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Q9Y6G9 (DC1L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytoplasmic dynein 1 light intermediate chain 1

Short name=LIC1
Alternative name(s):
Dynein light chain A
Short name=DLC-A
Dynein light intermediate chain 1, cytosolic
Gene names
Name:DYNC1LI1
Synonyms:DNCLI1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length523 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.12

Subunit structure

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. Interacts with human adenovirus 5 hexon protein; this interaction probably allows virus intracellular transport. Ref.12 Ref.13

Subcellular location

Cytoplasm By similarity. Chromosomecentromerekinetochore. Cytoplasmcytoskeletonspindle pole Ref.12.

Post-translational modification

Phosphorylated during mitosis but not in interphase. Ref.12

Sequence similarities

Belongs to the dynein light intermediate chain family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Host-virus interaction
Mitosis
Transport
   Cellular componentCentromere
Chromosome
Cytoplasm
Cytoskeleton
Dynein
Kinetochore
Microtubule
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionMotor protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processmicrotubule-based movement

Inferred from electronic annotation. Source: InterPro

mitotic nuclear division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of mitotic cell cycle spindle assembly checkpoint

Inferred from mutant phenotype Ref.12. Source: UniProtKB

transport

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcentrosome

Inferred from direct assay PubMed 21399614. Source: UniProtKB

condensed chromosome kinetochore

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay. Source: HPA

cytoplasmic dynein complex

Inferred from direct assay Ref.12. Source: UniProtKB

kinetochore

Inferred from direct assay Ref.12. Source: UniProtKB

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay. Source: HPA

spindle pole

Inferred from direct assay Ref.12. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule motor activity

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 523523Cytoplasmic dynein 1 light intermediate chain 1
PRO_0000114666

Regions

Nucleotide binding74 – 818ATP Potential

Amino acid modifications

Modified residue2071Phosphoserine Ref.5 Ref.8 Ref.9 Ref.10 Ref.12 Ref.15 Ref.16 Ref.18
Modified residue2131Phosphothreonine Ref.10
Modified residue3981Phosphoserine Ref.9 Ref.12 Ref.16
Modified residue4051Phosphoserine Ref.12
Modified residue4081Phosphothreonine Ref.12
Modified residue4191Phosphoserine Ref.10 Ref.16
Modified residue4211Phosphoserine Ref.10 Ref.16
Modified residue4871Phosphoserine Ref.9 Ref.16
Modified residue5101Phosphoserine Ref.10 Ref.15
Modified residue5121Phosphothreonine Ref.10 Ref.15
Modified residue5131Phosphothreonine Ref.10 Ref.15
Modified residue5151Phosphothreonine Ref.10 Ref.15
Modified residue5161Phosphoserine Ref.10 Ref.15 Ref.16 Ref.18

Natural variations

Natural variant1471M → T.
Corresponds to variant rs34181332 [ dbSNP | Ensembl ].
VAR_061141
Natural variant2771Q → R. Ref.1 Ref.2
Corresponds to variant rs2303857 [ dbSNP | Ensembl ].
VAR_023325

Experimental info

Sequence conflict1861M → I in BAD96293. Ref.2
Sequence conflict2101R → G in BAD96293. Ref.2
Sequence conflict2251L → V in AAD44481. Ref.1
Sequence conflict2671I → F in AAD44481. Ref.1
Sequence conflict3511D → G in BAD96293. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9Y6G9 [UniParc].

Last modified March 20, 2007. Version 3.
Checksum: 29159F560E382095

FASTA52356,579
        10         20         30         40         50         60 
MAAVGRVGSF GSSPPGLSST YTGGPLGNEI ASGNGGAAAG DDEDGQNLWS CILSEVSTRS 

        70         80         90        100        110        120 
RSKLPAGKNV LLLGEDGAGK TSLIRKIQGI EEYKKGRGLE YLYLNVHDED RDDQTRCNVW 

       130        140        150        160        170        180 
ILDGDLYHKG LLKFSLDAVS LKDTLVMLVV DMSKPWTALD SLQKWASVVR EHVDKLKIPP 

       190        200        210        220        230        240 
EEMKQMEQKL IRDFQEYVEP GEDFPASPQR RNTASQEDKD DSVVLPLGAD TLTHNLGIPV 

       250        260        270        280        290        300 
LVVCTKCDAI SVLEKEHDYR DEHFDFIQSH IRKFCLQYGA ALIYTSVKEN KNIDLVYKYI 

