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Dynein light chain 1, cytoplasmic (8 kDa dynein light chain) (DLC8) (Dynein light chain LC8-type 1) (Protein inhibitor of neuronal nitric oxide synthase) (PIN)

 DYL1_HUMAN              Reviewed;          89 AA.
P63167; Q15701;
27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
27-SEP-2004, sequence version 1.
25-OCT-2017, entry version 148.
RecName: Full=Dynein light chain 1, cytoplasmic;
AltName: Full=8 kDa dynein light chain;
Short=DLC8;
AltName: Full=Dynein light chain LC8-type 1;
AltName: Full=Protein inhibitor of neuronal nitric oxide synthase;
Short=PIN;
Name=DYNLL1; Synonyms=DLC1, DNCL1, DNCLC1, HDLC1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=8628263; DOI=10.1128/MCB.16.5.1966;
Dick T., Ray K., Salz H.K., Chia W.;
"Cytoplasmic dynein (ddlc1) mutations cause morphogenetic defects and
apoptotic cell death in Drosophila melanogaster.";
Mol. Cell. Biol. 16:1966-1977(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[3]
FUNCTION IN REGULATION OF APOPTOSIS, AND INTERACTION WITH BCL2L11 AND
BCL2.
PubMed=10198631; DOI=10.1016/S1097-2765(00)80456-6;
Puthalakath H., Huang D.C., O'Reilly L.A., King S.M., Strasser A.;
"The proapoptotic activity of the Bcl-2 family member Bim is regulated
by interaction with the dynein motor complex.";
Mol. Cell 3:287-296(1999).
[4]
INTERACTION WITH HUMAN SPUMARETROVIRUS GAG.
PubMed=12857789; DOI=10.1242/jcs.00613;
Petit C., Giron M.L., Tobaly-Tapiero J., Bittoun P., Real E.,
Jacob Y., Tordo N., De The H., Saib A.;
"Targeting of incoming retroviral Gag to the centrosome involves a
direct interaction with the dynein light chain 8.";
J. Cell Sci. 116:3433-3442(2003).
[5]
FUNCTION IN REGULATION OF BCL2L11, INTERACTION WITH PAK1 AND BCL2L11,
PHOSPHORYLATION AT SER-88, AND MUTAGENESIS OF SER-88.
PubMed=15193260; DOI=10.1016/j.ccr.2004.05.022;
Vadlamudi R.K., Bagheri-Yarmand R., Yang Z., Balasenthil S.,
Nguyen D., Sahin A.A., den Hollander P., Kumar R.;
"Dynein light chain 1, a p21-activated kinase 1-interacting substrate,
promotes cancerous phenotypes.";
Cancer Cell 5:575-585(2004).
[6]
INTERACTION WITH TXNDC17.
PubMed=14607843; DOI=10.1074/jbc.M307959200;
Jeong W., Chang T.-S., Boja E.S., Fales H.M., Rhee S.G.;
"Roles of TRP14, a thioredoxin-related protein in tumor necrosis
factor-alpha signaling pathways.";
J. Biol. Chem. 279:3151-3159(2004).
[7]
FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND INTERACTION WITH ESR1.
PubMed=15891768; DOI=10.1038/sj.embor.7400417;
Rayala S.K., den Hollander P., Balasenthil S., Yang Z., Broaddus R.R.,
Kumar R.;
"Functional regulation of oestrogen receptor pathway by the dynein
light chain 1.";
EMBO Rep. 6:538-544(2005).
[8]
ERRATUM.
Rayala S.K., den Hollander P., Balasenthil S., Yang Z., Broaddus R.R.,
Kumar R.;
EMBO Rep. 6:1101-1101(2005).
[9]
FUNCTION, AND INTERACTION WITH WWC1.
