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Protein

Dynein light chain roadblock-type 1

Gene

Dynlrb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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.

GO - Molecular functioni

  • identical protein binding Source: UniProtKB
  • motor activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Motor protein

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiR-MMU-5620924. Intraflagellar transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Dynein light chain roadblock-type 1
Alternative name(s):
Dynein light chain 2A, cytoplasmic
Gene namesi
Name:Dynlrb1
Synonyms:Dncl2a, Dnlc2a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1914318. Dynlrb1.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: MGI
  • cytoplasm Source: UniProtKB
  • cytoplasmic dynein complex Source: UniProtKB
  • membrane Source: MGI
  • microtubule Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Dynein, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 9695Dynein light chain roadblock-type 1PRO_0000220956Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP62627.
MaxQBiP62627.
PaxDbiP62627.
PRIDEiP62627.
TopDownProteomicsiP62627.

2D gel databases

UCD-2DPAGEP62627.

PTM databases

iPTMnetiP62627.
PhosphoSiteiP62627.

Expressioni

Gene expression databases

BgeeiP62627.
CleanExiMM_DYNLRB1.
ExpressionAtlasiP62627. baseline and differential.
GenevisibleiP62627. MM.

Interactioni

Subunit structurei

Homodimer. 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 DYNC1I1 and DYNC1I2. Self-associates. Interacts with DYNLRB2. Interacts with RAB6A; the interaction is direct. Interacts with RAB6B (GDP-bound) (By similarity).By similarity

GO - Molecular functioni

  • identical protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi211916. 15 interactions.
IntActiP62627. 15 interactions.
MINTiMINT-4093134.
STRINGi10090.ENSMUSP00000105304.

Structurei

Secondary structure

1
96
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1312Combined sources
Beta strandi17 – 248Combined sources
Turni25 – 273Combined sources
Beta strandi28 – 347Combined sources
Helixi36 – 6025Combined sources
Beta strandi66 – 7510Combined sources
Beta strandi77 – 826Combined sources
Beta strandi84 – 929Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y4ONMR-A/B2-96[»]
ProteinModelPortaliP62627.
SMRiP62627. Positions 2-95.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62627.

Family & Domainsi

Sequence similaritiesi

Belongs to the GAMAD family.Curated

Phylogenomic databases

eggNOGiKOG4115. Eukaryota.
ENOG4111NDV. LUCA.
GeneTreeiENSGT00390000011067.
HOGENOMiHOG000232033.
HOVERGENiHBG058598.
InParanoidiP62627.
KOiK10419.
OrthoDBiEOG7X0VKJ.
PhylomeDBiP62627.
TreeFamiTF315165.

Family and domain databases

InterProiIPR016561. DYNLRB1/2.
IPR004942. Roadblock/LAMTOR2_dom.
[Graphical view]
PfamiPF03259. Robl_LC7. 1 hit.
[Graphical view]
PIRSFiPIRSF009998. DLC7. 1 hit.
SMARTiSM00960. Robl_LC7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62627-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEVEETLKR LQSQKGVQGI IVVNTEGIPI KSTMDNPTTT QYANLMHNFI
60 70 80 90
LKARSTVREI DPQNDLTFLR IRSKKNEIMV APDKDYFLIV IQNPTE
Length:96
Mass (Da):10,990
Last modified:January 23, 2007 - v3
Checksum:i666734B413AFE7D0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31E → D in BAB25768 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002359 mRNA. Translation: BAB22038.1.
AK003435 mRNA. Translation: BAB22788.1.
AK008595 mRNA. Translation: BAB25768.1.
AK166685 mRNA. Translation: BAE38944.1.
AL929588 Genomic DNA. Translation: CAM27181.1.
BC099423 mRNA. Translation: AAH99423.1.
BC125610 mRNA. Translation: AAI25611.1.
BC125648 mRNA. Translation: AAI25649.1.
CCDSiCCDS38294.1.
RefSeqiNP_080223.2. NM_025947.3.
UniGeneiMm.23693.

Genome annotation databases

EnsembliENSMUST00000109682; ENSMUSP00000105304; ENSMUSG00000047459.
GeneIDi67068.
KEGGimmu:67068.
UCSCiuc008nkg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002359 mRNA. Translation: BAB22038.1.
AK003435 mRNA. Translation: BAB22788.1.
AK008595 mRNA. Translation: BAB25768.1.
AK166685 mRNA. Translation: BAE38944.1.
AL929588 Genomic DNA. Translation: CAM27181.1.
BC099423 mRNA. Translation: AAH99423.1.
BC125610 mRNA. Translation: AAI25611.1.
BC125648 mRNA. Translation: AAI25649.1.
CCDSiCCDS38294.1.
RefSeqiNP_080223.2. NM_025947.3.
UniGeneiMm.23693.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y4ONMR-A/B2-96[»]
ProteinModelPortaliP62627.
SMRiP62627. Positions 2-95.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211916. 15 interactions.
IntActiP62627. 15 interactions.
MINTiMINT-4093134.
STRINGi10090.ENSMUSP00000105304.

PTM databases

iPTMnetiP62627.
PhosphoSiteiP62627.

2D gel databases

UCD-2DPAGEP62627.

Proteomic databases

EPDiP62627.
MaxQBiP62627.
PaxDbiP62627.
PRIDEiP62627.
TopDownProteomicsiP62627.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000109682; ENSMUSP00000105304; ENSMUSG00000047459.
GeneIDi67068.
KEGGimmu:67068.
UCSCiuc008nkg.2. mouse.

Organism-specific databases

CTDi83658.
MGIiMGI:1914318. Dynlrb1.

Phylogenomic databases

eggNOGiKOG4115. Eukaryota.
ENOG4111NDV. LUCA.
GeneTreeiENSGT00390000011067.
HOGENOMiHOG000232033.
HOVERGENiHBG058598.
InParanoidiP62627.
KOiK10419.
OrthoDBiEOG7X0VKJ.
PhylomeDBiP62627.
TreeFamiTF315165.

Enzyme and pathway databases

ReactomeiR-MMU-5620924. Intraflagellar transport.

Miscellaneous databases

ChiTaRSiDynlrb1. mouse.
EvolutionaryTraceiP62627.
PROiP62627.
SOURCEiSearch...

Gene expression databases

BgeeiP62627.
CleanExiMM_DYNLRB1.
ExpressionAtlasiP62627. baseline and differential.
GenevisibleiP62627. MM.

Family and domain databases

InterProiIPR016561. DYNLRB1/2.
IPR004942. Roadblock/LAMTOR2_dom.
[Graphical view]
PfamiPF03259. Robl_LC7. 1 hit.
[Graphical view]
PIRSFiPIRSF009998. DLC7. 1 hit.
SMARTiSM00960. Robl_LC7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryo, Kidney and Small intestine.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Oocyte.
  4. "The Roadblock light chains are ubiquitous components of cytoplasmic dynein that form homo- and heterodimers."
    Nikulina K., Patel-King R.S., Takebe S., Pfister K.K., King S.M.
    Cell Motil. Cytoskeleton 57:233-245(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SELF-ASSOCIATION, INTERACTION WITH DYNLRB2, IDENTIFICATION IN THE CYTOPLASMIC DYNEIN I COMPLEX.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Lung, Pancreas, Spleen and Testis.
  6. "Solution structure of isoform 1 of Roadblock/LC7, a light chain in the dynein complex."
    Song J., Tyler R.C., Lee M.S., Tyler E.M., Markley J.L.
    J. Mol. Biol. 354:1043-1051(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-96, SUBUNIT, INTERACTION WITH DYNC1I1.

Entry informationi

Entry nameiDLRB1_MOUSE
AccessioniPrimary (citable) accession number: P62627
Secondary accession number(s): A2AVR8
, O88567, Q4FZJ8, Q9D812
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.