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Q9BZ95

- NSD3_HUMAN

UniProt

Q9BZ95 - NSD3_HUMAN

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Protein

Histone-lysine N-methyltransferase NSD3

Gene

WHSC1L1

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

Functioni

Histone methyltransferase. Preferentially methylates 'Lys-4' and 'Lys-27' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation, while 'Lys-27' is a mark for transcriptional repression.1 Publication

Catalytic activityi

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri701 – 74848PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri749 – 80557PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri862 – 95594PHD-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1321 – 136848PHD-type 4; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. histone-lysine N-methyltransferase activity Source: UniProtKB
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. histone lysine methylation Source: GOC
  2. histone methylation Source: UniProtKB
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, 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 NSD3 (EC:2.1.1.43)
Alternative name(s):
Nuclear SET domain-containing protein 3
Protein whistle
WHSC1-like 1 isoform 9 with methyltransferase activity to lysine
Wolf-Hirschhorn syndrome candidate 1-like protein 1
Short name:
WHSC1-like protein 1
Gene namesi
Name:WHSC1L1
Synonyms:NSD3
ORF Names:DC28
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:12767. WHSC1L1.

Subcellular locationi

Nucleus By similarity. Chromosome By similarity

GO - Cellular componenti

  1. chromosome Source: UniProtKB-KW
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Involvement in diseasei

Defects in WHSC1L1 may be involved in non small cell lung carcinomas (NSCLC). Amplified or overexpressed in NSCLC.
A chromosomal aberration involving WHSC1L1 is found in childhood acute myeloid leukemia. Translocation t(8;11)(p11.2;p15) with NUP98.

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA37370.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14371437Histone-lysine N-methyltransferase NSD3PRO_0000259521Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei150 – 1501Phosphoserine1 Publication
Modified residuei790 – 7901N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9BZ95.
PaxDbiQ9BZ95.
PRIDEiQ9BZ95.

PTM databases

PhosphoSiteiQ9BZ95.

Expressioni

Tissue specificityi

Highly expressed in brain, heart and skeletal muscle. Expressed at lower level in liver and lung.1 Publication

Gene expression databases

BgeeiQ9BZ95.
ExpressionAtlasiQ9BZ95. baseline and differential.
GenevestigatoriQ9BZ95.

Organism-specific databases

HPAiCAB013721.
HPA005659.
HPA018893.

Interactioni

Subunit structurei

Interacts with BRD4.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DAXXQ9UER72EBI-3390132,EBI-77321
HOXC4P090172EBI-3390132,EBI-3923226
MNDAP412182EBI-3390132,EBI-2829677
SLU7O953912EBI-3390132,EBI-750559

Protein-protein interaction databases

BioGridi120250. 20 interactions.
IntActiQ9BZ95. 16 interactions.
MINTiMINT-4830664.

Structurei

Secondary structure

1
1437
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi960 – 9678
Beta strandi969 – 9713
Beta strandi973 – 9786
Turni981 – 9833
Helixi986 – 9894
Beta strandi998 – 10025
Turni1003 – 10064
Beta strandi1007 – 10115
Beta strandi1013 – 10186
Beta strandi1025 – 10273
Helixi1036 – 105217
Turni1325 – 13273
Beta strandi1331 – 13355
Helixi1348 – 13503
Beta strandi1357 – 13593
Helixi1363 – 13653
Turni1368 – 13703
Beta strandi1375 – 13773
Beta strandi1379 – 13824
Turni1387 – 13893
Turni1391 – 13933
Turni1398 – 14014

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DAQNMR-A957-1053[»]
4GNDX-ray2.27A/C1310-1413[»]
4GNEX-ray1.47A1310-1413[»]
4GNFX-ray1.55A1310-1413[»]
4GNGX-ray1.73A/D1310-1413[»]
ProteinModelPortaliQ9BZ95.
SMRiQ9BZ95. Positions 266-332, 701-746, 920-954, 957-1285, 1316-1413.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BZ95.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini270 – 33364PWWP 1PROSITE-ProRule annotationAdd
BLAST
Domaini960 – 102263PWWP 2PROSITE-ProRule annotationAdd
BLAST
Domaini1093 – 114351AWSPROSITE-ProRule annotationAdd
BLAST
Domaini1145 – 1262118SETPROSITE-ProRule annotationAdd
BLAST
Domaini1269 – 128517Post-SETPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1033 – 106937Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily.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 2 PWWP domains.PROSITE-ProRule annotation
Contains 1 SET domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri701 – 74848PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri749 – 80557PHD-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri862 – 95594PHD-type 3PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1321 – 136848PHD-type 4; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG2940.
GeneTreeiENSGT00760000118855.
HOVERGENiHBG079979.
InParanoidiQ9BZ95.
KOiK11425.
OMAiMEKDIHK.
OrthoDBiEOG7Z69BG.
PhylomeDBiQ9BZ95.
TreeFamiTF329088.

