DYNLL1

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DYNLL1

From Wikipedia, the free encyclopedia

DYNLL1

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
1CMI, 3ZKE, 3ZKF, 1F95, 1F3C, 1F96

Identifiers

Aliases

DYNLL1, DLC1, DLC8, DNCL1, DNCLC1, LC8, LC8a, PIN, hdlc1, dynein light chain LC8-type 1

External IDs

OMIM: 601562; MGI: 1861457; HomoloGene: 133063; GeneCards: DYNLL1; OMA:DYNLL1 - orthologs

Gene location (Human)

Chr.	Chromosome 12 (human)^[1]

Band	12q24.31	Start	120,469,850 bp^[1]
Band	12q24.31	End	120,498,493 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 5 (mouse)^[2]

Band	5\|5 F	Start	115,435,169 bp^[2]
Band	5\|5 F	End	115,439,058 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

prefrontal cortex

frontal pole

gingival epithelium

cingulate gyrus

anterior cingulate cortex

Brodmann area 9

bronchial epithelial cell

right testis

Brodmann area 10

right frontal lobe

Top expressed in

medial ganglionic eminence

endocardial cushion

dentate gyrus of hippocampal formation granule cell

maxillary prominence

condyle

mandibular prominence

spermatid

hair follicle

seminiferous tubule

abdominal wall

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	protein domain specific binding protein C-terminus binding protein binding cytoskeletal motor activity cytoskeletal protein binding plus-end-directed microtubule motor activity dynein intermediate chain binding dynein light intermediate chain binding enzyme binding nitric-oxide synthase regulator activity protein homodimerization activity protein heterodimerization activity scaffold protein binding
Cellular component	cytoplasm cytosol centrosome membrane plasma membrane microtubule associated complex ciliary tip mitochondrion dynein complex COP9 signalosome mitotic spindle microtubule cytoskeleton extracellular exosome nucleus kinetochore cytoplasmic dynein complex cilium tertiary granule membrane ficolin-1-rich granule membrane microtubule organizing center secretory granule axon cytoplasm
Biological process	regulation of transcription, DNA-templated substantia nigra development antigen processing and presentation of exogenous peptide antigen via MHC class II transcription, DNA-templated endoplasmic reticulum to Golgi vesicle-mediated transport positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway G2/M transition of mitotic cell cycle microtubule-based process intraciliary retrograde transport viral process negative regulation of phosphorylation macroautophagy apoptotic process intraciliary transport involved in cilium assembly neutrophil degranulation motile cilium assembly ciliary basal body-plasma membrane docking positive regulation of non-motile cilium assembly transport along microtubule cilium assembly sister chromatid cohesion regulation of G2/M transition of mitotic cell cycle transport spermatid development positive regulation of insulin secretion involved in cellular response to glucose stimulus
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


8655


56455

Ensembl


ENSG00000088986


ENSMUSG00000009013

UniProt


P63167


P63168

RefSeq (mRNA)


NM_003746 NM_001037494 NM_001037495


NM_019682

RefSeq (protein)


NP_001032583 NP_001032584 NP_003737


NP_062656

Location (UCSC)

Chr 12: 120.47 – 120.5 Mb

Chr 5: 115.44 – 115.44 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Dynein light chain 1, cytoplasmic is a protein that in humans is encoded by the DYNLL1 gene.^[5]^[6]^[7]^[8]

Function

[edit]

Cytoplasmic dyneins are large enzyme complexes with a molecular mass of about 1,200 kD. They contain two force-producing heads formed primarily from dynein heavy chains, and stalks linking the heads to a basal domain, which contains a varying number of accessory intermediate chains. The complex is involved in intracellular transport and motility. The protein described in this record is a light chain and exists as part of this complex but also physically interacts with and inhibits the activity of neuronal nitric oxide synthase. Binding of this protein destabilizes the neuronal nitric oxide synthase dimer, a conformation necessary for activity, and it may regulate numerous biologic processes through its effects on nitric oxide synthase activity. Alternate transcriptional splice variants have been characterized.^[8]

Interactions

[edit]

DYNLL1 has been shown to interact with:

