DC1L1_HUMAN - dbPTM
DC1L1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DC1L1_HUMAN
UniProt AC Q9Y6G9
Protein Name Cytoplasmic dynein 1 light intermediate chain 1
Gene Name DYNC1LI1
Organism Homo sapiens (Human).
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..
Protein Sequence MAAVGRVGSFGSSPPGLSSTYTGGPLGNEIASGNGGAAAGDDEDGQNLWSCILSEVSTRSRSKLPAGKNVLLLGEDGAGKTSLIRKIQGIEEYKKGRGLEYLYLNVHDEDRDDQTRCNVWILDGDLYHKGLLKFSLDAVSLKDTLVMLVVDMSKPWTALDSLQKWASVVREHVDKLKIPPEEMKQMEQKLIRDFQEYVEPGEDFPASPQRRNTASQEDKDDSVVLPLGADTLTHNLGIPVLVVCTKCDAISVLEKEHDYRDEHFDFIQSHIRKFCLQYGAALIYTSVKENKNIDLVYKYIVQKLYGFPYKIPAVVVEKDAVFIPAGWDNDKKIGILHENFQTLKAEDNFEDIITKPPVRKFVHEKEIMAEDDQVFLMKLQSLLAKQPPTAAGRPVDASPRVPGGSPRTPNRSVSSNVASVSPIPAGSKKIDPNMKAGATSEGVLANFFNSLLSKKTGSPGGPGVSGGSPAGGAGGGSSGLPPSTKKSGQKPVLDVHAELDRITRKPVTVSPTTPTSPTEGEAS
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		24.4720068231
12PhosphorylationGRVGSFGSSPPGLSS
CCCCCCCCCCCCCCC		37.3520068231
13PhosphorylationRVGSFGSSPPGLSST
CCCCCCCCCCCCCCC		35.1828464451
18PhosphorylationGSSPPGLSSTYTGGP
CCCCCCCCCCCCCCC		26.9226074081
19PhosphorylationSSPPGLSSTYTGGPL
CCCCCCCCCCCCCCC		30.4026074081
20PhosphorylationSPPGLSSTYTGGPLG
CCCCCCCCCCCCCCC		23.0226074081
21PhosphorylationPPGLSSTYTGGPLGN
CCCCCCCCCCCCCCC		12.8226074081
22PhosphorylationPGLSSTYTGGPLGNE
CCCCCCCCCCCCCCC		35.4326074081
32PhosphorylationPLGNEIASGNGGAAA
CCCCCCCCCCCCCCC		38.1528464451
50PhosphorylationEDGQNLWSCILSEVS
CCCCCHHHHHHHHHC		8.4120068231
54PhosphorylationNLWSCILSEVSTRSR
CHHHHHHHHHCCCCC		18.9520068231
57PhosphorylationSCILSEVSTRSRSKL
HHHHHHHCCCCCCCC		17.6620873877
58PhosphorylationCILSEVSTRSRSKLP
HHHHHHCCCCCCCCC		37.5320068231
68UbiquitinationRSKLPAGKNVLLLGE
CCCCCCCCEEEEECC		46.09-
82PhosphorylationEDGAGKTSLIRKIQG
CCCCCHHHHHHHHHC		25.8624719451
86UbiquitinationGKTSLIRKIQGIEEY
CHHHHHHHHHCHHHH		32.18-
93PhosphorylationKIQGIEEYKKGRGLE
HHHCHHHHHCCCCCE		12.76-
94UbiquitinationIQGIEEYKKGRGLEY
HHCHHHHHCCCCCEE		52.62-
942-HydroxyisobutyrylationIQGIEEYKKGRGLEY
HHCHHHHHCCCCCEE		52.62-
95AcetylationQGIEEYKKGRGLEYL
HCHHHHHCCCCCEEE		53.6030583627
103PhosphorylationGRGLEYLYLNVHDED
CCCCEEEEEECCCCC		8.70-
111MethylationLNVHDEDRDDQTRCN
EECCCCCCCCCCCEE		47.56-
117GlutathionylationDRDDQTRCNVWILDG
CCCCCCCEEEEEECC		5.6722555962
135PhosphorylationHKGLLKFSLDAVSLK
CCCCCCEEECCCCCC		24.6121406692
140PhosphorylationKFSLDAVSLKDTLVM
CEEECCCCCCCEEEE		31.2721406692
1752-HydroxyisobutyrylationVVREHVDKLKIPPEE
HHHHHHHHCCCCHHH		51.06-
197PhosphorylationLIRDFQEYVEPGEDF
HHHHHHHHCCCCCCC		10.1823927012
207PhosphorylationPGEDFPASPQRRNTA
CCCCCCCCHHHCCCC		23.0819664994
213PhosphorylationASPQRRNTASQEDKD
CCHHHCCCCCCCCCC		26.3525159151
215PhosphorylationPQRRNTASQEDKDDS
HHHCCCCCCCCCCCC		31.8728464451
222PhosphorylationSQEDKDDSVVLPLGA
CCCCCCCCEEEECCC		25.0225159151
231PhosphorylationVLPLGADTLTHNLGI
EEECCCCHHHHCCCC		32.7824732914
233PhosphorylationPLGADTLTHNLGIPV
ECCCCHHHHCCCCCE		15.7124732914
245PhosphorylationIPVLVVCTKCDAISV
CCEEEEEECCCHHHH		24.0923090842
255UbiquitinationDAISVLEKEHDYRDE
CHHHHHHHCCCCCHH		57.07-
310UbiquitinationKLYGFPYKIPAVVVE
HHHCCCCCCCEEEEE		42.31-
3312-HydroxyisobutyrylationPAGWDNDKKIGILHE
CCCCCCCCEEEEEEC		53.17-
331UbiquitinationPAGWDNDKKIGILHE
CCCCCCCCEEEEEEC		53.17-
344UbiquitinationHENFQTLKAEDNFED
ECCCCCEECCCCHHH		53.79-
355UbiquitinationNFEDIITKPPVRKFV
CHHHHCCCCCCCCCC		36.59-
368SulfoxidationFVHEKEIMAEDDQVF
CCCHHHHCCCCCHHH		3.3321406390
377SulfoxidationEDDQVFLMKLQSLLA
CCCHHHHHHHHHHHH		2.5030846556
381PhosphorylationVFLMKLQSLLAKQPP
HHHHHHHHHHHCCCC		35.4723312004
385MalonylationKLQSLLAKQPPTAAG
HHHHHHHCCCCCCCC		64.4126320211
385UbiquitinationKLQSLLAKQPPTAAG
HHHHHHHCCCCCCCC		64.41-
389PhosphorylationLLAKQPPTAAGRPVD
HHHCCCCCCCCCCCC		35.5023403867
398PhosphorylationAGRPVDASPRVPGGS
CCCCCCCCCCCCCCC		14.5830266825
405PhosphorylationSPRVPGGSPRTPNRS
CCCCCCCCCCCCCCC		19.6822167270
408PhosphorylationVPGGSPRTPNRSVSS
CCCCCCCCCCCCCCC		28.4422167270
411MethylationGSPRTPNRSVSSNVA
CCCCCCCCCCCCCCC		39.37-
412PhosphorylationSPRTPNRSVSSNVAS
CCCCCCCCCCCCCCC		32.7525159151
412O-linked_GlycosylationSPRTPNRSVSSNVAS
CCCCCCCCCCCCCCC		32.7523301498
414PhosphorylationRTPNRSVSSNVASVS
CCCCCCCCCCCCCCC		19.9023401153
415PhosphorylationTPNRSVSSNVASVSP
CCCCCCCCCCCCCCC		32.9221712546
419PhosphorylationSVSSNVASVSPIPAG
CCCCCCCCCCCCCCC		20.8825159151
421PhosphorylationSSNVASVSPIPAGSK
CCCCCCCCCCCCCCC		18.0225159151
427PhosphorylationVSPIPAGSKKIDPNM
CCCCCCCCCCCCCCC		32.6425159151
428AcetylationSPIPAGSKKIDPNMK
CCCCCCCCCCCCCCC		53.4825953088
4282-HydroxyisobutyrylationSPIPAGSKKIDPNMK
CCCCCCCCCCCCCCC		53.48-
429AcetylationPIPAGSKKIDPNMKA
CCCCCCCCCCCCCCC		54.7888121
435MethylationKKIDPNMKAGATSEG
CCCCCCCCCCCCCHH		50.76-
435UbiquitinationKKIDPNMKAGATSEG
CCCCCCCCCCCCCHH		50.76-
439PhosphorylationPNMKAGATSEGVLAN
CCCCCCCCCHHHHHH		26.7921406692
440PhosphorylationNMKAGATSEGVLANF
CCCCCCCCHHHHHHH		31.6421406692
450PhosphorylationVLANFFNSLLSKKTG
HHHHHHHHHHCCCCC		26.0721406692
453PhosphorylationNFFNSLLSKKTGSPG
HHHHHHHCCCCCCCC		37.0821406692
454UbiquitinationFFNSLLSKKTGSPGG
HHHHHHCCCCCCCCC		55.08-
455UbiquitinationFNSLLSKKTGSPGGP
HHHHHCCCCCCCCCC		55.53-
456PhosphorylationNSLLSKKTGSPGGPG
HHHHCCCCCCCCCCC		46.7825159151
458O-linked_GlycosylationLLSKKTGSPGGPGVS
HHCCCCCCCCCCCCC		26.1323301498
458PhosphorylationLLSKKTGSPGGPGVS
HHCCCCCCCCCCCCC		26.1325159151
465PhosphorylationSPGGPGVSGGSPAGG
CCCCCCCCCCCCCCC		43.2725159151
468O-linked_GlycosylationGPGVSGGSPAGGAGG
CCCCCCCCCCCCCCC		18.3323301498
468PhosphorylationGPGVSGGSPAGGAGG
CCCCCCCCCCCCCCC		18.3320044836
477PhosphorylationAGGAGGGSSGLPPST
CCCCCCCCCCCCCCC		25.2222199227
478PhosphorylationGGAGGGSSGLPPSTK
CCCCCCCCCCCCCCC		47.8522199227
483PhosphorylationGSSGLPPSTKKSGQK
CCCCCCCCCCCCCCC		51.4225159151
484PhosphorylationSSGLPPSTKKSGQKP
CCCCCCCCCCCCCCC		48.5429496963
485AcetylationSGLPPSTKKSGQKPV
CCCCCCCCCCCCCCE		49.6426051181
487PhosphorylationLPPSTKKSGQKPVLD
CCCCCCCCCCCCEEE		48.2725159151
490MalonylationSTKKSGQKPVLDVHA
CCCCCCCCCEEEEEE		40.3926320211
490AcetylationSTKKSGQKPVLDVHA
CCCCCCCCCEEEEEE		40.3926822725
503PhosphorylationHAELDRITRKPVTVS
EEEHHHCCCCCEEEC		33.2723927012
505AcetylationELDRITRKPVTVSPT
EHHHCCCCCEEECCC		34.8826051181
508PhosphorylationRITRKPVTVSPTTPT
HCCCCCEEECCCCCC		24.6429255136
510PhosphorylationTRKPVTVSPTTPTSP
CCCCEEECCCCCCCC		13.7319664994
512PhosphorylationKPVTVSPTTPTSPTE
CCEEECCCCCCCCCC		37.5929255136
513PhosphorylationPVTVSPTTPTSPTEG
CEEECCCCCCCCCCC		28.1429255136
515PhosphorylationTVSPTTPTSPTEGEA
EECCCCCCCCCCCCC		45.2929255136
516PhosphorylationVSPTTPTSPTEGEAS
ECCCCCCCCCCCCCC		30.9119664994
518PhosphorylationPTTPTSPTEGEAS--
CCCCCCCCCCCCC--		57.2929255136
523PhosphorylationSPTEGEAS-------
CCCCCCCC-------		36.1322167270
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

Oops, there are no upstream regulatory protein records of DC1L1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DC1L1_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 DC1L1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NEMO_HUMANIKBKGphysical
20026645
DYHC1_HUMANDYNC1H1physical
22939629
DC1L2_HUMANDYNC1LI2physical
22939629
DYLT1_HUMANDYNLT1physical
22939629
RAGP1_HUMANRANGAP1physical
22939629
TRXR1_HUMANTXNRD1physical
22939629
DYLT3_HUMANDYNLT3physical
22939629
TKT_HUMANTKTphysical
22939629
ZFR_HUMANZFRphysical
22939629
DYHC1_HUMANDYNC1H1physical
22863883
DC1I2_HUMANDYNC1I2physical
22863883
DYLT3_HUMANDYNLT3physical
22863883
EIF3E_HUMANEIF3Ephysical
22863883
ROA0_HUMANHNRNPA0physical
22863883
PRS10_HUMANPSMC6physical
22863883
PSMD8_HUMANPSMD8physical
22863883
RS12_HUMANRPS12physical
22863883
PAIRB_HUMANSERBP1physical
22863883
BICD2_HUMANBICD2physical
22956769
DCTN1_HUMANDCTN1physical
22956769
DC1I1_HUMANDYNC1I1physical
22956769
DYHC1_HUMANDYNC1H1physical
26344197
DYLT1_HUMANDYNLT1physical
26344197
XRCC6_HUMANXRCC6physical
26344197
DC1I2_HUMANDYNC1I2physical
28514442
DYHC1_HUMANDYNC1H1physical
28514442
NFS1_HUMANNFS1physical
28514442
LIS1_HUMANPAFAH1B1physical
27173435
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 DC1L1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-510; THR-512;THR-513; THR-515 AND SER-516, AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207 AND SER-516, ANDMASS SPECTROMETRY.
"Dynein light intermediate chain 1 is required for progress throughthe spindle assembly checkpoint.";
Sivaram M.V., Wadzinski T.L., Redick S.D., Manna T., Doxsey S.J.;
EMBO J. 28:902-914(2009).
Cited for: FUNCTION IN THE SPINDLE ASSEMBLY CHECKPOINT, SUBUNIT, PHOSPHORYLATIONAT SER-207; SER-398; SER-405 AND THR-408, AND SUBCELLULAR LOCATION.
"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-207; SER-421; SER-510;THR-512; THR-513; THR-515; SER-516 AND THR-518, 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-207; SER-405; THR-408;SER-419; SER-421; SER-487; SER-510; THR-512; THR-513; THR-515 ANDSER-516, 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-207; SER-398; SER-405;THR-408; SER-421; SER-487; SER-510; THR-513 AND SER-516, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; THR-408; SER-419AND SER-421, AND MASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, 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-207 AND SER-405, ANDMASS SPECTROMETRY.
"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-516, AND MASSSPECTROMETRY.

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