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O96028 (NSD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone-lysine N-methyltransferase NSD2

EC=2.1.1.43
Alternative name(s):
Multiple myeloma SET domain-containing protein
Short name=MMSET
Nuclear SET domain-containing protein 2
Short name=NSD2
Protein trithorax-5
Wolf-Hirschhorn syndrome candidate 1 protein
Short name=WHSC1
Gene names
Name:WHSC1
Synonyms:KIAA1090, MMSET, NSD2, TRX5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1365 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histone methyltransferase with histone H3 'Lys-27' (H3K27me) methyltransferase activity. Isoform RE-IIBPmay act as a transcription regulator that binds DNA and suppresses IL5 transcription through HDAC recruitment. Ref.4 Ref.16 Ref.20

Catalytic activity

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.20

Subcellular location

Nucleus. Chromosome Potential Ref.5 Ref.17.

Isoform 4: Cytoplasm Ref.5 Ref.17.

Tissue specificity

Widely expressed. Ref.2

Involvement in disease

A chromosomal aberration involving WHSC1 is a cause of multiple myeloma tumors. Translocation t(4;14)(p16.3;q32.3) with IgH.

WHSC1 is located in the Wolf-Hirschhorn syndrome (WHS) critical region. WHS results from by sub-telomeric deletions in the short arm of chromosome 4. WHSC1 is deleted in every case, however deletion of linked genes contributes to both the severity of the core characteristics and the presence of the additional syndromic problems. Ref.18

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily.

Contains 1 AWS domain.

Contains 1 HMG box DNA-binding domain.

Contains 4 PHD-type zinc fingers.

Contains 1 post-SET domain.

Contains 2 PWWP domains.

Contains 1 SET domain.

Sequence caution

The sequence BAA83042.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentChromosome
Cytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DiseaseProto-oncogene
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionChromatin regulator
Methyltransferase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processanatomical structure morphogenesis

Traceable author statement Ref.2. Source: ProtInc

atrial septum primum morphogenesis

Inferred from electronic annotation. Source: Ensembl

atrial septum secundum morphogenesis

Inferred from electronic annotation. Source: Ensembl

bone development

Inferred from electronic annotation. Source: Ensembl

membranous septum morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear membrane

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin binding

Inferred from electronic annotation. Source: Ensembl

histone-lysine N-methyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ARP102755EBI-2693298,EBI-608057

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O96028-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O96028-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-652: Missing.
     653-712: VSSKKSERGV...GRFTCSECAS → MAGSFCWRML...SLHPFFNFLL
Isoform 3 (identifier: O96028-3)

The sequence of this isoform differs from the canonical sequence as follows:
     628-647: VSDSPGDEPSESPYESADET → LLWEPTPVKLDLNPAALYCT
     648-1365: Missing.
Isoform 4 (identifier: O96028-4)

Also known as: REII-BP; IL-5 promoter REII-region-binding protein;

The sequence of this isoform differs from the canonical sequence as follows:
     1-781: Missing.
Isoform 5 (identifier: O96028-5)

The sequence of this isoform differs from the canonical sequence as follows:
     629-629: S → K
     630-1365: Missing.
Isoform 6 (identifier: O96028-6)

The sequence of this isoform differs from the canonical sequence as follows:
     472-484: VAEHPDASGEEIE → STKLCFMLASFRI
     485-1365: Missing.
Note: No experimental confirmation available.
Isoform 7 (identifier: O96028-7)

The sequence of this isoform differs from the canonical sequence as follows:
     255-273: QKKSARQYHVQFFGDAPER → IFKSKKFEHLKTSQIVLKD
     274-1365: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13651365Histone-lysine N-methyltransferase NSD2
PRO_0000259519

