UniProt Accession

 DYL1_HUMAN; P63167; Q15701 

Genbank Protein ID

 U32944; CR407672 

Genbank Nucleotide ID

 AAB04149.1; CAG28600.1 

Protein Name

 Dynein light chain 1, cytoplasmic 

Protein Synonyms/Alias

 8 kDa dynein light chain; DLC8; Dynein light chain LC8-type 1; Protein inhibitor of neuronal nitric oxide synthase; PIN 

Gene Name

 DYNLL1 

Gene Synonyms/Alias

 DLC1; DNCL1; DNCLC1; HDLC1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
9	CDRKAVIKNADMSEE	ubiquitination	[1]
31	CATQALEKYNIEKDI	ubiquitination	[1, 2]
36	LEKYNIEKDIAAHIK	acetylation	[3]
36	LEKYNIEKDIAAHIK	ubiquitination	[1, 4, 5, 6, 7, 8]
43	KDIAAHIKKEFDKKY	ubiquitination	[1]
44	DIAAHIKKEFDKKYN	ubiquitination	[1]
48	HIKKEFDKKYNPTWH	ubiquitination	[1]
49	IKKEFDKKYNPTWHC	methylation	[9]
49	IKKEFDKKYNPTWHC	ubiquitination	[1, 2, 5, 7, 8, 10]

Reference

 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [7] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [8] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [9] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [10] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 

Functional Description

 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. 

Sequence Annotation

 REGION 67 89 Interaction with ESR1.
 MOD_RES 36 36 N6-acetyllysine.
 MOD_RES 88 88 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Activator; Apoptosis; Complete proteome; Cytoplasm; Cytoskeleton; Dynein; Host-virus interaction; Microtubule; Mitochondrion; Motor protein; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 89 AA 

Protein Sequence

Gene Ontology

 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0000776; C:kinetochore; IDA:UniProtKB.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
 GO:0072686; C:mitotic spindle; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0003774; F:motor activity; TAS:ProtInc.
 GO:0030235; F:nitric-oxide synthase regulator activity; IEA:Compara.
 GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
 GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
 GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
 GO:0007292; P:female gamete generation; TAS:ProtInc.
 GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
 GO:0097193; P:intrinsic apoptotic signaling pathway; TAS:Reactome.
 GO:0007017; P:microtubule-based process; IEA:InterPro.
 GO:0042326; P:negative regulation of phosphorylation; IDA:UniProtKB.
 GO:1900740; P:positive regulation of protein insertion into mitochondrial membrane involved in apoptotic signaling pathway; TAS:Reactome.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006810; P:transport; IEA:UniProtKB-KW.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 

Interpro

 IPR019763; Dynein_light_1/2_CS.
 IPR001372; Dynein_light_chain_typ-1/2. 

Pfam

 PF01221; Dynein_light 

SMART

  

PROSITE

 PS01239; DYNEIN_LIGHT_1 

PRINTS