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Entry version 160 (31 Jul 2019)
Sequence version 3 (10 Aug 2010)
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Protein

Denticleless protein homolog

Gene

DTL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex required for cell cycle control, DNA damage response and translesion DNA synthesis. The DCX(DTL) complex, also named CRL4(CDT2) complex, mediates the polyubiquitination and subsequent degradation of CDT1, CDKN1A/p21(CIP1), FBH1, KMT5A and SDE2 (PubMed:16861906, PubMed:16949367, PubMed:16964240, PubMed:17085480, PubMed:18703516, PubMed:18794347, PubMed:18794348, PubMed:19332548, PubMed:20129063, PubMed:23478441, PubMed:23478445, PubMed:23677613, PubMed:27906959). CDT1 degradation in response to DNA damage is necessary to ensure proper cell cycle regulation of DNA replication (PubMed:16861906, PubMed:16949367, PubMed:17085480). CDKN1A/p21(CIP1) degradation during S phase or following UV irradiation is essential to control replication licensing (PubMed:18794348, PubMed:19332548). KMT5A degradation is also important for a proper regulation of mechanisms such as TGF-beta signaling, cell cycle progression, DNA repair and cell migration (PubMed:23478445). Most substrates require their interaction with PCNA for their polyubiquitination: substrates interact with PCNA via their PIP-box, and those containing the 'K+4' motif in the PIP box, recruit the DCX(DTL) complex, leading to their degradation. In undamaged proliferating cells, the DCX(DTL) complex also promotes the 'Lys-164' monoubiquitination of PCNA, thereby being involved in PCNA-dependent translesion DNA synthesis (PubMed:20129063, PubMed:23478441, PubMed:23478445, PubMed:23677613). The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207).14 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processBiological rhythms, DNA damage, DNA replication, Ubl conjugation pathway

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-110314 Recognition of DNA damage by PCNA-containing replication complex
R-HSA-8951664 Neddylation

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q9NZJ0

SIGNOR Signaling Network Open Resource

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SIGNORi
Q9NZJ0

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00143

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Denticleless protein homolog
Alternative name(s):
DDB1- and CUL4-associated factor 2
Lethal(2) denticleless protein homolog
Retinoic acid-regulated nuclear matrix-associated protein
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:DTL
Synonyms:CDT2, CDW1, DCAF2, L2DTL, RAMP
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:30288 DTL

Online Mendelian Inheritance in Man (OMIM)

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MIMi
610617 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q9NZJ0

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Chromosome, Cytoplasm, Cytoskeleton, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi246R → A: Blocks association with DDB1 and ubiquitination by DCX(DTL). No effect on ubiquitination by SCF(FBXO11). 2 Publications1
Mutagenesisi457D → A: Increases protein stability, but no effect on interaction with FBXO11 and polyubiquitination. Delays cell migration. 1 Publication1
Mutagenesisi462S → A: Blocks interaction with FBXO11 and ubiquitination, increasing protein stability. Delays cell migration. 1 Publication1
Mutagenesisi463N → A: No effect on interaction with FBXO11. Increases protein stability. 1 Publication1
Mutagenesisi464T → A: Blocks interaction with FBXO11 and increases protein stability. Not phosphorylated by CDK1 or CDK2. 1 Publication1
Mutagenesisi464T → D: Blocks interaction with FBXO11. 1 Publication1
Mutagenesisi465P → A: Inhibits phosphorylation on T-464. No effect on interaction with FBXO11. 1 Publication1
Mutagenesisi466T → A: No effect on interaction with FBXO11. 1 Publication1
Mutagenesisi466T → D: No effect on interaction with FBXO11. 1 Publication1
Mutagenesisi467F → A: No effect on interaction with FBXO11. 1 Publication1
Mutagenesisi468S → A: No effect on interaction with FBXO11. 1 Publication1
Mutagenesisi468S → D: No effect on interaction with FBXO11. 1 Publication1
Mutagenesisi471T → A: No effect on interaction with FBXO11. 1 Publication1
Mutagenesisi471T → D: No effect on interaction with FBXO11. 1 Publication1
Mutagenesisi472S → A: No effect on interaction with FBXO11. 1 Publication1
Mutagenesisi472S → D: No effect on interaction with FBXO11. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
51514

Open Targets

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OpenTargetsi
ENSG00000143476

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA142671941

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
DTL

Domain mapping of disease mutations (DMDM)

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DMDMi
302393825

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002748671 – 730Denticleless protein homologAdd BLAST730

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineCombined sources1
Modified residuei196PhosphothreonineCombined sources1
Modified residuei410PhosphoserineCombined sources1
Modified residuei426PhosphoserineCombined sources1
Modified residuei464Phosphothreonine; by CDK1 and CDK21 Publication1
Modified residuei485PhosphoserineCombined sources1
Modified residuei490PhosphoserineCombined sources1
Modified residuei495PhosphoserineCombined sources1
Modified residuei512PhosphoserineCombined sources1
Modified residuei516PhosphothreonineCombined sources1
Modified residuei557PhosphoserineCombined sources1
Modified residuei676PhosphoserineCombined sources1
Modified residuei679PhosphoserineCombined sources1
Modified residuei684PhosphothreonineCombined sources1
Modified residuei702PhosphothreonineCombined sources1
Modified residuei717PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Ubiquitinated by the anaphase promoting complex/cyclosome (APC/C). Autoubiquitinated through 'Lys-48'-polyubiquitin chains in a PCNA-independent reaction, allowing proteasomal turnover. Polyubiquitinated by SCF(FBXO11) when not phosphorylated, leading to its degradation. A tight regulation of the polyubiquitination by SCF(FBXO11) is involved in the control of different processes such as TGF-beta signaling, cell cycle progression and exit.3 Publications
Phosphorylated at Thr-464 by CDK1/Cyclin-B and CDK2/Cyclin-A but not by CDK2/Cyclin-E, MAPK1 or PLK1. Phosphorylation at Thr-464 inhibits the interaction with FBXO11 and decreases upon cell cycle exit induced by TGF-beta or serum starvation.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9NZJ0

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9NZJ0

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9NZJ0

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q9NZJ0

PeptideAtlas

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PeptideAtlasi
Q9NZJ0

PRoteomics IDEntifications database

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PRIDEi
Q9NZJ0

ProteomicsDB human proteome resource

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ProteomicsDBi
83411 [Q9NZJ0-1]
83412 [Q9NZJ0-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9NZJ0

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q9NZJ0

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in placenta and testis, very low expression seen in skeletal muscle. Detected in all hematopoietic tissues examined, with highest expression in thymus and bone marrow. A low level detected in the spleen and lymph node, and barely detectable level in the peripheral leukocytes. RA treatment down-regulated the expression in NT2 cell.2 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed in all fetal tissues examined, included brain, lung, liver, and kidney. Protein levels peak at G1 and decrease through S-phase.2 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Induced by TGF-beta, the up-regulation is immediate and transient.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000143476 Expressed in 143 organ(s), highest expression level in secondary oocyte

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9NZJ0 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9NZJ0 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA028016
HPA032023
HPA032031

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the DCX(DTL) E3 ubiquitin ligase complex (also called CRL4(CDT2)), at least composed of CUL4 (CUL4A or CUL4B), DDB1, DTL/CDT2 and RBX1.

Interacts with CDKN1A and CDT1.

Interacts with FBXO11; SCF(FBXWO11) controls DTL stability but DCX(DTL) does not control FBXO11 stability.

Interacts with CRY1 (PubMed:26431207).

9 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
DDB1Q165313EBI-1176075,EBI-350322

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
119582, 93 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9NZJ0

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
Q9NZJ0

Protein interaction database and analysis system

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IntActi
Q9NZJ0, 8 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000355958

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1730
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q9NZJ0

Database of comparative protein structure models

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ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati47 – 89WD 1Add BLAST43
Repeati96 – 135WD 2Add BLAST40
Repeati138 – 178WD 3Add BLAST41
Repeati214 – 253WD 4Add BLAST40
Repeati267 – 308WD 5Add BLAST42
Repeati313 – 354WD 6Add BLAST42
Repeati358 – 398WD 7Add BLAST41

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi168 – 171DDB1-binding motif4
Motifi197 – 203Nuclear localization signalSequence analysis7
Motifi243 – 246DDB1-binding motif4

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the WD repeat cdt2 family.Curated

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0321 Eukaryota
ENOG410XRWK LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00530000064210

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9NZJ0

KEGG Orthology (KO)

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KOi
K11790

Identification of Orthologs from Complete Genome Data

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OMAi
PWHPPTV

Database of Orthologous Groups

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OrthoDBi
1288134at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9NZJ0

TreeFam database of animal gene trees

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TreeFami
TF324483

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.130.10.10, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR015943 WD40/YVTN_repeat-like_dom_sf
IPR001680 WD40_repeat
IPR019775 WD40_repeat_CS
IPR017986 WD40_repeat_dom
IPR036322 WD40_repeat_dom_sf

Pfam protein domain database

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Pfami
View protein in Pfam
PF00400 WD40, 5 hits

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00320 WD40, 6 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF50978 SSF50978, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00678 WD_REPEATS_1, 2 hits
PS50082 WD_REPEATS_2, 5 hits
PS50294 WD_REPEATS_REGION, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9NZJ0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MLFNSVLRQP QLGVLRNGWS SQYPLQSLLT GYQCSGNDEH TSYGETGVPV
60 70 80 90 100
PPFGCTFSSA PNMEHVLAVA NEEGFVRLYN TESQSFRKKC FKEWMAHWNA
110 120 130 140 150
VFDLAWVPGE LKLVTAAGDQ TAKFWDVKAG ELIGTCKGHQ CSLKSVAFSK
160 170 180 190 200
FEKAVFCTGG RDGNIMVWDT RCNKKDGFYR QVNQISGAHN TSDKQTPSKP
210 220 230 240 250
KKKQNSKGLA PSVDFQQSVT VVLFQDENTL VSAGAVDGII KVWDLRKNYT
260 270 280 290 300
AYRQEPIASK SFLYPGSSTR KLGYSSLILD STGSTLFANC TDDNIYMFNM
310 320 330 340 350
TGLKTSPVAI FNGHQNSTFY VKSSLSPDDQ FLVSGSSDEA AYIWKVSTPW
360 370 380 390 400
QPPTVLLGHS QEVTSVCWCP SDFTKIATCS DDNTLKIWRL NRGLEEKPGG
410 420 430 440 450
DKLSTVGWAS QKKKESRPGL VTVTSSQSTP AKAPRAKCNP SNSSPSSAAC
460 470 480 490 500
APSCAGDLPL PSNTPTFSIK TSPAKARSPI NRRGSVSSVS PKPPSSFKMS
510 520 530 540 550
IRNWVTRTPS SSPPITPPAS ETKIMSPRKA LIPVSQKSSQ AEACSESRNR
560 570 580 590 600
VKRRLDSSCL ESVKQKCVKS CNCVTELDGQ VENLHLDLCC LAGNQEDLSK
610 620 630 640 650
DSLGPTKSSK IEGAGTSISE PPSPISPYAS ESCGTLPLPL RPCGEGSEMV
660 670 680 690 700
GKENSSPENK NWLLAMAAKR KAENPSPRSP SSQTPNSRRQ SGKKLPSPVT
710 720 730
ITPSSMRKIC TYFHRKSQED FCGPEHSTEL
Length:730
Mass (Da):79,468
Last modified:August 10, 2010 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iCE8D54234D44F002
GO
Isoform 2 (identifier: Q9NZJ0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     18-59: Missing.
     240-253: IKVWDLRKNYTAYR → FKSDFGFHWLYFIC
     254-730: Missing.

Note: No experimental confirmation available.
Show »
Length:211
Mass (Da):23,682
Checksum:i23E4B52CFC514F80
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F5GZ90F5GZ90_HUMAN
Denticleless protein homolog
DTL
688Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence BAA91552 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAA91586 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti83S → P in BAA91355 (PubMed:14702039).Curated1
Sequence conflicti356L → F in BAF85032 (PubMed:14702039).Curated1
Sequence conflicti532I → T in BAA91552 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_062095425S → N. Corresponds to variant dbSNP:rs35137676Ensembl.1
Natural variantiVAR_030353436A → V6 PublicationsCorresponds to variant dbSNP:rs3135474Ensembl.1
Natural variantiVAR_030354694K → TCombined sources5 PublicationsCorresponds to variant dbSNP:rs6540718Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_02287918 – 59Missing in isoform 2. 1 PublicationAdd BLAST42
Alternative sequenceiVSP_022880240 – 253IKVWD…YTAYR → FKSDFGFHWLYFIC in isoform 2. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_022881254 – 730Missing in isoform 2. 1 PublicationAdd BLAST477

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF345896 mRNA Translation: AAK54706.1
DQ641253 mRNA Translation: ABG23317.1
AF195765 mRNA Translation: AAF35182.1
AK000742 mRNA Translation: BAA91355.1
AK001206 mRNA Translation: BAA91552.1 Different initiation.
AK001261 mRNA Translation: BAA91586.1 Different initiation.
AK027651 mRNA Translation: BAB55267.1
AK292343 mRNA Translation: BAF85032.1
AC092814 Genomic DNA No translation available.
AL592297 Genomic DNA No translation available.
AL606468 Genomic DNA No translation available.
CH471100 Genomic DNA Translation: EAW93395.1
CH471100 Genomic DNA Translation: EAW93397.1
BC033540 mRNA Translation: AAH33540.1
BC033297 mRNA Translation: AAH33297.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS1502.1 [Q9NZJ0-1]

NCBI Reference Sequences

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RefSeqi
NP_001273158.1, NM_001286229.1
NP_057532.3, NM_016448.3 [Q9NZJ0-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000366991; ENSP00000355958; ENSG00000143476 [Q9NZJ0-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
51514

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:51514

UCSC genome browser

More...
UCSCi
uc009xdc.5 human [Q9NZJ0-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF345896 mRNA Translation: AAK54706.1
DQ641253 mRNA Translation: ABG23317.1
AF195765 mRNA Translation: AAF35182.1
AK000742 mRNA Translation: BAA91355.1
AK001206 mRNA Translation: BAA91552.1 Different initiation.
AK001261 mRNA Translation: BAA91586.1 Different initiation.
AK027651 mRNA Translation: BAB55267.1
AK292343 mRNA Translation: BAF85032.1
AC092814 Genomic DNA No translation available.
AL592297 Genomic DNA No translation available.
AL606468 Genomic DNA No translation available.
CH471100 Genomic DNA Translation: EAW93395.1
CH471100 Genomic DNA Translation: EAW93397.1
BC033540 mRNA Translation: AAH33540.1
BC033297 mRNA Translation: AAH33297.1
CCDSiCCDS1502.1 [Q9NZJ0-1]
RefSeqiNP_001273158.1, NM_001286229.1
NP_057532.3, NM_016448.3 [Q9NZJ0-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6QC0X-ray3.50B/D/F704-717[»]
SMRiQ9NZJ0
ModBaseiSearch...

Protein-protein interaction databases

BioGridi119582, 93 interactors
CORUMiQ9NZJ0
ELMiQ9NZJ0
IntActiQ9NZJ0, 8 interactors
STRINGi9606.ENSP00000355958

PTM databases

iPTMnetiQ9NZJ0
PhosphoSitePlusiQ9NZJ0

Polymorphism and mutation databases

BioMutaiDTL
DMDMi302393825

Proteomic databases

EPDiQ9NZJ0
jPOSTiQ9NZJ0
MaxQBiQ9NZJ0
PaxDbiQ9NZJ0
PeptideAtlasiQ9NZJ0
PRIDEiQ9NZJ0
ProteomicsDBi83411 [Q9NZJ0-1]
83412 [Q9NZJ0-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
51514
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366991; ENSP00000355958; ENSG00000143476 [Q9NZJ0-1]
GeneIDi51514
KEGGihsa:51514
UCSCiuc009xdc.5 human [Q9NZJ0-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
51514
DisGeNETi51514

GeneCards: human genes, protein and diseases

More...
GeneCardsi
DTL
HGNCiHGNC:30288 DTL
HPAiHPA028016
HPA032023
HPA032031
MIMi610617 gene
neXtProtiNX_Q9NZJ0
OpenTargetsiENSG00000143476
PharmGKBiPA142671941

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0321 Eukaryota
ENOG410XRWK LUCA
GeneTreeiENSGT00530000064210
InParanoidiQ9NZJ0
KOiK11790
OMAiPWHPPTV
OrthoDBi1288134at2759
PhylomeDBiQ9NZJ0
TreeFamiTF324483

Enzyme and pathway databases

UniPathwayiUPA00143
ReactomeiR-HSA-110314 Recognition of DNA damage by PCNA-containing replication complex
R-HSA-8951664 Neddylation
SignaLinkiQ9NZJ0
SIGNORiQ9NZJ0

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
DTL human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
DTL_(gene)

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
51514

Protein Ontology

More...
PROi
PR:Q9NZJ0

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000143476 Expressed in 143 organ(s), highest expression level in secondary oocyte
ExpressionAtlasiQ9NZJ0 baseline and differential
GenevisibleiQ9NZJ0 HS

Family and domain databases

Gene3Di2.130.10.10, 2 hits
InterProiView protein in InterPro
IPR015943 WD40/YVTN_repeat-like_dom_sf
IPR001680 WD40_repeat
IPR019775 WD40_repeat_CS
IPR017986 WD40_repeat_dom
IPR036322 WD40_repeat_dom_sf
PfamiView protein in Pfam
PF00400 WD40, 5 hits
SMARTiView protein in SMART
SM00320 WD40, 6 hits
SUPFAMiSSF50978 SSF50978, 1 hit
PROSITEiView protein in PROSITE
PS00678 WD_REPEATS_1, 2 hits
PS50082 WD_REPEATS_2, 5 hits
PS50294 WD_REPEATS_REGION, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiDTL_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9NZJ0
Secondary accession number(s): A8K8H8
, D3DT98, Q5VT77, Q96SN0, Q9NW03, Q9NW34, Q9NWM5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 6, 2007
Last sequence update: August 10, 2010
Last modified: July 31, 2019
This is version 160 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
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