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P63168 (DYL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Dynll1
Synonyms:Dlc1, Dncl1, Dnclc1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length89 AA.
Sequence statusComplete.
Protein existenceEvidence 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 changing or maintaining the spatial distribution of cytoskeletal structures 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.

Subunit structure

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. Ref.4

Subcellular location

Cytoplasmcytoskeleton By similarity. Nucleus By similarity. Mitochondrion By similarity.

Post-translational modification

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

Sequence similarities

Belongs to the dynein light chain family.

Ontologies

Keywords
   Biological processApoptosis
Transcription
Transcription regulation
Transport
   Cellular componentCytoplasm
Cytoskeleton
Dynein
Microtubule
Mitochondrion
Nucleus
   Molecular functionActivator
Motor protein
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule-based movement

Traceable author statement PubMed 8702622. Source: MGI

negative regulation of phosphorylation

Inferred from electronic annotation. Source: Ensembl

regulation of catalytic activity

Inferred from electronic annotation. Source: GOC

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentCOP9 signalosome

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from electronic annotation. Source: Ensembl

cytoplasmic dynein complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 15136728. Source: MGI

kinetochore

Inferred from sequence or structural similarity. Source: UniProtKB

membrane

Inferred from direct assay PubMed 15136728. Source: MGI

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitotic spindle

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionmotor activity

Inferred from electronic annotation. Source: UniProtKB-KW

nitric-oxide synthase regulator activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DazlQ6436812EBI-349121,EBI-2024439
Dync1i1O884852EBI-349121,EBI-492834
PAX6P263673EBI-349121,EBI-747278From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 8989Dynein light chain 1, cytoplasmic
PRO_0000195127

Regions

Region67 – 8923Interaction with ESR1 By similarity

Amino acid modifications

Modified residue361N6-acetyllysine
Modified residue881Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P63168 [UniParc].

Last modified September 27, 2004. Version 1.
Checksum: F5E7647D092BEB3A

FASTA8910,366
        10         20         30         40         50         60 
MCDRKAVIKN ADMSEEMQQD SVECATQALE KYNIEKDIAA HIKKEFDKKY NPTWHCIVGR 

        70         80 
NFGSYVTHET KHFIYFYLGQ VAILLFKSG 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_062656.3. NM_019682.4.
UniGeneMm.256858.

3D structure databases

ProteinModelPortalP63168.
SMRP63168. Positions 5-89.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207994. 71 interactions.
IntActP63168. 74 interactions.
MINTMINT-1858885.

PTM databases

PhosphoSiteP63168.

Proteomic databases

PaxDbP63168.
PRIDEP63168.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000009157; ENSMUSP00000009157; ENSMUSG00000009013.
ENSMUST00000112090; ENSMUSP00000107720; ENSMUSG00000009013.
GeneID56455.
KEGGmmu:56455.
UCSCuc008zdp.2. mouse.

Organism-specific databases

CTD8655.
MGIMGI:1861457. Dynll1.

Phylogenomic databases

eggNOGNOG312371.
GeneTreeENSGT00390000000378.
HOVERGENHBG002133.
InParanoidP63168.
KOK10418.
OMALECATQA.
OrthoDBEOG7BZVVQ.
TreeFamTF300264.

Gene expression databases

BgeeP63168.
CleanExMM_DLC1.
MM_DYNLL1.
GenevestigatorP63168.

Family and domain databases

Gene3D3.30.740.10. 1 hit.
InterProIPR019763. Dynein_light_1/2_CS.
IPR001372. Dynein_light_chain_typ-1/2.
[Graphical view]
PANTHERPTHR11886. PTHR11886. 1 hit.
PfamPF01221. Dynein_light. 1 hit.
[Graphical view]
PROSITEPS01239. DYNEIN_LIGHT_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio312686.
PROP63168.
SOURCESearch...

Entry information

Entry nameDYL1_MOUSE
AccessionPrimary (citable) accession number: P63168
Secondary accession number(s): Q15701, Q3UGE7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: March 19, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot