DC1L2_HUMAN - dbPTM
DC1L2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DC1L2_HUMAN
UniProt AC O43237
Protein Name Cytoplasmic dynein 1 light intermediate chain 2
Gene Name DYNC1LI2
Organism Homo sapiens (Human).
Sequence Length 492
Subcellular Localization Cytoplasm, cytoskeleton.
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..
Protein Sequence MAPVGVEKKLLLGPNGPAVAAAGDLTSEEEEGQSLWSSILSEVSTRARSKLPSGKNILVFGEDGSGKTTLMTKLQGAEHGKKGRGLEYLYLSVHDEDRDDHTRCNVWILDGDLYHKGLLKFAVSAESLPETLVIFVADMSRPWTVMESLQKWASVLREHIDKMKIPPEKMRELERKFVKDFQDYMEPEEGCQGSPQRRGPLTSGSDEENVALPLGDNVLTHNLGIPVLVVCTKCDAVSVLEKEHDYRDEHLDFIQSHLRRFCLQYGAALIYTSVKEEKNLDLLYKYIVHKTYGFHFTTPALVVEKDAVFIPAGWDNEKKIAILHENFTTVKPEDAYEDFIVKPPVRKLVHDKELAAEDEQVFLMKQQSLLAKQPATPTRASESPARGPSGSPRTQGRGGPASVPSSSPGTSVKKPDPNIKNNAASEGVLASFFNSLLSKKTGSPGSPGAGGVQSTAKKSGQKTVLSNVQEELDRMTRKPDSMVTNSSTENEA
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
26PhosphorylationVAAAGDLTSEEEEGQ
EEECCCCCCHHHHHH		38.5420873877
27PhosphorylationAAAGDLTSEEEEGQS
EECCCCCCHHHHHHH		50.7520873877
34PhosphorylationSEEEEGQSLWSSILS
CHHHHHHHHHHHHHH		42.5420873877
37PhosphorylationEEGQSLWSSILSEVS
HHHHHHHHHHHHHHH		16.8829523821
38PhosphorylationEGQSLWSSILSEVST
HHHHHHHHHHHHHHH		18.9029523821
53PhosphorylationRARSKLPSGKNILVF
HHHHCCCCCCEEEEE		73.2224719451
55MethylationRSKLPSGKNILVFGE
HHCCCCCCEEEEEEC		45.1923644510
55MethylationRSKLPSGKNILVFGE
HHCCCCCCEEEEEEC		45.19-
55UbiquitinationRSKLPSGKNILVFGE
HHCCCCCCEEEEEEC		45.19-
104GlutathionylationDRDDHTRCNVWILDG
CCCCCCCEEEEEECC		5.1822555962
184PhosphorylationFVKDFQDYMEPEEGC
HHHHHHHHCCCCCCC		7.8122167270
185SulfoxidationVKDFQDYMEPEEGCQ
HHHHHHHCCCCCCCC		10.4830846556
194PhosphorylationPEEGCQGSPQRRGPL
CCCCCCCCCCCCCCC		7.6219664994
202PhosphorylationPQRRGPLTSGSDEEN
CCCCCCCCCCCCCCC		33.8925159151
203PhosphorylationQRRGPLTSGSDEENV
CCCCCCCCCCCCCCE		43.9425159151
205PhosphorylationRGPLTSGSDEENVAL
CCCCCCCCCCCCEEE		41.4325159151
220PhosphorylationPLGDNVLTHNLGIPV
ECCCCHHHCCCCCCE		12.3928450419
232PhosphorylationIPVLVVCTKCDAVSV
CCEEEEEECCCHHHH		24.0922777824
284PhosphorylationEKNLDLLYKYIVHKT
HCCHHHHHHHHHHHH		14.7220068231
291PhosphorylationYKYIVHKTYGFHFTT
HHHHHHHHCCCCCCC		17.6320071362
292PhosphorylationKYIVHKTYGFHFTTP
HHHHHHHCCCCCCCC		23.6920071362
297PhosphorylationKTYGFHFTTPALVVE
HHCCCCCCCCEEEEE		24.2520071362
318UbiquitinationPAGWDNEKKIAILHE
CCCCCCHHHEEEEEE		56.59-
331UbiquitinationHENFTTVKPEDAYED
EECCEECCHHHHCCC		40.37-
336PhosphorylationTVKPEDAYEDFIVKP
ECCHHHHCCCCCCCC		28.4921253578
352MalonylationVRKLVHDKELAAEDE
CCHHCCCHHHHHHHH		39.4926320211
364SulfoxidationEDEQVFLMKQQSLLA
HHHHHHHHHHHHHHH		2.2130846556
368PhosphorylationVFLMKQQSLLAKQPA
HHHHHHHHHHHCCCC		23.9029514088
372UbiquitinationKQQSLLAKQPATPTR
HHHHHHHCCCCCCCC		57.70-
376PhosphorylationLLAKQPATPTRASES
HHHCCCCCCCCCCCC		31.6923663014
378PhosphorylationAKQPATPTRASESPA
HCCCCCCCCCCCCCC		34.2223663014
381PhosphorylationPATPTRASESPARGP
CCCCCCCCCCCCCCC		35.0026846344
383PhosphorylationTPTRASESPARGPSG
CCCCCCCCCCCCCCC		22.7422167270
389PhosphorylationESPARGPSGSPRTQG
CCCCCCCCCCCCCCC		55.5222167270
391PhosphorylationPARGPSGSPRTQGRG
CCCCCCCCCCCCCCC		18.6222167270
393MethylationRGPSGSPRTQGRGGP
CCCCCCCCCCCCCCC		41.18-
394PhosphorylationGPSGSPRTQGRGGPA
CCCCCCCCCCCCCCC		38.4723090842
397MethylationGSPRTQGRGGPASVP
CCCCCCCCCCCCCCC		36.7624129315
402PhosphorylationQGRGGPASVPSSSPG
CCCCCCCCCCCCCCC		37.3825159151
405PhosphorylationGGPASVPSSSPGTSV
CCCCCCCCCCCCCCC		41.0930266825
406PhosphorylationGPASVPSSSPGTSVK
CCCCCCCCCCCCCCC		34.1930266825
407PhosphorylationPASVPSSSPGTSVKK
CCCCCCCCCCCCCCC		31.5222167270
410PhosphorylationVPSSSPGTSVKKPDP
CCCCCCCCCCCCCCC		33.4630266825
411PhosphorylationPSSSPGTSVKKPDPN
CCCCCCCCCCCCCCC		37.5430266825
425PhosphorylationNIKNNAASEGVLASF
CCCCCCCHHHHHHHH		32.2624719451
435PhosphorylationVLASFFNSLLSKKTG
HHHHHHHHHHCCCCC		26.0724719451
438PhosphorylationSFFNSLLSKKTGSPG
HHHHHHHCCCCCCCC		37.0824719451
440UbiquitinationFNSLLSKKTGSPGSP
HHHHHCCCCCCCCCC		55.53-
441PhosphorylationNSLLSKKTGSPGSPG
HHHHCCCCCCCCCCC		46.7822167270
443PhosphorylationLLSKKTGSPGSPGAG
HHCCCCCCCCCCCCC		31.1822167270
446PhosphorylationKKTGSPGSPGAGGVQ
CCCCCCCCCCCCCCC		24.4422167270
454PhosphorylationPGAGGVQSTAKKSGQ
CCCCCCCCCCCHHCC		28.1123927012
455PhosphorylationGAGGVQSTAKKSGQK
CCCCCCCCCCHHCCC		25.9623663014
459PhosphorylationVQSTAKKSGQKTVLS
CCCCCCHHCCCCHHH		45.8321712546
462UbiquitinationTAKKSGQKTVLSNVQ
CCCHHCCCCHHHHHH		44.09-
466PhosphorylationSGQKTVLSNVQEELD
HCCCCHHHHHHHHHH		30.5321712546
482SulfoxidationMTRKPDSMVTNSSTE
HHCCCCCCCCCCCCC		5.8521406390
484PhosphorylationRKPDSMVTNSSTENE
CCCCCCCCCCCCCCC		22.2723090842
486PhosphorylationPDSMVTNSSTENEA-
CCCCCCCCCCCCCC-		29.3023403867
487PhosphorylationDSMVTNSSTENEA--
CCCCCCCCCCCCC--		41.6425159151
488PhosphorylationSMVTNSSTENEA---
CCCCCCCCCCCC---		42.5223403867
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
-KUbiquitinationE3 ubiquitin ligaseTRIM58Q8NG06
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DC1L2_HUMAN !!
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 DC1L2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
DYHC1_HUMANDYNC1H1physical
22939629
DYLT1_HUMANDYNLT1physical
22939629
DYLT3_HUMANDYNLT3physical
22939629
DYHC1_HUMANDYNC1H1physical
22863883
DC1I2_HUMANDYNC1I2physical
22863883
DC1L1_HUMANDYNC1LI1physical
22863883
DYL1_HUMANDYNLL1physical
22863883
EIF3K_HUMANEIF3Kphysical
22863883
RACK1_HUMANGNB2L1physical
22863883
ROA2_HUMANHNRNPA2B1physical
22863883
RSSA_HUMANRPSAphysical
22863883
NMT1_HUMANNMT1physical
22863883
RS23_HUMANRPS23physical
22863883
RS26_HUMANRPS26physical
22863883
RS5_HUMANRPS5physical
22863883
YBOX1_HUMANYBX1physical
22863883
DYHC1_HUMANDYNC1H1physical
26344197
DYLT1_HUMANDYNLT1physical
26344197
DYLT1_HUMANDYNLT1physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DC1L2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-407; THR-441;SER-443; SER-446 AND SER-487, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-383; SER-391;SER-443 AND SER-446, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194; SER-443 ANDSER-446, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-446, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND MASSSPECTROMETRY.

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