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Protein

Protein dpy-30 homolog

Gene

DPY30

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

Functioni

As part of the MLL1/MLL complex, involved in the methylation of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. May play some role in histone H3 acetylation. In a teratocarcinoma cell, plays a crucial role in retinoic acid-induced differentiation along the neural lineage, regulating gene induction and H3 'Lys-4' methylation at key developmental loci. May also play an indirect or direct role in endosomal transport.3 Publications

GO - Molecular functioni

  • histone-lysine N-methyltransferase activity Source: Reactome
  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • chromatin silencing at telomere Source: GO_Central
  • endosomal transport Source: UniProtKB
  • histone H3-K4 methylation Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-3214841. PKMTs methylate histone lysines.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein dpy-30 homolog
Alternative name(s):
Dpy-30-like protein
Short name:
Dpy-30L
Gene namesi
Name:DPY30
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:24590. DPY30.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: GOC
  • Golgi apparatus Source: HPA
  • histone methyltransferase complex Source: UniProtKB
  • MLL3/4 complex Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • Set1C/COMPASS complex Source: UniProtKB
  • trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162384063.

Polymorphism and mutation databases

BioMutaiDPY30.
DMDMi14916555.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9999Protein dpy-30 homologPRO_0000114683Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei19 – 191PhosphoserineCombined sources
Modified residuei35 – 351N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9C005.
MaxQBiQ9C005.
PaxDbiQ9C005.
PeptideAtlasiQ9C005.
PRIDEiQ9C005.
TopDownProteomicsiQ9C005.

PTM databases

iPTMnetiQ9C005.
PhosphoSiteiQ9C005.

Expressioni

Gene expression databases

BgeeiQ9C005.
CleanExiHS_DPY30.
GenevisibleiQ9C005. HS.

Organism-specific databases

HPAiHPA043761.

Interactioni

Subunit structurei

Homodimer. Core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7. Each complex is at least composed of ASH2L, RBBP5, WDR5, DPY30, one or more specific histone methyltransferases (KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and KMT2B/MLL4), and the facultative components MEN1, HCFC1, HCFC2, NCOA6, KDM6A, PAXIP1/PTIP, PAGR1 and alpha- and beta-tubulin (By similarity). Interacts with ASH2L; the interaction is direct. Interacts with ARFGEF1. Component of the SET1 complex, at least composed of the catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-744973,EBI-744973
ASH2LQ9UBL312EBI-744973,EBI-540797
PSMD14O004873EBI-744973,EBI-722193
TMCC2Q7Z6C63EBI-744973,EBI-10177480

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi124181. 53 interactions.
DIPiDIP-34476N.
IntActiQ9C005. 45 interactions.
MINTiMINT-1447664.
STRINGi9606.ENSP00000295066.

Structurei

Secondary structure

1
99
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi31 – 344Combined sources
Helixi48 – 503Combined sources
Helixi53 – 586Combined sources
Turni59 – 613Combined sources
Helixi62 – 7514Combined sources
Helixi80 – 9112Combined sources
Helixi92 – 954Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3G36X-ray1.20A/B/C/D45-99[»]
4RIQX-ray2.23A/B/D/E/G/H/J/K/M/N/P/Q/S/T/V/Z45-99[»]
4RT4X-ray2.00A/B/C/D41-99[»]
4RTAX-ray2.12A/B1-99[»]
ProteinModelPortaliQ9C005.
SMRiQ9C005. Positions 45-95.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9C005.

Family & Domainsi

Sequence similaritiesi

Belongs to the dpy-30 family.Curated

Phylogenomic databases

eggNOGiKOG4109. Eukaryota.
ENOG41123UZ. LUCA.
GeneTreeiENSGT00390000008808.
HOGENOMiHOG000006847.
HOVERGENiHBG051402.
InParanoidiQ9C005.
KOiK14965.
OMAiENPHAEY.
PhylomeDBiQ9C005.

Family and domain databases

InterProiIPR007858. Dpy-30_motif.
[Graphical view]
PfamiPF05186. Dpy-30. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9C005-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPEQMLEGQ TQVAENPHSE YGLTDNVERI VENEKINAEK SSKQKVDLQS
60 70 80 90
LPTRAYLDQT VVPILLQGLA VLAKERPPNP IEFLASYLLK NKAQFEDRN
Length:99
Mass (Da):11,250
Last modified:June 1, 2001 - v1
Checksum:i5356AC515B9C2ADB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF226998 mRNA. Translation: AAK00640.1.
CH471053 Genomic DNA. Translation: EAX00463.1.
CH471053 Genomic DNA. Translation: EAX00466.1.
BC015970 mRNA. Translation: AAH15970.1.
CCDSiCCDS1777.1.
RefSeqiNP_115963.1. NM_032574.3.
UniGeneiHs.531788.
Hs.679657.

Genome annotation databases

EnsembliENST00000295066; ENSP00000295066; ENSG00000162961.
ENST00000342166; ENSP00000345837; ENSG00000162961.
GeneIDi84661.
KEGGihsa:84661.
UCSCiuc002roa.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF226998 mRNA. Translation: AAK00640.1.
CH471053 Genomic DNA. Translation: EAX00463.1.
CH471053 Genomic DNA. Translation: EAX00466.1.
BC015970 mRNA. Translation: AAH15970.1.
CCDSiCCDS1777.1.
RefSeqiNP_115963.1. NM_032574.3.
UniGeneiHs.531788.
Hs.679657.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3G36X-ray1.20A/B/C/D45-99[»]
4RIQX-ray2.23A/B/D/E/G/H/J/K/M/N/P/Q/S/T/V/Z45-99[»]
4RT4X-ray2.00A/B/C/D41-99[»]
4RTAX-ray2.12A/B1-99[»]
ProteinModelPortaliQ9C005.
SMRiQ9C005. Positions 45-95.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi124181. 53 interactions.
DIPiDIP-34476N.
IntActiQ9C005. 45 interactions.
MINTiMINT-1447664.
STRINGi9606.ENSP00000295066.

PTM databases

iPTMnetiQ9C005.
PhosphoSiteiQ9C005.

Polymorphism and mutation databases

BioMutaiDPY30.
DMDMi14916555.

Proteomic databases

EPDiQ9C005.
MaxQBiQ9C005.
PaxDbiQ9C005.
PeptideAtlasiQ9C005.
PRIDEiQ9C005.
TopDownProteomicsiQ9C005.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295066; ENSP00000295066; ENSG00000162961.
ENST00000342166; ENSP00000345837; ENSG00000162961.
GeneIDi84661.
KEGGihsa:84661.
UCSCiuc002roa.2. human.

Organism-specific databases

CTDi84661.
GeneCardsiDPY30.
HGNCiHGNC:24590. DPY30.
HPAiHPA043761.
MIMi612032. gene.
neXtProtiNX_Q9C005.
PharmGKBiPA162384063.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4109. Eukaryota.
ENOG41123UZ. LUCA.
GeneTreeiENSGT00390000008808.
HOGENOMiHOG000006847.
HOVERGENiHBG051402.
InParanoidiQ9C005.
KOiK14965.
OMAiENPHAEY.
PhylomeDBiQ9C005.

Enzyme and pathway databases

ReactomeiR-HSA-3214841. PKMTs methylate histone lysines.

Miscellaneous databases

EvolutionaryTraceiQ9C005.
GenomeRNAii84661.
PROiQ9C005.
SOURCEiSearch...

Gene expression databases

BgeeiQ9C005.
CleanExiHS_DPY30.
GenevisibleiQ9C005. HS.

Family and domain databases

InterProiIPR007858. Dpy-30_motif.
[Graphical view]
PfamiPF05186. Dpy-30. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Dystrophin-related protein 2 (DRP2) is located in the postsynaptic density of the CNS."
    Roberts R.G., Sheng M.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Urinary bladder.
  4. Cited for: IDENTIFICATION IN THE MEN1-ASSOCIATED HISTONE METHYLTRANSFERASE COMPLEX.
  5. "PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex."
    Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T., Dressler G.R., Copeland T.D., Kalkum M., Ge K.
    J. Biol. Chem. 282:20395-20406(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MLL2/3 COMPLEX.
  6. "Molecular regulation of H3K4 trimethylation by Wdr82, a component of human Set1/COMPASS."
    Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M., Shilatifard A.
    Mol. Cell. Biol. 28:7337-7344(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN SET1 COMPLEX.
  7. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex."
    Patel A., Dharmarajan V., Vought V.E., Cosgrove M.S.
    J. Biol. Chem. 284:24242-24256(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DIMERIZATION, CHARACTERIZATION OF THE MLL1/MLL COMPLEX, INTERACTION WITH ASH2L.
  9. "A role of histone H3 lysine 4 methyltransferase components in endosomal trafficking."
    Xu Z., Gong Q., Xia B., Groves B., Zimmermann M., Mugler C., Mu D., Matsumoto B., Seaman M., Ma D.
    J. Cell Biol. 186:343-353(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARFGEF1.
  10. "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-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Role for Dpy-30 in ES cell-fate specification by regulation of H3K4 methylation within bivalent domains."
    Jiang H., Shukla A., Wang X., Chen W.Y., Bernstein B.E., Roeder R.G.
    Cell 144:513-525(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "Crystal structure of the C-terminal domain of human DPY-30-like protein: A component of the histone methyltransferase complex."
    Wang X., Lou Z., Dong X., Yang W., Peng Y., Yin B., Gong Y., Yuan J., Zhou W., Bartlam M., Peng X., Rao Z.
    J. Mol. Biol. 390:530-537(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 45-99, DIMERIZATION.

Entry informationi

Entry nameiDPY30_HUMAN
AccessioniPrimary (citable) accession number: Q9C005
Secondary accession number(s): D6W578
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2001
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 123 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 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.