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Protein

Dynein light chain 1, cytoplasmic

Gene

Dynll1

Organism
Mus musculus (Mouse)
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 changing or maintaining the spatial distribution of cytoskeletal structures (By similarity).By similarity
Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.By similarity
Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.By similarity
Regulates apoptotic activities of BCL2L11 by sequestering it to microtubules. Upon apoptotic stimuli the BCL2L11-DYNLL1 complex dissociates from cytoplasmic dynein and translocates to mitochondria and sequesters BCL2 thus neutralizing its antiapoptotic activity (By similarity).By similarity

GO - Molecular functioni

  1. enzyme inhibitor activity Source: MGI
  2. motor activity Source: UniProtKB-KW
  3. nitric-oxide synthase regulator activity Source: Ensembl
  4. protein C-terminus binding Source: MGI
  5. protein domain specific binding Source: MGI

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. microtubule-based movement Source: MGI
  3. negative regulation of catalytic activity Source: GOC
  4. negative regulation of nitric oxide biosynthetic process Source: MGI
  5. negative regulation of phosphorylation Source: MGI
  6. regulation of transcription, DNA-templated Source: UniProtKB-KW
  7. substantia nigra development Source: Ensembl
  8. transcription, DNA-templated Source: UniProtKB-KW
  9. transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Motor protein

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation, Transport

Enzyme and pathway databases

ReactomeiREACT_196550. MHC class II antigen presentation.
REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_243078. Loss of Nlp from mitotic centrosomes.
REACT_244487. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_245720. Recruitment of mitotic centrosome proteins and complexes.

Names & Taxonomyi

Protein namesi
Recommended name:
Dynein light chain 1, cytoplasmic
Alternative name(s):
8 kDa dynein light chain
Short name:
DLC8
Dynein light chain LC8-type 1
Protein inhibitor of neuronal nitric oxide synthase
Short name:
PIN
Short name:
mPIN
Gene namesi
Name:Dynll1
Synonyms:Dlc1, Dncl1, Dnclc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1861457. Dynll1.

Subcellular locationi

Cytoplasmcytoskeleton By similarity. Nucleus By similarity. Mitochondrion By similarity

GO - Cellular componenti

  1. centrosome Source: MGI
  2. COP9 signalosome Source: Ensembl
  3. cytoplasm Source: MGI
  4. cytoplasmic dynein complex Source: UniProtKB
  5. cytoskeleton Source: MGI
  6. cytosol Source: MGI
  7. extracellular vesicular exosome Source: MGI
  8. kinetochore Source: UniProtKB
  9. membrane Source: MGI
  10. microtubule Source: UniProtKB-KW
  11. mitochondrion Source: UniProtKB-SubCell
  12. mitotic spindle Source: UniProtKB
  13. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Dynein, Microtubule, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8989Dynein light chain 1, cytoplasmicPRO_0000195127Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361N6-acetyllysine1 Publication
Modified residuei88 – 881PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation at Ser-88 appears to control the dimer-monomer transition.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP63168.
PaxDbiP63168.
PRIDEiP63168.

PTM databases

PhosphoSiteiP63168.

Expressioni

Gene expression databases

BgeeiP63168.
CleanExiMM_DLC1.
MM_DYNLL1.
GenevestigatoriP63168.

Interactioni

Subunit structurei

Homodimer. Monomer; the monomeric form is incapable of binding to target proteins. 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. Interacts with TXNDC17. Interacts with WWC1 and ESR1. The interaction with WWC1 is mandatory for the recruitment and transactivation functions of ESR1 or DYNLL1 to the target chromatin. Interacts with BCL2L11. Interacts with BCL2; the interaction is greatly enhanced in the nucleus and in mitochondria upon induction of apoptosis. Interacts with PAK1; the interaction requires dimeric DYNLL1 (By similarity). Interacts with MYZAP (By similarity). Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGOL2 (By similarity). Interacts with ATMIN; this interaction inhibits ATMIN transcriptional activity and hence may play a role in a feedback loop whereby DYNLL1 inhibits transactivation of its own promoter by ATMIN. Interacts with NEK9 (not phosphorylated at 'Ser-944') (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
DazlQ6436812EBI-349121,EBI-2024439
Dync1i1O884852EBI-349121,EBI-492834
PAX6P263673EBI-349121,EBI-747278From a different organism.

Protein-protein interaction databases

BioGridi207994. 73 interactions.
IntActiP63168. 74 interactions.
MINTiMINT-1858885.

