSP00000250635; ENSG00000129691. [Q9UBL3-2]
ENST00000343823; 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. 50 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 ENST00000250635 ; ENSP00000250635 ; ENSG00000129691 . [Q9UBL3-2 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 129 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

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