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Conserved domains on  [gi|38570121|ref|NP_060603|]
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E3 ubiquitin-protein ligase MSL2 isoform 1 [Homo sapiens]

Protein Classification

E3 ubiquitin-protein ligase MSL2( domain architecture ID 11245032)

E3 ubiquitin-protein ligase MSL2 is a component of the histone acetyltransferase complex responsible for the majority of histone H4 acetylation at lysine 16 which is implicated in the formation of higher-order chromatin structure

CATH:  3.30.40.10
EC:  2.3.2.27
Gene Ontology:  GO:0016567|GO:0008270|GO:0004842
PubMed:  19033443|21726816|19925422|11007473|19489725
SCOP:  3000160

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-RING_10 pfam16685
zinc RING finger of MSL2; zf-RING_10 is an N-terminal domain on E3 ubiquitin-protein ligase ...
 42-111 2.65e-38

zinc RING finger of MSL2; zf-RING_10 is an N-terminal domain on E3 ubiquitin-protein ligase msl-2 proteins. The domain binds MSL1 and exhibits ubiquitin E3 ligase activity towards H2B K34, the histone proteins.


:

Pssm-ID: 435513 [Multi-domain]  Cd Length: 70  Bit Score: 135.12  E-value: 2.65e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38570121    42 LSCCVCGHLLQDPIAPTNSTCQHYVCKTCKGKKMMMKPSCSWCKDYEQFEENKQLSILVNCYKKLCEYIT 111
Cdd:pfam16685   1 LSCVVCCKLLVDPYTPTGSRCQHHVCRGCKGGRKRLKPSCSWCKDYSQYEENKQLRILLQCYKKLCEYLT 70
MSL2-CXC pfam16682
CXC domain of E3 ubiquitin-protein ligase MSL2; MSL2-CXC is an autonomously folded domain ...
 455-509 3.10e-23

CXC domain of E3 ubiquitin-protein ligase MSL2; MSL2-CXC is an autonomously folded domain containing that binds three zinc ions. It lies on the E3 ubiquitin-protein ligase MSL2 in eukaryotes. The CXC domain critically contributes to the DNA-binding activity of MSL2. It carries 9 invariant cysteines within about a 50 residue region.


:

Pssm-ID: 435512  Cd Length: 55  Bit Score: 92.88  E-value: 3.10e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 38570121   455 KPQEKKGCKCGRATQNPSVLTCRGQRCPCYSNRKACLDCICRGCQNSYMANGEKK 509
Cdd:pfam16682   1 KPPEKKGCRCGTSTPTPPKLTCRNQRCPCYSNGKSCTDCKCRGCKNPHKADSIDS 55
 
Name Accession Description Interval E-value
zf-RING_10 pfam16685
zinc RING finger of MSL2; zf-RING_10 is an N-terminal domain on E3 ubiquitin-protein ligase ...
 42-111 2.65e-38

zinc RING finger of MSL2; zf-RING_10 is an N-terminal domain on E3 ubiquitin-protein ligase msl-2 proteins. The domain binds MSL1 and exhibits ubiquitin E3 ligase activity towards H2B K34, the histone proteins.


Pssm-ID: 435513 [Multi-domain]  Cd Length: 70  Bit Score: 135.12  E-value: 2.65e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38570121    42 LSCCVCGHLLQDPIAPTNSTCQHYVCKTCKGKKMMMKPSCSWCKDYEQFEENKQLSILVNCYKKLCEYIT 111
Cdd:pfam16685   1 LSCVVCCKLLVDPYTPTGSRCQHHVCRGCKGGRKRLKPSCSWCKDYSQYEENKQLRILLQCYKKLCEYLT 70
RING-HC_MSL2 cd16522
RING finger found in Drosophila melanogaster male-specific lethal-2 (MSL2) and similar ...
 37-96 1.01e-36

