KLC1_HUMAN - dbPTM
KLC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KLC1_HUMAN
UniProt AC Q07866
Protein Name Kinesin light chain 1
Gene Name KLC1
Organism Homo sapiens (Human).
Sequence Length 573
Subcellular Localization Cell projection, growth cone. Cytoplasmic vesicle. 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..
Protein Sequence MYDNMSTMVYIKEDKLEKLTQDEIISKTKQVIQGLEALKNEHNSILQSLLETLKCLKKDDESNLVEEKSNMIRKSLEMLELGLSEAQVMMALSNHLNAVESEKQKLRAQVRRLCQENQWLRDELANTQQKLQKSEQSVAQLEEEKKHLEFMNQLKKYDDDISPSEDKDTDSTKEPLDDLFPNDEDDPGQGIQQQHSSAAAAAQQGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKDAANLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKDHPDVAKQLNNLALLCQNQGKYEEVEYYYQRALEIYQTKLGPDDPNVAKTKNNLASCYLKQGKFKQAETLYKEILTRAHEREFGSVDDENKPIWMHAEEREECKGKQKDGTSFGEYGGWYKACKVDSPTVTTTLKNLGALYRRQGKFEAAETLEEAAMRSRKQGLDNVHKQRVAEVLNDPENMEKRRSRESLNVDVVKYESGPDGGEEVSMSVEWNGGVSGRASFCGKRQQQQWPGRRHR
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
2Phosphorylation------MYDNMSTMV
------CCCCCCEEE		18.9430576142
6Phosphorylation--MYDNMSTMVYIKE
--CCCCCCEEEEEEH		21.4323401153
7Phosphorylation-MYDNMSTMVYIKED
-CCCCCCEEEEEEHH		10.4126471730
10PhosphorylationDNMSTMVYIKEDKLE
CCCCEEEEEEHHHHH		8.7518083107
18UbiquitinationIKEDKLEKLTQDEII
EEHHHHHHCCHHHHH		68.24-
272-HydroxyisobutyrylationTQDEIISKTKQVIQG
CHHHHHHHHHHHHHH		49.70-
27AcetylationTQDEIISKTKQVIQG
CHHHHHHHHHHHHHH		49.7025953088
54UbiquitinationQSLLETLKCLKKDDE
HHHHHHHHHHCCCCC		44.96-
57AcetylationLETLKCLKKDDESNL
HHHHHHHCCCCCCCH		64.7225953088
682-HydroxyisobutyrylationESNLVEEKSNMIRKS
CCCHHHHHHHHHHHH		33.36-
75PhosphorylationKSNMIRKSLEMLELG
HHHHHHHHHHHHHHC		21.5123322592
134PhosphorylationTQQKLQKSEQSVAQL
HHHHHHHHHHHHHHH		28.1024719451
134 (in isoform 10)Phosphorylation-28.1024719451
146UbiquitinationAQLEEEKKHLEFMNQ
HHHHHHHHHHHHHHH		57.62-
157PhosphorylationFMNQLKKYDDDISPS
HHHHHHHCCCCCCCC		24.0223312004
162PhosphorylationKKYDDDISPSEDKDT
HHCCCCCCCCCCCCC		29.3928355574
162 (in isoform 10)Phosphorylation-29.3927251275
164PhosphorylationYDDDISPSEDKDTDS
CCCCCCCCCCCCCCC		52.1929507054
169PhosphorylationSPSEDKDTDSTKEPL
CCCCCCCCCCCCCCH		37.2727794612
171PhosphorylationSEDKDTDSTKEPLDD
CCCCCCCCCCCCHHH		43.3930576142
207PhosphorylationAAAQQGGYEIPARLR
HHHHHCCCCCCHHHH		19.94-
223PhosphorylationLHNLVIQYASQGRYE
HHHHHHHHHHCCCCE		9.3328152594
225PhosphorylationNLVIQYASQGRYEVA
HHHHHHHHCCCCEEH		28.3828152594
236GlutathionylationYEVAVPLCKQALEDL
CEEHHHHHHHHHHHH		2.2222555962
237UbiquitinationEVAVPLCKQALEDLE
EEHHHHHHHHHHHHH		46.41-
271PhosphorylationVYRDQNKYKDAANLL
HHCCCCCCHHHHHHH		22.96-
272AcetylationYRDQNKYKDAANLLN
HCCCCCCHHHHHHHH		42.3623954790
307PhosphorylationLNNLAVLYGKRGKYK
HHHHHHHHCCCCCCC		17.6324260401
3092-HydroxyisobutyrylationNLAVLYGKRGKYKEA
HHHHHHCCCCCCCCC		44.41-
309AcetylationNLAVLYGKRGKYKEA
HHHHHHCCCCCCCCC		44.4125953088
309UbiquitinationNLAVLYGKRGKYKEA
HHHHHHCCCCCCCCC		44.41-
309 (in isoform 1)Ubiquitination-44.4121890473
309 (in isoform 2)Ubiquitination-44.4121890473
309 (in isoform 3)Ubiquitination-44.4121890473
309 (in isoform 4)Ubiquitination-44.4121890473
309 (in isoform 5)Ubiquitination-44.4121890473
309 (in isoform 6)Ubiquitination-44.4121890473
309 (in isoform 7)Ubiquitination-44.4121890473
