NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2462523137|ref|XP_054223747|]
View 

spindlin interactor and repressor of chromatin-binding protein isoform X5 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
zf-C2H2_12 pfam18658
Spin-doc zinc-finger; This is a zinc finger domain C2H2 type which can be found in SPIN1 ...
 70-134 3.37e-25

Spin-doc zinc-finger; This is a zinc finger domain C2H2 type which can be found in SPIN1 docking protein (SPIN-DOC) and Epm2a-interacting protein 1 (Epm2aip1). SPIN-DOC is a Spindlin1 (SPIN1) regulator that directly binds and strongly disrupts its histone methylation reading ability, causing it to disassociate from chromatin. Epm2aip1 is a glycogen synthase (GS)-associated protein. In the absence of Epm2aip1, the sensitivity of the liver to insulin, in which GS is a principal actor, is impaired.


:

Pssm-ID: 465831  Cd Length: 64  Bit Score: 96.19  E-value: 3.37e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462523137  70 QVSWEQEFLVGSSPGGsGRALCMVCGAEIRAPSADTARSHILEQHPHTLDLSPSEKSNILEAWSE 134
Cdd:pfam18658   1 QERWRLEYLMDYDPGR-NGLVCMVCGESLASLKLSTIKRHILQKHPDTLSLSPEEKEAILEAWEE 64
 
Name Accession Description Interval E-value
zf-C2H2_12 pfam18658
Spin-doc zinc-finger; This is a zinc finger domain C2H2 type which can be found in SPIN1 ...
 70-134 3.37e-25

Spin-doc zinc-finger; This is a zinc finger domain C2H2 type which can be found in SPIN1 docking protein (SPIN-DOC) and Epm2a-interacting protein 1 (Epm2aip1). SPIN-DOC is a Spindlin1 (SPIN1) regulator that directly binds and strongly disrupts its histone methylation reading ability, causing it to disassociate from chromatin. Epm2aip1 is a glycogen synthase (GS)-associated protein. In the absence of Epm2aip1, the sensitivity of the liver to insulin, in which GS is a principal actor, is impaired.


Pssm-ID: 465831  Cd Length: 64  Bit Score: 96.19  E-value: 3.37e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462523137  70 QVSWEQEFLVGSSPGGsGRALCMVCGAEIRAPSADTARSHILEQHPHTLDLSPSEKSNILEAWSE 134
Cdd:pfam18658   1 QERWRLEYLMDYDPGR-NGLVCMVCGESLASLKLSTIKRHILQKHPDTLSLSPEEKEAILEAWEE 64
 
Name Accession Description Interval E-value
zf-C2H2_12 pfam18658
Spin-doc zinc-finger; This is a zinc finger domain C2H2 type which can be found in SPIN1 ...
 70-134 3.37e-25

Spin-doc zinc-finger; This is a zinc finger domain C2H2 type which can be found in SPIN1 docking protein (SPIN-DOC) and Epm2a-interacting protein 1 (Epm2aip1). SPIN-DOC is a Spindlin1 (SPIN1) regulator that directly binds and strongly disrupts its histone methylation reading ability, causing it to disassociate from chromatin. Epm2aip1 is a glycogen synthase (GS)-associated protein. In the absence of Epm2aip1, the sensitivity of the liver to insulin, in which GS is a principal actor, is impaired.


Pssm-ID: 465831  Cd Length: 64  Bit Score: 96.19  E-value: 3.37e-25
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462523137  70 QVSWEQEFLVGSSPGGsGRALCMVCGAEIRAPSADTARSHILEQHPHTLDLSPSEKSNILEAWSE 134
Cdd:pfam18658   1 QERWRLEYLMDYDPGR-NGLVCMVCGESLASLKLSTIKRHILQKHPDTLSLSPEEKEAILEAWEE 64
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH