Q9Y6G9 (DC1L1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	DYNC1LI1
Synonyms:	DNCLI1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	523 AA.
Sequence status	Complete.
Protein existence	Evidence 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.11
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.11 Ref.12
Subcellular location	Cytoplasm By similarity. Chromosome › centromere › kinetochore. Cytoplasm › cytoskeleton › spindle pole Ref.11.
Post-translational modification	Phosphorylated during mitosis but not in interphase. Ref.11
Sequence similarities	Belongs to the dynein light intermediate chain family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Host-virus interaction Mitosis Transport
Cellular component	Centromere Chromosome Cytoplasm Cytoskeleton Dynein Kinetochore Microtubule
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Motor protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of mitotic cell cycle spindle assembly checkpoint Inferred from mutant phenotype Ref.11. Source: UniProtKB transport Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	centrosome Inferred from direct assay PubMed 21399614. Source: UniProtKB condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell cytoplasmic dynein complex Inferred from direct assay Ref.11. Source: UniProtKB kinetochore Inferred from direct assay Ref.11. 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.11. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW motor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 523	523	Cytoplasmic dynein 1 light intermediate chain 1		PRO_0000114666
Regions
	Nucleotide binding	74 – 81	8	ATP Potential
Amino acid modifications
	Modified residue	207	1	Phosphoserine Ref.5 Ref.8 Ref.9 Ref.10 Ref.11 Ref.14 Ref.15 Ref.17
	Modified residue	213	1	Phosphothreonine Ref.10
	Modified residue	398	1	Phosphoserine Ref.9 Ref.11 Ref.15
	Modified residue	405	1	Phosphoserine Ref.11
	Modified residue	408	1	Phosphothreonine Ref.11
	Modified residue	412	1	Phosphoserine By similarity
	Modified residue	414	1	Phosphoserine By similarity
	Modified residue	419	1	Phosphoserine Ref.10 Ref.15
	Modified residue	421	1	Phosphoserine Ref.10 Ref.15
	Modified residue	450	1	Phosphoserine By similarity
	Modified residue	487	1	Phosphoserine Ref.9 Ref.15
	Modified residue	510	1	Phosphoserine Ref.10 Ref.14
	Modified residue	512	1	Phosphothreonine Ref.10 Ref.14
	Modified residue	513	1	Phosphothreonine Ref.10 Ref.14
	Modified residue	515	1	Phosphothreonine Ref.10 Ref.14
	Modified residue	516	1	Phosphoserine Ref.10 Ref.14 Ref.15 Ref.17
	Modified residue	518	1	Phosphothreonine By similarity
Natural variations
	Natural variant	147	1	M → T. Corresponds to variant rs34181332 [ dbSNP | Ensembl ].		VAR_061141
	Natural variant	277	1	Q → R. Ref.1 Ref.2 Corresponds to variant rs2303857 [ dbSNP | Ensembl ].		VAR_023325
Experimental info
	Sequence conflict	186	1	M → I in BAD96293. Ref.2
	Sequence conflict	210	1	R → G in BAD96293. Ref.2
	Sequence conflict	225	1	L → V in AAD44481. Ref.1
	Sequence conflict	267	1	I → F in AAD44481. Ref.1
	Sequence conflict	351	1	D → G in BAD96293. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9Y6G9 [UniParc]. Last modified March 20, 2007. Version 3. Checksum: 29159F560E382095	FASTA	523	56,579
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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.
[12]	"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.
[13]	"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].
[14]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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].
[17]	"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, MASS SPECTROMETRY.
+	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.
IPI	IPI00007675.
RefSeq	NP_057225.2. NM_016141.3.
UniGene	Hs.529495.
3D structure databases
ProteinModelPortal	Q9Y6G9.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y6G9. 9 interactions.
STRING	9606.ENSP00000273130.
PTM databases
PhosphoSite	Q9Y6G9.
Polymorphism databases
DMDM	134047749.
Proteomic databases
PaxDb	Q9Y6G9.
PRIDE	Q9Y6G9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000273130; ENSP00000273130; ENSG00000144635.
GeneID	51143.
KEGG	hsa:51143.
UCSC	uc003cfb.4. human.
Organism-specific databases
CTD	51143.
GeneCards	GC03M032543.
HGNC	HGNC:18745. DYNC1LI1.
HPA	HPA035013.
neXtProt	NX_Q9Y6G9.
PharmGKB	PA38670.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG265404.
HOGENOM	HOG000236263.
HOVERGEN	HBG005546.
InParanoid	Q9Y6G9.
KO	K10416.
OMA	RISRKPE.
OrthoDB	EOG4W3SN1.
PhylomeDB	Q9Y6G9.
Gene expression databases
ArrayExpress	Q9Y6G9.
Bgee	Q9Y6G9.
CleanEx	HS_DYNC1LI1.
Genevestigator	Q9Y6G9.
GermOnline	ENSG00000144635. Homo sapiens.
Family and domain databases
InterPro	IPR008467. Dynein1_light_intermed_chain. IPR022780. Dynein_light_int_chain. IPR027417. P-loop_NTPase. [Graphical view]
PANTHER	PTHR12688. PTHR12688. 1 hit.
Pfam	PF05783. DLIC. 1 hit. [Graphical view]
SUPFAM	SSF52540. SSF52540. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	DYNC1LI1. human.
GenomeRNAi	51143.
NextBio	54004.

Entry information

Entry name

DC1L1_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 102 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.