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Protein

Cytoplasmic dynein 1 light intermediate chain 2

Gene

DYNC1LI2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi61 – 688ATPSequence Analysis

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Biological processi

Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.

Names & Taxonomyi

Protein namesi
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 namesi
Name:DYNC1LI2
Synonyms:DNCLI2, LIC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:2966. DYNC1LI2.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: UniProtKB
  • cytoplasmic dynein complex Source: ProtInc
  • cytosol Source: Reactome
  • membrane Source: UniProtKB
  • microtubule Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Dynein, Microtubule

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA27438.

Polymorphism and mutation databases

BioMutaiDYNC1LI2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492Cytoplasmic dynein 1 light intermediate chain 2PRO_0000114670Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941Phosphoserine5 Publications
Modified residuei383 – 3831Phosphoserine1 Publication
Modified residuei391 – 3911Phosphoserine1 Publication
Modified residuei394 – 3941PhosphothreonineBy similarity
Modified residuei405 – 4051PhosphoserineBy similarity
Modified residuei407 – 4071PhosphoserineBy similarity
Modified residuei441 – 4411Phosphothreonine1 Publication
Modified residuei443 – 4431Phosphoserine2 Publications
Modified residuei446 – 4461Phosphoserine4 Publications
Modified residuei459 – 4591PhosphoserineBy similarity
Modified residuei486 – 4861PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO43237.
PaxDbiO43237.
PeptideAtlasiO43237.
PRIDEiO43237.

PTM databases

PhosphoSiteiO43237.

Expressioni

Gene expression databases

BgeeiO43237.
CleanExiHS_DYNC1LI2.
ExpressionAtlasiO43237. baseline and differential.
GenevisibleiO43237. HS.

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi108120. 27 interactions.
IntActiO43237. 9 interactions.
MINTiMINT-2999261.
STRINGi9606.ENSP00000258198.

Structurei

3D structure databases

ProteinModelPortaliO43237.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG265404.
GeneTreeiENSGT00390000008295.
HOGENOMiHOG000236263.
HOVERGENiHBG005546.
InParanoidiO43237.
KOiK10416.
OMAiKKPDPNM.
OrthoDBiEOG7V7668.
PhylomeDBiO43237.
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.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O43237-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAPVGVEKKL LLGPNGPAVA AAGDLTSEEE EGQSLWSSIL SEVSTRARSK
60 70 80 90 100
LPSGKNILVF GEDGSGKTTL MTKLQGAEHG KKGRGLEYLY LSVHDEDRDD
110 120 130 140 150
HTRCNVWILD GDLYHKGLLK FAVSAESLPE TLVIFVADMS RPWTVMESLQ
160 170 180 190 200
KWASVLREHI DKMKIPPEKM RELERKFVKD FQDYMEPEEG CQGSPQRRGP
210 220 230 240 250
LTSGSDEENV ALPLGDNVLT HNLGIPVLVV CTKCDAVSVL EKEHDYRDEH
260 270 280 290 300
LDFIQSHLRR FCLQYGAALI YTSVKEEKNL DLLYKYIVHK TYGFHFTTPA
310 320 330 340 350
LVVEKDAVFI PAGWDNEKKI AILHENFTTV KPEDAYEDFI VKPPVRKLVH
360 370 380 390 400
DKELAAEDEQ VFLMKQQSLL AKQPATPTRA SESPARGPSG SPRTQGRGGP
410 420 430 440 450
ASVPSSSPGT SVKKPDPNIK NNAASEGVLA SFFNSLLSKK TGSPGSPGAG
460 470 480 490
GVQSTAKKSG QKTVLSNVQE ELDRMTRKPD SMVTNSSTEN EA
Length:492
Mass (Da):54,099
Last modified:June 1, 1998 - v1
Checksum:iAF7B4E49E3983DCC
GO
Isoform 2 (identifier: O43237-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     100-177: DHTRCNVWIL...EKMRELERKF → V

Note: No experimental confirmation available.
Show »
Length:415
Mass (Da):45,005
Checksum:i758F32BAD4482709
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti458 – 4581K → N in AAH25959 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei100 – 17778DHTRC…LERKF → V in isoform 2. 1 PublicationVSP_054663Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF035812 mRNA. Translation: AAB88513.1.
AK291766 mRNA. Translation: BAF84455.1.
AK303031 mRNA. Translation: BAG64156.1.
AC018557 Genomic DNA. No translation available.
AC044802 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83039.1.
BC025959 mRNA. Translation: AAH25959.1.
CCDSiCCDS10818.1. [O43237-1]
CCDS67049.1. [O43237-2]
RefSeqiNP_001273086.1. NM_001286157.1. [O43237-2]
NP_006132.1. NM_006141.2. [O43237-1]
UniGeneiHs.369068.

Genome annotation databases

EnsembliENST00000258198; ENSP00000258198; ENSG00000135720.
ENST00000443351; ENSP00000394289; ENSG00000135720. [O43237-2]
GeneIDi1783.
KEGGihsa:1783.
UCSCiuc002eqb.1. human. [O43237-1]
uc010vis.1. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF035812 mRNA. Translation: AAB88513.1.
AK291766 mRNA. Translation: BAF84455.1.
AK303031 mRNA. Translation: BAG64156.1.
AC018557 Genomic DNA. No translation available.
AC044802 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83039.1.
BC025959 mRNA. Translation: AAH25959.1.
CCDSiCCDS10818.1. [O43237-1]
CCDS67049.1. [O43237-2]
RefSeqiNP_001273086.1. NM_001286157.1. [O43237-2]
NP_006132.1. NM_006141.2. [O43237-1]
UniGeneiHs.369068.

3D structure databases

ProteinModelPortaliO43237.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108120. 27 interactions.
IntActiO43237. 9 interactions.
MINTiMINT-2999261.
STRINGi9606.ENSP00000258198.

PTM databases

PhosphoSiteiO43237.

Polymorphism and mutation databases

BioMutaiDYNC1LI2.

Proteomic databases

MaxQBiO43237.
PaxDbiO43237.
PeptideAtlasiO43237.
PRIDEiO43237.

Protocols and materials databases

DNASUi1783.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000258198; ENSP00000258198; ENSG00000135720.
ENST00000443351; ENSP00000394289; ENSG00000135720. [O43237-2]
GeneIDi1783.
KEGGihsa:1783.
UCSCiuc002eqb.1. human. [O43237-1]
uc010vis.1. human.

Organism-specific databases

CTDi1783.
GeneCardsiGC16M066754.
HGNCiHGNC:2966. DYNC1LI2.
MIMi611406. gene.
neXtProtiNX_O43237.
PharmGKBiPA27438.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG265404.
GeneTreeiENSGT00390000008295.
HOGENOMiHOG000236263.
HOVERGENiHBG005546.
InParanoidiO43237.
KOiK10416.
OMAiKKPDPNM.
OrthoDBiEOG7V7668.
PhylomeDBiO43237.
TreeFamiTF352602.

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.

Miscellaneous databases

ChiTaRSiDYNC1LI2. human.
GeneWikiiDYNC1LI2.
GenomeRNAii1783.
NextBioi35476533.
PROiO43237.
SOURCEiSearch...

Gene expression databases

BgeeiO43237.
CleanExiHS_DYNC1LI2.
ExpressionAtlasiO43237. baseline and differential.
GenevisibleiO43237. HS.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Zha D., Hu G.
    Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORMS 1 AND 2).
    Tissue: Placenta and Testis.
  3. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 1).
    Tissue: Uterus.
  6. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-383; SER-443 AND SER-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "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].
  11. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiDC1L2_HUMAN
AccessioniPrimary (citable) accession number: O43237
Secondary accession number(s): A8K6V1, B4DZP4, Q8TAT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 1, 1998
Last modified: July 22, 2015
This is version 122 of the entry and version 1 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 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.