RING finger found in Drosophila melanogaster male-specific lethal-2 (MSL2) and similar proteins; MSL2, also known as RING finger protein 184 (RNF184), is a putative DNA-binding protein required for X chromosome dosage compensation in Drosophila males. Its expression is sex specifically regulated by Sex-lethal. Drosophila dosage compensation proteins MOF, MSL1, MSL2, and MSL3 are essential for elevating transcription of the single X chromosome in the male (X chromosome dosage compensation). MSL2 plays a critical role in translation and/or stability of MSL1 in males. In complex with MSL1, it acts as an E3 ubiquitin ligase that promotes ubiquitination of histone H2B. MSL2 contains a C3HC4-type RING-HC finger and a metallothionein-like domain with eight conserved and two non-conserved cysteines, as well as a positively and a negatively charged amino acid residue cluster and a coiled coil domain that may be involved in protein-protein interactions. This subfamily also includes many male-specific lethal-2 homologs from bilaterians.


Pssm-ID: 438185  Cd Length: 60  Bit Score: 130.64  E-value: 1.01e-36
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38570121  37 YFRQSLSCCVCGHLLQDPIAPTNSTCQHYVCKTCKGKKMMMKPSCSWCKDYEQFEENKQL 96
Cdd:cd16522   1 YLRQALSCCVCGQLLVDPIGPTNSTCQHNVCKGCKGGKMRLKPSCSWCKDYSQFEENKQL 60
MSL2-CXC pfam16682
CXC domain of E3 ubiquitin-protein ligase MSL2; MSL2-CXC is an autonomously folded domain ...
 455-509 3.10e-23

CXC domain of E3 ubiquitin-protein ligase MSL2; MSL2-CXC is an autonomously folded domain containing that binds three zinc ions. It lies on the E3 ubiquitin-protein ligase MSL2 in eukaryotes. The CXC domain critically contributes to the DNA-binding activity of MSL2. It carries 9 invariant cysteines within about a 50 residue region.


Pssm-ID: 435512  Cd Length: 55  Bit Score: 92.88  E-value: 3.10e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 38570121   455 KPQEKKGCKCGRATQNPSVLTCRGQRCPCYSNRKACLDCICRGCQNSYMANGEKK 509
Cdd:pfam16682   1 KPPEKKGCRCGTSTPTPPKLTCRNQRCPCYSNGKSCTDCKCRGCKNPHKADSIDS 55
MSL2_CXC cd13122
DNA-binding cysteine-rich domain of male-specific lethal 2 and related proteins; The CXC ...
 456-505 6.40e-22

DNA-binding cysteine-rich domain of male-specific lethal 2 and related proteins; The CXC domain of Drosophila melanogaster MSL2 forms a Zn(3)Cys(9) cluster and is involved in recruiting members of the dosage compensation complex (DCC) to sites on the X chromosome.


Pssm-ID: 240555  Cd Length: 50  Bit Score: 88.99  E-value: 6.40e-22
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 38570121 456 PQEKKGCKCGRATQNPSVLTCRGQRCPCYSNRKACLDCICRGCQNSYMAN 505
Cdd:cd13122   1 PPEKKGCRCGTATQSPGVLTCRGQRCPCYSNGKSCLDCKCRGCKNPHKAD 50
 
Name Accession Description Interval E-value
zf-RING_10 pfam16685
zinc RING finger of MSL2; zf-RING_10 is an N-terminal domain on E3 ubiquitin-protein ligase ...
 42-111 2.65e-38

zinc RING finger of MSL2; zf-RING_10 is an N-terminal domain on E3 ubiquitin-protein ligase msl-2 proteins. The domain binds MSL1 and exhibits ubiquitin E3 ligase activity towards H2B K34, the histone proteins.