PubMed=16684779; DOI=10.1074/jbc.M600021200;
Rayala S.K., den Hollander P., Manavathi B., Talukder A.H., Song C.,
Peng S., Barnekow A., Kremerskothen J., Kumar R.;
"Essential role of KIBRA in co-activator function of dynein light
chain 1 in mammalian cells.";
J. Biol. Chem. 281:19092-19099(2006).
[10]
SUBUNIT, INTERACTION WITH BCL2L11, AND MUTAGENESIS OF SER-88.
PubMed=18084006; DOI=10.1074/jbc.M704512200;
Song C., Wen W., Rayala S.K., Chen M., Ma J., Zhang M., Kumar R.;
"Serine 88 phosphorylation of the 8-kDa dynein light chain 1 is a
molecular switch for its dimerization status and functions.";
J. Biol. Chem. 283:4004-4013(2008).
[11]
SUBUNIT, INTERACTION WITH PAK1, AND MUTAGENESIS OF THR-67.
PubMed=18650427; DOI=10.1074/jbc.M800758200;
Lightcap C.M., Sun S., Lear J.D., Rodeck U., Polenova T.,
Williams J.C.;
"Biochemical and structural characterization of the Pak1-LC8
interaction.";
J. Biol. Chem. 283:27314-27324(2008).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
INTERACTION WITH MYZAP.
PubMed=20412299; DOI=10.1111/j.1742-4658.2010.07649.x;
Garcia-Mayoral M.F., Martinez-Moreno M., Albar J.P.,
Rodriguez-Crespo I., Bruix M.;
"Structural basis for the interaction between dynein light chain 1 and
the glutamate channel homolog GRINL1A.";
FEBS J. 277:2340-2350(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
IDENTIFICATION IN A COMPLEX WITH KNSTRN; SPAG5; PLK1 AND SGO2.
PubMed=21402792; DOI=10.1083/jcb.201008023;
Dunsch A.K., Linnane E., Barr F.A., Gruneberg U.;
"The astrin-kinastrin/SKAP complex localizes to microtubule plus ends
and facilitates chromosome alignment.";
J. Cell Biol. 192:959-968(2011).
[16]
INTERACTION WITH ATMIN, AND INDUCTION.
PubMed=22167198; DOI=10.1074/jbc.M111.306019;
Jurado S., Conlan L.A., Baker E.K., Ng J.L., Tenis N., Hoch N.C.,
Gleeson K., Smeets M., Izon D., Heierhorst J.;
"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.";
J. Biol. Chem. 287:3156-3164(2012).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-43, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[19]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 5-89.
PubMed=10426949; DOI=10.1038/11501;
Liang J., Jaffrey S.R., Guo W., Snyder S.H., Clardy J.;
"Structure of the PIN/LC8 dimer with a bound peptide.";
Nat. Struct. Biol. 6:735-740(1999).
[20]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH NEK9, AND
INTERACTION WITH NEK9.
PubMed=23482567; DOI=10.1074/jbc.M113.459149;
Gallego P., Velazquez-Campoy A., Regue L., Roig J., Reverter D.;
"Structural analysis of the regulation of the DYNLL/LC8 binding to
Nek9 by phosphorylation.";
J. Biol. Chem. 288:12283-12294(2013).
-!- 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.
-!- FUNCTION: Binds and inhibits the catalytic activity of neuronal
nitric oxide synthase.
-!- FUNCTION: Promotes transactivation functions of ESR1 and plays a
role in the nuclear localization of ESR1.
-!- FUNCTION: 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.
-!- SUBUNIT: 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).
{ECO:0000250|UniProtKB:P63168, ECO:0000269|PubMed:10198631,
ECO:0000269|PubMed:12857789, ECO:0000269|PubMed:14607843,
ECO:0000269|PubMed:15193260, ECO:0000269|PubMed:15891768,
ECO:0000269|PubMed:16684779, ECO:0000269|PubMed:18084006,
ECO:0000269|PubMed:18650427, ECO:0000269|PubMed:20412299,
ECO:0000269|PubMed:21402792, ECO:0000269|PubMed:22167198,
ECO:0000269|PubMed:23482567}.
