KIF1C_HUMAN - dbPTM
KIF1C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIF1C_HUMAN
UniProt AC O43896
Protein Name Kinesin-like protein KIF1C
Gene Name KIF1C
Organism Homo sapiens (Human).
Sequence Length 1103
Subcellular Localization Cytoplasm, cytoskeleton .
Protein Description Motor required for the retrograde transport of Golgi vesicles to the endoplasmic reticulum. Has a microtubule plus end-directed motility..
Protein Sequence MAGASVKVAVRVRPFNARETSQDAKCVVSMQGNTTSIINPKQSKDAPKSFTFDYSYWSHTSTEDPQFASQQQVYRDIGEEMLLHAFEGYNVCIFAYGQTGAGKSYTMMGRQEPGQQGIVPQLCEDLFSRVSENQSAQLSYSVEVSYMEIYCERVRDLLNPKSRGSLRVREHPILGPYVQDLSKLAVTSYADIADLMDCGNKARTVAATNMNETSSRSHAVFTIVFTQRCHDQLTGLDSEKVSKISLVDLAGSERADSSGARGMRLKEGANINKSLTTLGKVISALADMQSKKRKSDFIPYRDSVLTWLLKENLGGNSRTAMIAALSPADINYEETLSTLRYADRTKQIRCNAIINEDPNARLIRELQEEVARLRELLMAQGLSASALEGLKTEEGSVRGALPAVSSPPAPVSPSSPTTHNGELEPSFSPNTESQIGPEEAMERLQETEKIIAELNETWEEKLRKTEALRMEREALLAEMGVAVREDGGTVGVFSPKKTPHLVNLNEDPLMSECLLYHIKDGVTRVGQVDMDIKLTGQFIREQHCLFRSIPQPDGEVVVTLEPCEGAETYVNGKLVTEPLVLKSGNRIVMGKNHVFRFNHPEQARLERERGVPPPPGPPSEPVDWNFAQKELLEQQGIDIKLEMEKRLQDLENQYRKEKEEADLLLEQQRLYADSDSGDDSDKRSCEESWRLISSLREQLPPTTVQTIVKRCGLPSSGKRRAPRRVYQIPQRRRLQGKDPRWATMADLKMQAVKEICYEVALADFRHGRAEIEALAALKMRELCRTYGKPDGPGDAWRAVARDVWDTVGEEEGGGAGSGGGSEEGARGAEVEDLRAHIDKLTGILQEVKLQNSSKDRELQALRDRMLRMERVIPLAQDHEDENEEGGEVPWAPPEGSEAAEEAAPSDRMPSARPPSPPLSSWERVSRLMEEDPAFRRGRLRWLKQEQLRLQGLQGSGGRGGGLRRPPARFVPPHDCKLRFPFKSNPQHRESWPGMGSGEAPTPLQPPEEVTPHPATPARRPPSPRRSHHPRRNSLDGGGRSRGAGSAQPEPQHFQPKKHNSYPQPPQPYPAQRPPGPRYPPYTTPPRMRRQRSAPDLKESGAAV
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
5Phosphorylation---MAGASVKVAVRV
---CCCCCEEEEEEE		22.8923403867
162PhosphorylationRDLLNPKSRGSLRVR
HHHCCCCCCCCCEEC		43.0323312004
210SulfoxidationRTVAATNMNETSSRS
HHEEECCCCCCCCCC		4.1030846556
217PhosphorylationMNETSSRSHAVFTIV
CCCCCCCCCEEEEEE		20.1130257219
222PhosphorylationSRSHAVFTIVFTQRC
CCCCEEEEEEEECCH		15.0530257219
243UbiquitinationLDSEKVSKISLVDLA
CCHHHCCCEEEEECC		39.0232015554
257PhosphorylationAGSERADSSGARGMR
CCCCCCCCCCCCCCC		29.68-
258PhosphorylationGSERADSSGARGMRL
CCCCCCCCCCCCCCC		36.70-
266UbiquitinationGARGMRLKEGANINK
CCCCCCCCCCCCCCH		43.68-
274PhosphorylationEGANINKSLTTLGKV
CCCCCCHHHHHHHHH		26.85-
276PhosphorylationANINKSLTTLGKVIS
CCCCHHHHHHHHHHH		27.37-
277PhosphorylationNINKSLTTLGKVISA
CCCHHHHHHHHHHHH		38.51-
295PhosphorylationMQSKKRKSDFIPYRD
HHHHCCHHCCCCHHH		41.6121815630
326PhosphorylationTAMIAALSPADINYE
HHHEEECCHHHCCHH		17.20-
332PhosphorylationLSPADINYEETLSTL
CCHHHCCHHHHHHHH		18.57-
385PhosphorylationMAQGLSASALEGLKT
HHCCCCHHHHCCCCC		29.9728555341
391UbiquitinationASALEGLKTEEGSVR
HHHHCCCCCCCCCCC		65.8232015554
405PhosphorylationRGALPAVSSPPAPVS
CCCCCCCCCCCCCCC		38.9527251275
406PhosphorylationGALPAVSSPPAPVSP
CCCCCCCCCCCCCCC		28.4423927012
412PhosphorylationSSPPAPVSPSSPTTH
CCCCCCCCCCCCCCC		20.2923927012
414PhosphorylationPPAPVSPSSPTTHNG
CCCCCCCCCCCCCCC		41.2523927012
415PhosphorylationPAPVSPSSPTTHNGE
CCCCCCCCCCCCCCE		29.6523927012