Pssm-ID: 435513 [Multi-domain]  Cd Length: 70  Bit Score: 135.12  E-value: 2.65e-38
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38570121    42 LSCCVCGHLLQDPIAPTNSTCQHYVCKTCKGKKMMMKPSCSWCKDYEQFEENKQLSILVNCYKKLCEYIT 111
Cdd:pfam16685   1 LSCVVCCKLLVDPYTPTGSRCQHHVCRGCKGGRKRLKPSCSWCKDYSQYEENKQLRILLQCYKKLCEYLT 70
RING-HC_MSL2 cd16522
RING finger found in Drosophila melanogaster male-specific lethal-2 (MSL2) and similar ...
 37-96 1.01e-36

RING finger found in Drosophila melanogaster male-specific lethal-2 (MSL2) and similar proteins; MSL2, also known as RING finger protein 184 (RNF184), is a putative DNA-binding protein required for X chromosome dosage compensation in Drosophila males. Its expression is sex specifically regulated by Sex-lethal. Drosophila dosage compensation proteins MOF, MSL1, MSL2, and MSL3 are essential for elevating transcription of the single X chromosome in the male (X chromosome dosage compensation). MSL2 plays a critical role in translation and/or stability of MSL1 in males. In complex with MSL1, it acts as an E3 ubiquitin ligase that promotes ubiquitination of histone H2B. MSL2 contains a C3HC4-type RING-HC finger and a metallothionein-like domain with eight conserved and two non-conserved cysteines, as well as a positively and a negatively charged amino acid residue cluster and a coiled coil domain that may be involved in protein-protein interactions. This subfamily also includes many male-specific lethal-2 homologs from bilaterians.


Pssm-ID: 438185  Cd Length: 60  Bit Score: 130.64  E-value: 1.01e-36
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 38570121  37 YFRQSLSCCVCGHLLQDPIAPTNSTCQHYVCKTCKGKKMMMKPSCSWCKDYEQFEENKQL 96
Cdd:cd16522   1 YLRQALSCCVCGQLLVDPIGPTNSTCQHNVCKGCKGGKMRLKPSCSWCKDYSQFEENKQL 60
MSL2-CXC pfam16682
CXC domain of E3 ubiquitin-protein ligase MSL2; MSL2-CXC is an autonomously folded domain ...
 455-509 3.10e-23

CXC domain of E3 ubiquitin-protein ligase MSL2; MSL2-CXC is an autonomously folded domain containing that binds three zinc ions. It lies on the E3 ubiquitin-protein ligase MSL2 in eukaryotes. The CXC domain critically contributes to the DNA-binding activity of MSL2. It carries 9 invariant cysteines within about a 50 residue region.


Pssm-ID: 435512  Cd Length: 55  Bit Score: 92.88  E-value: 3.10e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 38570121   455 KPQEKKGCKCGRATQNPSVLTCRGQRCPCYSNRKACLDCICRGCQNSYMANGEKK 509
Cdd:pfam16682   1 KPPEKKGCRCGTSTPTPPKLTCRNQRCPCYSNGKSCTDCKCRGCKNPHKADSIDS 55
MSL2_CXC cd13122
DNA-binding cysteine-rich domain of male-specific lethal 2 and related proteins; The CXC ...
 456-505 6.40e-22

DNA-binding cysteine-rich domain of male-specific lethal 2 and related proteins; The CXC domain of Drosophila melanogaster MSL2 forms a Zn(3)Cys(9) cluster and is involved in recruiting members of the dosage compensation complex (DCC) to sites on the X chromosome.


Pssm-ID: 240555  Cd Length: 50  Bit Score: 88.99  E-value: 6.40e-22
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 38570121 456 PQEKKGCKCGRATQNPSVLTCRGQRCPCYSNRKACLDCICRGCQNSYMAN 505
Cdd:cd13122   1 PPEKKGCRCGTATQSPGVLTCRGQRCPCYSNGKSCLDCKCRGCKNPHKAD 50
RING-HC_BARD1 cd16496
RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar ...
 39-106 2.89e-03

RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar proteins; BARD-1 is a critical factor in BRCA1-mediated tumor suppression and may also serve as a target for tumorigenic lesions in some human cancers. It associates with BRCA1 (breast cancer-1) to form a heterodimeric BRCA1/BARD1 complex that is responsible for maintaining genomic stability through nuclear functions involving DNA damage signaling and repair, transcriptional regulation, and cell cycle control. The BRCA1/BARD1 complex catalyzes autoubiquitination of BRCA1 and trans ubiquitination of other protein substrates. Its E3 ligase activity is dramatically reduced in the presence of UBX domain protein 1 (UBXN1). BARD-1 contains an C3HC4-type RING-HC finger that binds BRCA1 at its N-terminus and three tandem ankyrin repeats and tandem BRCT repeat domains at its C-terminus. The BRCT repeats bind CstF-50 (cleavage stimulation factor) to modulate mRNA processing and RNAP II stability in response to DNA damage.


Pssm-ID: 438159 [Multi-domain]  Cd Length: 86  Bit Score: 36.93  E-value: 2.89e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 38570121  39 RQSLSCCVCGHLLQDPIapTNSTCQHYVCKTCKGKKMMMK-PSCS---WCKDyeqFEENKQLSILVNCYKKL 106
Cdd:cd16496  13 ENLLRCSRCASILKEPV--TLGGCEHVFCRSCVGDRLGNGcPVCDtpaWARD---LQINRQLDSMVQLCRKL 79
RING-HC_RAG1 cd16530
RING finger, HC subclass, found in recombination activating gene-1 (RAG-1) and similar ...
 40-85 4.48e-03

RING finger, HC subclass, found in recombination activating gene-1 (RAG-1) and similar proteins; RAG-1, also known as V(D)J recombination-activating protein 1, RING finger protein 74 (RNF74), or endonuclease RAG1, is the catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. RAG1 is a lymphoid-specific factor that mediates DNA-binding to conserved recombination signal sequences (RSS) and catalyzes DNA cleavage activities by introducing a double-strand break between the RSS and the adjacent coding segment. It also functions as an E3 ubiquitin-protein ligase that mediates monoubiquitination of histone H3, which is required for the joining step of V(D)J recombination. RAG-1 contains an N-terminal C3HC4-type RING-HC finger that mediates monoubiquitylation of histone H3, an adjacent C2H2-type zinc finger, and a nonamer binding (NBD) DNA-binding domain.


Pssm-ID: 319444 [Multi-domain]  Cd Length: 46  Bit Score: 35.49  E-value: 4.48e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 38570121  40 QSLSCCVCGHLLQDPIaptNSTCQHYVCKTCKGKKM-MMKPSCSWCK 85
Cdd:cd16530   1 KSVSCQVCEHILADPV---QTPCKHLFCRTCILKCLkVMGSYCPSCR 44
RING-HC_BRCA1 cd16498
RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and ...
 29-106 6.02e-03

RING finger, HC subclass, found in breast cancer type 1 susceptibility protein (BRCA1) and similar proteins; BRCA1, also known as RING finger protein 53 (RNF53), is a RING finger protein encoded by the tumor suppressor gene BRCA1 that regulates all DNA double-strand break (DSB) repair pathways. BRCA1 is frequently mutated in patients with hereditary breast and ovarian cancer (HBOC). Its mutation is also associated with an increased risk of pancreatic, stomach, laryngeal, fallopian tube, and prostate cancer. It plays an important role in the DNA damage response signaling and has been implicated in various cellular processes such as cell cycle regulation, transcriptional regulation, chromatin remodeling, DNA DSBs, and apoptosis. BRCA1 contains an N-terminal C3HC4-type RING-HC finger, and two BRCT (BRCA1 C-terminus domain) repeats at the C-terminus.


Pssm-ID: 438161 [Multi-domain]  Cd Length: 94  Bit Score: 36.51  E-value: 6.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 38570121  29 TEINRLLPYFRQSLSCCVCGHLLQDPIaptnST-CQHYVCKTCKGKKMMMKPS---CSWCKDY---EQFEENKQLSILVN 101
Cdd:cd16498   4 ERVQEVISAMQKNLECPICLELLKEPV----STkCDHQFCRFCILKLLQKKKKpapCPLCKKSvtkRSLQESTRFKQLVE 79


                ....*
gi 38570121 102 CYKKL 106
Cdd:cd16498  80 AVKKL 84
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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