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Q96L73 (NSD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific

EC=2.1.1.43
Alternative name(s):
Androgen receptor coactivator 267 kDa protein
Androgen receptor-associated protein of 267 kDa
H3-K36-HMTase
H4-K20-HMTase
Lysine N-methyltransferase 3B
Nuclear receptor-binding SET domain-containing protein 1
Short name=NR-binding SET domain-containing protein
Gene names
Name:NSD1
Synonyms:ARA267, KMT3B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2696 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histone methyltransferase. Preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4 (in vitro). Transcriptional intermediary factor capable of both negatively or positively influencing transcription, depending on the cellular context. Ref.13

Catalytic activity

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. Ref.13

Subunit structure

Interacts with the ligand-binding domains of RARA and THRA in the absence of ligand; in the presence of ligand the interaction is severely disrupted but some binding still occurs. Interacts with the ligand-binding domains of RXRA and ESRRA only in the presence of ligand. Interacts with ZNF496 By similarity. Interacts with AR DNA- and ligand-binding domains. Ref.1

Subcellular location

Nucleus. Chromosome Probable.

Tissue specificity

Expressed in the fetal/adult brain, kidney, skeletal muscle, spleen, and the thymus, and faintly in the lung.

Involvement in disease

Sotos syndrome 1 (SOTOS1) [MIM:117550]: A childhood overgrowth syndrome characterized by pre- and postnatal overgrowth, developmental delay, mental retardation, advanced bone age, and abnormal craniofacial morphology including macrodolichocephaly with frontal bossing, frontoparietal sparseness of hair, apparent hypertelorism, downslanting palpebral fissures, and facial flushing. Common oral findings include: premature eruption of teeth; high, arched palate; pointed chin and, more rarely, prognathism.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.4 Ref.5 Ref.13 Ref.14 Ref.15

Beckwith-Wiedemann syndrome (BWS) [MIM:130650]: A disorder characterized by anterior abdominal wall defects including exomphalos (omphalocele), pre- and postnatal overgrowth, and macroglossia. Additional less frequent complications include specific developmental defects and a predisposition to embryonal tumors.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.5

A chromosomal aberration involving NSD1 is found in childhood acute myeloid leukemia. Translocation t(5;11)(q35;p15.5) with NUP98.

A chromosomal aberration involving NSD1 is found in an adult form of myelodysplastic syndrome (MDS). Insertion of NUP98 into NSD1 generates a NUP98-NSD1 fusion product.

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily.

Contains 1 AWS domain.

Contains 4 PHD-type zinc fingers.

Contains 1 post-SET domain.

Contains 2 PWWP domains.

Contains 1 SET domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentChromosome
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseDisease mutation
Proto-oncogene
   DomainRepeat
Zinc-finger
   LigandMetal-binding
S-adenosyl-L-methionine
Zinc
   Molecular functionActivator
Chromatin regulator
Methyltransferase
Repressor
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processgastrulation with mouth forming second

Inferred from electronic annotation. Source: Ensembl

histone H3-K36 methylation

Inferred from direct assay Ref.13. Source: GOC

histone H4-K20 methylation

Inferred from sequence or structural similarity. Source: GOC

histone methylation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay Ref.1. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionandrogen receptor binding

Inferred from direct assay Ref.1. Source: UniProtKB

chromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

estrogen receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone methyltransferase activity (H3-K36 specific)

Inferred from direct assay Ref.13. Source: UniProtKB

histone methyltransferase activity (H4-K20 specific)

Inferred from sequence or structural similarity. Source: UniProtKB

ligand-dependent nuclear receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

retinoic acid receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

retinoid X receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

thyroid hormone receptor binding

Inferred from sequence or structural similarity. Source: UniProtKB

transcription cofactor activity

Inferred from direct assay Ref.1. Source: UniProtKB

transcription corepressor activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.13. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96L73-1)

Also known as: ARA267-beta;

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: Q96L73-2)

Also known as: ARA267-alpha;

The sequence of this isoform differs from the canonical sequence as follows:
     1-269: Missing.
     270-279: QLNSINLSFQ → MPLKTRTALS
Isoform 3 (identifier: Q96L73-3)

The sequence of this isoform differs from the canonical sequence as follows:
     310-412: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 26962696Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific
PRO_0000186070

Regions

Domain323 – 38866PWWP 1
Domain1756 – 181863PWWP 2
Domain1890 – 194051AWS
Domain1942 – 2059118SET
Domain2066 – 208217Post-SET
Zinc finger1543 – 158947PHD-type 1
Zinc finger1590 – 164657PHD-type 2
Zinc finger1707 – 175145PHD-type 3
Zinc finger2118 – 216548PHD-type 4; atypical
Region1952 – 19543S-adenosyl-L-methionine binding
Region1994 – 19974S-adenosyl-L-methionine binding
Region2020 – 20212S-adenosyl-L-methionine binding
Region2060 – 20667Inhibits enzyme activity in the absence of bound histone
Compositional bias2207 – 2421215Pro-rich

Sites

Binding site20651S-adenosyl-L-methionine
Binding site20711S-adenosyl-L-methionine

Amino acid modifications

Modified residue4831Phosphoserine Ref.12
Modified residue4861Phosphoserine Ref.12
Modified residue7661Phosphoserine Ref.7
Modified residue24621Phosphothreonine Ref.11
Modified residue24711Phosphoserine Ref.8

Natural variations

Alternative sequence1 – 269269Missing in isoform 2.
VSP_007682
Alternative sequence270 – 27910QLNSINLSFQ → MPLKTRTALS in isoform 2.
VSP_007683
Alternative sequence310 – 412103Missing in isoform 3.
VSP_007684
Natural variant6141V → L. Ref.14
Corresponds to variant rs3733875 [ dbSNP | Ensembl ].
VAR_015775
Natural variant6911A → T. Ref.14
Corresponds to variant rs28932177 [ dbSNP | Ensembl ].
VAR_015776
Natural variant7261S → P. Ref.14 Ref.16
Corresponds to variant rs28932178 [ dbSNP | Ensembl ].
VAR_015777
Natural variant10361A → P. Ref.14
Corresponds to variant rs28932179 [ dbSNP | Ensembl ].
VAR_015778
Natural variant10911L → I. Ref.14
Corresponds to variant rs35597015 [ dbSNP | Ensembl ].
VAR_015779
Natural variant16161H → L in SOTOS1. Ref.14
VAR_015780
Natural variant16371L → P in SOTOS1. Ref.14
VAR_015781
Natural variant16741C → W in SOTOS1. Ref.14
VAR_015782
Natural variant16871I → N in SOTOS1. Ref.15
VAR_015783
Natural variant17921G → V in SOTOS1. Ref.14
VAR_015784
Natural variant19251C → R in SOTOS1. Ref.14
VAR_015785
Natural variant19551G → D in SOTOS1. Ref.15
VAR_015786
Natural variant19841R → Q in SOTOS1; loss of enzyme activity. Ref.13 Ref.15
VAR_015787
Natural variant19971Y → C in SOTOS1. Ref.15
VAR_015788
Natural variant20051R → Q in SOTOS1; strongly reduced enzyme activity. Ref.13 Ref.14
VAR_015789
Natural variant20171R → Q in SOTOS1; loss of enzyme activity. Ref.13 Ref.14
VAR_015790
Natural variant20171R → W in SOTOS1. Ref.15
VAR_015791
Natural variant21431H → Q in SOTOS1. Ref.14
VAR_015792
Natural variant21831C → S in SOTOS1. Ref.14
VAR_015793
Natural variant22501M → I. Ref.14
Corresponds to variant rs35848863 [ dbSNP | Ensembl ].
VAR_015794
Natural variant22611M → T. Ref.14
Corresponds to variant rs34165241 [ dbSNP | Ensembl ].
VAR_015795

Experimental info

Mutagenesis19141R → C: Reduced enzyme activity. Ref.13
Mutagenesis19521R → W: Nearly abolished enzyme activity. Ref.13
Sequence conflict13061H → D in AAK92049. Ref.3
Sequence conflict13971P → Q in AAK92049. Ref.3
Sequence conflict14781A → V in AAK92049. Ref.3
Sequence conflict1959 – 19602KT → QE in AAK92049. Ref.3
Sequence conflict19631K → R in AAK92049. Ref.3
Sequence conflict19821R → M in AAK92049. Ref.3
Sequence conflict1986 – 19916RYAQEH → KHAHEN in AAK92049. Ref.3
Sequence conflict19951N → H in AAK92049. Ref.3
Sequence conflict20011L → I in AAK92049. Ref.3
Sequence conflict20161A → S in AAK92049. Ref.3
Sequence conflict20221C → S in AAK92049. Ref.3
Sequence conflict20301Q → L in AAK92049. Ref.3
Sequence conflict20331S → T in AAK92049. Ref.3
Sequence conflict2045 – 20462LS → VC in AAK92049. Ref.3
Sequence conflict20491K → P in AAK92049. Ref.3
Sequence conflict20611E → D in AAK92049. Ref.3
Sequence conflict20661G → E in AAK92049. Ref.3
Sequence conflict20711K → R in AAK92049. Ref.3
Sequence conflict20751P → S in AAK92049. Ref.3
Sequence conflict2304 – 23052TK → AQ in AAK92049. Ref.3
Sequence conflict23521R → S in AAK92049. Ref.3
Sequence conflict25391L → S in AAK92049. Ref.3
Sequence conflict25431P → S in AAK92049. Ref.3
Sequence conflict2567 – 259125PGPLS…QQLPA → QGFFTKSPALVENKGKTKWV GRPTNYLH in AAK92049. Ref.3
Sequence conflict25971G → W in AAK92049. Ref.3
Sequence conflict2608 – 26125ASLPT → PSSPN in AAK92049. Ref.3

Secondary structure

................................... 2696
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ARA267-beta) [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 4E80E6DCD9A24C81

FASTA2,696296,652
        10         20         30         40         50         60 
MDQTCELPRR NCLLPFSNPV NLDAPEDKDS PFGNGQSNFS EPLNGCTMQL STVSGTSQNA 

        70         80         90        100        110        120 
YGQDSPSCYI PLRRLQDLAS MINVEYLNGS ADGSESFQDP EKSDSRAQTP IVCTSLSPGG 

       130        140        150        160        170        180 
PTALAMKQEP SCNNSPELQV KVTKTIKNGF LHFENFTCVD DADVDSEMDP EQPVTEDESI 

       190        200        210        220        230        240 
EEIFEETQTN ATCNYETKSE NGVKVAMGSE QDSTPESRHG AVKSPFLPLA PQTETQKNKQ 

       250        260        270        280        290        300 
RNEVDGSNEK AALLPAPFSL GDTNITIEEQ LNSINLSFQD DPDSSTSTLG NMLELPGTSS 

       310        320        330        340        350        360 
SSTSQELPFC QPKKKSTPLK YEVGDLIWAK FKRRPWWPCR ICSDPLINTH SKMKVSNRRP 

       370        380        390        400        410        420 
YRQYYVEAFG DPSERAWVAG KAIVMFEGRH QFEELPVLRR RGKQKEKGYR HKVPQKILSK 

       430        440        450        460        470        480 
WEASVGLAEQ YDVPKGSKNR KCIPGSIKLD SEEDMPFEDC TNDPESEHDL LLNGCLKSLA 

       490        500        510        520        530        540 
FDSEHSADEK EKPCAKSRAR KSSDNPKRTS VKKGHIQFEA HKDERRGKIP ENLGLNFISG 

       550        560        570        580        590        600 
DISDTQASNE LSRIANSLTG SNTAPGSFLF SSCGKNTAKK EFETSNGDSL LGLPEGALIS 

       610        620        630        640        650        660 
KCSREKNKPQ RSLVCGSKVK LCYIGAGDEE KRSDSISICT TSDDGSSDLD PIEHSSESDN 

       670        680        690        700        710        720 
SVLEIPDAFD RTENMLSMQK NEKIKYSRFA ATNTRVKAKQ KPLISNSHTD HLMGCTKSAE 

       730        740        750        760        770        780 
PGTETSQVNL SDLKASTLVH KPQSDFTNDA LSPKFNLSSS ISSENSLIKG GAANQALLHS 

       790        800        810        820        830        840 
KSKQPKFRSI KCKHKENPVM AEPPVINEEC SLKCCSSDTK GSPLASISKS GKVDGLKLLN 

       850        860        870        880        890        900 
NMHEKTRDSS DIETAVVKHV LSELKELSYR SLGEDVSDSG TSKPSKPLLF SSASSQNHIP 

       910        920        930        940        950        960 
IEPDYKFSTL LMMLKDMHDS KTKEQRLMTA QNLVSYRSPG RGDCSTNSPV GVSKVLVSGG 

       970        980        990       1000       1010       1020 
STHNSEKKGD GTQNSANPSP SGGDSALSGE LSASLPGLLS DKRDLPASGK SRSDCVTRRN 

      1030       1040       1050       1060       1070       1080 
CGRSKPSSKL RDAFSAQMVK NTVNRKALKT ERKRKLNQLP SVTLDAVLQG DRERGGSLRG 

      1090       1100       1110       1120       1130       1140 
GAEDPSKEDP LQIMGHLTSE DGDHFSDVHF DSKVKQSDPG KISEKGLSFE NGKGPELDSV 

      1150       1160       1170       1180       1190       1200 
MNSENDELNG VNQVVPKKRW QRLNQRRTKP RKRMNRFKEK ENSECAFRVL LPSDPVQEGR 

      1210       1220       1230       1240       1250       1260 
DEFPEHRTPS ASILEEPLTE QNHADCLDSA GPRLNVCDKS SASIGDMEKE PGIPSLTPQA 

      1270       1280       1290       1300       1310       1320 
ELPEPAVRSE KKRLRKPSKW LLEYTEEYDQ IFAPKKKQKK VQEQVHKVSS RCEEESLLAR 

      1330       1340       1350       1360       1370       1380 
GRSSAQNKQV DENSLISTKE EPPVLEREAP FLEGPLAQSE LGGGHAELPQ LTLSVPVAPE 

      1390       1400       1410       1420       1430       1440 
VSPRPALESE ELLVKTPGNY ESKRQRKPTK KLLESNDLDP GFMPKKGDLG LSKKCYEAGH 

      1450       1460       1470       1480       1490       1500 
LENGITESCA TSYSKDFGGG TTKIFDKPRK RKRQRHAAAK MQCKKVKNDD SSKEIPGSEG 

      1510       1520       1530       1540       1550       1560 
ELMPHRTATS PKETVEEGVE HDPGMPASKK MQGERGGGAA LKENVCQNCE KLGELLLCEA 

      1570       1580       1590       1600       1610       1620 
QCCGAFHLEC LGLTEMPRGK FICNECRTGI HTCFVCKQSG EDVKRCLLPL CGKFYHEECV 

      1630       1640       1650       1660       1670       1680 
QKYPPTVMQN KGFRCSLHIC ITCHAANPAN VSASKGRLMR CVRCPVAYHA NDFCLAAGSK 

      1690       1700       1710       1720       1730       1740 
ILASNSIICP NHFTPRRGCR NHEHVNVSWC FVCSEGGSLL CCDSCPAAFH RECLNIDIPE 

      1750       1760       1770       1780       1790       1800 
GNWYCNDCKA GKKPHYREIV WVKVGRYRWW PAEICHPRAV PSNIDKMRHD VGEFPVLFFG 

      1810       1820       1830       1840       1850       1860 
SNDYLWTHQA RVFPYMEGDV SSKDKMGKGV DGTYKKALQE AAARFEELKA QKELRQLQED 

      1870       1880       1890       1900       1910       1920 
RKNDKKPPPY KHIKVNRPIG RVQIFTADLS EIPRCNCKAT DENPCGIDSE CINRMLLYEC 

      1930       1940       1950       1960       1970       1980 
HPTVCPAGGR CQNQCFSKRQ YPEVEIFRTL QRGWGLRTKT DIKKGEFVNE YVGELIDEEE 

      1990       2000       2010       2020       2030       2040 
CRARIRYAQE HDITNFYMLT LDKDRIIDAG PKGNYARFMN HCCQPNCETQ KWSVNGDTRV 

      2050       2060       2070       2080       2090       2100 
GLFALSDIKA GTELTFNYNL ECLGNGKTVC KCGAPNCSGF LGVRPKNQPI ATEEKSKKFK 

      2110       2120       2130       2140       2150       2160 
KKQQGKRRTQ GEITKEREDE CFSCGDAGQL VSCKKPGCPK VYHADCLNLT KRPAGKWECP 

      2170       2180       2190       2200       2210       2220 
WHQCDICGKE AASFCEMCPS SFCKQHREGM LFISKLDGRL SCTEHDPCGP NPLEPGEIRE 

      2230       2240       2250       2260       2270       2280 
YVPPPVPLPP GPSTHLAEQS TGMAAQAPKM SDKPPADTNQ MLSLSKKALA GTCQRPLLPE 

      2290       2300       2310       2320       2330       2340 
RPLERTDSRP QPLDKVRDLA GSGTKSQSLV SSQRPLDRPP AVAGPRPQLS DKPSPVTSPS 

      2350       2360       2370       2380       2390       2400 
SSPSVRSQPL ERPLGTADPR LDKSIGAASP RPQSLEKTSV PTGLRLPPPD RLLITSSPKP 

      2410       2420       2430       2440       2450       2460 
QTSDRPTDKP HASLSQRLPP PEKVLSAVVQ TLVAKEKALR PVDQNTQSKN RAALVMDLID 

      2470       2480       2490       2500       2510       2520 
LTPRQKERAA SPHQVTPQAD EKMPVLESSS WPASKGLGHM PRAVEKGCVS DPLQTSGKAA 

      2530       2540       2550       2560       2570       2580 
APSEDPWQAV KSLTQARLLS QPPAKAFLYE PTTQASGRAS AGAEQTPGPL SQSPGLVKQA 

      2590       2600       2610       2620       2630       2640 
KQMVGGQQLP ALAAKSGQSF RSLGKAPASL PTEEKKLVTT EQSPWALGKA SSRAGLWPIV 

      2650       2660       2670       2680       2690 
AGQTLAQSCW SAGSTQTLAQ TCWSLGRGQD PKPEQNTLPA LNQAPSSHKC AESEQK 

« Hide

Isoform 2 (ARA267-alpha) [UniParc].

Checksum: 396219A152666E8E
Show »

FASTA2,427267,340
Isoform 3 [UniParc].

Checksum: C8B8A25ECD80728A
Show »

FASTA2,593284,264

References

« Hide 'large scale' references
[1]"Identification and characterization of a novel androgen receptor coregulator ARA267-alpha in prostate cancer cells."
Wang X., Yeh S., Wu G., Hsu C.-L., Wang L., Chang T., Yang Y., Guo Y., Chang C.
J. Biol. Chem. 276:40417-40423(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH AR.
[2]"Molecular characterization of NSD1, a human homologue of the mouse Nsd1 gene."
Kurotaki N., Harada N., Yoshiura K., Sugano S., Niikawa N., Matsumoto N.
Gene 279:197-204(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"A novel gene, NSD1, is fused to NUP98 in the t(5;11)(q35;p15.5) in de novo childhood acute myeloid leukemia."
Jaju R.J., Fidler C., Haas O.A., Strickson A.J., Watkins F., Clark K., Cross N.C., Cheng J.F., Aplan P.D., Kearney L., Boultwood J., Wainscoat J.S.
Blood 98:1264-1267(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), CHROMOSOMAL TRANSLOCATION WITH NUP98.
[4]"Haploinsufficiency of NSD1 causes Sotos syndrome."
Kurotaki N., Imaizumi K., Harada N., Masuno M., Kondoh T., Nagai T., Ohashi H., Naritomi K., Tsukahara M., Makita Y., Sugimoto T., Sonoda T., Hasegawa T., Chinen Y., Tomita Ha H.A., Kinoshita A., Mizuguchi T., Yoshiura Ki K. expand/collapse author list , Ohta T., Kishino T., Fukushima Y., Niikawa N., Matsumoto N.
Nat. Genet. 30:365-366(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SOTOS1.
[5]"Paradoxical NSD1 mutations in Beckwith-Wiedemann syndrome and 11p15 anomalies in Sotos syndrome."
Baujat G., Rio M., Rossignol S., Sanlaville D., Lyonnet S., Le Merrer M., Munnich A., Gicquel C., Cormier-Daire V., Colleaux L.
Am. J. Hum. Genet. 74:715-720(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SOTOS1 AND BWS.
[6]"Cryptic insertion producing two NUP98/NSD1 chimeric transcripts in adult refractory anemia with an excess of blasts."
La Starza R., Gorello P., Rosati R., Riezzo A., Veronese A., Ferrazzi E., Martelli M.F., Negrini M., Mecucci C.
Genes Chromosomes Cancer 41:395-399(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MYELODYSPLASTIC SYNDROME.
[7]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-766, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Prostate cancer.
[8]"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-2471, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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-2462, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483 AND SER-486, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"The structure of NSD1 reveals an autoregulatory mechanism underlying histone H3K36 methylation."
Qiao Q., Li Y., Chen Z., Wang M., Reinberg D., Xu R.M.
J. Biol. Chem. 286:8361-8368(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1852-2082 IN COMPLEX WITH S-ADENOSYL-L-METHIONINE AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-1914 AND ARG-1952, CHARACTERIZATION OF SOTOS1 VARIANTS GLN-1984; GLN-2005 AND GLN-2017.
[14]"NSD1 mutations are the major cause of Sotos syndrome and occur in some cases of Weaver syndrome but are rare in other overgrowth phenotypes."
Douglas J., Hanks S., Temple I.K., Davies S., Murray A., Upadhyaya M., Tomkins S., Hughes H.E., Cole T.R.P., Rahman N.
Am. J. Hum. Genet. 72:132-143(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SOTOS1 LEU-1616; PRO-1637; TRP-1674; VAL-1792; ARG-1925; GLN-2005; GLN-2017; GLN-2143 AND SER-2183, VARIANTS LEU-614; THR-691; PRO-726; PRO-1036; ILE-1091; ILE-2250 AND THR-2261.
[15]"Spectrum of NSD1 mutations in Sotos and Weaver syndromes."
Rio M., Clech L., Amiel J., Faivre L., Lyonnet S., Le Merrer M., Odent S., Lacombe D., Edery P., Brauner R., Raoul O., Gosset P., Prieur M., Vekemans M., Munnich A., Colleaux L., Cormier-Daire V.
J. Med. Genet. 40:436-440(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SOTOS1 ASN-1687; ASP-1955; GLN-1984; CYS-1997 AND TRP-2017.
[16]"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome."
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. expand/collapse author list , Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., DiPersio J.F., Wilson R.K.
Nature 456:66-72(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-726.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF380302 mRNA. Translation: AAL27991.1.
AY049721 mRNA. Translation: AAL06645.1.
AF395588 mRNA. Translation: AAL40694.1.
AF322907 mRNA. Translation: AAK92049.1.
CCDSCCDS4412.1. [Q96L73-1]
CCDS4413.1. [Q96L73-2]
RefSeqNP_071900.2. NM_022455.4. [Q96L73-1]
NP_758859.1. NM_172349.2. [Q96L73-2]
XP_005266016.1. XM_005265959.1. [Q96L73-1]
XP_005266017.1. XM_005265960.1. [Q96L73-2]
XP_005266018.1. XM_005265961.1. [Q96L73-2]
XP_006714964.1. XM_006714901.1. [Q96L73-1]
XP_006714965.1. XM_006714902.1. [Q96L73-2]
UniGeneHs.106861.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3OOIX-ray1.75A1852-2082[»]
ProteinModelPortalQ96L73.
SMRQ96L73. Positions 324-389, 1542-1589, 1591-1637, 1706-1748, 1753-1850, 1852-2082, 2118-2210.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122135. 8 interactions.
DIPDIP-58517N.
IntActQ96L73. 2 interactions.
STRING9606.ENSP00000348031.

