Q9NP97 (DLRB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dynein light chain roadblock-type 1

Alternative name(s):
Bithoraxoid-like protein
Short name=BLP
Dynein light chain 2A, cytoplasmic
Dynein-associated protein Km23
Roadblock domain-containing protein 1

Gene names

Name:	DYNLRB1
Synonyms:	BITH, DNCL2A, DNLC2A, ROBLD1
ORF Names:	HSPC162

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	96 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Subunit structure	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. Self-associates. Interacts with DYNLRB2. Interacts with DYNC1I1 and DYNC1I2. Interacts with RAB6A isoform 1 (GTP-bound); the interaction is direct. Interacts with RAB6A isoform 2 (GDP-bound); the interaction is direct. Interacts with RAB6B (GDP-bound). Ref.10 Ref.11 Ref.13 Ref.14
Subcellular location	Cytoplasm › cytoskeleton.
Tissue specificity	High expression in heart, liver, brain and pancreas; moderate in placenta, skeletal muscle and kidney; low in lung, prostate, testis, small intestine and colon. Isoform 1 expression is up-regulated in 64% hepatocellular carcinoma (HCC) patients. Ref.1
Sequence similarities	Belongs to the GAMAD family.

Ontologies

Keywords
Biological process	Transport
Cellular component	Cytoplasm Cytoskeleton Dynein Microtubule
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Motor protein
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	microtubule-based movement Non-traceable author statement Ref.1. Source: UniProtKB transport Inferred from electronic annotation. Source: UniProtKB-KW visual behavior Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	centrosome Inferred from direct assay PubMed 21399614. Source: UniProtKB cytoplasmic dynein complex Inferred from sequence or structural similarity. Source: UniProtKB microtubule Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	microtubule motor activity Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Bcl2l11	O54918-2	3	EBI-372128,EBI-526080	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q9NP97-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9NP97-2)

The sequence of this isoform differs from the canonical sequence as follows:
     28-47: IPIKSTMDNPTTTQYASLMH → GWEPLGHCGDRSRPPAQGCP
     48-96: Missing.

Note: May result from the retention of an intron in the cDNA.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 96

95

Dynein light chain roadblock-type 1

PRO_0000220955

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Natural variations

Alternative sequence

28 – 47

20

IPIKS…ASLMH → GWEPLGHCGDRSRPPAQGCP in isoform 2.

VSP_007236

Alternative sequence

48 – 96

49

Missing in isoform 2.

VSP_007237

Natural variant

13

1

S → R.
Corresponds to variant rs1063616 [ dbSNP | Ensembl ].

VAR_049124

Natural variant

71

1

I → F.
Corresponds to variant rs10036 [ dbSNP | Ensembl ].

VAR_049125

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

96

Helix Strand Turn

Details...

Helix

6 – 12

7

Beta strand

17 – 23

7

Beta strand

25 – 27

3

Beta strand

29 – 34

6

Helix

36 – 60

25

Beta strand

66 – 75

10

Beta strand

77 – 81

5

Beta strand

87 – 92

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: AAE1EFCD372897B3	FASTA	96	10,922
	10 20 30 40 50 60 MAEVEETLKR LQSQKGVQGI IVVNTEGIPI KSTMDNPTTT QYASLMHSFI LKARSTVRDI 70 80 90 DPQNDLTFLR IRSKKNEIMV APDKDYFLIV IQNPTE
	Isoform 2 [UniParc]. Checksum: 17421DC72701A8A2	FASTA	47	5,060
	10 20 30 40 MAEVEETLKR LQSQKGVQGI IVVNTEGGWE PLGHCGDRSR PPAQGCP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of two novel human dynein light chain genes, DNLC2A and DNLC2B, and their expression changes in hepatocellular carcinoma tissues from 68 Chinese patients." Jiang J., Yu L., Huang X., Chen X., Li D., Zhang Y., Tang L., Zhao S. Gene 281:103-113(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Liver and Testis.
[2]	"Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndrome patients." Gu J., Huang Q., Yu Y., Xu S., Han Z., Fu G., Zhou J., Wang Y., Huang C., Ren S., Tu Y., Chen Z. Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Hematopoietic stem cell.
[3]	"BitH, a human homolog of bithorax Drosophila melanogaster gene, on chromosome 20q." Fracchiolla N.S., Cortelezzi A., Lambertenghi-Deliliers G. Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"Km23: role in growth factor signaling." Tang Q., Staub C.M., Mulder K.M. Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Placenta.
[5]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Umbilical cord blood.
[6]	"The DNA sequence and comparative analysis of human chromosome 20." Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J. Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] (ISOFORMS 1 AND 2). Tissue: Kidney and Lymph.
[8]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-10. Tissue: Platelet.
[9]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 16-52 AND 59-70, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[10]	"The roadblock light chain binds a novel region of the cytoplasmic Dynein intermediate chain." Susalka S.J., Nikulina K., Salata M.W., Vaughan P.S., King S.M., Vaughan K.T., Pfister K.K. J. Biol. Chem. 277:32939-32946(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DYNC1I1 AND DYNC1I2.
[11]	"Rab6 family proteins interact with the dynein light chain protein DYNLRB1." Wanschers B.F.J., van de Vorstenbosch R., Wijers M., Wieringa B., King S.M., Fransen J. Cell Motil. Cytoskeleton 65:183-196(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAP6A AND RAP6B.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"Structure and dynamics of the homodimeric dynein light chain km23." Ilangovan U., Ding W., Zhong Y., Wilson C.L., Groppe J.C., Trbovich J.T., Zuniga J., Demeler B., Tang Q., Gao G., Mulder K.M., Hinck A.P. J. Mol. Biol. 352:338-354(2005) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR, SUBUNIT.
[14]	"Crystal structure of human dynein light chain Dnlc2A: structural insights into the interaction with IC74." Liu J.F., Wang Z.X., Wang X.Q., Tang Q., An X.M., Gui L.L., Liang D.C. Biochem. Biophys. Res. Commun. 349:1125-1129(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF132750 mRNA. Translation: AAL75951.1.
AF165516 mRNA. Translation: AAF86646.1.
AF178431 mRNA. Translation: AAK95342.1.
AY026513 mRNA. Translation: AAK18712.1.
AF161511 mRNA. Translation: AAF29126.1.
AL109923, AL136173 Genomic DNA. Translation: CAI21456.1.
AL136173, AL109923 Genomic DNA. Translation: CAI23308.1.
AL109923, AL136173 Genomic DNA. Translation: CAM28250.1.
AL136173, AL109923 Genomic DNA. Translation: CAM28343.1.
BC002481 mRNA. Translation: AAH02481.1.
BC007223 mRNA. No translation available.

IPI

IPI00063849.
IPI00643583.

RefSeq

NP_054902.1. NM_014183.2.

UniGene

Hs.593920.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Z09	NMR	-	A/B	1-96	[»]
2B95	NMR	-	A/B	1-96	[»]
2E8J	NMR	-	A/B	1-96	[»]
2HZ5	X-ray	2.10	A/B	1-96	[»]

ProteinModelPortal

Q9NP97.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NP97. 12 interactions.

MINT

MINT-1485399.

STRING

9606.ENSP00000349679.

PTM databases

PhosphoSite

Q9NP97.

Polymorphism databases

DMDM

30172967.

Proteomic databases

PaxDb

Q9NP97.

PRIDE

Q9NP97.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000300469; ENSP00000300469; ENSG00000125971.
ENST00000357156; ENSP00000349679; ENSG00000125971.

GeneID

83658.

KEGG

hsa:83658.

UCSC

uc002xal.3. human.

Organism-specific databases

CTD

83658.

GeneCards

GC20P033104.

HGNC

HGNC:15468. DYNLRB1.

HPA

CAB009845.

MIM

607167. gene.

neXtProt

NX_Q9NP97.

PharmGKB

PA27436.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG309619.

HOGENOM

HOG000232033.

HOVERGEN

HBG058598.

KO

K10419.

OrthoDB

EOG47PX7H.

PhylomeDB

Q9NP97.

Enzyme and pathway databases

Pathway_Interaction_DB

tgfbrpathway. TGF-beta receptor signaling.

Gene expression databases

ArrayExpress

Q9NP97.

Bgee

Q9NP97.

CleanEx

HS_DYNLRB1.

Genevestigator

Q9NP97.

GermOnline

ENSG00000125971. Homo sapiens.

Family and domain databases

InterPro

IPR004942. Dynein_light-rel.
IPR016561. Dynein_light_roadblock-type.
[Graphical view]

Pfam

PF03259. Robl_LC7. 1 hit.
[Graphical view]

PIRSF

PIRSF009998. DLC7. 1 hit.

SMART

SM00960. Robl_LC7. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

DYNLRB1. human.

EvolutionaryTrace

Q9NP97.

GenomeRNAi

83658.

NextBio

72623.

SOURCE

Search...

Entry information

Entry name

DLRB1_HUMAN

Accession

Primary (citable) accession number: Q9NP97
Secondary accession number(s): B1AKR5 , Q5TC72, Q96IV3, Q9NQM2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 23, 2003
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.