309 (in isoform 8)Ubiquitination-44.4121890473
309 (in isoform 9)Ubiquitination-44.4121890473
309UbiquitinationNLAVLYGKRGKYKEA
HHHHHHCCCCCCCCC		44.4121890473
314MalonylationYGKRGKYKEAEPLCK
HCCCCCCCCCHHHHH		54.6726320211
354AcetylationLLCQNQGKYEEVEYY
HHHHCCCCHHHHHHH		39.4626051181
355PhosphorylationLCQNQGKYEEVEYYY
HHHCCCCHHHHHHHH		24.9330576142
360PhosphorylationGKYEEVEYYYQRALE
CCHHHHHHHHHHHHH		16.7930576142
361PhosphorylationKYEEVEYYYQRALEI
CHHHHHHHHHHHHHH		4.6126356563
362PhosphorylationYEEVEYYYQRALEIY
HHHHHHHHHHHHHHH		7.2230576142
369PhosphorylationYQRALEIYQTKLGPD
HHHHHHHHHHHCCCC		10.7630576142
371PhosphorylationRALEIYQTKLGPDDP
HHHHHHHHHCCCCCC		15.9730576142
372UbiquitinationALEIYQTKLGPDDPN
HHHHHHHHCCCCCCC		35.60-
382AcetylationPDDPNVAKTKNNLAS
CCCCCHHHHHHCHHH		56.6125953088
384UbiquitinationDPNVAKTKNNLASCY
CCCHHHHHHCHHHHH		43.03-
389PhosphorylationKTKNNLASCYLKQGK
HHHHCHHHHHHHCCC		13.3720873877
393AcetylationNLASCYLKQGKFKQA
CHHHHHHHCCCHHHH		30.4519608861
393MalonylationNLASCYLKQGKFKQA
CHHHHHHHCCCHHHH		30.4526320211
393UbiquitinationNLASCYLKQGKFKQA
CHHHHHHHCCCHHHH		30.45-
418PhosphorylationAHEREFGSVDDENKP
HHHHHCCCCCCCCCC		27.9129507054
418 (in isoform 10)Phosphorylation-27.9127251275
441UbiquitinationEECKGKQKDGTSFGE
HHHCCCCCCCCCCCC		62.71-
444PhosphorylationKGKQKDGTSFGEYGG
CCCCCCCCCCCCCCC		30.8922199227
444 (in isoform 10)Phosphorylation-30.8924719451
445PhosphorylationGKQKDGTSFGEYGGW
CCCCCCCCCCCCCCC		36.4625159151
449PhosphorylationDGTSFGEYGGWYKAC
CCCCCCCCCCCEEEC		22.7125159151
453PhosphorylationFGEYGGWYKACKVDS
CCCCCCCEEECCCCC		7.6229978859
454MethylationGEYGGWYKACKVDSP
CCCCCCEEECCCCCC		40.58115972159
456GlutathionylationYGGWYKACKVDSPTV
CCCCEEECCCCCCCC		3.7422555962
456PhosphorylationYGGWYKACKVDSPTV
CCCCEEECCCCCCCC		3.7416964243
456 (in isoform 4)Phosphorylation-3.7418669648
458 (in isoform 4)Phosphorylation-9.9118669648
460PhosphorylationYKACKVDSPTVTTTL
EEECCCCCCCCHHHH		26.0019664994
460 (in isoform 10)Phosphorylation-26.0024719451
462PhosphorylationACKVDSPTVTTTLKN
ECCCCCCCCHHHHHH		34.1430266825
462 (in isoform 10)Phosphorylation-34.1424719451
464PhosphorylationKVDSPTVTTTLKNLG
CCCCCCCHHHHHHHH		19.2830266825
465PhosphorylationVDSPTVTTTLKNLGA
CCCCCCHHHHHHHHH		26.2923927012
466PhosphorylationDSPTVTTTLKNLGAL
CCCCCHHHHHHHHHH		26.7723927012
479AcetylationALYRRQGKFEAAETL
HHHHHCCCHHHHHHH		31.5225953088
491SulfoxidationETLEEAAMRSRKQGL
HHHHHHHHHHHHCCC		5.2821406390
495UbiquitinationEAAMRSRKQGLDNVH
HHHHHHHHCCCHHHH		50.38-
503UbiquitinationQGLDNVHKQRVAEVL
CCCHHHHHHHHHHHH		35.20-
505MethylationLDNVHKQRVAEVLND
CHHHHHHHHHHHHCC		34.12115386225
516SulfoxidationVLNDPENMEKRRSRE
HHCCHHHHHHHHCHH		6.4821406390
517 (in isoform 4)Phosphorylation-55.8018669648
518AcetylationNDPENMEKRRSRESL
CCHHHHHHHHCHHHC		42.2026051181
518UbiquitinationNDPENMEKRRSRESL
CCHHHHHHHHCHHHC		42.202190698
518 (in isoform 1)Ubiquitination-42.2021890473
518 (in isoform 2)Ubiquitination-42.2021890473
518 (in isoform 3)Ubiquitination-42.2021890473
518 (in isoform 4)Ubiquitination-42.2021890473
518 (in isoform 5)Ubiquitination-42.2021890473
518 (in isoform 6)Ubiquitination-42.2021890473
518 (in isoform 7)Ubiquitination-42.2021890473
518 (in isoform 8)Ubiquitination-42.2021890473
