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Conserved domains on  [gi|196259799|ref|NP_001124506|]
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probable E3 SUMO-protein ligase RNF212 isoform a [Homo sapiens]

Protein Classification

RING finger protein; RING finger protein 130( domain architecture ID 11616577)

RING finger protein may function as an E3 ubiquitin protein ligase that mediates the ubiquitination of target proteins by bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin| RING finger protein 130 (RNF130) acts as an E3 ubiquitin-protein ligase that may have a role during the programmed cell death of hematopoietic cells

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RING-HC_RNF212 cd16746
RING finger, HC subclass, found in RING finger protein 212 (RNF212) and similar proteins; ...
 4-50 3.95e-22

RING finger, HC subclass, found in RING finger protein 212 (RNF212) and similar proteins; RNF212 is a dosage-sensitive regulator of crossing-over during mammalian meiosis. It plays a central role in designating crossover sites and coupling chromosome synapsis to the formation of crossover-specific recombination complexes. It also functions as an E3 ligase for SUMO modification. RNF212 contains an N-terminal C3HC4-type RING-HC finger.


:

Pssm-ID: 438404  Cd Length: 48  Bit Score: 86.72  E-value: 3.95e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 196259799   4 WVFCNRCFQPPHR-TSCFSLTNCGHVYCDACLGKGKKNECLICKAPCR 50
Cdd:cd16746    1 RVFCNFCFQQPRPnCPSFILTNCGHVVCEACLQKGKKNECLVCKAPCR 48
 
Name Accession Description Interval E-value
RING-HC_RNF212 cd16746
RING finger, HC subclass, found in RING finger protein 212 (RNF212) and similar proteins; ...
 4-50 3.95e-22

RING finger, HC subclass, found in RING finger protein 212 (RNF212) and similar proteins; RNF212 is a dosage-sensitive regulator of crossing-over during mammalian meiosis. It plays a central role in designating crossover sites and coupling chromosome synapsis to the formation of crossover-specific recombination complexes. It also functions as an E3 ligase for SUMO modification. RNF212 contains an N-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438404  Cd Length: 48  Bit Score: 86.72  E-value: 3.95e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 196259799   4 WVFCNRCFQPPHR-TSCFSLTNCGHVYCDACLGKGKKNECLICKAPCR 50
Cdd:cd16746    1 RVFCNFCFQQPRPnCPSFILTNCGHVVCEACLQKGKKNECLVCKAPCR 48
zf-RING_5 pfam14634
zinc-RING finger domain;
6-46 2.77e-08

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 48.96  E-value: 2.77e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 196259799    6 FCNRCFQPPHRTSCFSLTNCGHVYCDACLGKGKKN-ECLICK 46
Cdd:pfam14634   1 HCNKCFKELSKTRPFYLTSCGHIFCEECLTRLLQErQCPICK 42
 
Name Accession Description Interval E-value
RING-HC_RNF212 cd16746
RING finger, HC subclass, found in RING finger protein 212 (RNF212) and similar proteins; ...
 4-50 3.95e-22

RING finger, HC subclass, found in RING finger protein 212 (RNF212) and similar proteins; RNF212 is a dosage-sensitive regulator of crossing-over during mammalian meiosis. It plays a central role in designating crossover sites and coupling chromosome synapsis to the formation of crossover-specific recombination complexes. It also functions as an E3 ligase for SUMO modification. RNF212 contains an N-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438404  Cd Length: 48  Bit Score: 86.72  E-value: 3.95e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 196259799   4 WVFCNRCFQPPHR-TSCFSLTNCGHVYCDACLGKGKKNECLICKAPCR 50
Cdd:cd16746    1 RVFCNFCFQQPRPnCPSFILTNCGHVVCEACLQKGKKNECLVCKAPCR 48
RING-HC_RNF212-like cd16560
RING finger, HC subclass, found in RING finger proteins RNF212, RNF212B and similar proteins; ...
 5-46 9.43e-18

RING finger, HC subclass, found in RING finger proteins RNF212, RNF212B and similar proteins; This subfamily includes RING finger protein RNF212, RNF212B, and their homologs. RNF212 is a dosage-sensitive regulator of crossing-over during mammalian meiosis. It plays a central role in designating crossover sites and coupling chromosome synapsis to the formation of crossover-specific recombination complexes. It also functions as an E3 ligase for small ubiquitin-related modifier (SUMO) modification. RNF212B shows high sequence similarity with RNF212, but its biological function remains unclear. Members of this subfamily contain an N-terminal C3HC4-type RING-HC finger. Also included are two homologs of RNF212, meiotic procrossover factors Zip3 and ZHP-3, which have been identified in Saccharomyces cerevisiae and Caenorhabditis elegans, respectively. Budding yeast Zip3 is a small ubiquitin-related modifier (SUMO) E3 ligase implicated in the SUMO pathway of post-translational modification. It sumoylates chromosome axis proteins, thus promoting synaptonemal complex polymerization. It also acts as an Smt3 E3 ligase. Zip3 includes a SUMO Interacting Motif (SIM) and a modified C3HCHC2-type RING-HC finger that are important for Zip3 in vitro E3 ligase activity and necessary for SC polymerization and correct sporulation. ZHP-3 acts at crossovers to couple meiotic recombination with synaptonemal complex disassembly and chiasma formation in Caenorhabditis elegans. It possesses a C3HC4-type RING-HC finger.


Pssm-ID: 438222  Cd Length: 42  Bit Score: 75.27  E-value: 9.43e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 196259799   5 VFCNRCFQPPHRTSCFSLTNCGHVYCDACLGKGKKNECLICK 46
Cdd:cd16560    1 VHCNTCFQLPGDTSKFFLTSCGHIYCDACVGKGKRNKCKICG 42
zf-RING_5 pfam14634
zinc-RING finger domain;
6-46 2.77e-08

zinc-RING finger domain;


Pssm-ID: 434085 [Multi-domain]  Cd Length: 43  Bit Score: 48.96  E-value: 2.77e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 196259799    6 FCNRCFQPPHRTSCFSLTNCGHVYCDACLGKGKKN-ECLICK 46
Cdd:pfam14634   1 HCNKCFKELSKTRPFYLTSCGHIFCEECLTRLLQErQCPICK 42
RING-HC_RNF212B cd16747
RING finger, HC subclass, found in RING finger protein 212B (RNF212B) and similar proteins; ...
 7-46 1.52e-04

RING finger, HC subclass, found in RING finger protein 212B (RNF212B) and similar proteins; RNF212B is an uncharacterized protein with high sequence similarity with RNF212, a dosage-sensitive regulator of crossing-over during mammalian meiosis. RNF212B contains an N-terminal C3HC4-type RING-HC finger.


Pssm-ID: 438405  Cd Length: 37  Bit Score: 38.55  E-value: 1.52e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 196259799   7 CNRCFQppHRTSCFSLTNCGHVYCDACLgkgKKNECLICK 46
Cdd:cd16747    3 CNKCFR--RDGASFFITSCGHIFCEKCI---KAEKCTVCG 37
RING-HC_BARD1 cd16496
RING finger, HC subclass, found in BRCA1-associated RING domain protein 1 (BARD-1) and similar ...
 7-78 9.44e-04

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: 37.70  E-value: 9.44e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 196259799   7 CNRCFQPPHRTSCfsLTNCGHVYCDACLGKGKKNECLICKAPCRTvllskhTDADIQAFFMSIDSLCKKYSR 78
Cdd:cd16496   18 CSRCASILKEPVT--LGGCEHVFCRSCVGDRLGNGCPVCDTPAWA------RDLQINRQLDSMVQLCRKLRN 81
 
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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