NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2023615237|ref|NP_776117|]
View 

protein lin-52 homolog isoform 1 [Mus musculus]

Protein Classification

LIN52 domain-containing protein( domain architecture ID 10562158)

LIN52 domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
LIN52 pfam10044
Retinal tissue protein; LIN52 is a family of proteins of approximately 112 amino acids in ...
14-107 1.73e-49

Retinal tissue protein; LIN52 is a family of proteins of approximately 112 amino acids in length which is conserved from nematodes to humans. The proposed tertiary structure is of almost entirely alpha helix interrupted only by loops located at proline residues. Three sites in the protein sequence reveal two types of possible post-translation modification. A serine residue, at position 41, is a candidate for protein kinase C phosphorylation. Glycine residues at position 69 and 91 are probable sites for acetylation by covalent amide linkage of myristate via N-myristoyl transferase. LIN52 is differentially expressed in the trout retina between parr and smolt developmental stages (smoltification). It is likely to be a house-keeping protein. LIN52 forms a complex (LINC) required for transcriptional activation of G2/M genes. The LINC core complex consists of at least five subunits including the chromatin-associated LIN-9 and RbAp48 proteins. LINC associates with a large number of E2F-regulated promoters in quiescent cells. Family members are required for spermatogenesis by repressing testis-specific gene expression.


:

Pssm-ID: 462950  Cd Length: 92  Bit Score: 152.00  E-value: 1.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023615237  14 LLSFEKLDRASPDLWPEQLPGVAEFAASfkSPITSSPPKWMAEIERDDIDMLKELGSLTTANLMEKVRGLQNLAYQLGLD 93
Cdd:pfam10044   1 LISMETLDRASPDLWPEQIPGMSEFLTM--SSPPPSTPKWLQELEKDDMAMLQELGSLTPSQLIEKVKSLHDLAYQLGLE 78
                          90
                  ....*....|....
gi 2023615237  94 ESREMTRGKFLNIL 107
Cdd:pfam10044  79 EAKEMTRGKLLNIF 92
 
Name Accession Description Interval E-value
LIN52 pfam10044
Retinal tissue protein; LIN52 is a family of proteins of approximately 112 amino acids in ...
14-107 1.73e-49

Retinal tissue protein; LIN52 is a family of proteins of approximately 112 amino acids in length which is conserved from nematodes to humans. The proposed tertiary structure is of almost entirely alpha helix interrupted only by loops located at proline residues. Three sites in the protein sequence reveal two types of possible post-translation modification. A serine residue, at position 41, is a candidate for protein kinase C phosphorylation. Glycine residues at position 69 and 91 are probable sites for acetylation by covalent amide linkage of myristate via N-myristoyl transferase. LIN52 is differentially expressed in the trout retina between parr and smolt developmental stages (smoltification). It is likely to be a house-keeping protein. LIN52 forms a complex (LINC) required for transcriptional activation of G2/M genes. The LINC core complex consists of at least five subunits including the chromatin-associated LIN-9 and RbAp48 proteins. LINC associates with a large number of E2F-regulated promoters in quiescent cells. Family members are required for spermatogenesis by repressing testis-specific gene expression.


Pssm-ID: 462950  Cd Length: 92  Bit Score: 152.00  E-value: 1.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023615237  14 LLSFEKLDRASPDLWPEQLPGVAEFAASfkSPITSSPPKWMAEIERDDIDMLKELGSLTTANLMEKVRGLQNLAYQLGLD 93
Cdd:pfam10044   1 LISMETLDRASPDLWPEQIPGMSEFLTM--SSPPPSTPKWLQELEKDDMAMLQELGSLTPSQLIEKVKSLHDLAYQLGLE 78
                          90
                  ....*....|....
gi 2023615237  94 ESREMTRGKFLNIL 107
Cdd:pfam10044  79 EAKEMTRGKLLNIF 92
 
Name Accession Description Interval E-value
LIN52 pfam10044
Retinal tissue protein; LIN52 is a family of proteins of approximately 112 amino acids in ...
14-107 1.73e-49

Retinal tissue protein; LIN52 is a family of proteins of approximately 112 amino acids in length which is conserved from nematodes to humans. The proposed tertiary structure is of almost entirely alpha helix interrupted only by loops located at proline residues. Three sites in the protein sequence reveal two types of possible post-translation modification. A serine residue, at position 41, is a candidate for protein kinase C phosphorylation. Glycine residues at position 69 and 91 are probable sites for acetylation by covalent amide linkage of myristate via N-myristoyl transferase. LIN52 is differentially expressed in the trout retina between parr and smolt developmental stages (smoltification). It is likely to be a house-keeping protein. LIN52 forms a complex (LINC) required for transcriptional activation of G2/M genes. The LINC core complex consists of at least five subunits including the chromatin-associated LIN-9 and RbAp48 proteins. LINC associates with a large number of E2F-regulated promoters in quiescent cells. Family members are required for spermatogenesis by repressing testis-specific gene expression.


Pssm-ID: 462950  Cd Length: 92  Bit Score: 152.00  E-value: 1.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2023615237  14 LLSFEKLDRASPDLWPEQLPGVAEFAASfkSPITSSPPKWMAEIERDDIDMLKELGSLTTANLMEKVRGLQNLAYQLGLD 93
Cdd:pfam10044   1 LISMETLDRASPDLWPEQIPGMSEFLTM--SSPPPSTPKWLQELEKDDMAMLQELGSLTPSQLIEKVKSLHDLAYQLGLE 78
                          90
                  ....*....|....
gi 2023615237  94 ESREMTRGKFLNIL 107
Cdd:pfam10044  79 EAKEMTRGKLLNIF 92
 
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