Q9UBL3 (ASH2L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Set1/Ash2 histone methyltransferase complex subunit ASH2

Alternative name(s):
ASH2-like protein

Gene names

Name:	ASH2L
Synonyms:	ASH2L1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	628 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.6 Ref.15
Subunit structure	Interacts with HCFC1. Core component of several methyltransferase-containing complexes including MLL1/MLL, ASCOM, MLL2/MLL3 and MLL3/MLL4. Each complex is at least composed of ASH2L, RBBP5, DPY30, WDR5, one or more specific histone methyltransferases (MLL, MLL2, MLL3 and MLL4), and the facultative components C16orf53/PA1, C17orf49, CHD8, E2F6, HCFC1, HCFC2, HSP70, IN80C, KDM6A, KIAA1267, LAS1L, MAX, MCRS1, MEN1, MGA, KAT8/MOF, NCOA6, PAXIP1/PTIP, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. 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. Ref.6 Ref.7 Ref.13 Ref.15
Subcellular location	Nucleus Probable Ref.11.
Tissue specificity	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. Ref.2
Sequence similarities	Contains 1 B30.2/SPRY domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	hemopoiesis Non-traceable author statement Ref.1. Source: UniProtKB histone H3-K4 methylation Inferred from direct assay Ref.11Ref.15. Source: UniProtKB positive regulation of cell proliferation Inferred from mutant phenotype. Source: UniProtKB regulation of transcription, DNA-dependent Non-traceable author statement Ref.2. Source: UniProtKB response to estrogen stimulus Inferred from direct assay. Source: UniProtKB transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc
Cellular component	Set1C/COMPASS complex Inferred from direct assay Ref.13Ref.14. Source: UniProtKB
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.6Ref.13Ref.15. Source: UniProtKB transcription regulatory region DNA binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DPY30	Q9C005	4	EBI-540797,EBI-744973
HCFC1	P51610	4	EBI-540797,EBI-396176
RBBP5	Q15291	10	EBI-540797,EBI-592823

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UBL3-1)

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.

Isoform 2 (identifier: Q9UBL3-2)

Also known as: ASH2L2;

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

Isoform 3 (identifier: Q9UBL3-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 628

628

Set1/Ash2 histone methyltransferase complex subunit ASH2

PRO_0000064697

Regions

Domain

360 – 583

224

B30.2/SPRY

Zinc finger

117 – 150

34

C4-type

Natural variations

Alternative sequence

1 – 94

94

Missing in isoform 2 and isoform 3.

VSP_007577

Alternative sequence

541 – 573

33

Missing in isoform 2.

VSP_007578

Natural variant

478

1

S → F.
Corresponds to variant rs34167006 [ dbSNP | Ensembl ].

VAR_050679

Experimental info

Sequence conflict

212

1

Q → H in AAC13564. Ref.1

Sequence conflict

217

1

M → T in AAC13564. Ref.1

Sequence conflict

292

1

S → T in AAC13563. Ref.1

Sequence conflict

351

1

H → Q in AAC13564. Ref.1

Sequence conflict

360

1

L → I in AAC13564. Ref.1

Sequence conflict

369

1

P → S in AAC13564. Ref.1

Secondary structure

1

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628

Helix Strand Turn

Details...