417PhosphorylationPVSPSSPTTHNGELE
CCCCCCCCCCCCEEC		42.5123927012
418PhosphorylationVSPSSPTTHNGELEP
CCCCCCCCCCCEECC		19.4123927012
426PhosphorylationHNGELEPSFSPNTES
CCCEECCCCCCCCCC		29.0523927012
428PhosphorylationGELEPSFSPNTESQI
CEECCCCCCCCCCCC		22.9023927012
431PhosphorylationEPSFSPNTESQIGPE
CCCCCCCCCCCCCHH		40.1623927012
433PhosphorylationSFSPNTESQIGPEEA
CCCCCCCCCCCHHHH		25.6723927012
489PhosphorylationAVREDGGTVGVFSPK
EEEECCCEEEEECCC		21.4429255136
494PhosphorylationGGTVGVFSPKKTPHL
CCEEEEECCCCCCCC		33.1430266825
496UbiquitinationTVGVFSPKKTPHLVN
EEEEECCCCCCCCCC		68.9932142685
654PhosphorylationLQDLENQYRKEKEEA
HHHHHHHHHHHHHHH		34.9226074081
658UbiquitinationENQYRKEKEEADLLL
HHHHHHHHHHHHHHH		64.98-
671PhosphorylationLLEQQRLYADSDSGD
HHHHHHHHCCCCCCC		15.5622167270
674PhosphorylationQQRLYADSDSGDDSD
HHHHHCCCCCCCCCC		26.0422167270
676PhosphorylationRLYADSDSGDDSDKR
HHHCCCCCCCCCCHH		48.3422167270
680PhosphorylationDSDSGDDSDKRSCEE
CCCCCCCCCHHHHHH		50.1722167270
684PhosphorylationGDDSDKRSCEESWRL
CCCCCHHHHHHHHHH		31.4625841592
688PhosphorylationDKRSCEESWRLISSL
CHHHHHHHHHHHHHH		8.6625841592
693PhosphorylationEESWRLISSLREQLP
HHHHHHHHHHHHHCC		28.1024719451
694PhosphorylationESWRLISSLREQLPP
HHHHHHHHHHHHCCC		25.1825954137
702PhosphorylationLREQLPPTTVQTIVK
HHHHCCCCHHHHHHH		37.3520164059
703PhosphorylationREQLPPTTVQTIVKR
HHHCCCCHHHHHHHH		19.1820164059
715PhosphorylationVKRCGLPSSGKRRAP
HHHCCCCCCCCCCCC		57.6821406692
716PhosphorylationKRCGLPSSGKRRAPR
HHCCCCCCCCCCCCC		46.5221406692
726PhosphorylationRRAPRRVYQIPQRRR
CCCCCCEEECCHHHC		10.0228796482
743PhosphorylationGKDPRWATMADLKMQ
CCCCCCHHHHHHHHH		13.1128857561
757PhosphorylationQAVKEICYEVALADF
HHHHHHHHHHHHHCC		21.0627642862
788UbiquitinationELCRTYGKPDGPGDA
HHHHHHCCCCCCHHH		29.5329967540
817PhosphorylationEEGGGAGSGGGSEEG
CCCCCCCCCCCCCCC		33.4628985074
821PhosphorylationGAGSGGGSEEGARGA
CCCCCCCCCCCCCCC		35.4328348404
839UbiquitinationDLRAHIDKLTGILQE
HHHHHHHHHHHHHHH		47.5529967540
848UbiquitinationTGILQEVKLQNSSKD
HHHHHHHHCCCCCHH		43.5329967540
852PhosphorylationQEVKLQNSSKDRELQ
HHHHCCCCCHHHHHH		26.2923403867
853PhosphorylationEVKLQNSSKDRELQA
HHHCCCCCHHHHHHH		46.2323403867
910PhosphorylationAPSDRMPSARPPSPP
CCCCCCCCCCCCCCC		27.8030266825
915PhosphorylationMPSARPPSPPLSSWE
CCCCCCCCCCCCHHH		41.6630266825
919PhosphorylationRPPSPPLSSWERVSR
CCCCCCCCHHHHHHH		38.9030266825
920PhosphorylationPPSPPLSSWERVSRL
CCCCCCCHHHHHHHH		40.4130266825
948MethylationWLKQEQLRLQGLQGS
HHHHHHHHHCCCCCC		25.3454549377
948DimethylationWLKQEQLRLQGLQGS
HHHHHHHHHCCCCCC		25.34-
955PhosphorylationRLQGLQGSGGRGGGL
HHCCCCCCCCCCCCC		25.7224670416
958DimethylationGLQGSGGRGGGLRRP
CCCCCCCCCCCCCCC		44.07-
958MethylationGLQGSGGRGGGLRRP
CCCCCCCCCCCCCCC		44.0718958329
963MethylationGGRGGGLRRPPARFV
CCCCCCCCCCCCCCC		52.9424394669
983PhosphorylationKLRFPFKSNPQHRES
EEECCCCCCCCCCCC		54.8727794612
990PhosphorylationSNPQHRESWPGMGSG
CCCCCCCCCCCCCCC		38.2328111955
996PhosphorylationESWPGMGSGEAPTPL
CCCCCCCCCCCCCCC		25.2727794612
1001PhosphorylationMGSGEAPTPLQPPEE
