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Q9Y6G9

- DC1L1_HUMAN

UniProt

Q9Y6G9 - DC1L1_HUMAN

Protein

Cytoplasmic dynein 1 light intermediate chain 1

Gene

DYNC1LI1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 3 (20 Mar 2007)
      Previous versions | rss
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    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.1 Publication

    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: InterPro
    3. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. microtubule-based movement Source: InterPro
    2. mitotic nuclear division Source: UniProtKB-KW
    3. positive regulation of mitotic cell cycle spindle assembly checkpoint Source: UniProtKB
    4. transport Source: UniProtKB-KW
    5. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Motor protein

    Keywords - Biological processi

    Cell cycle, Cell division, Host-virus interaction, Mitosis, Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:DYNC1LI1
    Synonyms:DNCLI1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:18745. DYNC1LI1.

    Subcellular locationi

    Cytoplasm By similarity. Chromosomecentromerekinetochore 1 Publication. Cytoplasmcytoskeletonspindle pole 1 Publication

    GO - Cellular componenti

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

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38670.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 523523Cytoplasmic dynein 1 light intermediate chain 1PRO_0000114666Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei207 – 2071Phosphoserine8 Publications
    Modified residuei213 – 2131Phosphothreonine1 Publication
    Modified residuei398 – 3981Phosphoserine3 Publications
    Modified residuei405 – 4051Phosphoserine1 Publication
    Modified residuei408 – 4081Phosphothreonine1 Publication
    Modified residuei419 – 4191Phosphoserine2 Publications
    Modified residuei421 – 4211Phosphoserine2 Publications
    Modified residuei487 – 4871Phosphoserine2 Publications
    Modified residuei510 – 5101Phosphoserine2 Publications
    Modified residuei512 – 5121Phosphothreonine2 Publications
    Modified residuei513 – 5131Phosphothreonine2 Publications
    Modified residuei515 – 5151Phosphothreonine2 Publications
    Modified residuei516 – 5161Phosphoserine4 Publications

    Post-translational modificationi

    Phosphorylated during mitosis but not in interphase.8 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y6G9.
    PaxDbiQ9Y6G9.
    PRIDEiQ9Y6G9.

    PTM databases

    PhosphoSiteiQ9Y6G9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y6G9.
    BgeeiQ9Y6G9.
    CleanExiHS_DYNC1LI1.
    GenevestigatoriQ9Y6G9.

    Organism-specific databases

    HPAiHPA035013.

    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. Interacts with human adenovirus 5 hexon protein; this interaction probably allows virus intracellular transport.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi119327. 30 interactions.
    IntActiQ9Y6G9. 11 interactions.
    STRINGi9606.ENSP00000273130.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y6G9.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG265404.
    HOGENOMiHOG000236263.
    HOVERGENiHBG005546.
    InParanoidiQ9Y6G9.
    KOiK10416.
    OMAiPNRSVTS.
    OrthoDBiEOG7V7668.
    PhylomeDBiQ9Y6G9.
    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.

    Q9Y6G9-1 [UniParc]FASTAAdd to Basket

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    MAAVGRVGSF GSSPPGLSST YTGGPLGNEI ASGNGGAAAG DDEDGQNLWS    50
    CILSEVSTRS RSKLPAGKNV LLLGEDGAGK TSLIRKIQGI EEYKKGRGLE 100
    YLYLNVHDED RDDQTRCNVW ILDGDLYHKG LLKFSLDAVS LKDTLVMLVV 150
    DMSKPWTALD SLQKWASVVR EHVDKLKIPP EEMKQMEQKL IRDFQEYVEP 200
    GEDFPASPQR RNTASQEDKD DSVVLPLGAD TLTHNLGIPV LVVCTKCDAI 250
    SVLEKEHDYR DEHFDFIQSH IRKFCLQYGA ALIYTSVKEN KNIDLVYKYI 300
    VQKLYGFPYK IPAVVVEKDA VFIPAGWDND KKIGILHENF QTLKAEDNFE 350
    DIITKPPVRK FVHEKEIMAE DDQVFLMKLQ SLLAKQPPTA AGRPVDASPR 400
    VPGGSPRTPN RSVSSNVASV SPIPAGSKKI DPNMKAGATS EGVLANFFNS 450
    LLSKKTGSPG GPGVSGGSPA GGAGGGSSGL PPSTKKSGQK PVLDVHAELD 500
    RITRKPVTVS PTTPTSPTEG EAS 523
    Length:523
    Mass (Da):56,579
    Last modified:March 20, 2007 - v3
    Checksum:i29159F560E382095
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti186 – 1861M → I in BAD96293. 1 PublicationCurated
    Sequence conflicti210 – 2101R → G in BAD96293. 1 PublicationCurated
    Sequence conflicti225 – 2251L → V in AAD44481. 1 PublicationCurated
    Sequence conflicti267 – 2671I → F in AAD44481. 1 PublicationCurated
    Sequence conflicti351 – 3511D → G in BAD96293. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti147 – 1471M → T.
    Corresponds to variant rs34181332 [ dbSNP | Ensembl ].
    VAR_061141
    Natural varianti277 – 2771Q → R.2 Publications
    Corresponds to variant rs2303857 [ dbSNP | Ensembl ].
    VAR_023325

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS2654.1.
    RefSeqiNP_057225.2. NM_016141.3.
    UniGeneiHs.529495.

    Genome annotation databases

    EnsembliENST00000273130; ENSP00000273130; ENSG00000144635.
    GeneIDi51143.
    KEGGihsa:51143.
    UCSCiuc003cfb.4. human.

    Polymorphism databases

    DMDMi134047749.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS2654.1.
    RefSeqi NP_057225.2. NM_016141.3.
    UniGenei Hs.529495.

    3D structure databases

    ProteinModelPortali Q9Y6G9.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119327. 30 interactions.
    IntActi Q9Y6G9. 11 interactions.
    STRINGi 9606.ENSP00000273130.

    PTM databases

    PhosphoSitei Q9Y6G9.

    Polymorphism databases

    DMDMi 134047749.

    Proteomic databases

    MaxQBi Q9Y6G9.
    PaxDbi Q9Y6G9.
    PRIDEi Q9Y6G9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000273130 ; ENSP00000273130 ; ENSG00000144635 .
    GeneIDi 51143.
    KEGGi hsa:51143.
    UCSCi uc003cfb.4. human.

    Organism-specific databases

    CTDi 51143.
    GeneCardsi GC03M032543.
    HGNCi HGNC:18745. DYNC1LI1.
    HPAi HPA035013.
    neXtProti NX_Q9Y6G9.
    PharmGKBi PA38670.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG265404.
    HOGENOMi HOG000236263.
    HOVERGENi HBG005546.
    InParanoidi Q9Y6G9.
    KOi K10416.
    OMAi PNRSVTS.
    OrthoDBi EOG7V7668.
    PhylomeDBi Q9Y6G9.
    TreeFami TF352602.

    Miscellaneous databases

    ChiTaRSi DYNC1LI1. human.
    GeneWikii DYNC1LI1.
    GenomeRNAii 51143.
    NextBioi 54004.
    PROi Q9Y6G9.

    Gene expression databases

    ArrayExpressi Q9Y6G9.
    Bgeei Q9Y6G9.
    CleanExi HS_DYNC1LI1.
    Genevestigatori Q9Y6G9.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR008467. Dynein1_light_intermed_chain.
    IPR022780. Dynein_light_int_chain.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR12688. PTHR12688. 1 hit.
    Pfami PF05783. DLIC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 2 hits.
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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. 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].

    Entry informationi

    Entry nameiDC1L1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y6G9
    Secondary accession number(s): A2RRG7, Q53HC8, Q53HK7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: March 20, 2007
    Last modified: October 1, 2014
    This is version 114 of the entry and version 3 of the sequence. [Complete history]
    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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3