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Protein

Dynein light chain 2, cytoplasmic

Gene

Dynll2

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 changing or maintaining the spatial distribution of cytoskeletal structures (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • intracellular transport Source: UniProtKB
  • microtubule-based process Source: InterPro
  • synaptic target recognition Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiR-MMU-139910. Activation of BMF and translocation to mitochondria.
R-MMU-1632852. Macroautophagy.
R-MMU-2132295. MHC class II antigen presentation.
R-MMU-5620924. Intraflagellar transport.
R-MMU-6807878. COPI-mediated anterograde transport.
R-MMU-6811436. COPI-independent Golgi-to-ER retrograde traffic.

Names & Taxonomyi

Protein namesi
Recommended name:
Dynein light chain 2, cytoplasmic
Alternative name(s):
8 kDa dynein light chain b
Short name:
DLC8
Short name:
DLC8b
Dynein light chain LC8-type 2
Gene namesi
Name:Dynll2
Synonyms:Dlc2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1915347. Dynll2.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: MGI
  • cytoplasm Source: UniProtKB-KW
  • dynein complex Source: UniProtKB
  • membrane Source: MGI
  • microtubule Source: UniProtKB-KW
  • myosin complex Source: UniProtKB
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Dynein, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8989Dynein light chain 2, cytoplasmicPRO_0000195133Add
BLAST

Proteomic databases

EPDiQ9D0M5.
MaxQBiQ9D0M5.
PaxDbiQ9D0M5.
PeptideAtlasiQ9D0M5.
PRIDEiQ9D0M5.
TopDownProteomicsiQ9D0M5.

2D gel databases

REPRODUCTION-2DPAGEQ9D0M5.

PTM databases

iPTMnetiQ9D0M5.
PhosphoSiteiQ9D0M5.

Expressioni

Gene expression databases

BgeeiQ9D0M5.
CleanExiMM_DYNLL2.
ExpressionAtlasiQ9D0M5. baseline and differential.
GenevisibleiQ9D0M5. MM.

Interactioni

Subunit structurei

Homodimer. The cytoplasmic dynein 1 complex consists of two catalytic heavy chains (HCs) and a number of non-catalytic subunits which present 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. Dynein ICs and LICs bind directly to the HC dimer and the LCs assemble on the IC dimer. Interacts with DYNC1I1. Interacts with BMF. Component of the myosin V motor complex.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei41 – 411Interaction with myosin V motor complex

Protein-protein interaction databases

BioGridi212654. 1 interaction.
IntActiQ9D0M5. 4 interactions.
MINTiMINT-1845877.
STRINGi10090.ENSMUSP00000020775.

Structurei

Secondary structure

1
89
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 113Combined sources
Helixi15 – 3117Combined sources
Helixi35 – 4915Combined sources
Beta strandi54 – 563Combined sources
Beta strandi58 – 603Combined sources
Beta strandi70 – 723Combined sources
Beta strandi82 – 876Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RE6NMR-A/B1-89[»]
ProteinModelPortaliQ9D0M5.
SMRiQ9D0M5. Positions 1-89.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9D0M5.

Family & Domainsi

Sequence similaritiesi

Belongs to the dynein light chain family.Curated

Phylogenomic databases

eggNOGiKOG3430. Eukaryota.
ENOG4111NK2. LUCA.
GeneTreeiENSGT00390000000378.
HOVERGENiHBG002133.
InParanoidiQ9D0M5.
KOiK10418.
OMAiQIKSADM.
OrthoDBiEOG7BZVVQ.
PhylomeDBiQ9D0M5.
TreeFamiTF300264.

Family and domain databases

Gene3Di3.30.740.10. 1 hit.
InterProiIPR019763. Dynein_light_1/2_CS.
IPR001372. Dynein_light_chain_typ-1/2.
[Graphical view]
PANTHERiPTHR11886. PTHR11886. 1 hit.
PfamiPF01221. Dynein_light. 1 hit.
[Graphical view]
SMARTiSM01375. Dynein_light. 1 hit.
[Graphical view]
PROSITEiPS01239. DYNEIN_LIGHT_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D0M5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDRKAVIKN ADMSEDMQQD AVDCATQAME KYNIEKDIAA YIKKEFDKKY
60 70 80
NPTWHCIVGR NFGSYVTHET KHFIYFYLGQ VAILLFKSG
Length:89
Mass (Da):10,350
Last modified:June 1, 2001 - v1
Checksum:i45364D32C0077F8E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY029255 mRNA. Translation: AAK38749.1.
AK011284 mRNA. Translation: BAB27516.1.
AK028319 mRNA. Translation: BAC25877.1.
AK049645 mRNA. Translation: BAC33856.1.
AK078434 mRNA. Translation: BAC37271.1.
AK160114 mRNA. Translation: BAE35638.1.
AK169212 mRNA. Translation: BAE40984.1.
AL606805 Genomic DNA. Translation: CAO91831.1.
BC011289 mRNA. Translation: AAH11289.1.
BC040822 mRNA. Translation: AAH40822.1.
CCDSiCCDS36272.1.
RefSeqiNP_001161943.1. NM_001168471.1.
NP_001161944.1. NM_001168472.1.
NP_080832.1. NM_026556.4.
UniGeneiMm.246436.