-!- INTERACTION:
Q9Y2J4-4:AMOTL2; NbExp=3; IntAct=EBI-349105, EBI-10187270;
Q8IYA8:CCDC36; NbExp=5; IntAct=EBI-349105, EBI-8638439;
O96015:DNAL4; NbExp=4; IntAct=EBI-349105, EBI-742362;
Q6P1L5:FAM117B; NbExp=4; IntAct=EBI-349105, EBI-3893327;
Q9NQX3:GPHN; NbExp=2; IntAct=EBI-349105, EBI-2371891;
Q8NA54:IQUB; NbExp=3; IntAct=EBI-349105, EBI-10220600;
Q63ZY3:KANK2; NbExp=5; IntAct=EBI-349105, EBI-2556193;
P0CAP1:MYZAP; NbExp=6; IntAct=EBI-349105, EBI-7929343;
Q8TD19:NEK9; NbExp=4; IntAct=EBI-349105, EBI-1044009;
P63244:RACK1; NbExp=6; IntAct=EBI-349105, EBI-296739;
P49901:SMCP; NbExp=4; IntAct=EBI-349105, EBI-750494;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Nucleus.
Mitochondrion. Note=Upon induction of apoptosis translocates
together with BCL2L11 to mitochondria.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:8628263}.
-!- INDUCTION: Up-regulated by ATMIN, PAK1 and estrogen.
{ECO:0000269|PubMed:15891768, ECO:0000269|PubMed:22167198}.
-!- PTM: 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.
{ECO:0000269|PubMed:15193260}.
-!- SIMILARITY: Belongs to the dynein light chain family.
{ECO:0000305}.
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EMBL; U32944; AAB04149.1; -; mRNA.
EMBL; CR407672; CAG28600.1; -; mRNA.
CCDS; CCDS9200.1; -.
RefSeq; NP_001032583.1; NM_001037494.1.
RefSeq; NP_001032584.1; NM_001037495.1.
RefSeq; NP_003737.1; NM_003746.2.
UniGene; Hs.5120; -.
PDB; 1CMI; X-ray; 2.50 A; A/B=5-89.
PDB; 3ZKE; X-ray; 2.20 A; A/C/E/G/I/K=1-89.
PDB; 3ZKF; X-ray; 2.60 A; A/C/E/G/I/K=1-89.
PDBsum; 1CMI; -.
PDBsum; 3ZKE; -.
PDBsum; 3ZKF; -.
ProteinModelPortal; P63167; -.
SMR; P63167; -.
BioGrid; 114206; 229.
CORUM; P63167; -.
DIP; DIP-33150N; -.
IntAct; P63167; 187.
MINT; MINT-156345; -.
STRING; 9606.ENSP00000242577; -.
iPTMnet; P63167; -.
PhosphoSitePlus; P63167; -.
SwissPalm; P63167; -.
BioMuta; DYNLL1; -.
DMDM; 52783578; -.
EPD; P63167; -.
PaxDb; P63167; -.
PeptideAtlas; P63167; -.
PRIDE; P63167; -.
TopDownProteomics; P63167; -.
DNASU; 8655; -.
Ensembl; ENST00000242577; ENSP00000242577; ENSG00000088986.
Ensembl; ENST00000392508; ENSP00000376296; ENSG00000088986.
Ensembl; ENST00000392509; ENSP00000376297; ENSG00000088986.
Ensembl; ENST00000548342; ENSP00000447907; ENSG00000088986.
Ensembl; ENST00000549989; ENSP00000446614; ENSG00000088986.
GeneID; 8655; -.
KEGG; hsa:8655; -.
CTD; 8655; -.
DisGeNET; 8655; -.
EuPathDB; HostDB:ENSG00000088986.10; -.
GeneCards; DYNLL1; -.
HGNC; HGNC:15476; DYNLL1.
HPA; HPA039954; -.