References

[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000088986 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000009013 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Dick T, Ray K, Salz HK, Chia W (May 1996). "Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster". Molecular and Cellular Biology. 16 (5): 1966–77. doi:10.1128/mcb.16.5.1966. PMC 231184. PMID 8628263.
^ Jaffrey SR, Snyder SH (Nov 1996). "PIN: an associated protein inhibitor of neuronal nitric oxide synthase". Science. 274 (5288): 774–7. Bibcode:1996Sci...274..774J. doi:10.1126/science.274.5288.774. PMID 8864115. S2CID 46494691.
^ Pfister KK, Fisher EM, Gibbons IR, Hays TS, Holzbaur EL, McIntosh JR, Porter ME, Schroer TA, Vaughan KT, Witman GB, King SM, Vallee RB (Nov 2005). "Cytoplasmic dynein nomenclature". The Journal of Cell Biology. 171 (3): 411–3. doi:10.1083/jcb.200508078. PMC 2171247. PMID 16260502.
^ ^a ^b "Entrez Gene: DYNLL1 dynein, light chain, LC8-type 1".
^ Day CL, Puthalakath H, Skea G, Strasser A, Barsukov I, Lian LY, Huang DC, Hinds MG (Feb 2004). "Localization of dynein light chains 1 and 2 and their pro-apoptotic ligands". The Biochemical Journal. 377 (Pt 3): 597–605. doi:10.1042/BJ20031251. PMC 1223895. PMID 14561217.
^ ^a ^b Vadlamudi RK, Bagheri-Yarmand R, Yang Z, Balasenthil S, Nguyen D, Sahin AA, den Hollander P, Kumar R (Jun 2004). "Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes". Cancer Cell. 5 (6): 575–85. doi:10.1016/j.ccr.2004.05.022. PMID 15193260.
^ ^a ^b ^c Naisbitt S, Valtschanoff J, Allison DW, Sala C, Kim E, Craig AM, Weinberg RJ, Sheng M (Jun 2000). "Interaction of the postsynaptic density-95/guanylate kinase domain-associated protein complex with a light chain of myosin-V and dynein". The Journal of Neuroscience. 20 (12): 4524–34. doi:10.1523/JNEUROSCI.20-12-04524.2000. PMC 6772433. PMID 10844022.
^ Diefenbach RJ, Diefenbach E, Douglas MW, Cunningham AL (Dec 2002). "The heavy chain of conventional kinesin interacts with the SNARE proteins SNAP25 and SNAP23". Biochemistry. 41 (50): 14906–15. doi:10.1021/bi026417u. PMID 12475239.
^ Crépieux P, Kwon H, Leclerc N, Spencer W, Richard S, Lin R, Hiscott J (Dec 1997). "I kappaB alpha physically interacts with a cytoskeleton-associated protein through its signal response domain". Molecular and Cellular Biology. 17 (12): 7375–85. doi:10.1128/MCB.17.12.7375. PMC 232593. PMID 9372968.
^ Herzig RP, Andersson U, Scarpulla RC (Dec 2000). "Dynein light chain interacts with NRF-1 and EWG, structurally and functionally related transcription factors from humans and drosophila". Journal of Cell Science. 113 (23): 4263–73. doi:10.1242/jcs.113.23.4263. PMID 11069771.
^ Lo KW, Kan HM, Chan LN, Xu WG, Wang KP, Wu Z, Sheng M, Zhang M (Mar 2005). "The 8-kDa dynein light chain binds to p53-binding protein 1 and mediates DNA damage-induced p53 nuclear accumulation". The Journal of Biological Chemistry. 280 (9): 8172–9. doi:10.1074/jbc.M411408200. PMID 15611139.

External links

[edit]

Overview of all the structural information available in the PDB for UniProt: P63167 (Dynein light chain 1, cytoplasmic) at the PDBe-KB.

PDB gallery

1cmi: STRUCTURE OF THE HUMAN PIN/LC8 DIMER WITH A BOUND PEPTIDE
1f3c: REFINED SOLUTION STRUCTURE OF 8KDA DYNEIN LIGHT CHAIN (DLC8)
1f95: SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND BIM PEPTIDE COMPLEX
1f96: SOLUTION STRUCTURE OF DYNEIN LIGHT CHAIN 8 (DLC8) AND NNOS PEPTIDE COMPLEX
1pwj: Structure of the Monomeric 8-kDa Dynein Light Chain and Mechanism of Domain Swapped Dimer Assembly
1pwk: Structure of the Monomeric 8-kDa Dynein Light Chain and Mechanism of Domain Swapped Dimer Assembly
1re6: Localisation of Dynein Light Chains 1 and 2 and their Pro-apoptotic Ligands
1rhw: The solution structure of the pH-induced monomer of dynein light chain LC8 from Drosophila
2pg1: Structural analysis of a cytoplasmic dynein Light Chain-Intermediate Chain complex

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Category:

Genes on human chromosome 12

Hidden categories:

Function

Interactions

References

Further reading

External links