Regions

Domain222 – 28665PWWP 1
Domain880 – 94263PWWP 2
Domain1011 – 106151AWS
Domain1063 – 1180118SET
Domain1187 – 120317Post-SET
DNA binding453 – 52169HMG box Ref.4
Zinc finger667 – 71347PHD-type 1
Zinc finger714 – 77057PHD-type 2
Zinc finger831 – 87545PHD-type 3
Zinc finger1239 – 128648PHD-type 4; atypical

Amino acid modifications

Modified residue1101Phosphothreonine Ref.23
Modified residue1141Phosphothreonine Ref.23
Modified residue1211Phosphoserine Ref.21 Ref.23
Modified residue3761Phosphoserine Ref.23
Modified residue5441Phosphothreonine Ref.19 Ref.21 Ref.23 Ref.24

Natural variations

Alternative sequence1 – 781781Missing in isoform 4.
VSP_021413
Alternative sequence1 – 652652Missing in isoform 2.
VSP_021414
Alternative sequence255 – 27319QKKSA…DAPER → IFKSKKFEHLKTSQIVLKD in isoform 7.
VSP_021415
Alternative sequence274 – 13651092Missing in isoform 7.
VSP_021416
Alternative sequence472 – 48413VAEHP…GEEIE → STKLCFMLASFRI in isoform 6.
VSP_021417
Alternative sequence485 – 1365881Missing in isoform 6.
VSP_021418
Alternative sequence628 – 64720VSDSP…SADET → LLWEPTPVKLDLNPAALYCT in isoform 3.
VSP_021419
Alternative sequence6291S → K in isoform 5.
VSP_021420
Alternative sequence630 – 1365736Missing in isoform 5.
VSP_021421
Alternative sequence648 – 1365718Missing in isoform 3.
VSP_021422
Alternative sequence653 – 71260VSSKK…SECAS → MAGSFCWRMLGLVSKVGNRA RCFSSMAASEEELLDFSGSE LQFNSCSLHLSLHPFFNFLL in isoform 2.
VSP_021423

Experimental info

Sequence conflict2101T → A in AAU09264. Ref.5
Isoform 2:
Sequence conflict261M → V in BAA83042. Ref.7
Sequence conflict261M → V in AAI52413. Ref.11

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 7B3128E1FA893AAA

FASTA1,365152,258
        10         20         30         40         50         60 
MEFSIKQSPL SVQSVVKCIK MKQAPEILGS ANGKTPSCEV NRECSVFLSK AQLSSSLQEG 

        70         80         90        100        110        120 
VMQKFNGHDA LPFIPADKLK DLTSRVFNGE PGAHDAKLRF ESQEMKGIGT PPNTTPIKNG 

       130        140        150        160        170        180 
SPEIKLKITK TYMNGKPLFE SSICGDSAAD VSQSEENGQK PENKARRNRK RSIKYDSLLE 

       190        200        210        220        230        240 
QGLVEAALVS KISSPSDKKI PAKKESCPNT GRDKDHLLKY NVGDLVWSKV SGYPWWPCMV 

       250        260        270        280        290        300 
SADPLLHSYT KLKGQKKSAR QYHVQFFGDA PERAWIFEKS LVAFEGEGQF EKLCQESAKQ 

       310        320        330        340        350        360 
APTKAEKIKL LKPISGKLRA QWEMGIVQAE EAASMSVEER KAKFTFLYVG DQLHLNPQVA 

       370        380        390        400        410        420 
KEAGIAAESL GEMAESSGVS EEAAENPKSV REECIPMKRR RRAKLCSSAE TLESHPDIGK 

       430        440        450        460        470        480 
STPQKTAEAD PRRGVGSPPG RKKTTVSMPR SRKGDAASQF LVFCQKHRDE VVAEHPDASG 

       490        500        510        520        530        540 
EEIEELLRSQ WSLLSEKQRA RYNTKFALVA PVQAEEDSGN VNGKKRNHTK RIQDPTEDAE 

