O43237 (DC1L2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cytoplasmic dynein 1 light intermediate chain 2

Alternative name(s):
Dynein light intermediate chain 2, cytosolic
Short name=LIC-2
LIC53/55

Gene names

Name:	DYNC1LI2
Synonyms:	DNCLI2, LIC2

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	492 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.
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 By similarity.
Subcellular location	Cytoplasm › cytoskeleton By similarity.
Sequence similarities	Belongs to the dynein light intermediate chain family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cytoplasm Cytoskeleton Dynein Microtubule
Ligand	ATP-binding Nucleotide-binding
Molecular function	Motor protein
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	antigen processing and presentation of exogenous peptide antigen via MHC class II Traceable author statement. Source: Reactome centrosome localization Inferred from electronic annotation. Source: Compara microtubule cytoskeleton organization Inferred from electronic annotation. Source: Compara transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	centrosome Inferred from direct assay PubMed 21399614. Source: UniProtKB cytoplasmic dynein complex Traceable author statement PubMed 7738094. Source: ProtInc cytosol Traceable author statement. Source: Reactome microtubule Inferred from electronic annotation. Source: UniProtKB-KW
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 – 492	492	Cytoplasmic dynein 1 light intermediate chain 2		PRO_0000114670
Regions
	Nucleotide binding	61 – 68	8	ATP Potential
Amino acid modifications
	Modified residue	194	1	Phosphoserine Ref.5 Ref.7 Ref.8 Ref.9 Ref.11
	Modified residue	383	1	Phosphoserine Ref.8
	Modified residue	391	1	Phosphoserine Ref.9
	Modified residue	441	1	Phosphothreonine Ref.9
	Modified residue	443	1	Phosphoserine Ref.8 Ref.9
	Modified residue	446	1	Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9
Experimental info
	Sequence conflict	458	1	K → N in AAH25959. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	O43237 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: AF7B4E49E3983DCC	FASTA	492	54,099
	10 20 30 40 50 60 MAPVGVEKKL LLGPNGPAVA AAGDLTSEEE EGQSLWSSIL SEVSTRARSK LPSGKNILVF 70 80 90 100 110 120 GEDGSGKTTL MTKLQGAEHG KKGRGLEYLY LSVHDEDRDD HTRCNVWILD GDLYHKGLLK 130 140 150 160 170 180 FAVSAESLPE TLVIFVADMS RPWTVMESLQ KWASVLREHI DKMKIPPEKM RELERKFVKD 190 200 210 220 230 240 FQDYMEPEEG CQGSPQRRGP LTSGSDEENV ALPLGDNVLT HNLGIPVLVV CTKCDAVSVL 250 260 270 280 290 300 EKEHDYRDEH LDFIQSHLRR FCLQYGAALI YTSVKEEKNL DLLYKYIVHK TYGFHFTTPA 310 320 330 340 350 360 LVVEKDAVFI PAGWDNEKKI AILHENFTTV KPEDAYEDFI VKPPVRKLVH DKELAAEDEQ 370 380 390 400 410 420 VFLMKQQSLL AKQPATPTRA SESPARGPSG SPRTQGRGGP ASVPSSSPGT SVKKPDPNIK 430 440 450 460 470 480 NNAASEGVLA SFFNSLLSKK TGSPGSPGAG GVQSTAKKSG QKTVLSNVQE ELDRMTRKPD 490 SMVTNSSTEN EA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Zha D., Hu G. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[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]. Tissue: Uterus.
[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-194, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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-194 AND SER-446, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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-194; SER-383; SER-443 AND SER-446, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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-194; SER-391; THR-441; SER-443 AND SER-446, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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].
[11]	"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-194, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF035812 mRNA. Translation: AAB88513.1. AK291766 mRNA. Translation: BAF84455.1. CH471092 Genomic DNA. Translation: EAW83039.1. BC025959 mRNA. Translation: AAH25959.1.
IPI	IPI00011592.
RefSeq	NP_006132.1. NM_006141.2.
UniGene	Hs.369068.
3D structure databases
ProteinModelPortal	O43237.
ModBase	Search...
Protein-protein interaction databases
IntAct	O43237. 7 interactions.
STRING	9606.ENSP00000258198.
PTM databases
PhosphoSite	O43237.
Proteomic databases
PaxDb	O43237.
PeptideAtlas	O43237.
PRIDE	O43237.
Protocols and materials databases
DNASU	1783.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000258198; ENSP00000258198; ENSG00000135720.
GeneID	1783.
KEGG	hsa:1783.
UCSC	uc002eqb.1. human.
Organism-specific databases
CTD	1783.
GeneCards	GC16M066754.
HGNC	HGNC:2966. DYNC1LI2.
MIM	611406. gene.
neXtProt	NX_O43237.
PharmGKB	PA27438.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG265404.
HOGENOM	HOG000236263.
HOVERGEN	HBG005546.
InParanoid	O43237.
KO	K10416.
OMA	LNIHDED.
OrthoDB	EOG4PNXGQ.
PhylomeDB	O43237.
Enzyme and pathway databases
Reactome	REACT_6900. Immune System.
Gene expression databases
ArrayExpress	O43237.
Bgee	O43237.
CleanEx	HS_DYNC1LI2.
Genevestigator	O43237.
GermOnline	ENSG00000135720. Homo sapiens.
Family and domain databases
InterPro	IPR008467. Dynein1_light_intermed_chain. IPR022780. Dynein_light_int_chain. [Graphical view]
PANTHER	PTHR12688. PTHR12688. 1 hit.
Pfam	PF05783. DLIC. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	DYNC1LI2. human.
GenomeRNAi	1783.
NextBio	7251.
SOURCE	Search...

Entry information

Entry name

DC1L2_HUMAN

Accession

Primary (citable) accession number: O43237
Secondary accession number(s): A8K6V1, Q8TAT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	June 1, 1998
Last modified:	May 1, 2013
This is version 103 of the entry and version 1 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.