KLC4_HUMAN - dbPTM
KLC4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KLC4_HUMAN
UniProt AC Q9NSK0
Protein Name Kinesin light chain 4
Gene Name KLC4
Organism Homo sapiens (Human).
Sequence Length 619
Subcellular Localization Cytoplasm, cytoskeleton .
Protein Description Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport. The light chain may function in coupling of cargo to the heavy chain or in the modulation of its ATPase activity (By similarity)..
Protein Sequence MSGLVLGQRDEPAGHRLSQEEILGSTRLVSQGLEALRSEHQAVLQSLSQTIECLQQGGHEEGLVHEKARQLRRSMENIELGLSEAQVMLALASHLSTVESEKQKLRAQVRRLCQENQWLRDELAGTQQRLQRSEQAVAQLEEEKKHLEFLGQLRQYDEDGHTSEEKEGDATKDSLDDLFPNEEEEDPSNGLSRGQGATAAQQGGYEIPARLRTLHNLVIQYAAQGRYEVAVPLCKQALEDLERTSGRGHPDVATMLNILALVYRDQNKYKEAAHLLNDALSIRESTLGPDHPAVAATLNNLAVLYGKRGKYKEAEPLCQRALEIREKVLGTNHPDVAKQLNNLALLCQNQGKYEAVERYYQRALAIYEGQLGPDNPNVARTKNNLASCYLKQGKYAEAETLYKEILTRAHVQEFGSVDDDHKPIWMHAEEREEMSKSRHHEGGTPYAEYGGWYKACKVSSPTVNTTLRNLGALYRRQGKLEAAETLEECALRSRRQGTDPISQTKVAELLGESDGRRTSQEGPGDSVKFEGGEDASVAVEWSGDGSGTLQRSGSLGKIRDVLRRSSELLVRKLQGTEPRPSSSNMKRAASLNYLNQPSAAPLQVSRGLSASTMDLSSSS
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
2Acetylation------MSGLVLGQR
------CCCCCCCCC		40.6122223895
2Phosphorylation------MSGLVLGQR
------CCCCCCCCC		40.6128555341
4 (in isoform 3)Phosphorylation-1.9426029660
18PhosphorylationEPAGHRLSQEEILGS
CCCCCCCCHHHHHCH		35.1926657352
25PhosphorylationSQEEILGSTRLVSQG
CHHHHHCHHHHHHHH		13.6028857561
26PhosphorylationQEEILGSTRLVSQGL
HHHHHCHHHHHHHHH		26.6528857561
36 (in isoform 3)Phosphorylation-4.5227251275
74 (in isoform 5)Phosphorylation-24.8225690035
74PhosphorylationKARQLRRSMENIELG
HHHHHHHHHHHHHHC		24.8218187866
83 (in isoform 5)Phosphorylation-29.1425690035
83PhosphorylationENIELGLSEAQVMLA
HHHHHCCCHHHHHHH		29.1418187866
93PhosphorylationQVMLALASHLSTVES
HHHHHHHHHHHCHHH		26.3018187866
100PhosphorylationSHLSTVESEKQKLRA
HHHHCHHHHHHHHHH		45.8418187866
156PhosphorylationFLGQLRQYDEDGHTS
HHHHHHCCCCCCCCC		18.1827794612
162PhosphorylationQYDEDGHTSEEKEGD
CCCCCCCCCCCCCCC		43.2828985074
163PhosphorylationYDEDGHTSEEKEGDA
CCCCCCCCCCCCCCC		37.7828192239
171PhosphorylationEEKEGDATKDSLDDL
CCCCCCCCCCCHHHH		39.8730576142
174PhosphorylationEGDATKDSLDDLFPN
CCCCCCCCHHHHCCC		34.9424850871
181 (in isoform 3)Phosphorylation-63.0827251275
198PhosphorylationLSRGQGATAAQQGGY
CCCCCCCCHHHHCCC		29.3821945579
205PhosphorylationTAAQQGGYEIPARLR
CHHHHCCCCCCHHHH		19.9421945579
223 (in isoform 3)Phosphorylation-13.8727642862
270MalonylationYRDQNKYKEAAHLLN
HCCCCHHHHHHHHHH		42.3526320211
285PhosphorylationDALSIRESTLGPDHP
HHHHHHHHHCCCCCH		21.0528857561
286PhosphorylationALSIRESTLGPDHPA
HHHHHHHHCCCCCHH		30.8628857561
305PhosphorylationLNNLAVLYGKRGKYK
HHHHHHHHCCCCCCC		17.6324260401
307UbiquitinationNLAVLYGKRGKYKEA
HHHHHHCCCCCCCCC		44.41-
327UbiquitinationRALEIREKVLGTNHP
HHHHHHHHHHCCCCH		32.67-
382UbiquitinationNPNVARTKNNLASCY
CCCHHHHHCCHHHHH		37.98-
387PhosphorylationRTKNNLASCYLKQGK
HHHCCHHHHHHHCCC		13.3728857561
391UbiquitinationNLASCYLKQGKYAEA
CHHHHHHHCCCHHHH		30.45-
391AcetylationNLASCYLKQGKYAEA
CHHHHHHHCCCHHHH		30.4569559
405 (in isoform 3)Phosphorylation-4.1027251275
444PhosphorylationSRHHEGGTPYAEYGG
HCCCCCCCCCHHHCC		24.7925159151
446PhosphorylationHHEGGTPYAEYGGWY
CCCCCCCCHHHCCCE		16.35-
449PhosphorylationGGTPYAEYGGWYKAC
CCCCCHHHCCCEEEE		16.8728796482
453PhosphorylationYAEYGGWYKACKVSS
CHHHCCCEEEEECCC		7.62-
459PhosphorylationWYKACKVSSPTVNTT
CEEEEECCCCCHHHH		18.9830266825
460PhosphorylationYKACKVSSPTVNTTL
EEEEECCCCCHHHHH		27.8129255136
462PhosphorylationACKVSSPTVNTTLRN
EEECCCCCHHHHHHH		28.4730266825
464 (in isoform 3)Phosphorylation-29.8027642862
465PhosphorylationVSSPTVNTTLRNLGA
CCCCCHHHHHHHHHH		23.9125867546
466PhosphorylationSSPTVNTTLRNLGAL
CCCCHHHHHHHHHHH		20.6525867546
467 (in isoform 3)Phosphorylation-3.0027642862
474PhosphorylationLRNLGALYRRQGKLE
HHHHHHHHHHCCCHH		11.8322461510
477 (in isoform 3)Phosphorylation-44.3624719451
478 (in isoform 3)Phosphorylation-34.40-
485PhosphorylationGKLEAAETLEECALR
CCHHHHHHHHHHHHH		34.4428857561
493PhosphorylationLEECALRSRRQGTDP
HHHHHHHHHHCCCCC		32.4426074081
498PhosphorylationLRSRRQGTDPISQTK
HHHHHCCCCCCCHHH		30.2026074081
502PhosphorylationRQGTDPISQTKVAEL
HCCCCCCCHHHHHHH		36.8726074081
504PhosphorylationGTDPISQTKVAELLG
CCCCCCHHHHHHHHC		22.2426074081
513PhosphorylationVAELLGESDGRRTSQ
HHHHHCCCCCCCCCC		43.5026074081
518PhosphorylationGESDGRRTSQEGPGD
CCCCCCCCCCCCCCC		33.1429255136
519PhosphorylationESDGRRTSQEGPGDS
CCCCCCCCCCCCCCC		25.1529255136
526PhosphorylationSQEGPGDSVKFEGGE
CCCCCCCCEEECCCC		32.8723927012
536 (in isoform 3)Phosphorylation-23.9624719451
537 (in isoform 3)Phosphorylation-8.0927251275
542PhosphorylationASVAVEWSGDGSGTL
CEEEEEECCCCCCEE		17.3226074081
546PhosphorylationVEWSGDGSGTLQRSG
EEECCCCCCEEEECC		33.0926074081
548PhosphorylationWSGDGSGTLQRSGSL
ECCCCCCEEEECCCH		22.7826074081
552PhosphorylationGSGTLQRSGSLGKIR
CCCEEEECCCHHHHH		21.5526074081
554PhosphorylationGTLQRSGSLGKIRDV
CEEEECCCHHHHHHH		34.8826074081
565PhosphorylationIRDVLRRSSELLVRK
HHHHHHHCHHHHHHH		23.0223927012
566PhosphorylationRDVLRRSSELLVRKL
HHHHHHCHHHHHHHH		30.3823927012
576PhosphorylationLVRKLQGTEPRPSSS
HHHHHCCCCCCCCCH		29.8325072903
576O-linked_GlycosylationLVRKLQGTEPRPSSS
HHHHHCCCCCCCCCH		29.8330379171
581PhosphorylationQGTEPRPSSSNMKRA
CCCCCCCCCHHHHHH		47.9125072903
582PhosphorylationGTEPRPSSSNMKRAA
CCCCCCCCHHHHHHH		28.5425072903
583PhosphorylationTEPRPSSSNMKRAAS
CCCCCCCHHHHHHHH		45.3325072903
583 (in isoform 3)Phosphorylation-45.3324719451
584 (in isoform 3)Phosphorylation-41.7824719451
590PhosphorylationSNMKRAASLNYLNQP
HHHHHHHHCCCCCCC		19.0329255136
593PhosphorylationKRAASLNYLNQPSAA
HHHHHCCCCCCCCCC		16.6022167270
598PhosphorylationLNYLNQPSAAPLQVS