518 (in isoform 9)Ubiquitination-42.2021890473
520 (in isoform 4)Phosphorylation-51.6518669648
521PhosphorylationENMEKRRSRESLNVD
HHHHHHHCHHHCCCC		44.4229255136
521 (in isoform 10)Phosphorylation-44.4224719451
521 (in isoform 3)Phosphorylation-44.4223927012
521 (in isoform 8)Phosphorylation-44.4230624053
524PhosphorylationEKRRSRESLNVDVVK
HHHHCHHHCCCCEEE		24.9229255136
524 (in isoform 10)Phosphorylation-24.9224719451
524 (in isoform 3)Phosphorylation-24.9223927012
524 (in isoform 8)Phosphorylation-24.9230624053
532PhosphorylationLNVDVVKYESGPDGG
CCCCEEEECCCCCCC		12.0620736484
532 (in isoform 3)Phosphorylation-12.0628796482
532 (in isoform 6)Phosphorylation-12.0622199227
534PhosphorylationVDVVKYESGPDGGEE
CCEEEECCCCCCCCE		53.1628985074
534 (in isoform 6)Phosphorylation-53.1625850435
543PhosphorylationPDGGEEVSMSVEWNG
CCCCCEEEEEEEECC		14.5018212344
544 (in isoform 6)Phosphorylation-6.6826657352
545PhosphorylationGGEEVSMSVEWNGGV
CCCEEEEEEEECCCC		14.9120068231
546 (in isoform 6)Phosphorylation-8.0725159151
546 (in isoform 7)Phosphorylation-8.0722167270
547 (in isoform 7)Phosphorylation-28.1122167270
550 (in isoform 6)Phosphorylation-38.6620068231
552 (in isoform 6)Phosphorylation-6.0923927012
554 (in isoform 6)Phosphorylation-27.1120068231
555 (in isoform 10)Phosphorylation-21.39-
555 (in isoform 4)Phosphorylation-21.39-
555 (in isoform 5)Phosphorylation-21.39-
555 (in isoform 9)Phosphorylation-21.39-
557PhosphorylationGGVSGRASFCGKRQQ
CCCCCCCCCCCCCCC		21.5124719451
559 (in isoform 10)Phosphorylation-6.1020068231
559 (in isoform 4)Phosphorylation-6.1020068231
559 (in isoform 5)Phosphorylation-6.1020068231
559 (in isoform 6)Phosphorylation-6.1026434776
559 (in isoform 9)Phosphorylation-6.1020068231
561AcetylationGRASFCGKRQQQQWP
CCCCCCCCCCCCCCC		48.4925953088
561 (in isoform 10)Phosphorylation-48.4923927012
561 (in isoform 4)Phosphorylation-48.4923927012
561 (in isoform 5)Phosphorylation-48.4923927012
561 (in isoform 9)Phosphorylation-48.4923927012
563 (in isoform 10)Phosphorylation-49.2520068231
563 (in isoform 4)Phosphorylation-49.2520068231
563 (in isoform 5)Phosphorylation-49.2520068231
563 (in isoform 6)Phosphorylation-49.25-
563 (in isoform 9)Phosphorylation-49.2520068231
564 (in isoform 6)Phosphorylation-41.27-
568 (in isoform 10)Phosphorylation-23.2926434776
568 (in isoform 4)Phosphorylation-23.2926434776
568 (in isoform 5)Phosphorylation-23.2926434776
568 (in isoform 9)Phosphorylation-23.2926434776
572 (in isoform 10)Phosphorylation-38.14-
572 (in isoform 4)Phosphorylation-38.14-
572 (in isoform 5)Phosphorylation-38.14-
572 (in isoform 7)Phosphorylation-38.1421406692
572 (in isoform 9)Phosphorylation-38.14-
573 (in isoform 10)Phosphorylation-46.56-
573 (in isoform 4)Phosphorylation-46.56-
573 (in isoform 5)Phosphorylation-46.56-
573 (in isoform 9)Phosphorylation-46.56-
576 (in isoform 7)Phosphorylation-22167270
578 (in isoform 7)Phosphorylation-25159151
580 (in isoform 7)Phosphorylation-25072903
590 (in isoform 6)Phosphorylation-22167270
591 (in isoform 6)Phosphorylation-22167270
599 (in isoform 4)Phosphorylation-22167270
599 (in isoform 9)Phosphorylation-22167270
600 (in isoform 4)Phosphorylation-22167270
600 (in isoform 9)Phosphorylation-22167270
