SubmitCancel

Skip Header

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

Q9Y6G9

- DC1L1_HUMAN

UniProt

Q9Y6G9 - DC1L1_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Cytoplasmic dynein 1 light intermediate chain 1
Gene
DYNC1LI1, DNCLI1
Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi74 – 818ATP Reviewed prediction

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
Complete GO annotation...

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
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. 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. microtubule Source: UniProtKB-KW
  7. plasma membrane Source: HPA
  8. spindle pole Source: UniProtKB
Complete GO annotation...

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 1
PRO_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.1 Publication

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.2 Publications

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ9Y6G9.

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

« Hide

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

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 conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 113 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

Similar proteinsi