       550        560        570        580        590        600 
AEDTPRKRLR TDKHSLRKRD TITDKTARTS SYKAMEAASS LKSQAATKNL SDACKPLKKR 

       610        620        630        640        650        660 
NRASTAASSA LGFSKSSSPS ASLTENEVSD SPGDEPSESP YESADETQTE VSVSSKKSER 

       670        680        690        700        710        720 
GVTAKKEYVC QLCEKPGSLL LCEGPCCGAF HLACLGLSRR PEGRFTCSEC ASGIHSCFVC 

       730        740        750        760        770        780 
KESKTDVKRC VVTQCGKFYH EACVKKYPLT VFESRGFRCP LHSCVSCHAS NPSNPRPSKG 

       790        800        810        820        830        840 
KMMRCVRCPV AYHSGDACLA AGCSVIASNS IICTAHFTAR KGKRHHAHVN VSWCFVCSKG 

       850        860        870        880        890        900 
GSLLCCESCP AAFHPDCLNI EMPDGSWFCN DCRAGKKLHF QDIIWVKLGN YRWWPAEVCH 

       910        920        930        940        950        960 
PKNVPPNIQK MKHEIGEFPV FFFGSKDYYW THQARVFPYM EGDRGSRYQG VRGIGRVFKN 

       970        980        990       1000       1010       1020 
ALQEAEARFR EIKLQREARE TQESERKPPP YKHIKVNKPY GKVQIYTADI SEIPKCNCKP 

      1030       1040       1050       1060       1070       1080 
TDENPCGFDS ECLNRMLMFE CHPQVCPAGE FCQNQCFTKR QYPETKIIKT DGKGWGLVAK 

      1090       1100       1110       1120       1130       1140 
RDIRKGEFVN EYVGELIDEE ECMARIKHAH ENDITHFYML TIDKDRIIDA GPKGNYSRFM 

      1150       1160       1170       1180       1190       1200 
NHSCQPNCET LKWTVNGDTR VGLFAVCDIP AGTELTFNYN LDCLGNEKTV CRCGASNCSG 

      1210       1220       1230       1240       1250       1260 
FLGDRPKTST TLSSEEKGKK TKKKTRRRRA KGEGKRQSED ECFRCGDGGQ LVLCDRKFCT 

      1270       1280       1290       1300       1310       1320 
KAYHLSCLGL GKRPFGKWEC PWHHCDVCGK PSTSFCHLCP NSFCKEHQDG TAFSCTPDGR 

      1330       1340       1350       1360 
SYCCEHDLGA ASVRSTKTEK PPPEPGKPKG KRRRRRGWRR VTEGK 

« Hide

Isoform 2 [UniParc].

Checksum: A48D9FB6E1D06EB3
Show »

FASTA71380,777
Isoform 3 [UniParc].

Checksum: 84D0A99908BD7674
Show »

FASTA64771,410
Isoform 4 (REII-BP) (IL-5 promoter REII-region-binding protein) [UniParc].

Checksum: DEA3DCB455993E56
Show »

FASTA58466,387
Isoform 5 [UniParc].

Checksum: EC79BB4E13F1FA93
Show »

FASTA62969,398
Isoform 6 [UniParc].

Checksum: 80778F7E2CFB5C35
Show »

FASTA48453,484
Isoform 7 [UniParc].

Checksum: B8091D5246B40A60
Show »

FASTA27330,199

References

« Hide 'large scale' references
[1]"The t(4;14) translocation in myeloma dysregulates both FGFR3 and a novel gene, MMSET, resulting in IgH/MMSET hybrid transcripts."
Chesi M., Nardini E., Lim R.S.C., Smith K.D., Kuehl W.M., Bergsagel P.L.
Blood 92:3025-3034(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), CHROMOSOMAL TRANSLOCATION WITH IGH.
Tissue: Myeloma.
[2]"WHSC1, a 90 kb SET domain-containing gene, expressed in early development and homologous to a Drosophila dysmorphy gene maps in the Wolf-Hirschhorn syndrome critical region and is fused to IgH in t(4;14) multiple myeloma."
Stec I., Wright T.J., van Ommen G.-J.B., de Boer P.A., van Haeringen A., Moorman A.F.M., Altherr M.R., den Dunnen J.T.
Hum. Mol. Genet. 7:1071-1082(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 3 AND 5), TISSUE SPECIFICITY, CHROMOSOMAL TRANSLOCATION WITH IGH.
[3]Erratum
Stec I., Wright T.J., van Ommen G.-J.B., de Boer P.A., van Haeringen A., Moorman A.F.M., Altherr M.R., den Dunnen J.T.
Hum. Mol. Genet. 7:1527-1527(1998)
[4]"A unique mRNA initiated within a middle intron of WHSC1/MMSET encodes a DNA binding protein that suppresses human IL-5 transcription."
Garlisi C.G., Uss A.S., Xiao H., Tian F., Sheridan K.E., Wang L., Motasim Billah M., Egan R.W., Stranick K.S., Umland S.P.
Am. J. Respir. Cell Mol. Biol. 24:90-98(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, DNA-BINDING.
[5]"Overexpression of transcripts originating from the MMSET locus characterizes all t(4;14)(p16;q32)-positive multiple myeloma patients."
Keats J.J., Maxwell C.A., Taylor B.J., Hendzel M.J., Chesi M., Bergsagel P.L., Larratt L.M., Mant M.J., Reiman T., Belch A.R., Pilarski L.M.
Blood 105:4060-4069(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), SUBCELLULAR LOCATION.
[6]"Mammalian trithorax- and ASH1-like proteins: putative chromatin regulators which contain PHD fingers and SET domains."
Angrand P.-O., Valvatne H., Jeanmougin F., Adamson A., van der Hoeven F., Olsen L., Tekotte H., Huang N., Poch O., Lamerdin J., Chambon P., Losson R., Stewart A., Aasland R.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[7]"Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[8]"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. expand/collapse author list , 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).
Tissue: Amygdala.
[9]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]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. expand/collapse author list , 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].
[11]"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] (ISOFORMS 2; 3; 4 AND 6).
Tissue: Ovary and Spleen.
[12]"Detection of t(4;14)(p16.3;q32) chromosomal translocation in multiple myeloma by reverse transcription-polymerase chain reaction analysis of IGH-MMSET fusion transcripts."
Malgeri U., Baldini L., Perfetti V., Fabris S., Vignarelli M.C., Colombo G., Lotti V., Compasso S., Bogni S., Lombardi L., Maiolo A.T., Neri A.
Cancer Res. 60:4058-4061(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH IGH.
[13]"Translocation T(4;14)(p16.3;q32) is a recurrent genetic lesion in primary amyloidosis."
Perfetti V., Coluccia A.M., Intini D., Malgeri U., Vignarelli M.C., Casarini S., Merlini G., Neri A.
Am. J. Pathol. 158:1599-1603(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH IGH.
[14]"A subset of multiple myeloma harboring the t(4;14)(p16;q32) translocation lacks FGFR3 expression but maintains an IGH/MMSET fusion transcript."
Santra M., Zhan F., Tian E., Barlogie B., Shaughnessy J. Jr.
Blood 101:2374-2376(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH IGH.
