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Protein

Cytoplasmic dynein 1 light intermediate chain 1

Gene

Dync1li1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 binding dynein to membranous organelles or chromosomes. Probably involved in the microtubule-dependent transport of pericentrin. Is required for progress throuh the spindle assembly checkpoint. The phosphorylated form appears to be involved in the selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi74 – 818ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. microtubule motor activity Source: MGI
  3. poly(A) RNA binding Source: MGI

GO - Biological processi

  1. cell division Source: UniProtKB-KW
  2. metabolic process Source: GOC
  3. microtubule-based movement Source: MGI
  4. mitotic nuclear division Source: UniProtKB-KW
  5. positive regulation of mitotic cell cycle spindle assembly checkpoint Source: UniProtKB
  6. transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoplasmic dynein 1 light intermediate chain 1
Alternative name(s):
Dynein light chain A
Short name:
DLC-A
Dynein light intermediate chain 1, cytosolic
Gene namesi
Name:Dync1li1
Synonyms:Dncli1, Dnclic1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 9

Organism-specific databases

MGIiMGI:2135610. Dync1li1.

Subcellular locationi

Cytoplasm By similarity. Chromosomecentromerekinetochore By similarity. Cytoplasmcytoskeletonspindle pole By similarity

GO - Cellular componenti

  1. centrosome Source: MGI
  2. condensed chromosome kinetochore Source: UniProtKB-SubCell
  3. cytoplasm Source: MGI
  4. cytoplasmic dynein complex Source: UniProtKB
  5. kinetochore Source: UniProtKB
  6. membrane Source: MGI
  7. microtubule Source: UniProtKB-KW
  8. plasma membrane Source: MGI
  9. spindle pole Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Dynein, Kinetochore, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 523523Cytoplasmic dynein 1 light intermediate chain 1PRO_0000114667Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei207 – 2071Phosphoserine4 Publications
Modified residuei213 – 2131PhosphothreonineBy similarity
Modified residuei398 – 3981PhosphoserineBy similarity
Modified residuei405 – 4051Phosphoserine1 Publication
Modified residuei408 – 4081PhosphothreonineBy similarity
Modified residuei419 – 4191PhosphoserineBy similarity
Modified residuei421 – 4211PhosphoserineBy similarity
Modified residuei486 – 4861PhosphoserineBy similarity
Modified residuei510 – 5101Phosphoserine1 Publication
Modified residuei512 – 5121PhosphothreonineBy similarity
Modified residuei513 – 5131Phosphothreonine1 Publication
Modified residuei515 – 5151Phosphothreonine1 Publication
Modified residuei516 – 5161Phosphoserine2 Publications

Post-translational modificationi

Phosphorylated during mitosis but not in interphase.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8R1Q8.
PaxDbiQ8R1Q8.
PRIDEiQ8R1Q8.

PTM databases

PhosphoSiteiQ8R1Q8.

Expressioni

Gene expression databases

BgeeiQ8R1Q8.
CleanExiMM_DYNC1LI1.
ExpressionAtlasiQ8R1Q8. baseline and differential.
GenevestigatoriQ8R1Q8.

Interactioni

Subunit structurei

Homodimer (By similarity). 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. Self-associates. Interacts with DYNC1H1; DYNC1LI1 and DYNC1LI2 bind mutually exclusive to DYNC1H1. Interacts with PCNT (By similarity).By similarity

Protein-protein interaction databases

BioGridi231702. 2 interactions.
IntActiQ8R1Q8. 1 interaction.
MINTiMINT-4118631.

Structurei

3D structure databases

ProteinModelPortaliQ8R1Q8.
SMRiQ8R1Q8. Positions 63-367.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG265404.
GeneTreeiENSGT00390000008295.
HOGENOMiHOG000236263.
HOVERGENiHBG005546.
InParanoidiQ8R1Q8.
KOiK10416.
OMAiPNRSVTS.
OrthoDBiEOG7V7668.
PhylomeDBiQ8R1Q8.
TreeFamiTF352602.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR008467. Dynein1_light_intermed_chain.
IPR022780. Dynein_light_int_chain.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR12688. PTHR12688. 1 hit.
PfamiPF05783. DLIC. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

Q8R1Q8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAVGRVGSF GSSPPGLAST YASGPLANEL ASGSGGPAAG DDEDGQNLWS
60 70 80 90 100
CILSEVSTRS RSKLPTGKNV LLLGEDGAGK TSLIRRIQGI EEYKKGRGLE
110 120 130 140 150
YLYLNVHDED RDDQTRCNVW ILDGDLYHKG LLKFSLDALS LRDTLVMLVV
160 170 180 190 200
DMSKPWTALD SLQKWASVVR EHVDKLKIPP EEMKEMEQKL IRDFQEYVEP
210 220 230 240 250
GEDFPASPQR RTTGAQEDRG DSVVLPLGAD TLTHNLGLPV LVVCTKCDAI
260 270 280 290 300
SVLEKEHDYR DEHFDFIQSH IRKFCLQYGA ALIYTSVKEN KNIDLVYKYI
310 320 330 340 350
VQKLYGFPYK IPAVVVEKDA VFIPAGWDND KKIGILHENF QTLKVEDNFE
360 370 380 390 400
DIITKPPVRK FVHEKEIMAE DDQVFLMKLQ SLLAKQPPTA AGRPVDASPR
410 420 430 440 450
VPGGSPRTPN RSVSSNVASV SPIPAGSKKI DPNMKAGATS EGVLANFFNS
460 470 480 490 500
LLSKKTGSPG GPGVGGSPGG GAAGASPSLP PSAKKSGQKP VLSDVHAELD
510 520
RITRKPASVS PTTPTSPTEG EAS
Length:523
Mass (Da):56,614
Last modified:June 1, 2002 - v1
Checksum:iF080D6865A399498
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC023347 mRNA. Translation: AAH23347.1.
CCDSiCCDS23595.1.
RefSeqiNP_666341.1. NM_146229.2.
UniGeneiMm.128627.

Genome annotation databases

EnsembliENSMUST00000047404; ENSMUSP00000035366; ENSMUSG00000032435.
GeneIDi235661.
KEGGimmu:235661.
UCSCiuc009rxy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC023347 mRNA. Translation: AAH23347.1.
CCDSiCCDS23595.1.
RefSeqiNP_666341.1. NM_146229.2.
UniGeneiMm.128627.

3D structure databases

ProteinModelPortaliQ8R1Q8.
SMRiQ8R1Q8. Positions 63-367.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231702. 2 interactions.
IntActiQ8R1Q8. 1 interaction.
MINTiMINT-4118631.

PTM databases

PhosphoSiteiQ8R1Q8.

Proteomic databases

MaxQBiQ8R1Q8.
PaxDbiQ8R1Q8.
PRIDEiQ8R1Q8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000047404; ENSMUSP00000035366; ENSMUSG00000032435.
GeneIDi235661.
KEGGimmu:235661.
UCSCiuc009rxy.1. mouse.

Organism-specific databases

CTDi51143.
MGIiMGI:2135610. Dync1li1.

Phylogenomic databases

eggNOGiNOG265404.
GeneTreeiENSGT00390000008295.
HOGENOMiHOG000236263.
HOVERGENiHBG005546.
InParanoidiQ8R1Q8.
KOiK10416.
OMAiPNRSVTS.
OrthoDBiEOG7V7668.
PhylomeDBiQ8R1Q8.
TreeFamiTF352602.

Miscellaneous databases

ChiTaRSiDync1li1. mouse.
NextBioi382833.
PROiQ8R1Q8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R1Q8.
CleanExiMM_DYNC1LI1.
ExpressionAtlasiQ8R1Q8. baseline and differential.
GenevestigatoriQ8R1Q8.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR008467. Dynein1_light_intermed_chain.
IPR022780. Dynein_light_int_chain.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR12688. PTHR12688. 1 hit.
PfamiPF05783. DLIC. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney.
  2. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 134-142, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  4. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-405, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
    Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
    Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain cortex.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-510; THR-513; THR-515 AND SER-516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiDC1L1_MOUSE
AccessioniPrimary (citable) accession number: Q8R1Q8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: June 1, 2002
Last modified: February 4, 2015
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.