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. 2 hits.
PF00856. SET. 1 hit.
[Graphical view]
SMARTiSM00570. AWS. 1 hit.
SM00249. PHD. 5 hits.
SM00508. PostSET. 1 hit.
SM00293. PWWP. 2 hits.
SM00184. RING. 2 hits.
SM00317. SET. 1 hit.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 3 hits.
PROSITEiPS51215. AWS. 1 hit.
PS50868. POST_SET. 1 hit.
PS50812. PWWP. 2 hits.
PS50280. SET. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9BZ95-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDFSFSFMQG IMGNTIQQPP QLIDSANIRQ EDAFDNNSDI AEDGGQTPYE
60 70 80 90 100
ATLQQGFQYP ATTEDLPPLT NGYPSSISVY ETQTKYQSYN QYPNGSANGF
110 120 130 140 150
GAVRNFSPTD YYHSEIPNTR PHEILEKPSP PQPPPPPSVP QTVIPKKTGS
160 170 180 190 200
PEIKLKITKT IQNGRELFES SLCGDLLNEV QASEHTKSKH ESRKEKRKKS
210 220 230 240 250
NKHDSSRSEE RKSHKIPKLE PEEQNRPNER VDTVSEKPRE EPVLKEEAPV
260 270 280 290 300
QPILSSVPTT EVSTGVKFQV GDLVWSKVGT YPWWPCMVSS DPQLEVHTKI
310 320 330 340 350
NTRGAREYHV QFFSNQPERA WVHEKRVREY KGHKQYEELL AEATKQASNH
360 370 380 390 400
SEKQKIRKPR PQRERAQWDI GIAHAEKALK MTREERIEQY TFIYIDKQPE
410 420 430 440 450
EALSQAKKSV ASKTEVKKTR RPRSVLNTQP EQTNAGEVAS SLSSTEIRRH
460 470 480 490 500
SQRRHTSAEE EEPPPVKIAW KTAAARKSLP ASITMHKGSL DLQKCNMSPV
510 520 530 540 550
VKIEQVFALQ NATGDGKFID QFVYSTKGIG NKTEISVRGQ DRLIISTPNQ
560 570 580 590 600
RNEKPTQSVS SPEATSGSTG SVEKKQQRRS IRTRSESEKS TEVVPKKKIK
610 620 630 640 650
KEQVETVPQA TVKTGLQKGA SEISDSCKPL KKRSRASTDV EMTSSAYRDT
660 670 680 690 700
SDSDSRGLSD LQVGFGKQVD SPSATADADV SDVQSMDSSL SRRGTGMSKK
710 720 730 740 750
DTVCQICESS GDSLIPCEGE CCKHFHLECL GLASLPDSKF ICMECKTGQH
760 770 780 790 800
PCFSCKVSGK DVKRCSVGAC GKFYHEACVR KFPTAIFESK GFRCPQHCCS
810 820 830 840 850
ACSMEKDIHK ASKGRMMRCL RCPVAYHSGD ACIAAGSMLV SSYILICSNH
860 870 880 890 900
SKRSSNSSAV NVGFCFVCAR GLIVQDHSDP MFSSYAYKSH YLLNESNRAE
910 920 930 940 950
LMKLPMIPSS SASKKKCEKG GRLLCCESCP ASFHPECLSI EMPEGCWNCN
960 970 980 990 1000
DCKAGKKLHY KQIVWVKLGN YRWWPAEICN PRSVPLNIQG LKHDLGDFPV
1010 1020 1030 1040 1050
FFFGSHDYYW VHQGRVFPYV EGDKSFAEGQ TSINKTFKKA LEEAAKRFQE
1060 1070 1080 1090 1100
LKAQRESKEA LEIEKNSRKP PPYKHIKANK VIGKVQIQVA DLSEIPRCNC
1110 1120 1130 1140 1150
KPADENPCGL ESECLNRMLQ YECHPQVCPA GDRCQNQCFT KRLYPDAEII
1160 1170 1180 1190 1200
KTERRGWGLR TKRSIKKGEF VNEYVGELID EEECRLRIKR AHENSVTNFY
1210 1220 1230 1240 1250
MLTVTKDRII DAGPKGNYSR FMNHSCNPNC ETQKWTVNGD VRVGLFALCD
1260 1270 1280 1290 1300
IPAGMELTFN YNLDCLGNGR TECHCGADNC SGFLGVRPKS ACASTNEEKA
1310 1320 1330 1340 1350
KNAKLKQKRR KIKTEPKQMH EDYCFQCGDG GELVMCDKKD CPKAYHLLCL
1360 1370 1380 1390 1400
NLTQPPYGKW ECPWHQCDEC SSAAVSFCEF CPHSFCKDHE KGALVPSALE
1410 1420 1430
GRLCCSEHDP MAPVSPEYWS KIKCKWESQD HGEEVKE
Length:1,437
Mass (Da):161,613
Last modified:June 1, 2001 - v1
Checksum:i87E54997A996F7CC
GO
Isoform 2 (identifier: Q9BZ95-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     871-919: Missing.

