DLRB1_HUMAN
ID DLRB1_HUMAN Reviewed; 96 AA.
AC Q9NP97; B1AKR5; Q5TC72; Q96IV3; Q9NQM2;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Dynein light chain roadblock-type 1;
DE AltName: Full=Bithoraxoid-like protein;
DE Short=BLP;
DE AltName: Full=Dynein light chain 2A, cytoplasmic;
DE AltName: Full=Dynein-associated protein Km23;
DE AltName: Full=Roadblock domain-containing protein 1;
GN Name=DYNLRB1; Synonyms=BITH, DNCL2A, DNLC2A, ROBLD1; ORFNames=HSPC162;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Liver, and Testis;
RX PubMed=11750132; DOI=10.1016/s0378-1119(01)00787-9;
RA Jiang J., Yu L., Huang X., Chen X., Li D., Zhang Y., Tang L., Zhao S.;
RT "Identification of two novel human dynein light chain genes, DNLC2A and
RT DNLC2B, and their expression changes in hepatocellular carcinoma tissues
RT from 68 Chinese patients.";
RL Gene 281:103-113(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hematopoietic stem cell;
RA Gu J., Huang Q., Yu Y., Xu S., Han Z., Fu G., Zhou J., Wang Y., Huang C.,
RA Ren S., Tu Y., Chen Z.;
RT "Novel genes expressed in hematopoietic stem/progenitor cells from
RT myelodysplastic syndrome patients.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Fracchiolla N.S., Cortelezzi A., Lambertenghi-Deliliers G.;
RT "BitH, a human homolog of bithorax Drosophila melanogaster gene, on
RT chromosome 20q.";
RL Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RA Tang Q., Staub C.M., Mulder K.M.;
RT "Km23: role in growth factor signaling.";
RL Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-10.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP PROTEIN SEQUENCE OF 16-52 AND 59-70, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP INTERACTION WITH DYNC1I1 AND DYNC1I2.
RX PubMed=12077152; DOI=10.1074/jbc.m205510200;
RA Susalka S.J., Nikulina K., Salata M.W., Vaughan P.S., King S.M.,
RA Vaughan K.T., Pfister K.K.;
RT "The roadblock light chain binds a novel region of the cytoplasmic Dynein
RT intermediate chain.";
RL J. Biol. Chem. 277:32939-32946(2002).
RN [11]
RP INTERACTION WITH RAP6A AND RAP6B.
RX PubMed=18044744; DOI=10.1002/cm.20254;
RA Wanschers B.F.J., van de Vorstenbosch R., Wijers M., Wieringa B.,
RA King S.M., Fransen J.;
RT "Rab6 family proteins interact with the dynein light chain protein
RT DYNLRB1.";
RL Cell Motil. Cytoskeleton 65:183-196(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP STRUCTURE BY NMR, AND SUBUNIT.
RX PubMed=16083906; DOI=10.1016/j.jmb.2005.07.002;
RA Ilangovan U., Ding W., Zhong Y., Wilson C.L., Groppe J.C., Trbovich J.T.,
RA Zuniga J., Demeler B., Tang Q., Gao G., Mulder K.M., Hinck A.P.;
RT "Structure and dynamics of the homodimeric dynein light chain km23.";
RL J. Mol. Biol. 352:338-354(2005).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SUBUNIT.
RX PubMed=16970917; DOI=10.1016/j.bbrc.2006.08.161;
RA Liu J.F., Wang Z.X., Wang X.Q., Tang Q., An X.M., Gui L.L., Liang D.C.;
RT "Crystal structure of human dynein light chain Dnlc2A: structural insights
RT into the interaction with IC74.";
RL Biochem. Biophys. Res. Commun. 349:1125-1129(2006).
CC -!- FUNCTION: Acts as one of several non-catalytic accessory components of
CC the cytoplasmic dynein 1 complex that are thought to be involved in
CC linking dynein to cargos and to adapter proteins that regulate dynein
CC function. Cytoplasmic dynein 1 acts as a motor for the intracellular
CC retrograde motility of vesicles and organelles along microtubules.
CC -!- SUBUNIT: Homodimer. The cytoplasmic dynein 1 complex consists of two
CC catalytic heavy chains (HCs) and a number of non-catalytic subunits
CC presented by intermediate chains (ICs), light intermediate chains
CC (LICs) and light chains (LCs); the composition seems to vary in respect
CC to the IC, LIC and LC composition. The heavy chain homodimer serves as
CC a scaffold for the probable homodimeric assembly of the respective non-
CC catalytic subunits. The ICs and LICs bind directly to the HC dimer and
CC the LCs assemble on the IC dimer. Self-associates. Interacts with
CC DYNLRB2. Interacts with DYNC1I1 and DYNC1I2. Interacts with RAB6A
CC isoform 1 (GTP-bound); the interaction is direct. Interacts with RAB6A
CC isoform 2 (GDP-bound); the interaction is direct. Interacts with RAB6B
CC (GDP-bound). {ECO:0000269|PubMed:12077152, ECO:0000269|PubMed:16083906,
CC ECO:0000269|PubMed:16970917, ECO:0000269|PubMed:18044744}.
CC -!- INTERACTION:
CC Q9NP97; O75575-2: CRCP; NbExp=3; IntAct=EBI-372128, EBI-12880830;
CC Q9NP97; Q13409: DYNC1I2; NbExp=5; IntAct=EBI-372128, EBI-742998;
CC Q9NP97; P43356: MAGEA2B; NbExp=3; IntAct=EBI-372128, EBI-5650739;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9NP97-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NP97-2; Sequence=VSP_007236, VSP_007237;
CC -!- TISSUE SPECIFICITY: High expression in heart, liver, brain and
CC pancreas; moderate in placenta, skeletal muscle and kidney; low in
CC lung, prostate, testis, small intestine and colon. Isoform 1 expression
CC is up-regulated in 64% hepatocellular carcinoma (HCC) patients.
CC {ECO:0000269|PubMed:11750132}.
CC -!- MISCELLANEOUS: [Isoform 2]: May result from the retention of an intron
CC in the cDNA. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GAMAD family. {ECO:0000305}.
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DR EMBL; AF132750; AAL75951.1; -; mRNA.
DR EMBL; AF165516; AAF86646.1; -; mRNA.
DR EMBL; AF178431; AAK95342.1; -; mRNA.
DR EMBL; AY026513; AAK18712.1; -; mRNA.
DR EMBL; AF161511; AAF29126.1; -; mRNA.
DR EMBL; AL109923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL136173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002481; AAH02481.1; -; mRNA.
DR EMBL; BC007223; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS13235.1; -. [Q9NP97-1]
DR RefSeq; NP_001268656.1; NM_001281727.1.
DR RefSeq; NP_001268657.1; NM_001281728.1.
DR RefSeq; NP_001268658.1; NM_001281729.1.
DR RefSeq; NP_054902.1; NM_014183.3. [Q9NP97-1]
DR RefSeq; NP_808852.1; NM_177953.2.
DR PDB; 1Z09; NMR; -; A/B=1-96.
DR PDB; 2B95; NMR; -; A/B=1-96.
DR PDB; 2E8J; NMR; -; A/B=1-96.
DR PDB; 2HZ5; X-ray; 2.10 A; A/B=1-96.
DR PDB; 6F1T; EM; 3.50 A; k/l/s/t=1-96.
DR PDB; 6F1Z; EM; 3.40 A; s/t=1-96.
DR PDB; 6F38; EM; 6.70 A; k/l/s/t=1-96.
DR PDB; 6F3A; EM; 8.20 A; k/l=1-96.
DR PDB; 6RLB; EM; 4.50 A; G/H=1-96.
DR PDB; 6SC2; EM; 3.90 A; G/H=1-96.
DR PDBsum; 1Z09; -.
DR PDBsum; 2B95; -.
DR PDBsum; 2E8J; -.
DR PDBsum; 2HZ5; -.
DR PDBsum; 6F1T; -.
DR PDBsum; 6F1Z; -.
DR PDBsum; 6F38; -.
DR PDBsum; 6F3A; -.
DR PDBsum; 6RLB; -.
DR PDBsum; 6SC2; -.
DR AlphaFoldDB; Q9NP97; -.
DR BMRB; Q9NP97; -.
DR SMR; Q9NP97; -.
DR BioGRID; 123715; 89.
DR ComplexPortal; CPX-5025; Cytoplasmic dynein complex, variant 1.
DR CORUM; Q9NP97; -.
DR IntAct; Q9NP97; 34.
DR MINT; Q9NP97; -.
DR STRING; 9606.ENSP00000349679; -.
DR iPTMnet; Q9NP97; -.
DR PhosphoSitePlus; Q9NP97; -.
DR BioMuta; DYNLRB1; -.
DR EPD; Q9NP97; -.
DR jPOST; Q9NP97; -.
DR MassIVE; Q9NP97; -.
DR MaxQB; Q9NP97; -.
DR PaxDb; Q9NP97; -.
DR PeptideAtlas; Q9NP97; -.
DR PRIDE; Q9NP97; -.
