KLC2_HUMAN - dbPTM
KLC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KLC2_HUMAN
UniProt AC Q9H0B6
Protein Name Kinesin light chain 2
Gene Name KLC2
Organism Homo sapiens (Human).
Sequence Length 622
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 MAMMVFPREEKLSQDEIVLGTKAVIQGLETLRGEHRALLAPLVAPEAGEAEPGSQERCILLRRSLEAIELGLGEAQVILALSSHLGAVESEKQKLRAQVRRLVQENQWLREELAGTQQKLQRSEQAVAQLEEEKQHLLFMSQIRKLDEDASPNEEKGDVPKDTLDDLFPNEDEQSPAPSPGGGDVSGQHGGYEIPARLRTLHNLVIQYASQGRYEVAVPLCKQALEDLEKTSGHDHPDVATMLNILALVYRDQNKYKEAAHLLNDALAIREKTLGKDHPAVAATLNNLAVLYGKRGKYKEAEPLCKRALEIREKVLGKFHPDVAKQLSNLALLCQNQGKAEEVEYYYRRALEIYATRLGPDDPNVAKTKNNLASCYLKQGKYQDAETLYKEILTRAHEKEFGSVNGDNKPIWMHAEEREESKDKRRDSAPYGEYGSWYKACKVDSPTVNTTLRSLGALYRRQGKLEAAHTLEDCASRNRKQGLDPASQTKVVELLKDGSGRRGDRRSSRDMAGGAGPRSESDLEDVGPTAEWNGDGSGSLRRSGSFGKLRDALRRSSEMLVKKLQGGTPQEPPNPRMKRASSLNFLNKSVEEPTQPGGTGLSDSRTLSSSSMDLSRRSSLVG
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
11UbiquitinationMVFPREEKLSQDEIV
CCCCCHHHCCCCCCH		49.0029967540
13PhosphorylationFPREEKLSQDEIVLG
CCCHHHCCCCCCHHC		46.8020068231
21PhosphorylationQDEIVLGTKAVIQGL
CCCCHHCHHHHHHHH		16.2120068231
64 (in isoform 2)Phosphorylation-24.9129083192
97UbiquitinationSEKQKLRAQVRRLVQ
HHHHHHHHHHHHHHH		23.7421890473
98PhosphorylationEKQKLRAQVRRLVQE
HHHHHHHHHHHHHHH		23.8632142685
100UbiquitinationQKLRAQVRRLVQENQ
HHHHHHHHHHHHHCH		17.7122817900
102UbiquitinationLRAQVRRLVQENQWL
HHHHHHHHHHHCHHH		3.0622817900
119UbiquitinationELAGTQQKLQRSEQA
HHHHHHHHHHHHHHH		36.4529967540
141PhosphorylationKQHLLFMSQIRKLDE
HHHHHHHHHHHHCCC		18.3420363803
145UbiquitinationLFMSQIRKLDEDASP
HHHHHHHHCCCCCCC		63.0229967540
151PhosphorylationRKLDEDASPNEEKGD
HHCCCCCCCCCCCCC		40.3529255136
163PhosphorylationKGDVPKDTLDDLFPN
CCCCCCCCHHHHCCC		37.9129496963
175PhosphorylationFPNEDEQSPAPSPGG
CCCCCCCCCCCCCCC		22.4529743597
179PhosphorylationDEQSPAPSPGGGDVS
CCCCCCCCCCCCCCC		37.9829743597
186PhosphorylationSPGGGDVSGQHGGYE
CCCCCCCCCCCCCCC		37.1629523821
192PhosphorylationVSGQHGGYEIPARLR
CCCCCCCCCCCHHHH		18.4429523821
208PhosphorylationLHNLVIQYASQGRYE
HHHHHHHHHHCCCCE		9.3328152594
210PhosphorylationNLVIQYASQGRYEVA
HHHHHHHHCCCCEEH		28.3828152594
217UbiquitinationSQGRYEVAVPLCKQA