PTM databases

PhosphoSiteQ96L73.

Polymorphism databases

DMDM32469769.

Proteomic databases

MaxQBQ96L73.
PaxDbQ96L73.
PRIDEQ96L73.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000347982; ENSP00000343209; ENSG00000165671. [Q96L73-2]
ENST00000354179; ENSP00000346111; ENSG00000165671. [Q96L73-2]
ENST00000361032; ENSP00000354310; ENSG00000165671. [Q96L73-3]
ENST00000439151; ENSP00000395929; ENSG00000165671. [Q96L73-1]
GeneID64324.
KEGGhsa:64324.
UCSCuc003mfr.4. human. [Q96L73-1]
uc003mfs.1. human. [Q96L73-3]
uc003mft.4. human. [Q96L73-2]

Organism-specific databases

CTD64324.
GeneCardsGC05P176560.
GeneReviewsNSD1.
HGNCHGNC:14234. NSD1.
MIM117550. phenotype.
130650. phenotype.
606681. gene.
neXtProtNX_Q96L73.
Orphanet228415. 5q35 microduplication syndrome.
238613. Beckwith-Wiedemann syndrome due to NSD1 mutation.
821. Sotos syndrome.
3447. Weaver syndrome.
PharmGKBPA31790.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2940.
HOGENOMHOG000113857.
HOVERGENHBG007518.
InParanoidQ96L73.
KOK15588.
OMAECRTGIH.
OrthoDBEOG7Z69BG.
PhylomeDBQ96L73.
TreeFamTF329088.

Gene expression databases

ArrayExpressQ96L73.
BgeeQ96L73.
CleanExHS_NSD1.
GenevestigatorQ96L73.

Family and domain databases

Gene3D3.30.40.10. 3 hits.
InterProIPR006560. AWS.
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]
PfamPF00628. PHD. 1 hit.
PF00855. PWWP. 2 hits.
PF00856. SET. 1 hit.
[Graphical view]
SMARTSM00570. AWS. 1 hit.
SM00249. PHD. 5 hits.
SM00508. PostSET. 1 hit.
SM00293. PWWP. 2 hits.
SM00184. RING. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMSSF57903. SSF57903. 3 hits.
PROSITEPS51215. AWS. 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

ChiTaRSNSD1. human.
GenomeRNAi64324.
NextBio66241.
PROQ96L73.
SOURCESearch...

Entry information

Entry nameNSD1_HUMAN
AccessionPrimary (citable) accession number: Q96L73
Secondary accession number(s): Q96PD8, Q96RN7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 3, 2003
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 137 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM