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Protein

Cytoplasmic dynein 1 light intermediate chain 1

Gene

Dync1li1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • mitotic spindle organization Source: RGD
  • positive regulation of mitotic cell cycle spindle assembly checkpoint Source: UniProtKB
  • regulation of centrosome cycle Source: RGD
  • transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Biological processi

Cell cycle, Cell division, 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi71072. Dync1li1.

Subcellular locationi

GO - Cellular componenti

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_0000114668Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei207 – 2071PhosphoserineCombined sources
Modified residuei213 – 2131PhosphothreonineBy similarity
Modified residuei398 – 3981PhosphoserineBy similarity
Modified residuei405 – 4051PhosphoserineBy similarity
Modified residuei408 – 4081PhosphothreonineBy similarity
Modified residuei419 – 4191PhosphoserineBy similarity
Modified residuei421 – 4211PhosphoserineBy similarity
Modified residuei486 – 4861PhosphoserineBy similarity
Modified residuei510 – 5101PhosphoserineBy similarity
Modified residuei512 – 5121PhosphothreonineBy similarity
Modified residuei513 – 5131PhosphothreonineBy similarity
Modified residuei516 – 5161PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated during mitosis but not in interphase.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9QXU8.
PRIDEiQ9QXU8.

PTM databases

PhosphoSiteiQ9QXU8.
SwissPalmiQ9QXU8.

Interactioni

Subunit structurei

Homodimer (Probable). 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.Curated3 Publications

Protein-protein interaction databases

BioGridi251663. 1 interaction.
IntActiQ9QXU8. 1 interaction.
MINTiMINT-4619296.
STRINGi10116.ENSRNOP00000014532.

Structurei

3D structure databases

ProteinModelPortaliQ9QXU8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3905. Eukaryota.
ENOG410XQS4. LUCA.
HOGENOMiHOG000236263.
HOVERGENiHBG005546.
InParanoidiQ9QXU8.
KOiK10416.
PhylomeDBiQ9QXU8.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR022780. Dynein_light_int_chain.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF05783. DLIC. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.

Sequencei

Sequence statusi: Complete.

Q9QXU8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVGRVGSF GSSPPGLAST YASGPLANEL ASGSGGPAAG DDEDGQNLWS
60 70 80 90 100
RILREVSTRS 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 RATAAQEDRD DSVVLPLGAD TLTHNLGLPV LVVCTKCDAI
260 270 280 290 300
SVLEKEHDYR DEHFDFIQSH IRKFCLQYGA ALIYTSVKEN KNIDLVYKYI
310 320 330 340 350
VQKLYGFPYK IPAVVVEKDA VFIPAGWDND KKIGILHENF QTLKIEDNFE
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 GAAGASTSLP PSAKKSGQKP VLSDVHAELD
510 520
RITRKPASVS PTTPPSPTEG EAS
Length:523
Mass (Da):56,792
Last modified:May 1, 2000 - v1
Checksum:i3F393348FF90696B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF181992 mRNA. Translation: AAF22294.1.
RefSeqiNP_665715.1. NM_145772.1.
UniGeneiRn.228621.

Genome annotation databases

GeneIDi252902.
KEGGirno:252902.
UCSCiRGD:71072. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF181992 mRNA. Translation: AAF22294.1.
RefSeqiNP_665715.1. NM_145772.1.
UniGeneiRn.228621.

3D structure databases

ProteinModelPortaliQ9QXU8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi251663. 1 interaction.
IntActiQ9QXU8. 1 interaction.
MINTiMINT-4619296.
STRINGi10116.ENSRNOP00000014532.

PTM databases

PhosphoSiteiQ9QXU8.
SwissPalmiQ9QXU8.

Proteomic databases

PaxDbiQ9QXU8.
PRIDEiQ9QXU8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi252902.
KEGGirno:252902.
UCSCiRGD:71072. rat.

Organism-specific databases

CTDi51143.
RGDi71072. Dync1li1.

Phylogenomic databases

eggNOGiKOG3905. Eukaryota.
ENOG410XQS4. LUCA.
HOGENOMiHOG000236263.
HOVERGENiHBG005546.
InParanoidiQ9QXU8.
KOiK10416.
PhylomeDBiQ9QXU8.

Miscellaneous databases

NextBioi624037.
PROiQ9QXU8.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR022780. Dynein_light_int_chain.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF05783. DLIC. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Light intermediate chain 1 defines a functional subfraction of cytoplasmic dynein which binds to pericentrin."
    Tynan S.H., Purohit A., Doxsey S.J., Vallee R.B.
    J. Biol. Chem. 275:32763-32768(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, INTERACTION WITH PCNT.
  2. "Direct interaction of pericentrin with cytoplasmic dynein light intermediate chain contributes to mitotic spindle organization."
    Purohit A., Tynan S.H., Vallee R., Doxsey S.J.
    J. Cell Biol. 147:481-492(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PCNT.
  3. "Distinct but overlapping sites within the cytoplasmic dynein heavy chain for dimerization and for intermediate chain and light intermediate chain binding."
    Tynan S.H., Gee M.A., Vallee R.B.
    J. Biol. Chem. 275:32769-32774(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DYNC1H1.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDC1L1_RAT
AccessioniPrimary (citable) accession number: Q9QXU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: May 1, 2000
Last modified: April 13, 2016
This is version 94 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.