MIM; 601562; gene.
neXtProt; NX_P63167; -.
OpenTargets; ENSG00000088986; -.
PharmGKB; PA134972261; -.
eggNOG; KOG3430; Eukaryota.
eggNOG; ENOG4111NK2; LUCA.
GeneTree; ENSGT00390000000378; -.
HOVERGEN; HBG002133; -.
InParanoid; P63167; -.
KO; K10418; -.
OMA; QAIMSDR; -.
OrthoDB; EOG091G15JY; -.
PhylomeDB; P63167; -.
TreeFam; TF300264; -.
Reactome; R-HSA-111446; Activation of BIM and translocation to mitochondria.
Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-2132295; MHC class II antigen presentation.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR).
Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
Reactome; R-HSA-5620924; Intraflagellar transport.
Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
Reactome; R-HSA-68877; Mitotic Prometaphase.
Reactome; R-HSA-8854518; AURKA Activation by TPX2.
SIGNOR; P63167; -.
ChiTaRS; DYNLL1; human.
EvolutionaryTrace; P63167; -.
GeneWiki; DYNLL1; -.
GenomeRNAi; 8655; -.
PRO; PR:P63167; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000088986; -.
CleanEx; HS_DLC1; -.
CleanEx; HS_DYNLL1; -.
ExpressionAtlas; P63167; baseline and differential.
Genevisible; P63167; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0097542; C:ciliary tip; TAS:Reactome.
GO; GO:0005929; C:cilium; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005868; C:cytoplasmic dynein complex; IDA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0008092; F:cytoskeletal protein binding; IBA:GO_Central.
GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
GO; GO:0051959; F:dynein light intermediate chain binding; IBA:GO_Central.
GO; GO:0003774; F:motor activity; IEA:UniProtKB-KW.
GO; GO:0008022; F:protein C-terminus binding; IEA:Ensembl.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0097711; P:ciliary basal body-plasma membrane docking; TAS:Reactome.
GO; GO:0060271; P:cilium assembly; IBA:GO_Central.
GO; GO:0006888; P:ER to Golgi vesicle-mediated transport; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0035721; P:intraciliary retrograde transport; IEA:Ensembl.
GO; GO:0035735; P:intraciliary transport involved in cilium assembly; TAS:Reactome.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:0044458; P:motile cilium assembly; IEA:Ensembl.
GO; GO:0042326; P:negative regulation of phosphorylation; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:2000582; P:positive regulation of ATP-dependent microtubule motor activity, plus-end-directed; IBA:GO_Central.
GO; GO:1902857; P:positive regulation of non-motile cilium assembly; IEA:Ensembl.
GO; GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
GO; GO:0010389; P:regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007062; P:sister chromatid cohesion; TAS:Reactome.
GO; GO:0021762; P:substantia nigra development; IEP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0010970; P:transport along microtubule; IBA:GO_Central.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
Gene3D; 3.30.740.10; -; 1.
InterPro; IPR037177; DLC_sf.
InterPro; IPR019763; Dynein_light_1/2_CS.
InterPro; IPR001372; Dynein_light_chain_typ-1/2.
PANTHER; PTHR11886; PTHR11886; 1.
Pfam; PF01221; Dynein_light; 1.
SMART; SM01375; Dynein_light; 1.
SUPFAM; SSF54648; SSF54648; 1.
PROSITE; PS01239; DYNEIN_LIGHT_1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Apoptosis; Complete proteome;
Cytoplasm; Cytoskeleton; Dynein; Host-virus interaction;
Isopeptide bond; Microtubule; Mitochondrion; Motor protein; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Transport; Ubl conjugation.
CHAIN 1 89 Dynein light chain 1, cytoplasmic.
/FTId=PRO_0000195125.
REGION 67 89 Interaction with ESR1.
{ECO:0000269|PubMed:15891768}.
MOD_RES 36 36 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 88 88 Phosphoserine.
