Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P63168 (DYL1_MOUSE)

Entry version 158 (17 Jun 2020)
Sequence version 1 (27 Sep 2004)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Dynein light chain 1, cytoplasmic

Gene

Dynll1

Organism
Mus musculus (Mouse)
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

Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity).By similarity
Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.By similarity
Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.By similarity
Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity (By similarity).By similarity

<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 - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

Molecular functionActivator, Motor protein
Biological processApoptosis, Transcription, Transcription regulation, Transport

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-111446 Activation of BIM and translocation to mitochondria
R-MMU-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-MMU-1632852 Macroautophagy
R-MMU-2132295 MHC class II antigen presentation
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-2565942 Regulation of PLK1 Activity at G2/M Transition
R-MMU-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-MMU-380259 Loss of Nlp from mitotic centrosomes
R-MMU-380270 Recruitment of mitotic centrosome proteins and complexes
R-MMU-380284 Loss of proteins required for interphase microtubule organization from the centrosome
R-MMU-380320 Recruitment of NuMA to mitotic centrosomes
R-MMU-5620912 Anchoring of the basal body to the plasma membrane
R-MMU-5620924 Intraflagellar transport
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-6798695 Neutrophil degranulation
R-MMU-6807878 COPI-mediated anterograde transport
R-MMU-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-MMU-68877 Mitotic Prometaphase
R-MMU-8854518 AURKA Activation by TPX2
R-MMU-9646399 Aggrephagy
R-MMU-9648025 EML4 and NUDC in mitotic spindle formation

<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%5Fand%5Ftaxonomy%5Fsection">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:
Dynein light chain 1, cytoplasmic
Alternative name(s):
8 kDa dynein light chain
Short name:
DLC8
Dynein light chain LC8-type 1
Protein inhibitor of neuronal nitric oxide synthase
Short name:
PIN
Short name:
mPIN
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:Dynll1
Synonyms:Dlc1, Dncl1, Dnclc1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 5

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:1861457 Dynll1

<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

Cytoplasm, Cytoskeleton, Dynein, Microtubule, Mitochondrion, Nucleus

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001951271 – 89Dynein light chain 1, cytoplasmicAdd BLAST89

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 residuei36N6-acetyllysineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki43Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei88PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Phosphorylation at Ser-88 appears to control the dimer-monomer transition.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P63168

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P63168

MaxQB - The MaxQuant DataBase

More...MaxQBi		P63168

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

More...PaxDbi		P63168

PeptideAtlas

More...PeptideAtlasi		P63168

PRoteomics IDEntifications database

More...PRIDEi		P63168

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P63168

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P63168

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

More...PhosphoSitePlusi		P63168

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000009013 Expressed in floor plate of midbrain and 280 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P63168 MM

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. Monomer; the monomeric form is incapable of binding to target proteins. The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits presented by intermediate chains (ICs), light intermediate chains (LICs) and light chains (LCs); the composition seems to vary in respect to the IC, LIC and LC composition. The heavy chain homodimer serves as a scaffold for the probable homodimeric assembly of the respective non-catalytic subunits. The ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer.

Interacts with TXNDC17.

Interacts with WWC1 and ESR1. The interaction with WWC1 is mandatory for the recruitment and transactivation functions of ESR1 or DYNLL1 to the target chromatin.

Interacts with BCL2; the interaction is greatly enhanced in the nucleus and in mitochondria upon induction of apoptosis.

Interacts with PAK1; the interaction requires dimeric DYNLL1.

Interacts with MYZAP.

Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2.

Interacts with ATMIN; this interaction inhibits ATMIN transcriptional activity and hence may play a role in a feedback loop whereby DYNLL1 inhibits transactivation of its own promoter by ATMIN.

Interacts with NEK9 (not phosphorylated at 'Ser-944') (By similarity).

Interacts with BCL2L11 (PubMed:21478148).

Interacts with BICD2 (PubMed:22956769).

Interacts with BCAS1 (By similarity).

Interacts with Bassoon/BSN (By similarity).

Interacts with HDAC6 (By similarity).

Interacts with TPPP (By similarity).

By similarity2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		207994, 79 interactors

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		P63168

Protein interaction database and analysis system

More...IntActi		P63168, 76 interactors

Molecular INTeraction database

More...MINTi		P63168

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000009157

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P63168 protein

<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

3D structure databases

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

More...SMRi		P63168

Database of comparative protein structure models

More...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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni67 – 89Interaction with ESR1By similarityAdd BLAST23

<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 dynein light chain family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3430 Eukaryota
ENOG4111NK2 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00390000000378

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_070944_4_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P63168

KEGG Orthology (KO)

More...KOi		K10418

Identification of Orthologs from Complete Genome Data

More...OMAi		FVTHEKH

Database of Orthologous Groups

More...OrthoDBi		1520814at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P63168

TreeFam database of animal gene trees

More...TreeFami		TF300264

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.740.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR037177 DLC_sf
IPR019763 Dynein_light_1/2_CS
IPR001372 Dynein_light_chain_typ-1/2

The PANTHER Classification System

More...PANTHERi		PTHR11886 PTHR11886, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01221 Dynein_light, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM01375 Dynein_light, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF54648 SSF54648, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS01239 DYNEIN_LIGHT_1, 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%5Flength">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P63168-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MCDRKAVIKN ADMSEEMQQD SVECATQALE KYNIEKDIAA HIKKEFDKKY 
        60         70         80 
NPTWHCIVGR NFGSYVTHET KHFIYFYLGQ VAILLFKSG
Length:89
Mass (Da):10,366
Last modified:September 27, 2004 - v1
<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:iF5E7647D092BEB3A
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF020185 mRNA Translation: AAD01643.1
AK002522 mRNA Translation: BAB22160.1
AK010614 mRNA Translation: BAB27063.1
AK010685 mRNA Translation: BAB27117.1
AK013721 mRNA Translation: BAB28970.1
AK082923 mRNA Translation: BAC38691.1
AK147977 mRNA Translation: BAE28262.1
BC008106 mRNA Translation: AAH08106.1
BC034258 mRNA Translation: AAH34258.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS39227.1

NCBI Reference Sequences

More...RefSeqi		NP_062656.3, NM_019682.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000009157; ENSMUSP00000009157; ENSMUSG00000009013
ENSMUST00000112090; ENSMUSP00000107720; ENSMUSG00000009013

Database of genes from NCBI RefSeq genomes

More...GeneIDi		56455

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:56455

UCSC genome browser

More...UCSCi		uc008zdp.2 mouse

<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
AF020185 mRNA Translation: AAD01643.1
AK002522 mRNA Translation: BAB22160.1
AK010614 mRNA Translation: BAB27063.1
AK010685 mRNA Translation: BAB27117.1
AK013721 mRNA Translation: BAB28970.1
AK082923 mRNA Translation: BAC38691.1
AK147977 mRNA Translation: BAE28262.1
BC008106 mRNA Translation: AAH08106.1
BC034258 mRNA Translation: AAH34258.1
CCDSiCCDS39227.1
RefSeqiNP_062656.3, NM_019682.4

3D structure databases

SMRiP63168
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi207994, 79 interactors
ELMiP63168
IntActiP63168, 76 interactors
MINTiP63168
STRINGi10090.ENSMUSP00000009157

PTM databases

iPTMnetiP63168
PhosphoSitePlusiP63168

Proteomic databases

EPDiP63168
jPOSTiP63168
MaxQBiP63168
PaxDbiP63168
PeptideAtlasiP63168
PRIDEiP63168
TopDownProteomicsiP63168

Genome annotation databases

EnsembliENSMUST00000009157; ENSMUSP00000009157; ENSMUSG00000009013
ENSMUST00000112090; ENSMUSP00000107720; ENSMUSG00000009013
GeneIDi56455
KEGGimmu:56455
UCSCiuc008zdp.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		8655
MGIiMGI:1861457 Dynll1

Phylogenomic databases

eggNOGiKOG3430 Eukaryota
ENOG4111NK2 LUCA
GeneTreeiENSGT00390000000378
HOGENOMiCLU_070944_4_0_1
InParanoidiP63168
KOiK10418
OMAiFVTHEKH
OrthoDBi1520814at2759
PhylomeDBiP63168
TreeFamiTF300264

Enzyme and pathway databases

ReactomeiR-MMU-111446 Activation of BIM and translocation to mitochondria
R-MMU-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-MMU-1632852 Macroautophagy
R-MMU-2132295 MHC class II antigen presentation
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-2565942 Regulation of PLK1 Activity at G2/M Transition
R-MMU-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)
R-MMU-380259 Loss of Nlp from mitotic centrosomes
R-MMU-380270 Recruitment of mitotic centrosome proteins and complexes
R-MMU-380284 Loss of proteins required for interphase microtubule organization from the centrosome
R-MMU-380320 Recruitment of NuMA to mitotic centrosomes
R-MMU-5620912 Anchoring of the basal body to the plasma membrane
R-MMU-5620924 Intraflagellar transport
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-6798695 Neutrophil degranulation
R-MMU-6807878 COPI-mediated anterograde transport
R-MMU-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-MMU-68877 Mitotic Prometaphase
R-MMU-8854518 AURKA Activation by TPX2
R-MMU-9646399 Aggrephagy
R-MMU-9648025 EML4 and NUDC in mitotic spindle formation

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		56455 7 hits in 12 CRISPR screens

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

More...ChiTaRSi		Dynll1 mouse

Protein Ontology

More...PROi		PR:P63168
RNActiP63168 protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000009013 Expressed in floor plate of midbrain and 280 other tissues
GenevisibleiP63168 MM

Family and domain databases

Gene3Di3.30.740.10, 1 hit
InterProiView protein in InterPro
IPR037177 DLC_sf
IPR019763 Dynein_light_1/2_CS
IPR001372 Dynein_light_chain_typ-1/2
PANTHERiPTHR11886 PTHR11886, 1 hit
PfamiView protein in Pfam
PF01221 Dynein_light, 1 hit
SMARTiView protein in SMART
SM01375 Dynein_light, 1 hit
SUPFAMiSSF54648 SSF54648, 1 hit
PROSITEiView protein in PROSITE
PS01239 DYNEIN_LIGHT_1, 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 nameiDYL1_MOUSE
<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: P63168
Secondary accession number(s): Q15701, Q3UGE7
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: June 17, 2020
This is version 158 of the entry and version 1 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

<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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again