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Reviewed, UniProtKB/Swiss-Prot P63167 (DYL1_HUMAN)

Last modified February 9, 2010. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dynein light chain 1, cytoplasmic
Alternative name(s):
    Dynein light chain LC8-type 1
    8 kDa dynein light chain
      Short name=DLC8
    Protein inhibitor of neuronal nitric oxide synthase
      Short name=PIN
Gene names
Name: DYNLL1
Synonyms: DLC1, DNCL1, DNCLC1, HDLC1
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length89 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May be involved in some aspects of dynein-related intracellular transport and motility. 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.

Subunit structure

Consists of at least two heavy chains and a number of intermediate and light chains. Interacts with rabies P protein By similarity. Interacts with TXNDC17. Ref.3

Subcellular location

Cytoplasm Ref.1.

Tissue specificity

Ubiquitous. Ref.1

Sequence similarities

Belongs to the dynein light chain family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 8989Dynein light chain 1, cytoplasmic
PRO_0000195125

Amino acid modifications

Modified residue361N6-acetyllysine Ref.6
Modified residue651Phosphotyrosine Ref.5

Secondary structure

............. 89
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P63167-1 [UniParc].

Last modified September 27, 2004. Version 1.
Checksum: F5E7647D092BEB3A

FASTA8910,366
        10         20         30         40         50         60 
MCDRKAVIKN ADMSEEMQQD SVECATQALE KYNIEKDIAA HIKKEFDKKY NPTWHCIVGR 

        70         80 
NFGSYVTHET KHFIYFYLGQ VAILLFKSG 

« Hide

References

« Hide 'large scale' references
[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: 8628263] [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]"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: 14607843] [Abstract]
Cited for: INTERACTION WITH TXNDC17.
[4]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[5]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-65, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[6]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-36, MASS SPECTROMETRY.
[7]"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: 10426949] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 5-89.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U32944 mRNA. Translation: AAB04149.1.
CR407672 mRNA. Translation: CAG28600.1.
IPIIPI00019329.
RefSeqNP_001032583.1.
NP_001032584.1.
NP_003737.1.
UniGeneHs.5120

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CMIX-ray2.50A/B5-89[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP63167. 30 interactions.
STRINGP63167.

PTM databases

PhosphoSiteP63167.

Proteomic databases

PeptideAtlasP63167.
PRIDEP63167.

Genome annotation databases

EnsemblENST00000242577; ENSP00000242577; ENSG00000088986; Homo sapiens. [Genome view]
ENST00000392508; ENSP00000376296; ENSG00000088986; Homo sapiens. [Genome view]
ENST00000392509; ENSP00000376297; ENSG00000088986; Homo sapiens. [Genome view]
GeneID8655.
KEGGhsa:8655.
UCSCuc001tyj.1. human.

Organism-specific databases

CTD8655.
GeneCardsGC12P119397.
H-InvDBHIX0029546.
HIX0034107.
HIX0036835.
HIX0037247.
HIX0059369.
HGNCHGNC:15476. DYNLL1.
MIM601562. gene.
PharmGKBPA134972261.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG20803.
HOGENOMHBG627578.
HOVERGENP63167.
InParanoidP63167.
PhylomeDBP63167.

Enzyme and pathway databases

ReactomeREACT_152. Cell Cycle, Mitotic.
REACT_578. Apoptosis.

Gene expression databases

ArrayExpressP63167.
BgeeP63167.
CleanExHS_DLC1.
HS_DYNLL1.
GenevestigatorP63167.
GermOnlineENSG00000088986. Homo sapiens.

Family and domain databases

InterProIPR019763. Dynein_light_1/2_CS.
IPR001372. Dynein_light_chain_typ-1/2.
[Graphical view]
Gene3DG3DSA:3.30.740.10. Dynein_light1. 1 hit.
PANTHERPTHR11886. Dynein_light1. 1 hit.
PfamPF01221. Dynein_light. 1 hit.
[Graphical view]
PROSITEPS01239. DYNEIN_LIGHT_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio32461.
SOURCESearch...

Entry information

Entry nameDYL1_HUMAN
AccessionPrimary (citable) accession number: P63167
Secondary accession number(s): Q15701
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: September 27, 2004
Last modified: February 9, 2010
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents