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Protein

Dynein light chain 1, cytoplasmic

Gene

DYNLL1

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 changing or maintaining the spatial distribution of cytoskeletal structures.
Binds and inhibits the catalytic activity of neuronal nitric oxide synthase.
Promotes transactivation functions of ESR1 and plays a role in the nuclear localization of ESR1.
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.

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActivator, Motor protein
Biological processApoptosis, Host-virus interaction, Transcription, Transcription regulation, Transport

Enzyme and pathway databases

ReactomeiR-HSA-111446. Activation of BIM and translocation to mitochondria.
R-HSA-141444. Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
R-HSA-1632852. Macroautophagy.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-3371497. HSP90 chaperone cycle for steroid hormone receptors (SHR).
R-HSA-380259. Loss of Nlp from mitotic centrosomes.
R-HSA-380270. Recruitment of mitotic centrosome proteins and complexes.
R-HSA-380284. Loss of proteins required for interphase microtubule organization from the centrosome.
R-HSA-380320. Recruitment of NuMA to mitotic centrosomes.
R-HSA-5620912. Anchoring of the basal body to the plasma membrane.
R-HSA-5620924. Intraflagellar transport.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-6807878. COPI-mediated anterograde transport.
R-HSA-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-8854518. AURKA Activation by TPX2.
SIGNORiP63167.

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
Gene namesi
Name:DYNLL1
Synonyms:DLC1, DNCL1, DNCLC1, HDLC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

EuPathDBiHostDB:ENSG00000088986.10.
HGNCiHGNC:15476. DYNLL1.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Dynein, Microtubule, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi67T → A: Abolishes interaction with PAK1. 1 Publication1
Mutagenesisi88S → A: Abolishes growth factor-mediated phosphorylation. Increases BCL2L11 protein level and promotes apoptosis. 2 Publications1
Mutagenesisi88S → E: Abolishes homodimerization. Abolishes interaction with BCL2L11 isoform 1 and isoform 2. 2 Publications1

Organism-specific databases

DisGeNETi8655.
OpenTargetsiENSG00000088986.
PharmGKBiPA134972261.

Polymorphism and mutation databases

BioMutaiDYNLL1.
DMDMi52783578.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001951251 – 89Dynein light chain 1, cytoplasmicAdd BLAST89

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei36N6-acetyllysineND:1
Cross-linki43Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)ND:
Modified residuei88Phosphoserine1 Publication1

Post-translational modificationi

Phosphorylation at Ser-88 appears to control the dimer-monomer transition. According to PubMed:15193260, it is phosphorylated at Ser-88 by PAK1, however, according to PubMed:18650427, the DYNLL1 dimer is not accessible for PAK1 and the phosphorylation could not be demonstrated in vitro.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP63167.
PaxDbiP63167.
PeptideAtlasiP63167.
PRIDEiP63167.
TopDownProteomicsiP63167.

PTM databases

iPTMnetiP63167.
PhosphoSitePlusiP63167.
SwissPalmiP63167.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Inductioni

Up-regulated by ATMIN, PAK1 and estrogen.2 Publications

Gene expression databases

BgeeiENSG00000088986.
CleanExiHS_DLC1.
HS_DYNLL1.
ExpressionAtlasiP63167. baseline and differential.
GenevisibleiP63167. HS.

Organism-specific databases

HPAiHPA039954.

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 rabies P protein (By similarity). Interacts with TXNDC17. Interacts with WWC1 and ESR1. The WWC1-DYNLL1 interaction is mandatory for the recruitment and transactivation functions of ESR1 or DYNLL1 to the target chromatin. Interacts with BCL2L11 isoform 1 and isoform 2. 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. Interacts with human spumaretrovirus Gag protein; this interaction is critical for intracellular microtubule-dependent viral genome transport toward the centrosome. Interacts with MYZAP. Part of an astrin (SPAG5)-kinastrin (SKAP) complex containing KNSTRN, SPAG5, PLK1, DYNLL1 and SGO2. 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'). Interacts with BICD2 (By similarity).HMP:12 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi114206. 229 interactors.
CORUMiP63167.
DIPiDIP-33150N.
IntActiP63167. 187 interactors.
MINTiMINT-156345.
STRINGi9606.ENSP00000242577.

Structurei

Secondary structure

189
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 13ND:8
Helixi15 – 31ND:17
Beta strandi32 – 34ND:3
Helixi35 – 50ND:16
Beta strandi54 – 69ND:16
Beta strandi73 – 78ND:6
Beta strandi81 – 87ND:7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CMIX-ray2.50A/B5-89[»]
3ZKEX-ray2.20A/C/E/G/I/K1-89[»]
3ZKFX-ray2.60A/C/E/G/I/K1-89[»]
ProteinModelPortaliP63167.
SMRiP63167.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63167.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni67 – 89Interaction with ESR11 PublicationAdd BLAST23

Sequence similaritiesi

Belongs to the dynein light chain family.IKR:

Phylogenomic databases

eggNOGiKOG3430. Eukaryota.
ENOG4111NK2. LUCA.
GeneTreeiENSGT00390000000378.
HOVERGENiHBG002133.
InParanoidiP63167.
KOiK10418.
OMAiQAIMSDR.
OrthoDBiEOG091G15JY.
PhylomeDBiP63167.
TreeFamiTF300264.

Family and domain databases

Gene3Di3.30.740.10. 1 hit.
InterProiView protein in InterPro
IPR037177. DLC_sf.
IPR019763. Dynein_light_1/2_CS.
IPR001372. Dynein_light_chain_typ-1/2.
PANTHERiPTHR11886. PTHR11886. 1 hit.
PfamiView protein in Pfam
PF01221. Dynein_light. 1 hit.
SMARTiView protein in SMART
SM01375. Dynein_light. 1 hit.
SUPFAMiSSF54648. SSF54648. 1 hit.
PROSITEiView protein in PROSITE
PS01239. DYNEIN_LIGHT_1. 1 hit.

Sequencei

Sequence statusi: Complete.

P63167-1 [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
U32944 mRNA. Translation: AAB04149.1.
CR407672 mRNA. Translation: CAG28600.1.
CCDSiCCDS9200.1.
RefSeqiNP_001032583.1. NM_001037494.1.
NP_001032584.1. NM_001037495.1.
NP_003737.1. NM_003746.2.
UniGeneiHs.5120.

Genome annotation databases

EnsembliENST00000242577; ENSP00000242577; ENSG00000088986.
ENST00000392508; ENSP00000376296; ENSG00000088986.
ENST00000392509; ENSP00000376297; ENSG00000088986.
ENST00000548342; ENSP00000447907; ENSG00000088986.
ENST00000549989; ENSP00000446614; ENSG00000088986.
GeneIDi8655.
KEGGihsa:8655.

Similar proteinsi

Entry informationi

Entry nameiDYL1_HUMAN
AccessioniPrimary (citable) accession number: P63167
Secondary accession number(s): Q15701
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: October 25, 2017
This is version 148 of the entry and version 1 of the sequence. See 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families