DR ProteomicsDB; 81939; -. [Q9NP97-1]
DR ProteomicsDB; 81940; -. [Q9NP97-2]
DR TopDownProteomics; Q9NP97-1; -. [Q9NP97-1]
DR TopDownProteomics; Q9NP97-2; -. [Q9NP97-2]
DR Antibodypedia; 4076; 78 antibodies from 21 providers.
DR DNASU; 83658; -.
DR Ensembl; ENST00000300469.13; ENSP00000300469.9; ENSG00000125971.17. [Q9NP97-2]
DR Ensembl; ENST00000357156.7; ENSP00000349679.2; ENSG00000125971.17. [Q9NP97-1]
DR GeneID; 83658; -.
DR KEGG; hsa:83658; -.
DR MANE-Select; ENST00000357156.7; ENSP00000349679.2; NM_014183.4; NP_054902.1.
DR UCSC; uc002xal.5; human. [Q9NP97-1]
DR CTD; 83658; -.
DR DisGeNET; 83658; -.
DR GeneCards; DYNLRB1; -.
DR HGNC; HGNC:15468; DYNLRB1.
DR HPA; ENSG00000125971; Low tissue specificity.
DR MIM; 607167; gene.
DR neXtProt; NX_Q9NP97; -.
DR OpenTargets; ENSG00000125971; -.
DR PharmGKB; PA27436; -.
DR VEuPathDB; HostDB:ENSG00000125971; -.
DR eggNOG; KOG4115; Eukaryota.
DR GeneTree; ENSGT00390000011067; -.
DR HOGENOM; CLU_113002_3_2_1; -.
DR InParanoid; Q9NP97; -.
DR OMA; CAMATLL; -.
DR PhylomeDB; Q9NP97; -.
DR TreeFam; TF315165; -.
DR PathwayCommons; Q9NP97; -.
DR Reactome; R-HSA-5620924; Intraflagellar transport.
DR SignaLink; Q9NP97; -.
DR SIGNOR; Q9NP97; -.
DR BioGRID-ORCS; 83658; 755 hits in 1053 CRISPR screens.
DR ChiTaRS; DYNLRB1; human.
DR EvolutionaryTrace; Q9NP97; -.
DR GeneWiki; DYNLRB1; -.
DR GenomeRNAi; 83658; -.
DR Pharos; Q9NP97; Tbio.
DR PRO; PR:Q9NP97; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9NP97; protein.
DR Bgee; ENSG00000125971; Expressed in Brodmann (1909) area 9 and 93 other tissues.
DR ExpressionAtlas; Q9NP97; baseline and differential.
DR Genevisible; Q9NP97; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0097542; C:ciliary tip; TAS:Reactome.
DR GO; GO:0005929; C:cilium; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
DR GO; GO:0030286; C:dynein complex; IPI:ComplexPortal.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0045505; F:dynein intermediate chain binding; IBA:GO_Central.
DR GO; GO:0003777; F:microtubule motor activity; NAS:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007632; P:visual behavior; ISS:UniProtKB.
DR InterPro; IPR016561; DYNLRB1/2.
DR InterPro; IPR004942; Roadblock/LAMTOR2_dom.
DR Pfam; PF03259; Robl_LC7; 1.
DR PIRSF; PIRSF009998; DLC7; 1.
DR SMART; SM00960; Robl_LC7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Dynein; Microtubule; Motor protein;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P62628,
FT ECO:0000269|PubMed:12665801"
FT CHAIN 2..96
FT /note="Dynein light chain roadblock-type 1"
FT /id="PRO_0000220955"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P62628"
FT VAR_SEQ 28..47
FT /note="IPIKSTMDNPTTTQYASLMH -> GWEPLGHCGDRSRPPAQGCP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007236"
FT VAR_SEQ 48..96
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007237"
FT VARIANT 13
FT /note="S -> R (in dbSNP:rs1063616)"
FT /id="VAR_049124"
FT VARIANT 71
FT /note="I -> F (in dbSNP:rs10036)"
FT /id="VAR_049125"
FT HELIX 6..12
FT /evidence="ECO:0007829|PDB:2HZ5"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:6F1T"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:2HZ5"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:6F1Z"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:2HZ5"
FT HELIX 36..60
FT /evidence="ECO:0007829|PDB:2HZ5"
FT STRAND 66..75
FT /evidence="ECO:0007829|PDB:2HZ5"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:2HZ5"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:2HZ5"
SQ SEQUENCE 96 AA; 10922 MW; AAE1EFCD372897B3 CRC64;
MAEVEETLKR LQSQKGVQGI IVVNTEGIPI KSTMDNPTTT QYASLMHSFI LKARSTVRDI
DPQNDLTFLR IRSKKNEIMV APDKDYFLIV IQNPTE
