UniProt functional annotation for P61964



	UniProt functional annotation for P61964

UniProt code: P61964.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Contributes to histone modification (PubMed:19131338, PubMed:19556245, PubMed:19103755, PubMed:20018852, PubMed:16600877, PubMed:16829960). May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4' (PubMed:16829960). As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3 (PubMed:19556245). H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation (PubMed:18840606). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues (PubMed:19103755, PubMed:20018852). May regulate osteoblasts differentiation (By similarity). In association with RBBP5 and ASH2L, stimulates the histone methyltransferase activities of KMT2A, KMT2B, KMT2C, KMT2D, SETD1A and SETD1B (PubMed:21220120, PubMed:22266653). {ECO:0000250|UniProtKB:P61965, ECO:0000269|PubMed:16600877, ECO:0000269|PubMed:16829960, ECO:0000269|PubMed:18840606, ECO:0000269|PubMed:19103755, ECO:0000269|PubMed:19131338, ECO:0000269|PubMed:19556245, ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:21220120, ECO:0000269|PubMed:22266653}.

Subunit: Interacts with PAXBP1; the interaction is direct and links a WDR5-containing histone methyltransferase complex to PAX7 and PAX3 (By similarity). Interacts with HCFC1 (PubMed:12670868). Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4 (PubMed:19103755). 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 (PubMed:16253997, PubMed:17355966, PubMed:17998332, PubMed:18838538). Core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7 (PubMed:15199122, PubMed:15960975, PubMed:17021013, PubMed:17500065). 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 PAGR1, BAP18, CHD8, E2F6, HCFC1, HCFC2, HSP70, INO80C, KDM6A, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, MYST1/MOF, NCOA6, PAXIP1/PTIP, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9, TEX10 and alpha- and beta-tubulin (PubMed:14992727, PubMed:18378692). Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 (PubMed:20018852). Interacts with KMT2A/MLL1 (via WIN motif) and RBBP5; the interaction is direct (PubMed:19556245, PubMed:21220120, PubMed:22665483, PubMed:22266653, PubMed:18840606, PubMed:18829459). Component of the ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 (PubMed:19103755). In the complex, it probably interacts directly with KAT2A, MBIP and KAT14 (PubMed:19103755). Interacts with histone H3 (PubMed:16946699, PubMed:16600877, PubMed:16829960, PubMed:16829959). Interacts with SETD1A (via WIN motif) (PubMed:17998332, PubMed:22665483, PubMed:22266653). Component of a histone methylation complex composed of at least ZNF335, RBBP5, ASH2L and WDR5; the complex may have histone H3-specific methyltransferase activity, however does not have specificity for 'Lys-4' of histone H3 (PubMed:19131338). Interacts with ZNF335 (PubMed:19131338, PubMed:23178126). Components of this complex may associate with components of the ZNF335-CCAR2-EMSY nuclear receptor-mediated transcription complex to form a complex at least composed of ZNF335, HCFC1, CCAR2, EMSY, MKI67, RBBP5, ASH2L and WDR5 (PubMed:19131338). Interacts with PER1 (By similarity). Interacts with KMT2B (via WIN motif), KMT2C (via WIN motif), KMT2D (via WIN motif) and SETD1B (via WIN motif) (PubMed:22665483, PubMed:22266653, PubMed:18840606). {ECO:0000250|UniProtKB:P61965, ECO:0000250|UniProtKB:Q498M4, ECO:0000269|PubMed:12670868, ECO:0000269|PubMed:14992727, ECO:0000269|PubMed:15199122, ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:16253997, ECO:0000269|PubMed:16600877, ECO:0000269|PubMed:16829959, ECO:0000269|PubMed:16829960, ECO:0000269|PubMed:16946699, ECO:0000269|PubMed:17021013, ECO:0000269|PubMed:17355966, ECO:0000269|PubMed:17500065, ECO:0000269|PubMed:17998332, ECO:0000269|PubMed:18378692, ECO:0000269|PubMed:18829459, ECO:0000269|PubMed:18838538, ECO:0000269|PubMed:18840606, ECO:0000269|PubMed:19103755, ECO:0000269|PubMed:19131338, ECO:0000269|PubMed:19556245, ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:21220120, ECO:0000269|PubMed:22266653, ECO:0000269|PubMed:22665483, ECO:0000269|PubMed:23178126}.

Subcellular location: Nucleus {ECO:0000269|PubMed:17355966, ECO:0000269|PubMed:20018852}.

Similarity: Belongs to the WD repeat WDR5/wds family. {ECO:0000305}.

Sequence caution: Sequence=CAB66159.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Contributes to histone modification (PubMed:19131338, PubMed:19556245, PubMed:19103755, PubMed:20018852, PubMed:16600877, PubMed:16829960). May position the N-terminus of histone H3 for efficient trimethylation at 'Lys-4' (PubMed:16829960). As part of the MLL1/MLL complex it is involved in methylation and dimethylation at 'Lys-4' of histone H3 (PubMed:19556245). H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation (PubMed:18840606). As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues (PubMed:19103755, PubMed:20018852). May regulate osteoblasts differentiation (By similarity). In association with RBBP5 and ASH2L, stimulates the histone methyltransferase activities of KMT2A, KMT2B, KMT2C, KMT2D, SETD1A and SETD1B (PubMed:21220120, PubMed:22266653). {ECO:0000250\|UniProtKB:P61965, ECO:0000269\|PubMed:16600877, ECO:0000269\|PubMed:16829960, ECO:0000269\|PubMed:18840606, ECO:0000269\|PubMed:19103755, ECO:0000269\|PubMed:19131338, ECO:0000269\|PubMed:19556245, ECO:0000269\|PubMed:20018852, ECO:0000269\|PubMed:21220120, ECO:0000269\|PubMed:22266653}.


Subunit:		Interacts with PAXBP1; the interaction is direct and links a WDR5-containing histone methyltransferase complex to PAX7 and PAX3 (By similarity). Interacts with HCFC1 (PubMed:12670868). Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4 (PubMed:19103755). 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 (PubMed:16253997, PubMed:17355966, PubMed:17998332, PubMed:18838538). Core component of several methyltransferase-containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM complex) and MLL4/WBP7 (PubMed:15199122, PubMed:15960975, PubMed:17021013, PubMed:17500065). 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 PAGR1, BAP18, CHD8, E2F6, HCFC1, HCFC2, HSP70, INO80C, KDM6A, KANSL1, LAS1L, MAX, MCRS1, MEN1, MGA, MYST1/MOF, NCOA6, PAXIP1/PTIP, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9, TEX10 and alpha- and beta-tubulin (PubMed:14992727, PubMed:18378692). Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1 (PubMed:20018852). Interacts with KMT2A/MLL1 (via WIN motif) and RBBP5; the interaction is direct (PubMed:19556245, PubMed:21220120, PubMed:22665483, PubMed:22266653, PubMed:18840606, PubMed:18829459). Component of the ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 (PubMed:19103755). In the complex, it probably interacts directly with KAT2A, MBIP and KAT14 (PubMed:19103755). Interacts with histone H3 (PubMed:16946699, PubMed:16600877, PubMed:16829960, PubMed:16829959). Interacts with SETD1A (via WIN motif) (PubMed:17998332, PubMed:22665483, PubMed:22266653). Component of a histone methylation complex composed of at least ZNF335, RBBP5, ASH2L and WDR5; the complex may have histone H3-specific methyltransferase activity, however does not have specificity for 'Lys-4' of histone H3 (PubMed:19131338). Interacts with ZNF335 (PubMed:19131338, PubMed:23178126). Components of this complex may associate with components of the ZNF335-CCAR2-EMSY nuclear receptor-mediated transcription complex to form a complex at least composed of ZNF335, HCFC1, CCAR2, EMSY, MKI67, RBBP5, ASH2L and WDR5 (PubMed:19131338). Interacts with PER1 (By similarity). Interacts with KMT2B (via WIN motif), KMT2C (via WIN motif), KMT2D (via WIN motif) and SETD1B (via WIN motif) (PubMed:22665483, PubMed:22266653, PubMed:18840606). {ECO:0000250\|UniProtKB:P61965, ECO:0000250\|UniProtKB:Q498M4, ECO:0000269\|PubMed:12670868, ECO:0000269\|PubMed:14992727, ECO:0000269\|PubMed:15199122, ECO:0000269\|PubMed:15960975, ECO:0000269\|PubMed:16253997, ECO:0000269\|PubMed:16600877, ECO:0000269\|PubMed:16829959, ECO:0000269\|PubMed:16829960, ECO:0000269\|PubMed:16946699, ECO:0000269\|PubMed:17021013, ECO:0000269\|PubMed:17355966, ECO:0000269\|PubMed:17500065, ECO:0000269\|PubMed:17998332, ECO:0000269\|PubMed:18378692, ECO:0000269\|PubMed:18829459, ECO:0000269\|PubMed:18838538, ECO:0000269\|PubMed:18840606, ECO:0000269\|PubMed:19103755, ECO:0000269\|PubMed:19131338, ECO:0000269\|PubMed:19556245, ECO:0000269\|PubMed:20018852, ECO:0000269\|PubMed:21220120, ECO:0000269\|PubMed:22266653, ECO:0000269\|PubMed:22665483, ECO:0000269\|PubMed:23178126}.
Subcellular location:		Nucleus {ECO:0000269\|PubMed:17355966, ECO:0000269\|PubMed:20018852}.
Similarity:		Belongs to the WD repeat WDR5/wds family. {ECO:0000305}.
Sequence caution:		Sequence=CAB66159.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};