Show »
Length:1,388
Mass (Da):156,070
Checksum:i0832BD51DAB0DCFF
GO
Isoform 3 (identifier: Q9BZ95-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     620-645: ASEISDSCKPLKKRSRASTDVEMTSS → SADRGVQGSVRFSDSSVSAAIEETVD
     646-1437: Missing.

Show »
Length:645
Mass (Da):72,621
Checksum:iDE98E24AB088AC91
GO
Isoform 4 (identifier: Q9BZ95-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     67-129: Missing.

Note: No experimental confirmation available.

Show »
Length:1,374
Mass (Da):154,519
Checksum:i3013E618C16E19E0
GO
Isoform 5 (identifier: Q9BZ95-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1196-1206: Missing.

Note: No experimental confirmation available.

Show »
Length:1,426
Mass (Da):160,314
Checksum:i9CB22AD6F0A765A7
GO

Sequence cautioni

The sequence AAI07735.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
The sequence AAG44637.1 differs from that shown. Reason: Frameshift at several positions.
The sequence BAA91110.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti436 – 4361G → R in AAI15007. (PubMed:15489334)Curated
Sequence conflicti578 – 5781R → G in AAI15007. (PubMed:15489334)Curated
Sequence conflicti829 – 8291G → E in CAC28350. (PubMed:11374904)Curated
Sequence conflicti829 – 8291G → E in CAC28351. (PubMed:11374904)Curated
Sequence conflicti926 – 9261C → R in AAI15007. (PubMed:15489334)Curated
Sequence conflicti1308 – 13081K → R in AAI15007. (PubMed:15489334)Curated
Sequence conflicti1430 – 14301D → G in AAI15007. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti186 – 1861T → M.
Corresponds to variant rs13034 [ dbSNP | Ensembl ].
VAR_061215
Natural varianti383 – 3831R → P.
Corresponds to variant rs2234552 [ dbSNP | Ensembl ].
VAR_028950

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei67 – 12963Missing in isoform 4. 1 PublicationVSP_021427Add
BLAST
Alternative sequencei620 – 64526ASEIS…EMTSS → SADRGVQGSVRFSDSSVSAA IEETVD in isoform 3. 5 PublicationsVSP_021428Add
BLAST
Alternative sequencei646 – 1437792Missing in isoform 3. 5 PublicationsVSP_021429Add
BLAST
Alternative sequencei871 – 91949Missing in isoform 2. 1 PublicationVSP_021430Add
BLAST
Alternative sequencei1196 – 120611Missing in isoform 5. 1 PublicationVSP_054489Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF332468 mRNA. Translation: AAK00354.1.
AF332469 mRNA. Translation: AAK00355.1.
AJ295990 mRNA. Translation: CAC28350.1.
AJ295991 mRNA. Translation: CAC28351.1.
AJ295992 mRNA. Translation: CAC28352.1.
AF255649 mRNA. Translation: AAG44637.1. Frameshift.
AK000360 mRNA. Translation: BAA91110.1. Different initiation.
AK022560 mRNA. Translation: BAB14099.1.
AK127594 mRNA. No translation available.
CH471080 Genomic DNA. Translation: EAW63320.1.
CH471080 Genomic DNA. Translation: EAW63321.1.
BC012059 mRNA. Translation: AAH12059.1.
BC062631 mRNA. Translation: AAH62631.1.
BC101717 mRNA. Translation: AAI01718.1.
BC107734 mRNA. Translation: AAI07735.1. Sequence problems.
BC113469 mRNA. Translation: AAI13470.1.
BC115006 mRNA. Translation: AAI15007.1.
BC143510 mRNA. Translation: AAI43511.1.
AC087362 Genomic DNA. No translation available.
AC087623 Genomic DNA. No translation available.
CCDSiCCDS43729.1. [Q9BZ95-1]
CCDS6105.1. [Q9BZ95-3]
RefSeqiNP_060248.2. NM_017778.2. [Q9BZ95-3]
NP_075447.1. NM_023034.1. [Q9BZ95-1]
XP_005273604.1. XM_005273547.1. [Q9BZ95-5]
XP_005273605.1. XM_005273548.1. [Q9BZ95-2]
UniGeneiHs.434966.
Hs.608111.
Hs.655314.