Beta strand

114 – 116

3

Beta strand

123 – 125

3

Helix

126 – 128

3

Beta strand

142 – 146

5

Turn

148 – 150

3

Beta strand

157 – 160

4

Helix

165 – 183

19

Turn

193 – 196

4

Helix

197 – 203

7

Helix

205 – 207

3

Helix

219 – 221

3

Helix

223 – 228

6

Turn

231 – 233

3

Beta strand

237 – 239

3

Helix

248 – 250

3

Beta strand

252 – 254

3

Helix

261 – 263

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (ASH2L1) [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 8F5F007430D4B863	FASTA	628	68,723
	10 20 30 40 50 60 MAAAGAGPGQ EAGAGPGPGA VANATGAEEG EMKPVAAGAA APPGEGISAA PTVEPSSGEA 70 80 90 100 110 120 EGGEANLVDV SGGLETESSN GKDTLEGAGD TSEVMDTQAG SVDEENGRQL GEVELQCGIC 130 140 150 160 170 180 TKWFTADTFG IDTSSCLPFM TNYSFHCNVC HHSGNTYFLR KQANLKEMCL SALANLTWQS 190 200 210 220 230 240 RTQDEHPKTM FSKDKDIIPF IDKYWECMTT RQRPGKMTWP NNIVKTMSKE RDVFLVKEHP 250 260 270 280 290 300 DPGSKDPEED YPKFGLLDQD LSNIGPAYDN QKQSSAVSTS GNLNGGIAAG SSGKGRGAKR 310 320 330 340 350 360 KQQDGGTTGT TKKARSDPLF SAQRLPPHGY PLEHPFNKDG YRYILAEPDP HAPDPEKLEL 370 380 390 400 410 420 DCWAGKPIPG DLYRACLYER VLLALHDRAP QLKISDDRLT VVGEKGYSMV RASHGVRKGA 430 440 450 460 470 480 WYFEITVDEM PPDTAARLGW SQPLGNLQAP LGYDKFSYSW RSKKGTKFHQ SIGKHYSSGY 490 500 510 520 530 540 GQGDVLGFYI NLPEDTETAK SLPDTYKDKA LIKFKSYLYF EEKDFVDKAE KSLKQTPHSE 550 560 570 580 590 600 IIFYKNGVNQ GVAYKDIFEG VYFPAISLYK SCTVSINFGP CFKYPPKDLT YRPMSDMGWG 610 620 AVVEHTLADV LYHVETEVDG RRSPPWEP
	Isoform 2 (ASH2L2) [UniParc]. Checksum: BD76059C4DE39703	FASTA	501	56,477
	10 20 30 40 50 60 MDTQAGSVDE ENGRQLGEVE LQCGICTKWF TADTFGIDTS SCLPFMTNYS FHCNVCHHSG 70 80 90 100 110 120 NTYFLRKQAN LKEMCLSALA NLTWQSRTQD EHPKTMFSKD KDIIPFIDKY WECMTTRQRP 130 140 150 160 170 180 GKMTWPNNIV KTMSKERDVF LVKEHPDPGS KDPEEDYPKF GLLDQDLSNI GPAYDNQKQS 190 200 210 220 230 240 SAVSTSGNLN GGIAAGSSGK GRGAKRKQQD GGTTGTTKKA RSDPLFSAQR LPPHGYPLEH 250 260 270 280 290 300 PFNKDGYRYI LAEPDPHAPD PEKLELDCWA GKPIPGDLYR ACLYERVLLA LHDRAPQLKI 310 320 330 340 350 360 SDDRLTVVGE KGYSMVRASH GVRKGAWYFE ITVDEMPPDT AARLGWSQPL GNLQAPLGYD 370 380 390 400 410 420 KFSYSWRSKK GTKFHQSIGK HYSSGYGQGD VLGFYINLPE DTETAKSLPD TYKDKALIKF 430 440 450 460 470 480 KSYLYFEEKD FVDKAEKSLK QTPHSEVSIN FGPCFKYPPK DLTYRPMSDM GWGAVVEHTL 490 500 ADVLYHVETE VDGRRSPPWE P
	Isoform 3 [UniParc]. Checksum: 4317F1206E97C897	FASTA	534	60,208
	10 20 30 40 50 60 MDTQAGSVDE ENGRQLGEVE LQCGICTKWF TADTFGIDTS SCLPFMTNYS FHCNVCHHSG 70 80 90 100 110 120 NTYFLRKQAN LKEMCLSALA NLTWQSRTQD EHPKTMFSKD KDIIPFIDKY WECMTTRQRP 130 140 150 160 170 180 GKMTWPNNIV KTMSKERDVF LVKEHPDPGS KDPEEDYPKF GLLDQDLSNI GPAYDNQKQS 190 200 210 220 230 240 SAVSTSGNLN GGIAAGSSGK GRGAKRKQQD GGTTGTTKKA RSDPLFSAQR LPPHGYPLEH 250 260 270 280 290 300 PFNKDGYRYI LAEPDPHAPD PEKLELDCWA GKPIPGDLYR ACLYERVLLA LHDRAPQLKI 310 320 330 340 350 360 SDDRLTVVGE KGYSMVRASH GVRKGAWYFE ITVDEMPPDT AARLGWSQPL GNLQAPLGYD 370 380 390 400 410 420 KFSYSWRSKK GTKFHQSIGK HYSSGYGQGD VLGFYINLPE DTETAKSLPD TYKDKALIKF 430 440 450 460 470 480 KSYLYFEEKD FVDKAEKSLK QTPHSEIIFY KNGVNQGVAY KDIFEGVYFP AISLYKSCTV 490 500 510 520 530 SINFGPCFKY PPKDLTYRPM SDMGWGAVVE HTLADVLYHV ETEVDGRRSP PWEP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11466562] [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: 10393421] [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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [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: 12670868] [Abstract] Cited for: FUNCTION, INTERACTION WITH HCFC1.
[7]	"Menin associates with a trithorax family histone methyltransferase complex and with the hoxc8 locus." Hughes C.M., Rozenblatt-Rosen O., Milne T.A., Copeland T.D., Levine S.S., Lee J.C., Hayes D.N., Shanmugam K.S., Bhattacharjee A., Biondi C.A., Kay G.F., Hayward N.K., Hess J.L., Meyerson M. Mol. Cell 13:587-597(2004) [PubMed: 14992727] [Abstract] Cited for: INTERACTION WITH MEN1.
[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: 15199122] [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: 15960975] [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: 16253997] [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: 17355966] [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: 17500065] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MLL-LIKE 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: 17998332] [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: 18838538] [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: 19556245] [Abstract] Cited for: FUNCTION, CHARACTERIZATION OF THE MLL1/MLL COMPLEX, INTERACTION WITH DPY30 AND RBBP5.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00328658.
IPI00328659.
IPI00333837.

RefSeq

NP_001098684.1. NM_001105214.1.
NP_004665.2. NM_004674.3.

UniGene

Hs.521530.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3RSN	X-ray	2.10	A	96-271	[»]
3S32	X-ray	2.45	A	95-280	[»]

ProteinModelPortal

Q9UBL3.

SMR

Q9UBL3. Positions 105-269.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29222N.

IntAct

Q9UBL3. 26 interactions.

MINT

MINT-1194078.

STRING

Q9UBL3.

PTM databases

PhosphoSite

Q9UBL3.

Polymorphism databases

DMDM

32141382.

Proteomic databases

PRIDE

Q9UBL3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000343823; ENSP00000340896; ENSG00000129691.

GeneID

9070.

KEGG

hsa:9070.

UCSC

uc003xkt.2. human.
uc003xku.2. human.
uc010lwa.1. human.

Organism-specific databases

CTD

9070.

GeneCards

GC08P037963.

H-InvDB

HIX0007454.

HGNC

HGNC:744. ASH2L.

HPA

HPA042289.

MIM

604782. gene.

neXtProt

NX_Q9UBL3.

PharmGKB

PA25044.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG11720.

GeneTree

ENSGT00390000010474.

HOGENOM

HBG380330.

HOVERGEN

HBG050592.

InParanoid

Q9UBL3.

OMA

HPMSDMG.

OrthoDB

EOG42Z4PS.

PhylomeDB

Q9UBL3.

Gene expression databases

ArrayExpress

Q9UBL3.

Bgee

Q9UBL3.

CleanEx

HS_ASH2L.

Genevestigator

Q9UBL3.

Family and domain databases

InterPro

IPR001870. B30.2/SPRY.
IPR008985. ConA-like_lec_gl.
IPR018355. SPla/RYanodine_receptor_subgr.
IPR003877. SPRY_rcpt.
[Graphical view]

KO

K14964.

Pfam

PF00622. SPRY. 1 hit.
[Graphical view]

SMART

SM00449. SPRY. 1 hit.
[Graphical view]

SUPFAM

SSF49899. ConA_like_lec_gl. 1 hit.

PROSITE

PS50188. B302_SPRY. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

33985.

SOURCE

Search...

Entry information

Entry name

ASH2L_HUMAN

Accession

Primary (citable) accession number: Q9UBL3
Secondary accession number(s): A8K7C3 , D3DSW9, O60659, O60660, Q96B62

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2003
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 102 of the entry and version 1 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.