[15]"Identification of a novel IGH-MMSET fusion transcript in a human myeloma cell line with the t(4;14)(p16.3;q32) chromosomal translocation."
Intini D., Fabris S., Storlazzi T., Otsuki T., Ciceri G., Verdelli D., Lombardi L., Rocchi M., Neri A.
Br. J. Haematol. 126:437-439(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH IGH.
[16]"Identification of ID-1 as a potential target gene of MMSET in multiple myeloma."
Hudlebusch H.R., Theilgaard-Moench K., Lodahl M., Johnsen H.E., Rasmussen T.
Br. J. Haematol. 130:700-708(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Transcription repression activity is associated with the type I isoform of the MMSET gene involved in t(4;14) in multiple myeloma."
Todoerti K., Ronchetti D., Agnelli L., Castellani S., Marelli S., Deliliers G.L., Zanella A., Lombardi L., Neri A.
Br. J. Haematol. 131:214-218(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[18]"The etiology of Wolf-Hirschhorn syndrome."
Bergemann A.D., Cole F., Hirschhorn K.
Trends Genet. 21:188-195(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN WHS.
[19]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"Multiple-myeloma-related WHSC1/MMSET isoform RE-IIBP is a histone methyltransferase with transcriptional repression activity."
Kim J.Y., Kee H.J., Choe N.W., Kim S.M., Eom G.H., Baek H.J., Kook H., Kook H., Seo S.B.
Mol. Cell. Biol. 28:2023-2034(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[21]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND THR-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110; THR-114; SER-121; SER-376 AND THR-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[24]"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 THR-544, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF071593 mRNA. Translation: AAC24150.1.
AF071594 mRNA. Translation: AAC24151.1.
AF083386 mRNA. Translation: AAD19343.1.
AF083387 mRNA. Translation: AAD21770.1.
AF083388 mRNA. Translation: AAD21771.1.
AF083389 mRNA. Translation: AAD19344.1.
AF083390 mRNA. Translation: AAD19345.1.
AF083391 mRNA. Translation: AAD19346.1.
AF178206 expand/collapse EMBL AC list , AF178199, AF178198, AF178202, AF178204, AF178205, AF178203, AF178201, AF178200 Genomic DNA. Translation: AAF23369.1.
AF178219 expand/collapse EMBL AC list , AF178198, AF178199, AF178200, AF178202, AF178204, AF178207, AF178216, AF178215, AF178214, AF178213, AF178212, AF178211, AF178210, AF178209, AF178208, AF178218, AF178217, AF178205, AF178203, AF178201 Genomic DNA. Translation: AAF23370.1.
AF330040 mRNA. Translation: AAK00344.1.
AY694128 mRNA. Translation: AAU09264.1.
AJ007042 mRNA. Translation: CAB45386.1.
AB029013 mRNA. Translation: BAA83042.2. Different initiation.
AK289697 mRNA. Translation: BAF82386.1.
AC105448 Genomic DNA. No translation available.
AL132868 Genomic DNA. Translation: CAM15220.1.
AL132868 Genomic DNA. Translation: CAM15221.1.
AL132868 Genomic DNA. Translation: CAM15222.1.
CH471131 Genomic DNA. Translation: EAW82548.1.
CH471131 Genomic DNA. Translation: EAW82552.1.
CH471131 Genomic DNA. Translation: EAW82557.1.
CH471131 Genomic DNA. Translation: EAW82553.1.
CH471131 Genomic DNA. Translation: EAW82556.1.
BC052254 mRNA. Translation: AAH52254.1.
BC070176 mRNA. Translation: AAH70176.1.
BC094825 mRNA. Translation: AAH94825.2.
BC141815 mRNA. Translation: AAI41816.1.
BC152412 mRNA. Translation: AAI52413.1.
RefSeqNP_001035889.1. NM_001042424.2.
NP_015627.1. NM_007331.1.
NP_579877.1. NM_133330.2.
NP_579878.1. NM_133331.2.
NP_579889.1. NM_133334.2.
NP_579890.1. NM_133335.3.
XP_005248058.1. XM_005248001.2.
XP_005248062.1. XM_005248005.1.
UniGeneHs.113876.

3D structure databases

ProteinModelPortalO96028.
SMRO96028. Positions 211-344, 664-973, 976-1203, 1239-1327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113306. 134 interactions.
DIPDIP-57224N.
IntActO96028. 2 interactions.
MINTMINT-7103764.

PTM databases

PhosphoSiteO96028.

Proteomic databases

PaxDbO96028.
PRIDEO96028.

Protocols and materials databases

DNASU7468.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000312087; ENSP00000308780; ENSG00000109685. [O96028-3]
ENST00000353275; ENSP00000329167; ENSG00000109685. [O96028-3]
ENST00000382888; ENSP00000372344; ENSG00000109685. [O96028-2]
ENST00000382891; ENSP00000372347; ENSG00000109685. [O96028-1]
ENST00000382892; ENSP00000372348; ENSG00000109685. [O96028-1]
ENST00000382895; ENSP00000372351; ENSG00000109685. [O96028-1]
ENST00000398261; ENSP00000381311; ENSG00000109685. [O96028-3]
ENST00000420906; ENSP00000399251; ENSG00000109685. [O96028-5]
ENST00000436793; ENSP00000416725; ENSG00000109685. [O96028-7]
ENST00000503128; ENSP00000425761; ENSG00000109685. [O96028-3]
ENST00000508803; ENSP00000423972; ENSG00000109685. [O96028-1]
ENST00000512700; ENSP00000427516; ENSG00000109685. [O96028-7]
ENST00000514045; ENSP00000421681; ENSG00000109685. [O96028-5]
GeneID7468.
KEGGhsa:7468.
UCSCuc003gdx.3. human. [O96028-6]
uc003gdy.1. human. [O96028-5]
uc003gdz.4. human. [O96028-1]
uc003geg.1. human. [O96028-7]
uc003geh.1. human. [O96028-3]
uc003gei.4. human. [O96028-4]
uc010icf.3. human. [O96028-2]

Organism-specific databases

CTD7468.
GeneCardsGC04P001840.
HGNCHGNC:12766. WHSC1.
HPAHPA015315.
HPA015801.
MIM602952. gene.
neXtProtNX_O96028.
Orphanet280. Wolf-Hirschhorn syndrome.
PharmGKBPA37369.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2940.
HOVERGENHBG053345.
InParanoidO96028.
KOK11424.
OMAPSKGKMM.
OrthoDBEOG7Z69BG.
PhylomeDBO96028.
TreeFamTF329088.

Gene expression databases

ArrayExpressO96028.
BgeeO96028.
GenevestigatorO96028.

Family and domain databases

Gene3D1.10.30.10. 1 hit.
3.30.40.10. 3 hits.
InterProIPR006560. AWS.
IPR009071. HMG_box_dom.
IPR003616. Post-SET_dom.
IPR000313. PWWP_dom.
IPR001214. SET_dom.
IPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamPF00505. HMG_box. 1 hit.
PF00628. PHD. 1 hit.
PF00855. PWWP. 2 hits.
PF00856. SET. 1 hit.
[Graphical view]
SMARTSM00570. AWS. 1 hit.
SM00398. HMG. 1 hit.
SM00249. PHD. 4 hits.
SM00508. PostSET. 1 hit.
SM00293. PWWP. 2 hits.
SM00184. RING. 2 hits.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMSSF47095. SSF47095. 1 hit.
SSF57903. SSF57903. 3 hits.
PROSITEPS51215. AWS. 1 hit.
PS50118. HMG_BOX_2. 1 hit.
PS50868. POST_SET. 1 hit.
PS50812. PWWP. 2 hits.
PS50280. SET. 1 hit.
PS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSWHSC1. human.
GeneWikiWHSC1.
GenomeRNAi7468.
NextBio29246.
PROO96028.
SOURCESearch...

Entry information

Entry nameNSD2_HUMAN
AccessionPrimary (citable) accession number: O96028
Secondary accession number(s): A2A2T2 expand/collapse secondary AC list , A2A2T3, A2A2T4, A7MCZ1, D3DVQ2, O96031, Q4VBY8, Q672J1, Q6IS00, Q86V01, Q9BZB4, Q9UI92, Q9UPR2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM