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Protein

Cytoplasmic dynein 1 light intermediate chain 2

Gene

Dync1li2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

Regions

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

GO - Molecular functioni

GO - Biological processi

  • centrosome localization Source: MGI
  • microtubule-based movement Source: InterPro
  • microtubule cytoskeleton organization Source: MGI
  • transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Biological processi

Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-2132295. MHC class II antigen presentation.
R-MMU-6807878. COPI-mediated anterograde transport.
R-MMU-6811436. COPI-independent Golgi-to-ER retrograde traffic.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytoplasmic dynein 1 light intermediate chain 2
Alternative name(s):
Dynein light intermediate chain 2, cytosolic
Gene namesi
Name:Dync1li2
Synonyms:Dncli2, Dnclic2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:107738. Dync1li2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Dynein, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492Cytoplasmic dynein 1 light intermediate chain 2PRO_0000114672Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei194 – 1941PhosphoserineCombined sources
Modified residuei383 – 3831PhosphoserineBy similarity
Modified residuei391 – 3911PhosphoserineBy similarity
Modified residuei394 – 3941PhosphothreonineBy similarity
Modified residuei405 – 4051PhosphoserineBy similarity
Modified residuei407 – 4071PhosphoserineBy similarity
Modified residuei441 – 4411PhosphothreonineBy similarity
Modified residuei443 – 4431PhosphoserineBy similarity
Modified residuei446 – 4461PhosphoserineCombined sources
Modified residuei459 – 4591PhosphoserineBy similarity
Modified residuei486 – 4861PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6PDL0.
MaxQBiQ6PDL0.
PaxDbiQ6PDL0.
PeptideAtlasiQ6PDL0.
PRIDEiQ6PDL0.

PTM databases

iPTMnetiQ6PDL0.
PhosphoSiteiQ6PDL0.

Expressioni

Gene expression databases

BgeeiQ6PDL0.
CleanExiMM_DYNC1LI2.
GenevisibleiQ6PDL0. MM.

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

BioGridi231551. 1 interaction.
STRINGi10090.ENSMUSP00000045480.

Structurei

3D structure databases

ProteinModelPortaliQ6PDL0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3905. Eukaryota.
ENOG410XQS4. LUCA.
GeneTreeiENSGT00390000008295.
HOGENOMiHOG000236263.
HOVERGENiHBG005546.
InParanoidiQ6PDL0.
KOiK10416.
OMAiKKPDPNM.
OrthoDBiEOG7V7668.
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.

Q6PDL0-1 [UniParc]FASTAAdd to basket

« 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 FAVSAESLRE TLVIFVADMS RPWTIMESLQ
160 170 180 190 200
KWASVLREHI DKMKIPPEEM RDLERKFMKE FQDYIEPEEG CQGSPQRRGP
210 220 230 240 250
LTSGSDEDSV ALPLGDNVLT HNLGIPVLVV CTKCDAMSVL EKEHDYRDEH
260 270 280 290 300
LDFIQAHLRR FCLQYGAALI YTSVKEEKNL DLLYKYIVHK TYGFHFTIPA
310 320 330 340 350
LVVEKDAVFI PAGWDNEKKI AILHENFTTV KPEDAYEDFI VKPPVRKLVH
360 370 380 390 400
DKELAAEDEQ VFLMKQQSLL AKQPATPTRT SESPARGPSG SPRTQGRGGP
410 420 430 440 450
ASVPSASPGT SVKKPDPNIK NNAASEGVLA SFFNSLLSKK TGSPGSPSAG
460 470 480 490
GVQSTAKKSG QKTVLSNVQE ELDRMTRKPD SMVTNSSTEN EA
Length:492
Mass (Da):54,218
Last modified:July 27, 2011 - v2
Checksum:i6418DF74FFD7175E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti353 – 3531E → K in AAH58645 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK140743 mRNA. Translation: BAE24463.1.
AK147899 mRNA. Translation: BAE28215.1.
AK152157 mRNA. Translation: BAE30992.1.
AK161434 mRNA. Translation: BAE36394.1.
BC058645 mRNA. Translation: AAH58645.1.
CCDSiCCDS22579.1.
RefSeqiNP_001013398.2. NM_001013380.2.
UniGeneiMm.289583.

Genome annotation databases

EnsembliENSMUST00000041769; ENSMUSP00000045480; ENSMUSG00000035770.
GeneIDi234663.
KEGGimmu:234663.
UCSCiuc009nao.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK140743 mRNA. Translation: BAE24463.1.
AK147899 mRNA. Translation: BAE28215.1.
AK152157 mRNA. Translation: BAE30992.1.
AK161434 mRNA. Translation: BAE36394.1.
BC058645 mRNA. Translation: AAH58645.1.
CCDSiCCDS22579.1.
RefSeqiNP_001013398.2. NM_001013380.2.
UniGeneiMm.289583.

3D structure databases

ProteinModelPortaliQ6PDL0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi231551. 1 interaction.
STRINGi10090.ENSMUSP00000045480.

PTM databases

iPTMnetiQ6PDL0.
PhosphoSiteiQ6PDL0.

Proteomic databases

EPDiQ6PDL0.
MaxQBiQ6PDL0.
PaxDbiQ6PDL0.
PeptideAtlasiQ6PDL0.
PRIDEiQ6PDL0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000041769; ENSMUSP00000045480; ENSMUSG00000035770.
GeneIDi234663.
KEGGimmu:234663.
UCSCiuc009nao.2. mouse.

Organism-specific databases

CTDi1783.
MGIiMGI:107738. Dync1li2.

Phylogenomic databases

eggNOGiKOG3905. Eukaryota.
ENOG410XQS4. LUCA.
GeneTreeiENSGT00390000008295.
HOGENOMiHOG000236263.
HOVERGENiHBG005546.
InParanoidiQ6PDL0.
KOiK10416.
OMAiKKPDPNM.
OrthoDBiEOG7V7668.
TreeFamiTF352602.

Enzyme and pathway databases

ReactomeiR-MMU-2132295. MHC class II antigen presentation.
R-MMU-6807878. COPI-mediated anterograde transport.
R-MMU-6811436. COPI-independent Golgi-to-ER retrograde traffic.

Miscellaneous databases

ChiTaRSiDync1li2. mouse.
PROiQ6PDL0.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PDL0.
CleanExiMM_DYNC1LI2.
GenevisibleiQ6PDL0. MM.

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

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow, Head and Testis.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Brain.
  3. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194 AND SER-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiDC1L2_MOUSE
AccessioniPrimary (citable) accession number: Q6PDL0
Secondary accession number(s): Q3UGJ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 103 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.