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Protein

Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific

Gene

Nsd1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Histone methyltransferase. Preferentially methylates 'Lys-36' of histone H3 and 'Lys-20' of histone H4 (in vitro). Transcriptional intermediary factor capable of negatively influencing transcription. May also positively influence transcription. Essential for early post-implantation development.2 Publications

Catalytic activityi

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1963 – 19631S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei1969 – 19691S-adenosyl-L-methioninePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1441 – 148747PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1488 – 154457PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1605 – 164945PHD-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri2016 – 206348PHD-type 4; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • androgen receptor binding Source: UniProtKB
  • chromatin binding Source: MGI
  • estrogen receptor binding Source: UniProtKB
  • histone methyltransferase activity Source: MGI
  • histone methyltransferase activity (H3-K36 specific) Source: UniProtKB
  • histone methyltransferase activity (H4-K20 specific) Source: UniProtKB
  • retinoic acid receptor binding Source: UniProtKB
  • retinoid X receptor binding Source: UniProtKB
  • RNA polymerase II core promoter sequence-specific DNA binding Source: MGI
  • thyroid hormone receptor binding Source: UniProtKB
  • transcription cofactor activity Source: UniProtKB
  • transcription corepressor activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Developmental protein, Methyltransferase, Receptor, Repressor, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, S-adenosyl-L-methionine, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specific (EC:2.1.1.43)
Alternative name(s):
H3-K36-HMTase
H4-K20-HMTase
Nuclear receptor-binding SET domain-containing protein 1
Short name:
NR-binding SET domain-containing protein
Gene namesi
Name:Nsd1Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1276545. Nsd1.

Subcellular locationi

  • Nucleus 1 Publication
  • Chromosome 1 Publication

GO - Cellular componenti

  • chromosome Source: UniProtKB-SubCell
  • histone methyltransferase complex Source: UniProtKB
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi803 – 8031F → A or Y: No effect on interaction with nuclear receptors. 1 Publication
Mutagenesisi804 – 8052ST → AA: Abolishes interaction with nuclear receptors. 1 Publication
Mutagenesisi806 – 8072LL → AA: Strongly decreases interaction with liganded nuclear receptors. No effect on interaction with non-liganded nuclear receptors. 1 Publication
Mutagenesisi1920 – 19201C → S: Increases methyltransferase activity towards H3 and H4. Increases methyltransferase activity; when associated with E-1950. 1 Publication
Mutagenesisi1950 – 19501T → E: Does not affect histone methyltransferase activity. Increases methyltransferase activity; when associated with S-1920. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25882588Histone-lysine N-methyltransferase, H3 lysine-36 and H4 lysine-20 specificPRO_0000186071Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei110 – 1101PhosphoserineCombined sources
Modified residuei118 – 1181PhosphoserineCombined sources
Modified residuei380 – 3801PhosphoserineBy similarity
Modified residuei383 – 3831PhosphoserineBy similarity
Modified residuei1408 – 14081PhosphoserineCombined sources
Modified residuei2267 – 22671PhosphoserineBy similarity
Modified residuei2360 – 23601PhosphothreonineBy similarity
Modified residuei2369 – 23691PhosphoserineCombined sources
Cross-linki2509 – 2509Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO88491.
MaxQBiO88491.
PaxDbiO88491.
PeptideAtlasiO88491.
PRIDEiO88491.

PTM databases

iPTMnetiO88491.
PhosphoSiteiO88491.

Expressioni

Tissue specificityi

Expressed in the embryo and the outer region of the uterine decidua at early post-implantation E5.5 stage. Uniformly expressed in embryonic and extraembryonic tissues during gastrulation stage E7.5. Expressed differentially after stage 14.5 with highest expression in proliferating cells. Enriched in the telencephalic region of the brain, spinal cord, intestinal crypt, tooth buds, thymus and salivary glands at stage E16.5. Also expressed in the ossification region of developing bones and in the periosteum.1 Publication

Gene expression databases

CleanExiMM_NSD1.

Interactioni

Subunit structurei

Interacts with AR DNA- and ligand-binding domains (By similarity). 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 similarity2 Publications

GO - Molecular functioni

  • androgen receptor binding Source: UniProtKB
  • estrogen receptor binding Source: UniProtKB
  • retinoic acid receptor binding Source: UniProtKB
  • retinoid X receptor binding Source: UniProtKB
  • thyroid hormone receptor binding Source: UniProtKB

Protein-protein interaction databases

IntActiO88491. 1 interaction.
MINTiMINT-1177495.
STRINGi10090.ENSMUSP00000097089.

Structurei

Secondary structure

1
2588
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2017 – 20193Combined sources
Turni2020 – 20223Combined sources
Beta strandi2026 – 20305Combined sources
Beta strandi2039 – 20413Combined sources
Turni2042 – 20465Combined sources
Helixi2058 – 20603Combined sources
Turni2063 – 20653Combined sources
Beta strandi2066 – 20683Combined sources
Turni2082 – 20843Combined sources
Turni2086 – 20883Combined sources
Beta strandi2089 – 20913Combined sources
Turni2093 – 20953Combined sources
Beta strandi2098 – 21003Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NAANMR-A2014-2104[»]
ProteinModelPortaliO88491.
SMRiO88491. Positions 1651-1748, 1750-1980, 2016-2108.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1654 – 171663PWWPPROSITE-ProRule annotationAdd
BLAST
Domaini1788 – 183851AWSPROSITE-ProRule annotationAdd
BLAST
Domaini1840 – 1957118SETPROSITE-ProRule annotationAdd
BLAST
Domaini1964 – 198017Post-SETPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1850 – 18523S-adenosyl-L-methionine bindingBy similarity
Regioni1892 – 18954S-adenosyl-L-methionine bindingBy similarity
Regioni1918 – 19192S-adenosyl-L-methionine bindingBy similarity
Regioni1958 – 19647Inhibits enzyme activity in the absence of bound histoneBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi841 – 89656Ser-richSequence analysisAdd
BLAST
Compositional biasi2213 – 225139Pro-richSequence analysisAdd
BLAST

Domaini

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily.PROSITE-ProRule annotation
Contains 1 AWS domain.PROSITE-ProRule annotation
Contains 4 PHD-type zinc fingers.PROSITE-ProRule annotation
Contains 1 post-SET domain.PROSITE-ProRule annotation
Contains 1 PWWP domain.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri1441 – 148747PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1488 – 154457PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1605 – 164945PHD-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri2016 – 206348PHD-type 4; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1081. Eukaryota.
COG2940. LUCA.
HOGENOMiHOG000113857.
HOVERGENiHBG007518.
InParanoidiO88491.
PhylomeDBiO88491.

Family and domain databases

Gene3Di3.30.40.10. 3 hits.
InterProiIPR006560. AWS_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]
PfamiPF00855. PWWP. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00570. AWS. 1 hit.
SM00249. PHD. 5 hits.
SM00508. PostSET. 1 hit.
SM00293. PWWP. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 3 hits.
PROSITEiPS51215. AWS. 1 hit.
PS50868. POST_SET. 1 hit.
PS50812. PWWP. 1 hit.
PS50280. SET. 1 hit.
PS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88491-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRTCELSRR NCLLSFSNPV NLDASEDKDS PFGNGQSNFS EPLNGCTMQL
60 70 80 90 100
PTAASGTSQN AYGQDSPSCY IPLRRLQDLA SMINVEYLSG SADGSESFQD
110 120 130 140 150
PAKSDSRAQS PIVCTSLSPG GPTALAMKQE PTCNNSPELQ LRVTKTTKNG
160 170 180 190 200
FLHFENFTGV DDADVDSEMD PEQPVTEDES IEEIFEETQT NATCNYEPKS
210 220 230 240 250
ENGVEVAMGS EQDSMPESRH GAVERPFLPL APQTEKQKNK QRSEVDGSNE
260 270 280 290 300
KTALLPAPTS LGDTNVTVEE QFNSINLSFQ DDPDSSPSPL GNMLEIPGTS
310 320 330 340 350
SPSTSQELPF VPQKILSKWE ASVGLAEQYD VPKGSKNQKC VSSSVKLDSE
360 370 380 390 400
EDMPFEDCTN DPDSEHLLLN GCLKSLAFDS EHSADEKEKP CAKSRVRKSS
410 420 430 440 450
DNIKRTSVKK DLVPFESRKE ERRGKIPDNL GLDFISGGVS DKQASNELSR
460 470 480 490 500
IANSLTGSST APGSFLFSSS VQNTAKTDFE TPDCDSLSGL SESALISKHS
510 520 530 540 550
GEKKKLHPGQ VCSSKVQLCY VGAGDEEKRS NSVSVSTTSD DGCSDLDPTE
560 570 580 590 600
HNSGFQNSVL GITDAFDKTE NALSVHKNET QYSRYPVTNR IKEKQKSLIT
610 620 630 640 650
NSHADHLMGS TKTMEPETAE LSQVNLSDLK ISSPIPKPQP EFRNDGLTTK
660 670 680 690 700
FSAPPGIRNE NPLTKGGLAN QTLLPLKCRQ PKFRSIKCKH KESPAVAETS
710 720 730 740 750
ATSEDLSLKC CSSDTNGSPL ANISKSGKGE GLKLLNNMHE KTRDSSDIET
760 770 780 790 800
AVVKHVLSEL KELSYRSLSE DVSDSGTAKA SKPLLFSSAS SQNHIPIEPD
810 820 830 840 850
YKFSTLLMML KDMHDSKTKE QRLMTAQNLA SYRTPDRGDC SSGSPVGTSK
860 870 880 890 900
VLVLGSSTPN SEKPGDSTQD SVHQSPGGGD SALSGELSSS LSSLASDKRE
910 920 930 940 950
LPACGKIRSN CIPRRNCGRA KPSSKLRETI SAQMVKPSVN PKALKTERKR
960 970 980 990 1000
KFSRLPAVTL AANRLGNKES GSVNGPSRGG AEDPGKEEPL QQMDLLRNED
1010 1020 1030 1040 1050
THFSDVHFDS KAKQSDPDKN LEKEPSFENR KGPELGSEMN TENDELHGVN
1060 1070 1080 1090 1100
QVVPKKRWQR LNQRRPKPGK RANRFREKEN SEGAFGVLLP ADAVQKARED
1110 1120 1130 1140 1150
YLEQRAPPTS KPEDSAADPN HGSHSESVAP RLNVCEKSSV GMGDVEKETG
1160 1170 1180 1190 1200
IPSLMPQTKL PEPAIRSEKK RLRKPSKWLL EYTEEYDQIF APKKKQKKVQ
1210 1220 1230 1240 1250
EQVHKVSSRC EDESLLARCQ PSAQNKQVDE NSLISTKEEP PVLEREAPFL
1260 1270 1280 1290 1300
EGPLAQSDLG VTHAELPQLT LSVPVAPEAS PRPALESEEL LVKTPGNYES
1310 1320 1330 1340 1350
KRQRKPTKKL LESNDLDPGF MPKKGDLGLS RKCFEASRSG NGIVESRATS
1360 1370 1380 1390 1400
HLKEFSGGTT KIFDKPRKRK RQRLVTARVH YKKVKKEDLT KDTPSSEGEL
1410 1420 1430 1440 1450
LIHRTAASPK EILEEGVEHD PGMSASKKLQ VERGGGAALK ENVCQNCEKL
1460 1470 1480 1490 1500
GELLLCEAQC CGAFHLECLG LPEMPRGKFI CNECHTGIHT CFVCKQSGED
1510 1520 1530 1540 1550
VKRCLLPLCG KFYHEECVQK YPPTVTQNKG FRCPLHICIT CHAANPANVS
1560 1570 1580 1590 1600
ASKGRLMRCV RCPVAYHAND FCLAAGSKIL ASNSIICPNH FTPRRGCRNH
1610 1620 1630 1640 1650
EHVNVSWCFV CSEGGSLLCC DSCPAAFHRE CLNIDIPEGN WYCNDCKAGK
1660 1670 1680 1690 1700
KPHYREIVWV KVGRYRWWPA EICHPRAVPS NIDKMRHDVG EFPVLFFGSN
1710 1720 1730 1740 1750
DYLWTHQARV FPYMEGDVSS KDKMGKGVDG TYKKALQEAA ARFEELKARK
1760 1770 1780 1790 1800
ELRQLQEDRK NDKKPPPYKH IKVNRPIGRV QIFTADLSEI PRCNCKATDE
1810 1820 1830 1840 1850
NPCGIDSECI NRMLLYECHP TVCPAGVRCQ NQCFSKRQYP DVEIFRTLQR
1860 1870 1880 1890 1900
GWGLRTKTDI KKGEFVNEYV GELIDEEECR ARIRYAQEHD ITNFYMLTLD
1910 1920 1930 1940 1950
KDRIIDAGPK GNYARFMNHC CQPNCETQKW SVNGDTRVGL FALSDIKAGT
1960 1970 1980 1990 2000
ELTFNYNLEC LGNGKTVCKC GAPNCSGFLG VRPKNQPIVT EEKSRKFKRK
2010 2020 2030 2040 2050
PHGKRRSQGE VTKEREDECF SCGDAGQLVS CKKPGCPKVY HADCLNLTKR
2060 2070 2080 2090 2100
PAGKWECPWH QCDVCGKEAA SFCEMCPSSF CKQHREGMLF ISKLDGRLSC
2110 2120 2130 2140 2150
TEHDPCGPNP LEPGEIREYV PPTATSPPSP GTQPKEQSSE MATQGPKKSD
2160 2170 2180 2190 2200
QPPTDATQLL PLSKKALTGS CQRPLLPERP PERTDSSSHL LDRIRDLAGS
2210 2220 2230 2240 2250
GTKSQSLVSS QRPQDRPPAK EGPRPQPPDR ASPMTRPSSS PSVSSLPLER
2260 2270 2280 2290 2300
PLRMTDSRLD KSIGAASPKS QAVEKTPAST GLRLSSPDRL LTTNSPKPQI
2310 2320 2330 2340 2350
SDRPPEKSHA SLTQRLPPPE KVLSAVVQSL VAKEKALRPV DQNTQSKHRP
2360 2370 2380 2390 2400
AVVMDLIDLT PRQKERAASP QEVTPQADEK TAMLESSSWP SSKGLGHIPR
2410 2420 2430 2440 2450
ATEKISVSES LQPSGKVAAP SEHPWQAVKS LTHARFLSPP SAKAFLYESA
2460 2470 2480 2490 2500
TQASGRTPVG AEQTPGPPSP APGLVKQVKQ LSRGLTAKSG QSFRSLGKIS
2510 2520 2530 2540 2550
ASLPNEEKKL TTTEQSPWGL GKASPGAGLW PIVAGQTLAQ ACWSAGGTQT
2560 2570 2580
LAQTCWSLGR GQDPKPENAI QALNQAPSSR KCADSEKK
Length:2,588
Mass (Da):284,084
Last modified:November 1, 1998 - v1
Checksum:i145DFCF2F285A959
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF064553 mRNA. Translation: AAC40182.1.
AK082820 mRNA. Translation: BAC38635.1.
AK004485 mRNA. Translation: BAB23326.1.
PIRiT14342.
UniGeneiMm.12964.
Mm.168965.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF064553 mRNA. Translation: AAC40182.1.
AK082820 mRNA. Translation: BAC38635.1.
AK004485 mRNA. Translation: BAB23326.1.
PIRiT14342.
UniGeneiMm.12964.
Mm.168965.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2NAANMR-A2014-2104[»]
ProteinModelPortaliO88491.
SMRiO88491. Positions 1651-1748, 1750-1980, 2016-2108.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO88491. 1 interaction.
MINTiMINT-1177495.
STRINGi10090.ENSMUSP00000097089.

PTM databases

iPTMnetiO88491.
PhosphoSiteiO88491.

Proteomic databases

EPDiO88491.
MaxQBiO88491.
PaxDbiO88491.
PeptideAtlasiO88491.
PRIDEiO88491.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:1276545. Nsd1.

Phylogenomic databases

eggNOGiKOG1081. Eukaryota.
COG2940. LUCA.
HOGENOMiHOG000113857.
HOVERGENiHBG007518.
InParanoidiO88491.
PhylomeDBiO88491.

Miscellaneous databases

ChiTaRSiNsd1. mouse.
PROiO88491.
SOURCEiSearch...

Gene expression databases

CleanExiMM_NSD1.

Family and domain databases

Gene3Di3.30.40.10. 3 hits.
InterProiIPR006560. AWS_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]
PfamiPF00855. PWWP. 1 hit.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00570. AWS. 1 hit.
SM00249. PHD. 5 hits.
SM00508. PostSET. 1 hit.
SM00293. PWWP. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 3 hits.
PROSITEiPS51215. AWS. 1 hit.
PS50868. POST_SET. 1 hit.
PS50812. PWWP. 1 hit.
PS50280. SET. 1 hit.
PS01359. ZF_PHD_1. 2 hits.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNSD1_MOUSE
AccessioniPrimary (citable) accession number: O88491
Secondary accession number(s): Q8C480, Q9CT70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: November 1, 1998
Last modified: September 7, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.