CCCCCCCCCCCCCCC		27.5723927012
605O-linked_GlycosylationSAAPLQVSRGLSAST
CCCCCCCCCCCCCHH		13.9930379171
605PhosphorylationSAAPLQVSRGLSAST
CCCCCCCCCCCCCHH		13.9923403867
608 (in isoform 3)Phosphorylation-3.6224719451
609PhosphorylationLQVSRGLSASTMDLS
CCCCCCCCCHHCCCC		24.0130266825
611PhosphorylationVSRGLSASTMDLSSS
CCCCCCCHHCCCCCC		22.3830266825
611 (in isoform 3)Phosphorylation-22.38-
612PhosphorylationSRGLSASTMDLSSSS
CCCCCCHHCCCCCCC		17.8930266825
616PhosphorylationSASTMDLSSSS----
CCHHCCCCCCC----		24.7429396449
617PhosphorylationASTMDLSSSS-----
CHHCCCCCCC-----		41.7329396449
618PhosphorylationSTMDLSSSS------
HHCCCCCCC------		36.3728985074
619PhosphorylationTMDLSSSS-------
HCCCCCCC-------		46.3029396449
627 (in isoform 3)Phosphorylation--
629 (in isoform 3)Phosphorylation-24719451
630 (in isoform 3)Phosphorylation--
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
590SPhosphorylationKinaseAMPKA2P54646
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KLC4_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 KLC4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
CARL1_HUMANLRRC16Aphysical
22939629
NUCB1_HUMANNUCB1physical
22939629
IMA1_HUMANKPNA2physical
21988832
KLC1_HUMANKLC1physical
22863883
KLC2_HUMANKLC2physical
22863883
SYNE4_HUMANSYNE4physical
25416956
MOT9_HUMANSLC16A9physical
25416956
CE57L_HUMANCEP57L1physical
25416956
KIF5A_HUMANKIF5Aphysical
26344197
KINH_HUMANKIF5Bphysical
26344197
KIF5C_HUMANKIF5Cphysical
26344197
CDK9_HUMANCDK9physical
26496610
E41L2_HUMANEPB41L2physical
26496610
KINH_HUMANKIF5Bphysical
26496610
KLC1_HUMANKLC1physical
26496610
MEF2A_HUMANMEF2Aphysical
26496610
UMPS_HUMANUMPSphysical
26496610
CLIP2_HUMANCLIP2physical
26496610
GANP_HUMANMCM3APphysical
26496610
KIF14_HUMANKIF14physical
26496610
PUF60_HUMANPUF60physical
26496610
PAR16_HUMANPARP16physical
26496610
PLXA3_HUMANPLXNA3physical
26496610
SYIM_HUMANIARS2physical
26496610
NEUL_HUMANNLNphysical
26496610
KLC2_HUMANKLC2physical
26496610
OSBL5_HUMANOSBPL5physical
26496610
CDR2_HUMANCDR2physical
27173435
CBY1_HUMANCBY1physical
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 KLC4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-391, AND MASS SPECTROMETRY.
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-460 AND SER-590, ANDMASS SPECTROMETRY.
"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-590; TYR-593 ANDTHR-612, 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-460 AND SER-590, ANDMASS 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-460, 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-590, AND MASSSPECTROMETRY.
"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-74; SER-83; SER-93 ANDSER-100, AND MASS 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-460, AND MASSSPECTROMETRY.

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