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P63167

- DYL1_HUMAN

UniProt

P63167 - DYL1_HUMAN

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Protein

Dynein light chain 1, cytoplasmic

Gene

DYNLL1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. motor activity Source: ProtInc
  2. nitric-oxide synthase regulator activity Source: Ensembl

GO - Biological processi

  1. actin cytoskeleton organization Source: ProtInc
  2. anatomical structure morphogenesis Source: ProtInc
  3. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  4. apoptotic process Source: Reactome
  5. female gamete generation Source: ProtInc
  6. G2/M transition of mitotic cell cycle Source: Reactome
  7. intrinsic apoptotic signaling pathway Source: Reactome
  8. microtubule-based process Source: InterPro
  9. mitotic cell cycle Source: Reactome
  10. negative regulation of phosphorylation Source: UniProtKB
  11. positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway Source: Reactome
  12. regulation of transcription, DNA-templated Source: UniProtKB-KW
  13. substantia nigra development Source: UniProt
  14. transcription, DNA-templated Source: UniProtKB-KW
  15. transport Source: UniProtKB-KW
  16. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Motor protein

Keywords - Biological processi

Apoptosis, Host-virus interaction, Transcription, Transcription regulation, Transport

Enzyme and pathway databases

ReactomeiREACT_121399. MHC class II antigen presentation.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

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
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:15476. DYNLL1.

Subcellular locationi

Cytoplasmcytoskeleton. Nucleus. Mitochondrion
Note: Upon induction of apoptosis translocates together with BCL2L11 to mitochondria.

GO - Cellular componenti

  1. centrosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytoplasmic dynein complex Source: UniProtKB
  4. cytosol Source: Reactome
  5. extracellular vesicular exosome Source: UniProt
  6. kinetochore Source: UniProtKB
  7. membrane Source: UniProtKB
  8. microtubule Source: UniProtKB-KW
  9. mitochondrion Source: UniProtKB-KW
  10. mitotic spindle Source: UniProtKB
  11. nucleus Source: UniProtKB
  12. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Dynein, Microtubule, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi67 – 671T → A: Abolishes interaction with PAK1. 1 Publication
Mutagenesisi88 – 881S → A: Abolishes growth factor-mediated phosphorylation. Increases BCL2L11 protein level and promotes apoptosis. 2 Publications
Mutagenesisi88 – 881S → E: Abolishes homodimerization. Abolishes interaction with BCL2L11 isoform 1 and isoform 2. 2 Publications

Organism-specific databases

PharmGKBiPA134972261.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 8989Dynein light chain 1, cytoplasmicPRO_0000195125Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361N6-acetyllysine1 Publication
Modified residuei88 – 881Phosphoserine1 Publication

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, Phosphoprotein

Proteomic databases

MaxQBiP63167.
PaxDbiP63167.
PeptideAtlasiP63167.
PRIDEiP63167.

PTM databases

PhosphoSiteiP63167.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Inductioni

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

Gene expression databases

BgeeiP63167.
CleanExiHS_DLC1.
HS_DYNLL1.
ExpressionAtlasiP63167. baseline and differential.
GenevestigatoriP63167.

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 SGOL2. 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 similarity12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GNB2L1P632446EBI-349105,EBI-296739
MYZAPP0CAP16EBI-349105,EBI-7929343

Protein-protein interaction databases

BioGridi114206. 125 interactions.
DIPiDIP-33150N.
IntActiP63167. 52 interactions.
MINTiMINT-156345.
STRINGi9606.ENSP00000242577.

Structurei

Secondary structure

1
89
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 138Combined sources
Helixi15 – 3117Combined sources
Beta strandi32 – 343Combined sources
Helixi35 – 5016Combined sources
Beta strandi54 – 6916Combined sources
Beta strandi73 – 786Combined sources
Beta strandi81 – 877Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 5-89.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63167.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni67 – 8923Interaction with ESR1Add
BLAST

Sequence similaritiesi

Belongs to the dynein light chain family.Curated

Phylogenomic databases

eggNOGiNOG312371.
HOVERGENiHBG002133.
InParanoidiP63167.
KOiK10418.
OMAiECATQAM.
OrthoDBiEOG7BZVVQ.
PhylomeDBiP63167.
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.

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:
EMBL
GenBank
DDBJ
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.
UCSCiuc001tyj.3. human.

Polymorphism databases

DMDMi52783578.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U32944 mRNA. Translation: AAB04149.1 .
CR407672 mRNA. Translation: CAG28600.1 .
CCDSi CCDS9200.1.
RefSeqi NP_001032583.1. NM_001037494.1.
NP_001032584.1. NM_001037495.1.
NP_003737.1. NM_003746.2.
UniGenei Hs.5120.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CMI X-ray 2.50 A/B 5-89 [» ]
3ZKE X-ray 2.20 A/C/E/G/I/K 1-89 [» ]
3ZKF X-ray 2.60 A/C/E/G/I/K 1-89 [» ]
ProteinModelPortali P63167.
SMRi P63167. Positions 5-89.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114206. 125 interactions.
DIPi DIP-33150N.
IntActi P63167. 52 interactions.
MINTi MINT-156345.
STRINGi 9606.ENSP00000242577.

PTM databases

PhosphoSitei P63167.

Polymorphism databases

DMDMi 52783578.

Proteomic databases

MaxQBi P63167.
PaxDbi P63167.
PeptideAtlasi P63167.
PRIDEi P63167.

Protocols and materials databases

DNASUi 8655.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000242577 ; ENSP00000242577 ; ENSG00000088986 .
ENST00000392508 ; ENSP00000376296 ; ENSG00000088986 .
ENST00000392509 ; ENSP00000376297 ; ENSG00000088986 .
ENST00000548342 ; ENSP00000447907 ; ENSG00000088986 .
ENST00000549989 ; ENSP00000446614 ; ENSG00000088986 .
GeneIDi 8655.
KEGGi hsa:8655.
UCSCi uc001tyj.3. human.

Organism-specific databases

CTDi 8655.
GeneCardsi GC12P120908.
HGNCi HGNC:15476. DYNLL1.
MIMi 601562. gene.
neXtProti NX_P63167.
PharmGKBi PA134972261.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG312371.
HOVERGENi HBG002133.
InParanoidi P63167.
KOi K10418.
OMAi ECATQAM.
OrthoDBi EOG7BZVVQ.
PhylomeDBi P63167.
TreeFami TF300264.

Enzyme and pathway databases

Reactomei REACT_121399. MHC class II antigen presentation.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.

Miscellaneous databases

EvolutionaryTracei P63167.
GeneWikii DYNLL1.
GenomeRNAii 8655.
NextBioi 32461.
PROi P63167.
SOURCEi Search...

Gene expression databases

Bgeei P63167.
CleanExi HS_DLC1.
HS_DYNLL1.
ExpressionAtlasi P63167. baseline and differential.
Genevestigatori P63167.