       310        320        330        340        350        360 
VQKLYGFPYK IPAVVVEKDA VFIPAGWDND KKIGILHENF QTLKAEDNFE DIITKPPVRK 

       370        380        390        400        410        420 
FVHEKEIMAE DDQVFLMKLQ SLLAKQPPTA AGRPVDASPR VPGGSPRTPN RSVSSNVASV 

       430        440        450        460        470        480 
SPIPAGSKKI DPNMKAGATS EGVLANFFNS LLSKKTGSPG GPGVSGGSPA GGAGGGSSGL 

       490        500        510        520 
PPSTKKSGQK PVLDVHAELD RITRKPVTVS PTTPTSPTEG EAS 

« Hide

References

« Hide 'large scale' references
[1]"Human dynein light chain-A mRNA, complete cds."
Dai M., Peng Y., Song H., Huang Q., Mao Y., Zhang Q., Mao M., Fu G., Luo M., Chen J., Hu R.
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-277.
Tissue: Pituitary.
[2]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ARG-277.
Tissue: Cerebellum and Coronary artery.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
[5]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-398 AND SER-487, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; THR-213; SER-419; SER-421; SER-510; THR-512; THR-513; THR-515 AND SER-516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Dynein light intermediate chain 1 is required for progress through the spindle assembly checkpoint."
Sivaram M.V., Wadzinski T.L., Redick S.D., Manna T., Doxsey S.J.
EMBO J. 28:902-914(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN THE SPINDLE ASSEMBLY CHECKPOINT, SUBUNIT, PHOSPHORYLATION AT SER-207; SER-398; SER-405 AND THR-408, SUBCELLULAR LOCATION.
[13]"Adenovirus transport via direct interaction of cytoplasmic dynein with the viral capsid hexon subunit."
Bremner K.H., Scherer J., Yi J., Vershinin M., Gross S.P., Vallee R.B.
Cell Host Microbe 6:523-535(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN ADENOVIRUS HEXON PROTEIN.
[14]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-510; THR-512; THR-513; THR-515 AND SER-516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-398; SER-419; SER-421; SER-487 AND SER-516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-516, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF078849 mRNA. Translation: AAD44481.1.
AK222573 mRNA. Translation: BAD96293.1.
AK222653 mRNA. Translation: BAD96373.1.
CH471055 Genomic DNA. Translation: EAW64433.1.
BC131620 mRNA. Translation: AAI31621.1.
CCDSCCDS2654.1.
RefSeqNP_057225.2. NM_016141.3.
UniGeneHs.529495.

3D structure databases

ProteinModelPortalQ9Y6G9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119327. 30 interactions.
IntActQ9Y6G9. 11 interactions.
STRING9606.ENSP00000273130.

PTM databases

PhosphoSiteQ9Y6G9.

Polymorphism databases

DMDM134047749.

Proteomic databases

MaxQBQ9Y6G9.
PaxDbQ9Y6G9.
PRIDEQ9Y6G9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000273130; ENSP00000273130; ENSG00000144635.
GeneID51143.
KEGGhsa:51143.
UCSCuc003cfb.4. human.

Organism-specific databases

CTD51143.
GeneCardsGC03M032543.
HGNCHGNC:18745. DYNC1LI1.
HPAHPA035013.
neXtProtNX_Q9Y6G9.
PharmGKBPA38670.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG265404.
HOGENOMHOG000236263.
HOVERGENHBG005546.
InParanoidQ9Y6G9.
KOK10416.
OMAPNRSVTS.
OrthoDBEOG7V7668.
PhylomeDBQ9Y6G9.
TreeFamTF352602.

Gene expression databases

ArrayExpressQ9Y6G9.
BgeeQ9Y6G9.
CleanExHS_DYNC1LI1.
GenevestigatorQ9Y6G9.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR008467. Dynein1_light_intermed_chain.
IPR022780. Dynein_light_int_chain.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR12688. PTHR12688. 1 hit.
PfamPF05783. DLIC. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

ChiTaRSDYNC1LI1. human.
GeneWikiDYNC1LI1.
GenomeRNAi51143.
NextBio54004.
PROQ9Y6G9.

Entry information

Entry nameDC1L1_HUMAN
AccessionPrimary (citable) accession number: Q9Y6G9
Secondary accession number(s): A2RRG7, Q53HC8, Q53HK7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 20, 2007
Last modified: July 9, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM