DC1L1_MOUSE - dbPTM
DC1L1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DC1L1_MOUSE
UniProt AC Q8R1Q8
Protein Name Cytoplasmic dynein 1 light intermediate chain 1
Gene Name Dync1li1
Organism Mus musculus (Mouse).
Sequence Length 523
Subcellular Localization Cytoplasm. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle pole.
Protein 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 binding dynein to membranous organelles or chromosomes. Probably involved in the microtubule-dependent transport of pericentrin. Is required for progress through the spindle assembly checkpoint. The phosphorylated form appears to be involved in the selective removal of MAD1L1 and MAD1L2 but not BUB1B from kinetochores (By similarity)..
Protein Sequence MAAVGRVGSFGSSPPGLASTYASGPLANELASGSGGPAAGDDEDGQNLWSCILSEVSTRSRSKLPTGKNVLLLGEDGAGKTSLIRRIQGIEEYKKGRGLEYLYLNVHDEDRDDQTRCNVWILDGDLYHKGLLKFSLDALSLRDTLVMLVVDMSKPWTALDSLQKWASVVREHVDKLKIPPEEMKEMEQKLIRDFQEYVEPGEDFPASPQRRTTGAQEDRGDSVVLPLGADTLTHNLGLPVLVVCTKCDAISVLEKEHDYRDEHFDFIQSHIRKFCLQYGAALIYTSVKENKNIDLVYKYIVQKLYGFPYKIPAVVVEKDAVFIPAGWDNDKKIGILHENFQTLKVEDNFEDIITKPPVRKFVHEKEIMAEDDQVFLMKLQSLLAKQPPTAAGRPVDASPRVPGGSPRTPNRSVSSNVASVSPIPAGSKKIDPNMKAGATSEGVLANFFNSLLSKKTGSPGGPGVGGSPGGGAAGASPSLPPSAKKSGQKPVLSDVHAELDRITRKPASVSPTTPTSPTEGEAS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
9PhosphorylationAAVGRVGSFGSSPPG
CCCCCCCCCCCCCCC		24.4723649490
12PhosphorylationGRVGSFGSSPPGLAS
CCCCCCCCCCCCHHH		37.3523649490
13PhosphorylationRVGSFGSSPPGLAST
CCCCCCCCCCCHHHC		35.1823649490
20PhosphorylationSPPGLASTYASGPLA
CCCCHHHCCCCCCHH		19.9428059163
32PhosphorylationPLANELASGSGGPAA
CHHHHHHCCCCCCCC		46.2223649490
34PhosphorylationANELASGSGGPAAGD
HHHHHCCCCCCCCCC		37.7723649490
63AcetylationVSTRSRSKLPTGKNV
HHCCCCCCCCCCCEE		58.336568501
197PhosphorylationLIRDFQEYVEPGEDF
HHHHHHHHCCCCCCC		10.1825619855
207PhosphorylationPGEDFPASPQRRTTG
CCCCCCCCCCCCCCC		23.0824925903
212PhosphorylationPASPQRRTTGAQEDR
CCCCCCCCCCCCCCC		31.6022802335
213PhosphorylationASPQRRTTGAQEDRG
CCCCCCCCCCCCCCC		28.80-
233PhosphorylationPLGADTLTHNLGLPV
ECCCCHHHHCCCCCE		15.7122802335
303AcetylationVYKYIVQKLYGFPYK
HHHHHHHHHHCCCCC		32.5522826441
385UbiquitinationKLQSLLAKQPPTAAG
HHHHHHHCCCCCCCC		64.41-
385MalonylationKLQSLLAKQPPTAAG
HHHHHHHCCCCCCCC		64.4132601280
389PhosphorylationLLAKQPPTAAGRPVD
HHHCCCCCCCCCCCC		35.5023140645
398PhosphorylationAGRPVDASPRVPGGS
CCCCCCCCCCCCCCC		14.5825619855
405PhosphorylationSPRVPGGSPRTPNRS
CCCCCCCCCCCCCCC		19.6823527152
408PhosphorylationVPGGSPRTPNRSVSS
CCCCCCCCCCCCCCC		28.4424899341
412PhosphorylationSPRTPNRSVSSNVAS
CCCCCCCCCCCCCCC		32.7525521595
414PhosphorylationRTPNRSVSSNVASVS
CCCCCCCCCCCCCCC		19.9025521595
415PhosphorylationTPNRSVSSNVASVSP
CCCCCCCCCCCCCCC		32.9225521595
419PhosphorylationSVSSNVASVSPIPAG
CCCCCCCCCCCCCCC		20.8825293948
421PhosphorylationSSNVASVSPIPAGSK
CCCCCCCCCCCCCCC		18.0226824392
427PhosphorylationVSPIPAGSKKIDPNM
CCCCCCCCCCCCCCC		32.6425619855
428AcetylationSPIPAGSKKIDPNMK
CCCCCCCCCCCCCCC		53.4870977
435UbiquitinationKKIDPNMKAGATSEG
CCCCCCCCCCCCCHH		50.76-
439PhosphorylationPNMKAGATSEGVLAN
CCCCCCCCCHHHHHH		26.7923984901
440PhosphorylationNMKAGATSEGVLANF
CCCCCCCCHHHHHHH		31.6423984901
453PhosphorylationNFFNSLLSKKTGSPG
HHHHHHHCCCCCCCC		37.0829899451
455UbiquitinationFNSLLSKKTGSPGGP
HHHHHCCCCCCCCCC		55.53-
456PhosphorylationNSLLSKKTGSPGGPG
HHHHCCCCCCCCCCC		46.7824759943
458PhosphorylationLLSKKTGSPGGPGVG
HHCCCCCCCCCCCCC		26.1324759943
467PhosphorylationGGPGVGGSPGGGAAG
CCCCCCCCCCCCCCC		17.9124759943
476PhosphorylationGGGAAGASPSLPPSA
CCCCCCCCCCCCCCC		17.6927180971
478PhosphorylationGAAGASPSLPPSAKK
CCCCCCCCCCCCCCC		51.5227180971
482PhosphorylationASPSLPPSAKKSGQK
CCCCCCCCCCCCCCC		51.2727180971
486PhosphorylationLPPSAKKSGQKPVLS
CCCCCCCCCCCCCHH		45.8328066266
503PhosphorylationHAELDRITRKPASVS
HHHHHHHCCCCCCCC		33.2720531401
508PhosphorylationRITRKPASVSPTTPT
HHCCCCCCCCCCCCC		31.4924925903
510PhosphorylationTRKPASVSPTTPTSP
CCCCCCCCCCCCCCC		17.6524925903
512PhosphorylationKPASVSPTTPTSPTE
CCCCCCCCCCCCCCC		37.5925521595
513PhosphorylationPASVSPTTPTSPTEG
CCCCCCCCCCCCCCC		28.1424925903
515PhosphorylationSVSPTTPTSPTEGEA
CCCCCCCCCCCCCCC		45.2924925903
516PhosphorylationVSPTTPTSPTEGEAS
CCCCCCCCCCCCCCC		30.9124925903
518PhosphorylationPTTPTSPTEGEAS--
CCCCCCCCCCCCC--		57.2924925903
523PhosphorylationSPTEGEAS-------
CCCCCCCC-------		36.1324925903
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
516SPhosphorylationKinaseMAPK1P63085
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DC1L1_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of DC1L1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ASSY_HUMANASS1physical
26496610
BLMH_HUMANBLMHphysical
26496610
LYST_HUMANLYSTphysical
26496610
DCTN1_HUMANDCTN1physical
26496610
DYHC1_HUMANDYNC1H1physical
26496610
DC1I2_HUMANDYNC1I2physical
26496610
DC1L2_HUMANDYNC1LI2physical
26496610
DYN2_HUMANDNM2physical
26496610
BPTF_HUMANBPTFphysical
26496610
I5P2_HUMANINPP5Bphysical
26496610
MSH3_HUMANMSH3physical
26496610
PIPNA_HUMANPITPNAphysical
26496610
ROCK1_HUMANROCK1physical
26496610
AAAT_HUMANSLC1A5physical
26496610
SSRG_HUMANSSR3physical
26496610
DYLT1_HUMANDYNLT1physical
26496610
SF01_HUMANSF1physical
26496610
KCAB2_HUMANKCNAB2physical
26496610
DYL1_HUMANDYNLL1physical
26496610
BCL7B_HUMANBCL7Bphysical
26496610
PSMD6_HUMANPSMD6physical
26496610
PJA2_HUMANPJA2physical
26496610
SCAM3_HUMANSCAMP3physical
26496610
SPN1_HUMANSNUPNphysical
26496610
ACTZ_HUMANACTR1Aphysical
26496610
DCTN2_HUMANDCTN2physical
26496610
F1142_HUMANFAM114A2physical
26496610
DCTN3_HUMANDCTN3physical
26496610
DNJC8_HUMANDNAJC8physical
26496610
COBL1_HUMANCOBLL1physical
26496610
FND3A_HUMANFNDC3Aphysical
26496610
TBC9B_HUMANTBC1D9Bphysical
26496610
SI1L3_HUMANSIPA1L3physical
26496610
MGAP_HUMANMGAphysical
26496610
SR140_HUMANU2SURPphysical
26496610
HIG1A_HUMANHIGD1Aphysical
26496610
GOLI4_HUMANGOLIM4physical
26496610
RNC_HUMANDROSHAphysical
26496610
AGRE2_HUMANEMR2physical
26496610
IMPCT_HUMANIMPACTphysical
26496610
SUGP1_HUMANSUGP1physical
26496610
TTC31_HUMANTTC31physical
26496610
RHG39_HUMANARHGAP39physical
26496610
MED25_HUMANMED25physical
26496610
DLRB1_HUMANDYNLRB1physical
26496610
ANM9_HUMANPRMT9physical
26496610
ASB6_HUMANASB6physical
26496610
TTC9C_HUMANTTC9Cphysical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DC1L1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510 AND SER-516, ANDMASS SPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510; THR-513; THR-515AND SER-516, AND MASS SPECTROMETRY.
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-510; THR-515AND THR-518, AND MASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-405, ANDMASS SPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; THR-513 ANDSER-516, AND MASS SPECTROMETRY.

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