607 (in isoform 10)Phosphorylation-28348404
608 (in isoform 10)Phosphorylation-28348404
609 (in isoform 10)Phosphorylation-28348404
610 (in isoform 10)Phosphorylation-28348404
616 (in isoform 10)Phosphorylation-28348404
616 (in isoform 6)Phosphorylation-21406692
620 (in isoform 6)Phosphorylation-22167270
622 (in isoform 6)Phosphorylation-25159151
624 (in isoform 6)Phosphorylation-25072903
625 (in isoform 4)Phosphorylation-21406692
629 (in isoform 4)Phosphorylation-22167270
631 (in isoform 4)Phosphorylation-25159151
633 (in isoform 4)Phosphorylation-25072903
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
521SPhosphorylationKinaseAMPKQ9Y478
Uniprot
521SPhosphorylationKinasePRKAA1Q13131
GPS
524SPhosphorylationKinaseAMPKQ9Y478
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KLC1_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 KLC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KINH_HUMANKIF5Bphysical
9624122
KIF5C_HUMANKIF5Cphysical
9624122
KIF5A_HUMANKIF5Aphysical
9624122
KIF5A_HUMANKIF5Aphysical
10491391
KINH_HUMANKIF5Bphysical
10491391
A4_HUMANAPPphysical
11144355
KLC2_HUMANKLC2physical
22939629
KLC4_HUMANKLC4physical
22939629
KINH_HUMANKIF5Bphysical
22863883
PTN23_HUMANPTPN23physical
22863883
P4R3B_HUMANSMEK2physical
22863883
K1H1_HUMANKRT31physical
25416956
CC114_HUMANCCDC114physical
25416956
KIF5A_HUMANKIF5Aphysical
26344197
KINH_HUMANKIF5Bphysical
26344197
KIF5C_HUMANKIF5Cphysical
26344197
CLK1_HUMANCLK1physical
26496610
KC1D_HUMANCSNK1Dphysical
26496610
KINH_HUMANKIF5Bphysical
26496610
RPB3_HUMANPOLR2Cphysical
26496610
PIAS1_HUMANPIAS1physical
26496610
NOLC1_HUMANNOLC1physical
26496610
RFIP2_HUMANRAB11FIP2physical
26496610
AVL9_HUMANAVL9physical
26496610
ORC3_HUMANORC3physical
26496610
RFOX1_HUMANRBFOX1physical
26496610
KLC2_HUMANKLC2physical
26496610
RFIP1_HUMANRAB11FIP1physical
26496610
CEP44_HUMANCEP44physical
26496610
DPY30_HUMANDPY30physical
26496610
ZN503_HUMANZNF503physical
26496610
KLC4_HUMANKLC4physical
26496610
KLC3_HUMANKLC3physical
28514442
KIF5A_HUMANKIF5Aphysical
28514442
KLC2_HUMANKLC2physical
28514442
KLC4_HUMANKLC4physical
28514442
KIF5C_HUMANKIF5Cphysical
28514442
KINH_HUMANKIF5Bphysical
28514442
SNAPN_HUMANSNAPINphysical
28514442
RABE2_HUMANRABEP2physical
28514442
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 KLC1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Cell-wide analysis of secretory granule dynamics in three dimensionsin living pancreatic beta-cells: evidence against a role for AMPK-dependent phosphorylation of KLC1 at Ser517/Ser520 in glucose-stimulated insulin granule movement.";
McDonald A., Fogarty S., Leclerc I., Hill E.V., Hardie D.G.,Rutter G.A.;
Biochem. Soc. Trans. 38:205-208(2010).
Cited for: PHOSPHORYLATION AT SER-521 AND SER-524, AND MUTAGENESIS OF SER-521 ANDSER-524.
"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 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 SER-460 AND THR-462, 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 SER-460; SER-521 ANDSER-524, 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-460, 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-460, AND MASSSPECTROMETRY.

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