Family and domain databases

Gene3Di 3.30.740.10. 1 hit.
InterProi IPR019763. Dynein_light_1/2_CS.
IPR001372. Dynein_light_chain_typ-1/2.
[Graphical view ]
PANTHERi PTHR11886. PTHR11886. 1 hit.
Pfami PF01221. Dynein_light. 1 hit.
[Graphical view ]
PROSITEi PS01239. DYNEIN_LIGHT_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and apoptotic cell death in Drosophila melanogaster."
    Dick T., Ray K., Salz H.K., Chia W.
    Mol. Cell. Biol. 16:1966-1977(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The proapoptotic activity of the Bcl-2 family member Bim is regulated by interaction with the dynein motor complex."
    Puthalakath H., Huang D.C., O'Reilly L.A., King S.M., Strasser A.
    Mol. Cell 3:287-296(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF APOPTOSIS, INTERACTION WITH BCL2L11 AND BCL2.
  4. "Targeting of incoming retroviral Gag to the centrosome involves a direct interaction with the dynein light chain 8."
    Petit C., Giron M.L., Tobaly-Tapiero J., Bittoun P., Real E., Jacob Y., Tordo N., De The H., Saib A.
    J. Cell Sci. 116:3433-3442(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HUMAN SPUMARETROVIRUS GAG.
  5. "Dynein light chain 1, a p21-activated kinase 1-interacting substrate, promotes cancerous phenotypes."
    Vadlamudi R.K., Bagheri-Yarmand R., Yang Z., Balasenthil S., Nguyen D., Sahin A.A., den Hollander P., Kumar R.
    Cancer Cell 5:575-585(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF BCL2L11, INTERACTION WITH PAK1 AND BCL2L11, PHOSPHORYLATION AT SER-88, MUTAGENESIS OF SER-88.
  6. "Roles of TRP14, a thioredoxin-related protein in tumor necrosis factor-alpha signaling pathways."
    Jeong W., Chang T.-S., Boja E.S., Fales H.M., Rhee S.G.
    J. Biol. Chem. 279:3151-3159(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TXNDC17.
  7. "Functional regulation of oestrogen receptor pathway by the dynein light chain 1."
    Rayala S.K., den Hollander P., Balasenthil S., Yang Z., Broaddus R.R., Kumar R.
    EMBO Rep. 6:538-544(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH ESR1.
  8. "Essential role of KIBRA in co-activator function of dynein light chain 1 in mammalian cells."
    Rayala S.K., den Hollander P., Manavathi B., Talukder A.H., Song C., Peng S., Barnekow A., Kremerskothen J., Kumar R.
    J. Biol. Chem. 281:19092-19099(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH WWC1.
  9. "Serine 88 phosphorylation of the 8-kDa dynein light chain 1 is a molecular switch for its dimerization status and functions."
    Song C., Wen W., Rayala S.K., Chen M., Ma J., Zhang M., Kumar R.
    J. Biol. Chem. 283:4004-4013(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH BCL2L11, MUTAGENESIS OF SER-88.
  10. "Biochemical and structural characterization of the Pak1-LC8 interaction."
    Lightcap C.M., Sun S., Lear J.D., Rodeck U., Polenova T., Williams J.C.
    J. Biol. Chem. 283:27314-27324(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH PAK1, MUTAGENESIS OF THR-67.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Structural basis for the interaction between dynein light chain 1 and the glutamate channel homolog GRINL1A."
    Garcia-Mayoral M.F., Martinez-Moreno M., Albar J.P., Rodriguez-Crespo I., Bruix M.
    FEBS J. 277:2340-2350(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYZAP.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "The astrin-kinastrin/SKAP complex localizes to microtubule plus ends and facilitates chromosome alignment."
    Dunsch A.K., Linnane E., Barr F.A., Gruneberg U.
    J. Cell Biol. 192:959-968(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH KNSTRN; SPAG5; PLK1 AND SGOL2.
  15. "ATM substrate Chk2-interacting Zn2+ finger (ASCIZ) Is a bi-functional transcriptional activator and feedback sensor in the regulation of dynein light chain (DYNLL1) expression."
    Jurado S., Conlan L.A., Baker E.K., Ng J.L., Tenis N., Hoch N.C., Gleeson K., Smeets M., Izon D., Heierhorst J.
    J. Biol. Chem. 287:3156-3164(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATMIN, INDUCTION.
  16. "Structure of the PIN/LC8 dimer with a bound peptide."
    Liang J., Jaffrey S.R., Guo W., Snyder S.H., Clardy J.
    Nat. Struct. Biol. 6:735-740(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 5-89.
  17. "Structural analysis of the regulation of the DYNLL/LC8 binding to Nek9 by phosphorylation."
    Gallego P., Velazquez-Campoy A., Regue L., Roig J., Reverter D.
    J. Biol. Chem. 288:12283-12294(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NEK9, INTERACTION WITH NEK9.

Entry informationi

Entry nameiDYL1_HUMAN
AccessioniPrimary (citable) accession number: P63167
Secondary accession number(s): Q15701
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: October 29, 2014
This is version 114 of the entry and version 1 of the sequence. [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

External Data

Dasty 3