Genome annotation databases

EnsembliENST00000316985; ENSP00000313410; ENSG00000147548. [Q9BZ95-3]
ENST00000317025; ENSP00000313983; ENSG00000147548. [Q9BZ95-1]
ENST00000433384; ENSP00000393284; ENSG00000147548. [Q9BZ95-2]
ENST00000527502; ENSP00000434730; ENSG00000147548. [Q9BZ95-5]
GeneIDi54904.
KEGGihsa:54904.
UCSCiuc003xli.3. human. [Q9BZ95-1]
uc003xlj.3. human. [Q9BZ95-3]
uc010lwe.3. human. [Q9BZ95-2]
uc011lbm.2. human.

Polymorphism databases

DMDMi74761342.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF332468 mRNA. Translation: AAK00354.1 .
AF332469 mRNA. Translation: AAK00355.1 .
AJ295990 mRNA. Translation: CAC28350.1 .
AJ295991 mRNA. Translation: CAC28351.1 .
AJ295992 mRNA. Translation: CAC28352.1 .
AF255649 mRNA. Translation: AAG44637.1 . Frameshift.
AK000360 mRNA. Translation: BAA91110.1 . Different initiation.
AK022560 mRNA. Translation: BAB14099.1 .
AK127594 mRNA. No translation available.
CH471080 Genomic DNA. Translation: EAW63320.1 .
CH471080 Genomic DNA. Translation: EAW63321.1 .
BC012059 mRNA. Translation: AAH12059.1 .
BC062631 mRNA. Translation: AAH62631.1 .
BC101717 mRNA. Translation: AAI01718.1 .
BC107734 mRNA. Translation: AAI07735.1 . Sequence problems.
BC113469 mRNA. Translation: AAI13470.1 .
BC115006 mRNA. Translation: AAI15007.1 .
BC143510 mRNA. Translation: AAI43511.1 .
AC087362 Genomic DNA. No translation available.
AC087623 Genomic DNA. No translation available.
CCDSi CCDS43729.1. [Q9BZ95-1 ]
CCDS6105.1. [Q9BZ95-3 ]
RefSeqi NP_060248.2. NM_017778.2. [Q9BZ95-3 ]
NP_075447.1. NM_023034.1. [Q9BZ95-1 ]
XP_005273604.1. XM_005273547.1. [Q9BZ95-5 ]
XP_005273605.1. XM_005273548.1. [Q9BZ95-2 ]
UniGenei Hs.434966.
Hs.608111.
Hs.655314.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DAQ NMR - A 957-1053 [» ]
4GND X-ray 2.27 A/C 1310-1413 [» ]
4GNE X-ray 1.47 A 1310-1413 [» ]
4GNF X-ray 1.55 A 1310-1413 [» ]
4GNG X-ray 1.73 A/D 1310-1413 [» ]
ProteinModelPortali Q9BZ95.
SMRi Q9BZ95. Positions 266-332, 701-746, 920-954, 957-1285, 1316-1413.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120250. 20 interactions.
IntActi Q9BZ95. 16 interactions.
MINTi MINT-4830664.

Chemistry

ChEMBLi CHEMBL3108646.

PTM databases

PhosphoSitei Q9BZ95.

Polymorphism databases

DMDMi 74761342.

Proteomic databases

MaxQBi Q9BZ95.
PaxDbi Q9BZ95.
PRIDEi Q9BZ95.

Protocols and materials databases

DNASUi 54904.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000316985 ; ENSP00000313410 ; ENSG00000147548 . [Q9BZ95-3 ]
ENST00000317025 ; ENSP00000313983 ; ENSG00000147548 . [Q9BZ95-1 ]
ENST00000433384 ; ENSP00000393284 ; ENSG00000147548 . [Q9BZ95-2 ]
ENST00000527502 ; ENSP00000434730 ; ENSG00000147548 . [Q9BZ95-5 ]
GeneIDi 54904.
KEGGi hsa:54904.
UCSCi uc003xli.3. human. [Q9BZ95-1 ]
uc003xlj.3. human. [Q9BZ95-3 ]
uc010lwe.3. human. [Q9BZ95-2 ]
uc011lbm.2. human.

Organism-specific databases

CTDi 54904.
GeneCardsi GC08M038132.
HGNCi HGNC:12767. WHSC1L1.
HPAi CAB013721.
HPA005659.
HPA018893.
MIMi 607083. gene.
neXtProti NX_Q9BZ95.
PharmGKBi PA37370.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2940.
GeneTreei ENSGT00760000118855.
HOVERGENi HBG079979.
InParanoidi Q9BZ95.
KOi K11425.
OMAi MEKDIHK.
OrthoDBi EOG7Z69BG.
PhylomeDBi Q9BZ95.
TreeFami TF329088.

Miscellaneous databases

ChiTaRSi WHSC1L1. human.
EvolutionaryTracei Q9BZ95.
GeneWikii WHSC1L1.
GenomeRNAii 54904.
NextBioi 35481221.
PROi Q9BZ95.
SOURCEi Search...

Gene expression databases

Bgeei Q9BZ95.
ExpressionAtlasi Q9BZ95. baseline and differential.
Genevestigatori Q9BZ95.

Family and domain databases

Gene3Di 3.30.40.10. 3 hits.
InterProi IPR006560. 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 ]
Pfami PF00855. PWWP. 2 hits.
PF00856. SET. 1 hit.
[Graphical view ]
SMARTi SM00570. AWS. 1 hit.
SM00249. PHD. 5 hits.
SM00508. PostSET. 1 hit.
SM00293. PWWP. 2 hits.
SM00184. RING. 2 hits.
SM00317. SET. 1 hit.
[Graphical view ]
SUPFAMi SSF57903. SSF57903. 3 hits.
PROSITEi PS51215. AWS. 1 hit.
PS50868. POST_SET. 1 hit.
PS50812. PWWP. 2 hits.
PS50280. SET. 1 hit.
PS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
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Publicationsi

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  1. "WHSC1L1, on human chromosome 8p11.2, closely resembles WHSC1 and maps to a duplicated region shared with 4p16.3."
    Stec I., van Ommen G.-J.B., den Dunnen J.T.
    Genomics 76:5-8(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
  2. "NSD3, a new SET domain-containing gene, maps to 8p12 and is amplified in human breast cancer cell lines."
    Angrand P.-O., Apiou F., Stewart F., Dutrillaux B., Losson R., Chambon P.
    Genomics 74:79-88(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), TISSUE SPECIFICITY.
  3. "A novel gene from human dendritic cells."
    Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Dendritic cell.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-383 (ISOFORM 4).
    Tissue: Brain and Teratocarcinoma.
  5. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 1; 3 AND 5).
    Tissue: Brain and Placenta.
  8. "NUP98 is fused to the NSD3 gene in acute myeloid leukemia associated with t(8;11)(p11.2;p15)."
    Rosati R., La Starza R., Veronese A., Aventin A., Schwienbacher C., Vallespi T., Negrini M., Martelli M.F., Mecucci C.
    Blood 99:3857-3860(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH NUP98.
  9. Cited for: INVOLVEMENT IN NSCLC.
  10. "Characterization of a novel WHSC1-associated SET domain protein with H3K4 and H3K27 methyltransferase activity."
    Kim S.M., Kee H.J., Eom G.H., Choe N.W., Kim J.Y., Kim Y.S., Kim S.K., Kook H., Kook H., Seo S.B.
    Biochem. Biophys. Res. Commun. 345:318-323(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, FUNCTION.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-790, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "The Brd4 extraterminal domain confers transcription activation independent of pTEFb by recruiting multiple proteins, including NSD3."
    Rahman S., Sowa M.E., Ottinger M., Smith J.A., Shi Y., Harper J.W., Howley P.M.
    Mol. Cell. Biol. 31:2641-2652(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRD4.
  13. "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-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Solution structure of second PWWP domain of WHSC1L1 protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (DEC-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 957-1053.

Entry informationi

Entry nameiNSD3_HUMAN
AccessioniPrimary (citable) accession number: Q9BZ95
Secondary accession number(s): B7ZL11
, D3DSX1, Q1RMD3, Q3B796, Q6ZSA5, Q9BYU8, Q9BYU9, Q9H2M8, Q9H9W9, Q9NXA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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