Transmembrane protein 131-like; Transmembrane protein 131-like (TMEM131L) was identified as a ...
185-1518
0e+00
Transmembrane protein 131-like; Transmembrane protein 131-like (TMEM131L) was identified as a negative regulator of thymocyte proliferation that acts through mixed Wnt-dependent and independent mechanisms. It has two isoforms, L and S, which have different subcellular localization. L isoform, the membrane-associated form, inhibits canonical Wnt/beta-catenin signalling through the induction of lysosome-dependent degradation of the active phosphorylated form of the LRP6 coreceptor. This protein contains three conserved homology domains (CHD1, 2 and 3), a transmembrane region and a C-terminal serine-rich region. This family is related to pfam12371.
:
Pssm-ID: 437364 Cd Length: 1429 Bit Score: 2349.78 E-value: 0e+00
Transmembrane protein 131-like N-terminal; TMEM131_like is a family of bacterial, plant and ...
91-174
1.77e-17
Transmembrane protein 131-like N-terminal; TMEM131_like is a family of bacterial, plant and other metazoa transmembrane proteins. Many of the members are multi-pass transmembrane proteins. This domain represents the N-terminal region which contains a conserved homology domain (CHD1).
The actual alignment was detected with superfamily member pfam12371:
Pssm-ID: 463553 Cd Length: 84 Bit Score: 78.47 E-value: 1.77e-17
Transmembrane protein 131-like; Transmembrane protein 131-like (TMEM131L) was identified as a ...
185-1518
0e+00
Transmembrane protein 131-like; Transmembrane protein 131-like (TMEM131L) was identified as a negative regulator of thymocyte proliferation that acts through mixed Wnt-dependent and independent mechanisms. It has two isoforms, L and S, which have different subcellular localization. L isoform, the membrane-associated form, inhibits canonical Wnt/beta-catenin signalling through the induction of lysosome-dependent degradation of the active phosphorylated form of the LRP6 coreceptor. This protein contains three conserved homology domains (CHD1, 2 and 3), a transmembrane region and a C-terminal serine-rich region. This family is related to pfam12371.
Pssm-ID: 437364 Cd Length: 1429 Bit Score: 2349.78 E-value: 0e+00
Transmembrane protein 131-like N-terminal; TMEM131_like is a family of bacterial, plant and ...
91-174
1.77e-17
Transmembrane protein 131-like N-terminal; TMEM131_like is a family of bacterial, plant and other metazoa transmembrane proteins. Many of the members are multi-pass transmembrane proteins. This domain represents the N-terminal region which contains a conserved homology domain (CHD1).
Pssm-ID: 463553 Cd Length: 84 Bit Score: 78.47 E-value: 1.77e-17
Transmembrane protein 131-like; Transmembrane protein 131-like (TMEM131L) was identified as a ...
185-1518
0e+00
Transmembrane protein 131-like; Transmembrane protein 131-like (TMEM131L) was identified as a negative regulator of thymocyte proliferation that acts through mixed Wnt-dependent and independent mechanisms. It has two isoforms, L and S, which have different subcellular localization. L isoform, the membrane-associated form, inhibits canonical Wnt/beta-catenin signalling through the induction of lysosome-dependent degradation of the active phosphorylated form of the LRP6 coreceptor. This protein contains three conserved homology domains (CHD1, 2 and 3), a transmembrane region and a C-terminal serine-rich region. This family is related to pfam12371.
Pssm-ID: 437364 Cd Length: 1429 Bit Score: 2349.78 E-value: 0e+00
Transmembrane protein 131-like N-terminal; TMEM131_like is a family of bacterial, plant and ...
91-174
1.77e-17
Transmembrane protein 131-like N-terminal; TMEM131_like is a family of bacterial, plant and other metazoa transmembrane proteins. Many of the members are multi-pass transmembrane proteins. This domain represents the N-terminal region which contains a conserved homology domain (CHD1).
Pssm-ID: 463553 Cd Length: 84 Bit Score: 78.47 E-value: 1.77e-17
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
92-184
2.30e-03
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function.
Pssm-ID: 464865 [Multi-domain] Cd Length: 98 Bit Score: 38.80 E-value: 2.30e-03
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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of your query sequence and the protein sequences used to curate the domain model,
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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Domains are color coded according to superfamilies
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
meet or exceed the RPS-BLAST threshold for statistical significance (default E-value cutoff of 0.01, or an E-value selected by user via the
advanced search options)
the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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