{ECO:0000269|PubMed:15193260}.
CROSSLNK 43 43 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
MUTAGEN 67 67 T->A: Abolishes interaction with PAK1.
{ECO:0000269|PubMed:18650427}.
MUTAGEN 88 88 S->A: Abolishes growth factor-mediated
phosphorylation. Increases BCL2L11
protein level and promotes apoptosis.
{ECO:0000269|PubMed:15193260,
ECO:0000269|PubMed:18084006}.
MUTAGEN 88 88 S->E: Abolishes homodimerization.
Abolishes interaction with BCL2L11
isoform 1 and isoform 2.
{ECO:0000269|PubMed:15193260,
ECO:0000269|PubMed:18084006}.
STRAND 6 13 {ECO:0000244|PDB:3ZKE}.
HELIX 15 31 {ECO:0000244|PDB:3ZKE}.
STRAND 32 34 {ECO:0000244|PDB:1CMI}.
HELIX 35 50 {ECO:0000244|PDB:3ZKE}.
STRAND 54 69 {ECO:0000244|PDB:3ZKE}.
STRAND 73 78 {ECO:0000244|PDB:3ZKE}.
STRAND 81 87 {ECO:0000244|PDB:3ZKE}.
SEQUENCE 89 AA; 10366 MW; F5E7647D092BEB3A CRC64;
MCDRKAVIKN ADMSEEMQQD SVECATQALE KYNIEKDIAA HIKKEFDKKY NPTWHCIVGR
NFGSYVTHET KHFIYFYLGQ VAILLFKSG


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Catalog number Product name Quantity
EIAAB12178 8 kDa dynein light chain,DLC8,Dncl1,Dnclc1,Dynein light chain 1, cytoplasmic,Dynein light chain LC8-type 1,Dynll1,PIN,Pin,Protein inhibitor of neuronal nitric oxide synthase,Rat,Rattus norvegicus
EIAAB12177 8 kDa dynein light chain,DLC1,DLC8,DNCL1,DNCLC1,Dynein light chain 1, cytoplasmic,Dynein light chain LC8-type 1,DYNLL1,Oryctolagus cuniculus,PIN,Protein inhibitor of neuronal nitric oxide synthase,Rab
EIAAB12180 8 kDa dynein light chain,Dlc1,DLC8,Dncl1,Dnclc1,Dynein light chain 1, cytoplasmic,Dynein light chain LC8-type 1,Dynll1,Mouse,mPIN,Mus musculus,PIN,Protein inhibitor of neuronal nitric oxide synthase
EIAAB12176 8 kDa dynein light chain,DLC1,DLC8,DNCL1,DNCLC1,Dynein light chain 1, cytoplasmic,Dynein light chain LC8-type 1,DYNLL1,HDLC1,Homo sapiens,Human,PIN,Protein inhibitor of neuronal nitric oxide synthase
EIAAB12181 8 kDa dynein light chain b,Dlc2,DLC8,DLC8b,Dynein light chain 2, cytoplasmic,Dynein light chain LC8-type 2,Dynll2,Mouse,Mus musculus
EIAAB12184 8 kDa dynein light chain b,DLC2,DLC8b,Dynein light chain 2, cytoplasmic,Dynein light chain LC8-type 2,DYNLL2,Homo sapiens,Human
EIAAB10520 Cytoplasmic dynein 1 light intermediate chain 1,DLC-A,DNCLI1,DYNC1LI1,Dynein light chain A,Dynein light intermediate chain 1, cytosolic,Homo sapiens,Human,LIC1
EIAAB11426 Bithoraxoid-like protein,BLP,Dncl2a,Dnlc2a,Dynein light chain 2A, cytoplasmic,Dynein light chain roadblock-type 1,Dynein-associated protein Km23,Dynlrb1,Rat,Rattus norvegicus,robl_LC7-like protein