Genome annotation databases

EnsembliENSMUST00000020775; ENSMUSP00000020775; ENSMUSG00000020483.
ENSMUST00000107923; ENSMUSP00000103556; ENSMUSG00000020483.
ENSMUST00000178105; ENSMUSP00000136241; ENSMUSG00000020483.
GeneIDi68097.
KEGGimmu:68097.
UCSCiuc007kva.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY029255 mRNA. Translation: AAK38749.1.
AK011284 mRNA. Translation: BAB27516.1.
AK028319 mRNA. Translation: BAC25877.1.
AK049645 mRNA. Translation: BAC33856.1.
AK078434 mRNA. Translation: BAC37271.1.
AK160114 mRNA. Translation: BAE35638.1.
AK169212 mRNA. Translation: BAE40984.1.
AL606805 Genomic DNA. Translation: CAO91831.1.
BC011289 mRNA. Translation: AAH11289.1.
BC040822 mRNA. Translation: AAH40822.1.
CCDSiCCDS36272.1.
RefSeqiNP_001161943.1. NM_001168471.1.
NP_001161944.1. NM_001168472.1.
NP_080832.1. NM_026556.4.
UniGeneiMm.246436.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RE6NMR-A/B1-89[»]
ProteinModelPortaliQ9D0M5.
SMRiQ9D0M5. Positions 1-89.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212654. 1 interaction.
IntActiQ9D0M5. 4 interactions.
MINTiMINT-1845877.
STRINGi10090.ENSMUSP00000020775.

PTM databases

iPTMnetiQ9D0M5.
PhosphoSiteiQ9D0M5.

2D gel databases

REPRODUCTION-2DPAGEQ9D0M5.

Proteomic databases

EPDiQ9D0M5.
MaxQBiQ9D0M5.
PaxDbiQ9D0M5.
PeptideAtlasiQ9D0M5.
PRIDEiQ9D0M5.
TopDownProteomicsiQ9D0M5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020775; ENSMUSP00000020775; ENSMUSG00000020483.
ENSMUST00000107923; ENSMUSP00000103556; ENSMUSG00000020483.
ENSMUST00000178105; ENSMUSP00000136241; ENSMUSG00000020483.
GeneIDi68097.
KEGGimmu:68097.
UCSCiuc007kva.2. mouse.

Organism-specific databases

CTDi140735.
MGIiMGI:1915347. Dynll2.

Phylogenomic databases

eggNOGiKOG3430. Eukaryota.
ENOG4111NK2. LUCA.
GeneTreeiENSGT00390000000378.
HOVERGENiHBG002133.
InParanoidiQ9D0M5.
KOiK10418.
OMAiQIKSADM.
OrthoDBiEOG7BZVVQ.
PhylomeDBiQ9D0M5.
TreeFamiTF300264.

Enzyme and pathway databases

ReactomeiR-MMU-139910. Activation of BMF and translocation to mitochondria.
R-MMU-1632852. Macroautophagy.
R-MMU-2132295. MHC class II antigen presentation.
R-MMU-5620924. Intraflagellar transport.
R-MMU-6807878. COPI-mediated anterograde transport.
R-MMU-6811436. COPI-independent Golgi-to-ER retrograde traffic.

Miscellaneous databases

ChiTaRSiDynll2. mouse.
EvolutionaryTraceiQ9D0M5.
PROiQ9D0M5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D0M5.
CleanExiMM_DYNLL2.
ExpressionAtlasiQ9D0M5. baseline and differential.
GenevisibleiQ9D0M5. MM.

Family and domain databases

Gene3Di3.30.740.10. 1 hit.
InterProiIPR019763. Dynein_light_1/2_CS.
IPR001372. Dynein_light_chain_typ-1/2.
[Graphical view]
PANTHERiPTHR11886. PTHR11886. 1 hit.
PfamiPF01221. Dynein_light. 1 hit.
[Graphical view]
SMARTiSM01375. Dynein_light. 1 hit.
[Graphical view]
PROSITEiPS01239. DYNEIN_LIGHT_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis."
    Puthalakath H., Villunger A., O'Reilly L.A., Beaumont J.G., Coultas L., Cheney R.E., Huang D.C.S., Strasser A.
    Science 293:1829-1832(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH BMF, IDENTIFICATION IN THE CYTOPLASMIC DYNEIN 1 COMPLEX, IDENTIFICATION IN THE MYOSIN V COMPLEX.
    Strain: C57BL/6J.
  2. "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: Brain, Kidney and Spinal cord.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. "The 8-kDa dynein light chain binds to its targets via a conserved (K/R)XTQT motif."
    Lo K.W., Naisbitt S., Fan J.S., Sheng M., Zhang M.
    J. Biol. Chem. 276:14059-14066(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DYNC1I1.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney and Liver.
  7. "Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands."
    Day C.L., Puthalakath H., Skea G., Strasser A., Barsukov I., Lian L.Y., Huang D.C., Hinds M.G.
    Biochem. J. 377:597-605(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, SUBCELLULAR LOCATION, BINDING SITE.

Entry informationi

Entry nameiDYL2_MOUSE
AccessioniPrimary (citable) accession number: Q9D0M5
Secondary accession number(s): A7M7R8, Q3TFB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 21, 2004
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.