CCCCCCCCCCCCCCC		43.6128111955
1015PhosphorylationEVTPHPATPARRPPS
CCCCCCCCCCCCCCC		23.1826425664
1022PhosphorylationTPARRPPSPRRSHHP
CCCCCCCCCCCCCCC		33.4526846344
1033PhosphorylationSHHPRRNSLDGGGRS
CCCCCCCCCCCCCCC		26.4826846344
1041MethylationLDGGGRSRGAGSAQP
CCCCCCCCCCCCCCC		37.3124129315
1045PhosphorylationGRSRGAGSAQPEPQH
CCCCCCCCCCCCCCC		24.1728555341
1057MethylationPQHFQPKKHNSYPQP
CCCCCCCCCCCCCCC		55.49115972071
1060PhosphorylationFQPKKHNSYPQPPQP
CCCCCCCCCCCCCCC		37.6028348404
1061PhosphorylationQPKKHNSYPQPPQPY
CCCCCCCCCCCCCCC		15.9429214152
1072DimethylationPQPYPAQRPPGPRYP
CCCCCCCCCCCCCCC		41.30-
1072MethylationPQPYPAQRPPGPRYP
CCCCCCCCCCCCCCC		41.3024377307
1077MethylationAQRPPGPRYPPYTTP
CCCCCCCCCCCCCCC		63.61115481191
1078PhosphorylationQRPPGPRYPPYTTPP
CCCCCCCCCCCCCCH		16.2226657352
1081PhosphorylationPGPRYPPYTTPPRMR
CCCCCCCCCCCHHHC		20.8126657352
1082PhosphorylationGPRYPPYTTPPRMRR
CCCCCCCCCCHHHCC		38.3016964243
1083PhosphorylationPRYPPYTTPPRMRRQ
CCCCCCCCCHHHCCC		26.0019664994
1092PhosphorylationPRMRRQRSAPDLKES
HHHCCCCCCCCHHHH		35.5028355574
1099PhosphorylationSAPDLKESGAAV---
CCCCHHHHCCCC---		31.9523403867
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
1092SPhosphorylationKinaseCK2-FAMILY-GPS
1092SPhosphorylationKinaseCK2_GROUP-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KIF1C_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 KIF1C_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
1433G_HUMANYWHAGphysical
10559254
BICL1_MOUSECcdc64physical
20360680
LAMC3_HUMANLAMC3physical
21988832
1433E_HUMANYWHAEphysical
21988832
1433Z_HUMANYWHAZphysical
21988832
1433T_HUMANYWHAQphysical
21988832
ANXA7_HUMANANXA7physical
26496610
LYST_HUMANLYSTphysical
26496610
HSP7C_HUMANHSPA8physical
26496610
MYO1A_HUMANMYO1Aphysical
26496610
RPB7_HUMANPOLR2Gphysical
26496610
RAN_HUMANRANphysical
26496610
ROBO2_HUMANROBO2physical
26496610
UBE2N_HUMANUBE2Nphysical
26496610
UTY_HUMANUTYphysical
26496610
MKNK1_HUMANMKNK1physical
26496610
PRP4B_HUMANPRPF4Bphysical
26496610
E41L3_HUMANEPB41L3physical
26496610
INT7_HUMANINTS7physical
26496610
NBEL1_HUMANNBEAL1physical
26496610
CING_HUMANCGNphysical
27173435
MAGI1_HUMANMAGI1physical
27173435
SYDE1_HUMANSYDE1physical
27173435
F110B_HUMANFAM110Bphysical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
611302Spastic ataxia 2, autosomal recessive (SPAX2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KIF1C_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-494 AND SER-1092, ANDMASS 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 THR-1083 AND SER-1092, ANDMASS SPECTROMETRY.
"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-1033 AND SER-1092, ANDMASS SPECTROMETRY.
"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-494, AND MASSSPECTROMETRY.
"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 THR-1082, 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 THR-1083, AND MASSSPECTROMETRY.

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