EIAAB10517 Cytoplasmic dynein 1 light intermediate chain 1,DLC-A,Dncli1,Dnclic1,Dync1li1,Dynein light chain A,Dynein light intermediate chain 1, cytosolic,Mouse,Mus musculus
EIAAB10519 Cytoplasmic dynein 1 light intermediate chain 1,DLC-A,Dncli1,Dync1li1,Dynein light chain A,Dynein light intermediate chain 1, cytosolic,Rat,Rattus norvegicus
EIAAB11425 BITH,Bithoraxoid-like protein,BLP,DNCL2A,DNLC2A,Dynein light chain 2A, cytoplasmic,Dynein light chain roadblock-type 1,Dynein-associated protein Km23,DYNLRB1,Homo sapiens,HSPC162,Human,Roadblock domai
EIAAB10518 Chicken,Cytoplasmic dynein 1 light intermediate chain 1,DLC-A,DNCLI1,DYNC1LI1,Dynein light chain A,Dynein light intermediate chain 1, cytosolic,Gallus gallus,LIC57_59
EIAAB11427 Dncl2a,Dnlc2a,Dynein light chain 2A, cytoplasmic,Dynein light chain roadblock-type 1,Dynlrb1,Mouse,Mus musculus
EIAAB11429 Dncl2b,Dnlc2b,Dynein light chain 2B, cytoplasmic,Dynein light chain roadblock-type 2,Dynlrb2,Mouse,Mus musculus
EIAAB11428 Bos taurus,Bovine,DNLC2A,Dynein light chain 2A, cytoplasmic,Dynein light chain roadblock-type 1,DYNLRB1
EIAAB11430 Bos taurus,Bovine,DNLC2B,Dynein light chain 2B, cytoplasmic,Dynein light chain roadblock-type 2,DYNLRB2
EIAAB12179 Bos taurus,Bovine,DNCL1,Dynein light chain 1, cytoplasmic,Dynein light chain LC8-type 1,DYNLL1
EIAAB12182 Dlc2,Dynein light chain 2, cytoplasmic,Dynein light chain LC8-type 2,Dynll2,Rat,Rattus norvegicus
EIAAB11431 DNCL2B,DNLC2B,Dynein light chain 2B, cytoplasmic,Dynein light chain roadblock-type 2,DYNLRB2,Homo sapiens,Human,Roadblock domain-containing protein 2,ROBLD2
EIAAB10523 Cytoplasmic dynein 1 light intermediate chain 2,DNCLI2,DYNC1LI2,Dynein light intermediate chain 2, cytosolic,Homo sapiens,Human,LIC2,LIC-2,LIC53_55
EIAAB10521 Cytoplasmic dynein 1 light intermediate chain 2,Dncli2,Dync1li2,Dynein light intermediate chain 2, cytosolic,LIC-2,LIC53_55,Rat,Rattus norvegicus
EIAAB10527 CGI-60,Cytoplasmic dynein 2 light intermediate chain 1,D2LIC,DYNC2LI1,Dynein 2 light intermediate chain,Homo sapiens,Human,LIC3
EIAAB10522 Cytoplasmic dynein 1 light intermediate chain 2,Dncli2,Dnclic2,Dync1li2,Dynein light intermediate chain 2, cytosolic,Mouse,Mus musculus
EIAAB12173 Cytoplasmic dynein 2 heavy chain,Cytoplasmic dynein 2 heavy chain 1,Dhc1b,Dlp4,Dnch2,Dnchc2,Dync2h1,Dynein cytoplasmic heavy chain 2,Dynein heavy chain isotype 1B,Dynein-like protein 4,Rat,Rattus norv
EIAAB12175 Cytoplasmic dynein 2 heavy chain,Cytoplasmic dynein 2 heavy chain 1,DHC1B,DHC2,DNCH2,DYH1B,DYNC2H1,Dynein cytoplasmic heavy chain 2,Dynein heavy chain 11,Dynein heavy chain isotype 1B,hDHC11,Homo sapi


 

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