Structurei

3D structure databases

ProteinModelPortaliP63168.
SMRiP63168. Positions 5-89.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni67 – 8923Interaction with ESR1By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the dynein light chain family.Curated

Phylogenomic databases

eggNOGiNOG312371.
GeneTreeiENSGT00390000000378.
HOVERGENiHBG002133.
InParanoidiP63168.
KOiK10418.
OMAiHNVEKDV.
OrthoDBiEOG7BZVVQ.
PhylomeDBiP63168.
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]
PROSITEiPS01239. DYNEIN_LIGHT_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P63168-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDRKAVIKN ADMSEEMQQD SVECATQALE KYNIEKDIAA HIKKEFDKKY
60 70 80
NPTWHCIVGR NFGSYVTHET KHFIYFYLGQ VAILLFKSG
Length:89
Mass (Da):10,366
Last modified:September 27, 2004 - v1
Checksum:iF5E7647D092BEB3A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF020185 mRNA. Translation: AAD01643.1.
AK002522 mRNA. Translation: BAB22160.1.
AK010614 mRNA. Translation: BAB27063.1.
AK010685 mRNA. Translation: BAB27117.1.
AK013721 mRNA. Translation: BAB28970.1.
AK082923 mRNA. Translation: BAC38691.1.
AK147977 mRNA. Translation: BAE28262.1.
BC008106 mRNA. Translation: AAH08106.1.
BC034258 mRNA. Translation: AAH34258.1.
CCDSiCCDS39227.1.
RefSeqiNP_062656.3. NM_019682.4.
UniGeneiMm.256858.

Genome annotation databases

EnsembliENSMUST00000009157; ENSMUSP00000009157; ENSMUSG00000009013.
ENSMUST00000112090; ENSMUSP00000107720; ENSMUSG00000009013.
GeneIDi56455.
KEGGimmu:56455.
UCSCiuc008zdp.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF020185 mRNA. Translation: AAD01643.1.
AK002522 mRNA. Translation: BAB22160.1.
AK010614 mRNA. Translation: BAB27063.1.
AK010685 mRNA. Translation: BAB27117.1.
AK013721 mRNA. Translation: BAB28970.1.
AK082923 mRNA. Translation: BAC38691.1.
AK147977 mRNA. Translation: BAE28262.1.
BC008106 mRNA. Translation: AAH08106.1.
BC034258 mRNA. Translation: AAH34258.1.
CCDSiCCDS39227.1.
RefSeqiNP_062656.3. NM_019682.4.
UniGeneiMm.256858.

3D structure databases

ProteinModelPortaliP63168.
SMRiP63168. Positions 5-89.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207994. 73 interactions.
IntActiP63168. 74 interactions.
MINTiMINT-1858885.

PTM databases

PhosphoSiteiP63168.

Proteomic databases

MaxQBiP63168.
PaxDbiP63168.
PRIDEiP63168.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000009157; ENSMUSP00000009157; ENSMUSG00000009013.
ENSMUST00000112090; ENSMUSP00000107720; ENSMUSG00000009013.
GeneIDi56455.
KEGGimmu:56455.
UCSCiuc008zdp.2. mouse.

Organism-specific databases

CTDi8655.
MGIiMGI:1861457. Dynll1.

Phylogenomic databases

eggNOGiNOG312371.
GeneTreeiENSGT00390000000378.
HOVERGENiHBG002133.
InParanoidiP63168.
KOiK10418.
OMAiHNVEKDV.
OrthoDBiEOG7BZVVQ.
PhylomeDBiP63168.
TreeFamiTF300264.

Enzyme and pathway databases

ReactomeiREACT_196550. MHC class II antigen presentation.
REACT_196635. Regulation of PLK1 Activity at G2/M Transition.
REACT_243078. Loss of Nlp from mitotic centrosomes.
REACT_244487. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_245720. Recruitment of mitotic centrosome proteins and complexes.

Miscellaneous databases

NextBioi312686.
PROiP63168.
SOURCEiSearch...

Gene expression databases

BgeeiP63168.
CleanExiMM_DLC1.
MM_DYNLL1.
GenevestigatoriP63168.

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]
PROSITEiPS01239. DYNEIN_LIGHT_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Intra-renal localization of mPIN (Protein Inhibitor of Nitric oxide synthase)."
    Mount D.B.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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: Hippocampus and Kidney.
  3. "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.
  4. "Identification of a novel Bcl-2-interacting mediator of cell death (Bim) E3 ligase, tripartite motif-containing protein 2 (TRIM2), and its role in rapid ischemic tolerance-induced neuroprotection."
    Thompson S., Pearson A.N., Ashley M.D., Jessick V., Murphy B.M., Gafken P., Henshall D.C., Morris K.T., Simon R.P., Meller R.
    J. Biol. Chem. 286:19331-19339(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BCL2L11.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiDYL1_MOUSE
AccessioniPrimary (citable) accession number: P63168
Secondary accession number(s): Q15701, Q3UGE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: March 4, 2015
This is version 108 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

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

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.