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Conserved domains on  [gi|723428422|ref|NP_001289732|]
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protein Mdm4 isoform 2 [Mus musculus]

Protein Classification

protein Mdm4( domain architecture ID 13026199)

protein Mdm4 exerts its oncogenic activity predominantly by binding the p53 tumor suppressor and blocking its transcriptional activity

Gene Symbol:  MDM4
Gene Ontology:  GO:0008270|GO:0002039
PubMed:  8895579

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MDM4 cd17673
p53-binding domain found in MDM4 and similar proteins; MDM4, also known as double minute 4 ...
29-107 2.21e-43

p53-binding domain found in MDM4 and similar proteins; MDM4, also known as double minute 4 protein, MDM2-like p53-binding protein, protein MDMX, HDMX, or p53-binding protein MDM4, exerts its oncogenic activity predominantly by binding the p53 tumor suppressor and blocking its transcriptional activity. MDM4 is phosphorylated and destabilized in response to DNA damage stress. It can also be specifically dephosphorylated through directly interacting with protein phosphatase 1 (PP1), which may increase its stability and thus inhibit p53 activity. MDM4 also has a p53-independent role in tumorigenesis and cell growth regulation. MDM4 contains an N-terminal p53-binding domain and a C-terminal zinc RING-finger domain responsible for its hetero-oligomerization, which is crucial for the suppression of P53 activity during embryonic development and the recruitment of E2 ubiquitin-conjugating enzymes. MDM4 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain near the central acidic region.


:

Pssm-ID: 349492  Cd Length: 79  Bit Score: 147.67  E-value: 2.21e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 723428422  29 PKLQLLKILHAAGAQGEVFTMKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGDLLGCQSFSVKDPSPLYDMLRKNLV 107
Cdd:cd17673    1 PKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDKQQQHIVYCGGDPLGELLGVQSFSVKDPSPLYDMLKRNLV 79
mRING-HC-C2H2C4_MDM4 cd16784
Modified RING finger, HC subclass (C2H2C4-type), found in protein MDM4 and similar proteins; ...
431-489 1.11e-33

Modified RING finger, HC subclass (C2H2C4-type), found in protein MDM4 and similar proteins; MDM4, also known as double minute 4 protein (Hdm4), MDM2-like p53-binding protein, protein MDMX, HDMX, or p53-binding protein MDM4, exerts its oncogenic activity predominantly by binding p53 tumor suppressor and blocking its transcriptional activity. MDM4 is phosphorylated and destabilized in response to DNA damage stress. It can also be specifically dephosphorylated by directly interacting with protein phosphatase 1 (PP1), which may increase its stability and thus inhibit p53 activity. Meanwhile, MDM4 has a p53-independent role in tumorigenesis and cell growth regulation. MDM4 contains an N-terminal p53-binding domain and a C-terminal modified C2H2C4-type RING-HC finger responsible for its hetero-oligomerization, which is crucial for the suppression of P53 activity during embryonic development and the recruitment of E2 ubiquitin-conjugating enzymes. MDM4 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain near the central acidic region.


:

Pssm-ID: 319698  Cd Length: 59  Bit Score: 121.04  E-value: 1.11e-33
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 723428422 431 NVLKPCSLCEKRPRDGNIIHGKTSHLTTCFHCARRLKKSGASCPACKKEIQLVIKVFIA 489
Cdd:cd16784    1 NLLEPCSLCQKRPRNGNIVHGRTAHLVTCFHCARRLKKAGAPCPVCKKEIQMVIKIFIA 59
zf-RanBP pfam00641
Zn-finger in Ran binding protein and others;
299-328 2.88e-07

Zn-finger in Ran binding protein and others;


:

Pssm-ID: 395516 [Multi-domain]  Cd Length: 30  Bit Score: 46.58  E-value: 2.88e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 723428422  299 SEDEWQCTECKKFNSPSKRYCFRCWALRKD 328
Cdd:pfam00641   1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30
 
Name Accession Description Interval E-value
MDM4 cd17673
p53-binding domain found in MDM4 and similar proteins; MDM4, also known as double minute 4 ...
29-107 2.21e-43

p53-binding domain found in MDM4 and similar proteins; MDM4, also known as double minute 4 protein, MDM2-like p53-binding protein, protein MDMX, HDMX, or p53-binding protein MDM4, exerts its oncogenic activity predominantly by binding the p53 tumor suppressor and blocking its transcriptional activity. MDM4 is phosphorylated and destabilized in response to DNA damage stress. It can also be specifically dephosphorylated through directly interacting with protein phosphatase 1 (PP1), which may increase its stability and thus inhibit p53 activity. MDM4 also has a p53-independent role in tumorigenesis and cell growth regulation. MDM4 contains an N-terminal p53-binding domain and a C-terminal zinc RING-finger domain responsible for its hetero-oligomerization, which is crucial for the suppression of P53 activity during embryonic development and the recruitment of E2 ubiquitin-conjugating enzymes. MDM4 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain near the central acidic region.


Pssm-ID: 349492  Cd Length: 79  Bit Score: 147.67  E-value: 2.21e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 723428422  29 PKLQLLKILHAAGAQGEVFTMKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGDLLGCQSFSVKDPSPLYDMLRKNLV 107
Cdd:cd17673    1 PKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDKQQQHIVYCGGDPLGELLGVQSFSVKDPSPLYDMLKRNLV 79
mRING-HC-C2H2C4_MDM4 cd16784
Modified RING finger, HC subclass (C2H2C4-type), found in protein MDM4 and similar proteins; ...
431-489 1.11e-33

Modified RING finger, HC subclass (C2H2C4-type), found in protein MDM4 and similar proteins; MDM4, also known as double minute 4 protein (Hdm4), MDM2-like p53-binding protein, protein MDMX, HDMX, or p53-binding protein MDM4, exerts its oncogenic activity predominantly by binding p53 tumor suppressor and blocking its transcriptional activity. MDM4 is phosphorylated and destabilized in response to DNA damage stress. It can also be specifically dephosphorylated by directly interacting with protein phosphatase 1 (PP1), which may increase its stability and thus inhibit p53 activity. Meanwhile, MDM4 has a p53-independent role in tumorigenesis and cell growth regulation. MDM4 contains an N-terminal p53-binding domain and a C-terminal modified C2H2C4-type RING-HC finger responsible for its hetero-oligomerization, which is crucial for the suppression of P53 activity during embryonic development and the recruitment of E2 ubiquitin-conjugating enzymes. MDM4 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain near the central acidic region.


Pssm-ID: 319698  Cd Length: 59  Bit Score: 121.04  E-value: 1.11e-33
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 723428422 431 NVLKPCSLCEKRPRDGNIIHGKTSHLTTCFHCARRLKKSGASCPACKKEIQLVIKVFIA 489
Cdd:cd16784    1 NLLEPCSLCQKRPRNGNIVHGRTAHLVTCFHCARRLKKAGAPCPVCKKEIQMVIKIFIA 59
zf-RanBP pfam00641
Zn-finger in Ran binding protein and others;
299-328 2.88e-07

Zn-finger in Ran binding protein and others;


Pssm-ID: 395516 [Multi-domain]  Cd Length: 30  Bit Score: 46.58  E-value: 2.88e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 723428422  299 SEDEWQCTECKKFNSPSKRYCFRCWALRKD 328
Cdd:pfam00641   1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
434-483 3.44e-05

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 41.21  E-value: 3.44e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 723428422  434 KPCSLCEKRPRdgNIIHGKTSHLTTCFHCARRLKKSGASCPACKKEIQLV 483
Cdd:pfam13920   3 LLCVICLDRPR--NVVLLPCGHLCLCEECAERLLRKKKKCPICRQPIESV 50
SWIB pfam02201
SWIB/MDM2 domain; This family includes the SWIB domain and the MDM2 domain. The p53-associated ...
26-76 1.37e-03

SWIB/MDM2 domain; This family includes the SWIB domain and the MDM2 domain. The p53-associated protein (MDM2) is an inhibitor of the p53 tumour suppressor gene binding the transactivation domain and down regulating the ability of p53 to activate transcription. This family contains the p53 binding domain of MDM2.


Pssm-ID: 460488 [Multi-domain]  Cd Length: 73  Bit Score: 37.46  E-value: 1.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 723428422   26 QVRPKLQLLKILHAagaqgEVFTMKEVMHYLGQYIMVKQLYDQQEQHMVYC 76
Cdd:pfam02201   2 PFKLSPELAELLGE-----EELSRPEVVKALWEYIKENNLQDPEDKREIIC 47
 
Name Accession Description Interval E-value
MDM4 cd17673
p53-binding domain found in MDM4 and similar proteins; MDM4, also known as double minute 4 ...
29-107 2.21e-43

p53-binding domain found in MDM4 and similar proteins; MDM4, also known as double minute 4 protein, MDM2-like p53-binding protein, protein MDMX, HDMX, or p53-binding protein MDM4, exerts its oncogenic activity predominantly by binding the p53 tumor suppressor and blocking its transcriptional activity. MDM4 is phosphorylated and destabilized in response to DNA damage stress. It can also be specifically dephosphorylated through directly interacting with protein phosphatase 1 (PP1), which may increase its stability and thus inhibit p53 activity. MDM4 also has a p53-independent role in tumorigenesis and cell growth regulation. MDM4 contains an N-terminal p53-binding domain and a C-terminal zinc RING-finger domain responsible for its hetero-oligomerization, which is crucial for the suppression of P53 activity during embryonic development and the recruitment of E2 ubiquitin-conjugating enzymes. MDM4 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain near the central acidic region.


Pssm-ID: 349492  Cd Length: 79  Bit Score: 147.67  E-value: 2.21e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 723428422  29 PKLQLLKILHAAGAQGEVFTMKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGDLLGCQSFSVKDPSPLYDMLRKNLV 107
Cdd:cd17673    1 PKLPLLKILHAAGAQGEMFTVKEVMHYLGQYIMVKQLYDKQQQHIVYCGGDPLGELLGVQSFSVKDPSPLYDMLKRNLV 79
mRING-HC-C2H2C4_MDM4 cd16784
Modified RING finger, HC subclass (C2H2C4-type), found in protein MDM4 and similar proteins; ...
431-489 1.11e-33

Modified RING finger, HC subclass (C2H2C4-type), found in protein MDM4 and similar proteins; MDM4, also known as double minute 4 protein (Hdm4), MDM2-like p53-binding protein, protein MDMX, HDMX, or p53-binding protein MDM4, exerts its oncogenic activity predominantly by binding p53 tumor suppressor and blocking its transcriptional activity. MDM4 is phosphorylated and destabilized in response to DNA damage stress. It can also be specifically dephosphorylated by directly interacting with protein phosphatase 1 (PP1), which may increase its stability and thus inhibit p53 activity. Meanwhile, MDM4 has a p53-independent role in tumorigenesis and cell growth regulation. MDM4 contains an N-terminal p53-binding domain and a C-terminal modified C2H2C4-type RING-HC finger responsible for its hetero-oligomerization, which is crucial for the suppression of P53 activity during embryonic development and the recruitment of E2 ubiquitin-conjugating enzymes. MDM4 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain near the central acidic region.


Pssm-ID: 319698  Cd Length: 59  Bit Score: 121.04  E-value: 1.11e-33
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 723428422 431 NVLKPCSLCEKRPRDGNIIHGKTSHLTTCFHCARRLKKSGASCPACKKEIQLVIKVFIA 489
Cdd:cd16784    1 NLLEPCSLCQKRPRNGNIVHGRTAHLVTCFHCARRLKKAGAPCPVCKKEIQMVIKIFIA 59
MDM2 cd17672
p53-binding domain found in E3 ubiquitin-protein ligase MDM2 and similar proteins; MDM2, also ...
25-106 8.06e-30

p53-binding domain found in E3 ubiquitin-protein ligase MDM2 and similar proteins; MDM2, also known as double minute 2 protein (Hdm2), or oncoprotein MDM2, or p53-binding protein, exerts its oncogenic activity predominantly by binding the p53 tumor suppressor and blocking its transcriptional activity. It forms homo-oligomers and displays E3 ubiquitin ligase activity, catalyzing the attachment of ubiquitin to p53 as an essential step in the regulation of its expression levels in cells. Moreover, in response to ribosomal stress, MDM2-mediated p53 ubiquitination and degradation can be inhibited through the interaction with ribosomal proteins L5, L11, and L23. MDM2 also has a p53-independent role in tumorigenesis and cell growth regulation. In addition, it binds interferon (IFN) regulatory factor-2 (IRF-2), an IFN-regulated transcription factor, and mediates its ubiquitination. MDM2 contains an N-terminal p53-binding domain and a C-terminal zinc RING-finger domain conferring E3 ligase activity that is required for ubiquitination and nuclear export of p53. It is also responsible for the hetero-oligomerization of MDM2, which is crucial for the suppression of P53 activity during embryonic development, and the recruitment of E2 ubiquitin-conjugating enzymes. MDM2 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain, as well as a nuclear localization signal (NLS) and a nuclear export signal (NES), near the central acidic region.


Pssm-ID: 349491  Cd Length: 83  Bit Score: 111.45  E-value: 8.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 723428422  25 SQVRPKLQLLKILHAAGAQGEVFTMKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGDLLGCQSFSVKDPSPLYDMLRK 104
Cdd:cd17672    2 KLVRPKPLLLKLLKSAGAQKDTFTMKEVLFYLGQYIMAKQLYDEKQQHIVHCSNDPLGDLFGVQSFSVKEHRRIYAMISR 81

                 ..
gi 723428422 105 NL 106
Cdd:cd17672   82 NL 83
MDM2_like cd10566
p53-binding domain found in E3 ubiquitin-protein ligase MDM2, MDM4, and similar proteins; MDM2 ...
29-106 5.59e-28

p53-binding domain found in E3 ubiquitin-protein ligase MDM2, MDM4, and similar proteins; MDM2 (also termed HDM2) and MDM4 (also termed MDMX or HDMX) are the primary negative regulators of p53 tumor suppressor. They have non-redundant roles in the regulation of p53. MDM2 mainly functions to control p53 stability, while MDM4 controls p53 transcriptional activity. Both MDM2 and MDM4 contain an N-terminal p53-binding domain, a RanBP2-type zinc finger (zf-RanBP2) domain near the central acidic region, and a C-terminal RING domain. Mdm2 can form homo-oligomers through its RING domain and display E3 ubiquitin ligase activity that catalyzes the attachment of ubiquitin to p53 as an essential step in the regulation of its level in cells. Despite its RING domain and structural similarity with MDM2, MDM4 does not homo-oligomerize and lacks ubiquitin-ligase function, but inhibits the transcriptional activity of p53. In addition, both their RING domains are responsible for the hetero-oligomerization, which is crucial for the suppression of p53 activity during embryonic development and the recruitment of E2 ubiquitin-conjugating enzymes. Moreover, MDM2 and MDM4 can be phosphorylated and destabilized in response to DNA damage stress. In response to ribosomal stress, MDM2-mediated p53 ubiquitination and degradation can be inhibited through the interaction with ribosomal proteins L5, L11 and L23. However, MDM4 is not bound to ribosomal proteins, suggesting its different response to regulation by small basic proteins such as ribosomal proteins and ARF.


Pssm-ID: 349488  Cd Length: 75  Bit Score: 106.11  E-value: 5.59e-28
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 723428422  29 PKLQLLKILHAAGAQGEVFTMKEVMHYLGQYIMVKQLYDQQEQHMVYCGGDLLGDLLGCQSFSVKDpspLYDMLRKNL 106
Cdd:cd10566    1 PKPELLKLLKSVGAKGEVFTRKEVLHYLKQYISSRKLYDPLDPRIVYCKNDPLGKVFGVQSFTIKD---VLGLLAKNL 75
mRING-HC-C2H2C4_MDM2-like cd16646
Modified RING finger, HC subclass (C2H2C4-type), found in E3 ubiquitin-protein ligase MDM2, ...
435-485 6.55e-21

Modified RING finger, HC subclass (C2H2C4-type), found in E3 ubiquitin-protein ligase MDM2, protein MDM4 and similar proteins; MDM2 (also known as HDM2) and MDM4 (also known as MDMX or HDMX) are the primary p53 tumor suppressor negative regulators. They have non-redundant roles in the regulation of p53. MDM2 mainly functions to control p53 stability, while MDM4 controls p53 transcriptional activity. Both MDM2 and MDM4 contain an N-terminal p53-binding domain, a RanBP2-type zinc finger (zf-RanBP2) domain near the central acidic region, and a C-terminal modified C2H2C4-type RING-HC finger. Mdm2 can form homo-oligomers through its RING domain and displays E3 ubiquitin ligase activity that catalyzes the attachment of ubiquitin to p53 as an essential step in the regulation of its levels in cells. Despite its RING domain and structural similarity with MDM2, MDM4 does not homo-oligomerize and lacks ubiquitin-ligase function, but inhibits the transcriptional activity of p53. In addition, both their RING domains are responsible for the hetero-oligomerization, which is crucial for the suppression of P53 activity during embryonic development and the recruitment of E2 ubiquitin-conjugating enzymes. Moreover, MDM2 and MDM4 can be phosphorylated and destabilized in response to DNA damage stress. In response to ribosomal stress, MDM2-mediated p53 ubiquitination and degradation can be inhibited through the interaction with ribosomal proteins L5, L11, and L23. However, MDM4 is not bound to ribosomal proteins, suggesting its different response to regulation by small basic proteins such as ribosomal proteins and ARF.


Pssm-ID: 438308 [Multi-domain]  Cd Length: 52  Bit Score: 85.84  E-value: 6.55e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 723428422 435 PCSLCEKRPRDGNIIHGKTSHLTTCFHCARRLKKSGASCPACKKEIQLVIK 485
Cdd:cd16646    2 LCVICLSRPRTAAIVHGKTGHQVACYTCAKKLKRRGKPCPVCRRPIQNVIK 52
mRING-HC-C2H2C4_MDM2 cd16783
Modified RING finger, HC subclass (C2H2C4-type), found in E3 ubiquitin-protein ligase MDM2 and ...
433-489 2.70e-16

Modified RING finger, HC subclass (C2H2C4-type), found in E3 ubiquitin-protein ligase MDM2 and similar proteins; MDM2, also known as double minute 2 protein (Hdm2), oncoprotein MDM2, or p53-binding protein, exerts its oncogenic activity predominantly by binding p53 tumor suppressor and blocking its transcriptional activity. It forms homo-oligomers and displays E3 ubiquitin ligase activity that catalyzes the attachment of ubiquitin to p53 as an essential step in the regulation of its levels in cells. Moreover, in response to ribosomal stress, MDM2-mediated p53 ubiquitination and degradation can be inhibited through its interaction with ribosomal proteins L5, L11, and L23. MDM2 can be phosphorylated in the DNA damage. Meanwhile, MDM2 has a p53-independent role in tumorigenesis and cell growth regulation. In addition, it binds interferon (IFN) regulatory factor-2 (IRF-2), an IFN-regulated transcription factor, and mediates its ubiquitination. MDM2 contains an N-terminal p53-binding domain, and a C-terminal modified C2H2C4-type RING-HC finger conferring E3 ligase activity that is required for ubiquitination and nuclear export of p53. It is also responsible for the hetero-oligomerization of MDM2, which is crucial for the suppression of P53 activity during embryonic development, and the recruitment of E2 ubiquitin-conjugating enzymes. MDM2 also harbors a RanBP2-type zinc finger (zf-RanBP2) domain, as well as a nuclear localization signal (NLS) and a nuclear export signal (NES), near the central acidic region. The zf-RanBP2 domain plays an important role in mediating MDM2 binding to ribosomal proteins and thus is involved in MDM2-mediated p53 suppression.


Pssm-ID: 438438  Cd Length: 57  Bit Score: 73.06  E-value: 2.70e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 723428422 433 LKPCSLCEKRPRDGNIIHGKTSHLTTCFHCARRLKKSGASCPACKKEIQLVIKVFIA 489
Cdd:cd16783    1 IEPCVICQTRPKNGCIVHGKTGHLMACFTCAKKLKKRNKPCPVCRQPIQMIVLTYFP 57
zf-RanBP pfam00641
Zn-finger in Ran binding protein and others;
299-328 2.88e-07

Zn-finger in Ran binding protein and others;


Pssm-ID: 395516 [Multi-domain]  Cd Length: 30  Bit Score: 46.58  E-value: 2.88e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 723428422  299 SEDEWQCTECKKFNSPSKRYCFRCWALRKD 328
Cdd:pfam00641   1 REGDWDCSKCLVQNFATSTKCVACQAPKPD 30
mRING-HC-C3HC5_NEU1 cd16647
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein NEURL1A, ...
435-487 5.79e-07

Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein NEURL1A, NEURL1B, and similar proteins; This subfamily includes Drosophila neuralized (D-neu) protein, and its two mammalian homologs, NEURL1A and NEURL1B. D-neu is a regulator of the developmentally important Notch signaling pathway. NEURL1A, also known as NEURL1, NEU, neuralized 1, or RING finger protein 67 (RNF67), is a mammalian homolog of D-neu. It functions as an E3 ubiquitin-protein ligase that directly interacts with and monoubiquitinates cytoplasmic polyadenylation element-binding protein 3 (CPEB3), an RNA binding protein and a translational regulator of local protein synthesis, which facilitates hippocampal plasticity and hippocampal-dependent memory storage. It also acts as a potential tumor suppressor that causes apoptosis and downregulates Notch target genes in medulloblastoma. NEURL1B, also known as neuralized-2 (NEUR2) or neuralized-like protein 3, is another mammalian homolog of D-neu protein. It functions as an E3 ubiquitin-protein ligase that interacts with and ubiquitinates Delta. Thus, it plays a role in the endocytic pathways for Notch signaling by working cooperatively with another E3 ligase, Mind bomb-1 (Mib1), in Delta endocytosis to hepatocyte growth factor-regulated tyrosine kinase substrate (Hrs)-positive vesicles. Members of this subfamily contain two neuralized homology regions (NHRs) responsible for Neural-ligand interactions and a modified C3HC5-type RING-HC finger required for ubiquitin ligase activity. The C3HC5-type RING-HC finger is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438309 [Multi-domain]  Cd Length: 53  Bit Score: 46.14  E-value: 5.79e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 723428422 435 PCSLCEKRPRDGNIIhgKTSHLTTCFHCARRLKKSGASCPACKKEIQLVIKVF 487
Cdd:cd16647    3 ECVICYERPVDTVLY--RCGHMCMCYDCALQLKRRGGSCPICRAPIKDVIKIY 53
SWIB-MDM2 cd00855
SWIB/MDM2 domain family; The SWIB/MDM2 protein domain, short for SWI/SNF complex B/MDM2, has ...
32-105 7.53e-07

SWIB/MDM2 domain family; The SWIB/MDM2 protein domain, short for SWI/SNF complex B/MDM2, has been found in both SWI/SNF complex B (SWIB) and the negative regulator of the p53 tumor suppressor MDM2, which are homologous and share a common fold. The SWIB domain is a conserved region found within proteins in the SWI/SNF (SWItch/Sucrose Non-Fermentable) family of complexes. SWI/SNF complex proteins display helicase and ATPase activities and are thought to regulate transcription of certain genes by altering the chromatin structure around those genes. The mammalian complexes are made up of 9-12 proteins called BAFs (BRG1-associated factors). MDM2 is an inhibitor of p53 tumor repressor. It binds to the transactivation domain and down-regulates the ability of p53 to activate transcription. This family corresponds to the SWIB domain and the p53 binding domain of MDM2.


Pssm-ID: 349487 [Multi-domain]  Cd Length: 69  Bit Score: 46.45  E-value: 7.53e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 723428422  32 QLLKILHAAgaqgEVFTMKEVMHYLGQYIMVKQLYDQQEQHMVYCgGDLLGDLLGCQSFSVKDpspLYDMLRKN 105
Cdd:cd00855    4 ELEALLKSY----ETFTLKEILQALWQYIKKKNLMDPDDPSIVVC-DERLRQLFEVPSFPFSE---IPKALKKH 69
RING-HC_XBAT35-like cd23129
RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and ...
436-487 1.69e-05

RING finger, HC subclass, found in Arabidopsis thaliana protein XB3 homolog 5 (XBAT35) and similar proteins; XBAT35, also known as ankyrin repeat domain and RING finger-containing protein XBAT35, or RING-type E3 ubiquitin transferase XBAT35, has no E3 ubiquitin-protein ligase activity observed when associated with the E2 enzyme UBC8 in vitro. It contains a typical C3HC4-type RING-HC finger.


Pssm-ID: 438491 [Multi-domain]  Cd Length: 54  Bit Score: 42.25  E-value: 1.69e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 723428422 436 CSLCEKRPRDGNIIhgKTSHLTTCFHCARRLKKSGASCPACKKEIQLVIKVF 487
Cdd:cd23129    5 CVVCMDAPRDAVCV--PCGHVAGCMSCLKALMQSSPLCPICRAPVRQVIKVY 54
zf-C3HC4_3 pfam13920
Zinc finger, C3HC4 type (RING finger);
434-483 3.44e-05

Zinc finger, C3HC4 type (RING finger);


Pssm-ID: 464042 [Multi-domain]  Cd Length: 50  Bit Score: 41.21  E-value: 3.44e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 723428422  434 KPCSLCEKRPRdgNIIHGKTSHLTTCFHCARRLKKSGASCPACKKEIQLV 483
Cdd:pfam13920   3 LLCVICLDRPR--NVVLLPCGHLCLCEECAERLLRKKKKCPICRQPIESV 50
mRING-HC-C3HC5_NEU1A cd16785
Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1A (NEURL1A) ...
436-487 2.72e-04

Modified RING finger, HC subclass (C3HC5-type), found in neuralized-like protein 1A (NEURL1A) and similar proteins; NEURL1A, also known as NEURL1, NEU, neuralized 1, or RING finger protein 67 (RNF67), is a mammalian homolog of the Drosophila neuralized (D-neu) protein. It functions as an E3 ubiquitin-protein ligase that directly interacts with and monoubiquitinates cytoplasmic polyadenylation element-binding protein 3 (CPEB3), an RNA binding protein and a translational regulator of local protein synthesis, which facilitates hippocampal plasticity and hippocampal-dependent memory storage. It also acts as a potential tumor suppressor that causes apoptosis and downregulates Notch target genes in the medulloblastoma. NEURL1A contains two neuralized homology regions (NHRs) responsible for Neural-ligand interactions and a modified C3HC5-type RING-HC finger required for ubiquitin ligase activity. The C3HC5-type RING-HC finger is distinguished from typical C3HC4-type RING-HC finger due to the existence of the additional cysteine residue in the middle portion of the RING finger domain.


Pssm-ID: 438439 [Multi-domain]  Cd Length: 59  Bit Score: 38.81  E-value: 2.72e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 723428422 436 CSLCEKRPRDGNIIhgKTSHLTTCFHCARRLKK-SGASCPACKKEIQLVIKVF 487
Cdd:cd16785    7 CTICYENAVDTVIY--TCGHMCLCYACGLRLKKmLNACCPICRRAIKDIIKTY 57
SWIB pfam02201
SWIB/MDM2 domain; This family includes the SWIB domain and the MDM2 domain. The p53-associated ...
26-76 1.37e-03

SWIB/MDM2 domain; This family includes the SWIB domain and the MDM2 domain. The p53-associated protein (MDM2) is an inhibitor of the p53 tumour suppressor gene binding the transactivation domain and down regulating the ability of p53 to activate transcription. This family contains the p53 binding domain of MDM2.


Pssm-ID: 460488 [Multi-domain]  Cd Length: 73  Bit Score: 37.46  E-value: 1.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 723428422   26 QVRPKLQLLKILHAagaqgEVFTMKEVMHYLGQYIMVKQLYDQQEQHMVYC 76
Cdd:pfam02201   2 PFKLSPELAELLGE-----EELSRPEVVKALWEYIKENNLQDPEDKREIIC 47
 
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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