HCCCCEEHHHHHHHH		5.8121890473
217UbiquitinationSQGRYEVAVPLCKQA
HCCCCEEHHHHHHHH		5.8133845483
220UbiquitinationRYEVAVPLCKQALED
CCEEHHHHHHHHHHH		4.5922817900
222UbiquitinationEVAVPLCKQALEDLE
EEHHHHHHHHHHHHH		46.4122817900
241UbiquitinationHDHPDVATMLNILAL
CCCHHHHHHHHHHHH		23.2629967540
257MalonylationYRDQNKYKEAAHLLN
HCCCCCHHHHHHHHH		42.3526320211
292PhosphorylationLNNLAVLYGKRGKYK
HHHHHHHHCCCCCCC		17.6324260401
294UbiquitinationNLAVLYGKRGKYKEA
HHHHHHCCCCCCCCH		44.4121906983
297UbiquitinationVLYGKRGKYKEAEPL
HHHCCCCCCCCHHHH		58.1222817900
299UbiquitinationYGKRGKYKEAEPLCK
HCCCCCCCCHHHHHH		54.6722817900
313UbiquitinationKRALEIREKVLGKFH
HHHHHHHHHHHHCCC		53.8529967540
318UbiquitinationIREKVLGKFHPDVAK
HHHHHHHCCCHHHHH		36.0229967540
328PhosphorylationPDVAKQLSNLALLCQ
HHHHHHHHHHHHHHH		27.5728348404
345PhosphorylationGKAEEVEYYYRRALE
CCHHHHHHHHHHHHH		15.8025884760
346PhosphorylationKAEEVEYYYRRALEI
CHHHHHHHHHHHHHH		4.1328152594
347PhosphorylationAEEVEYYYRRALEIY
HHHHHHHHHHHHHHH		7.8528152594
365UbiquitinationLGPDDPNVAKTKNNL
CCCCCCCHHHHHCCH		7.6132142685
369UbiquitinationDPNVAKTKNNLASCY
CCCHHHHHCCHHHHH		43.03-
374PhosphorylationKTKNNLASCYLKQGK
HHHCCHHHHHHHCCC		13.3728857561
378AcetylationNLASCYLKQGKYQDA
CHHHHHHHCCCCCCH		30.4522424773
378UbiquitinationNLASCYLKQGKYQDA
CHHHHHHHCCCCCCH		30.45-
389PhosphorylationYQDAETLYKEILTRA
CCCHHHHHHHHHHHH		17.6227642862
390UbiquitinationQDAETLYKEILTRAH
CCHHHHHHHHHHHHH		41.2029967540
403PhosphorylationAHEKEFGSVNGDNKP
HHHHHHCCCCCCCCC		20.1020873877
428PhosphorylationSKDKRRDSAPYGEYG
HCCCCCCCCCCCCCC		29.3620044836
431PhosphorylationKRRDSAPYGEYGSWY
CCCCCCCCCCCCHHH		23.4728796482
434PhosphorylationDSAPYGEYGSWYKAC
CCCCCCCCCHHHHCC		16.4628796482
436PhosphorylationAPYGEYGSWYKACKV
CCCCCCCHHHHCCCC		26.7428796482
438PhosphorylationYGEYGSWYKACKVDS
CCCCCHHHHCCCCCC		7.1528796482
439MethylationGEYGSWYKACKVDSP
CCCCHHHHCCCCCCC		40.84115972171
442UbiquitinationGSWYKACKVDSPTVN
CHHHHCCCCCCCCHH		54.6732142685
445PhosphorylationYKACKVDSPTVNTTL
HHCCCCCCCCHHHHH		26.0029255136
447PhosphorylationACKVDSPTVNTTLRS
CCCCCCCCHHHHHHH		30.2722167270
450PhosphorylationVDSPTVNTTLRSLGA
CCCCCHHHHHHHHHH		23.9122199227
451PhosphorylationDSPTVNTTLRSLGAL
CCCCHHHHHHHHHHH		18.2529396449
454PhosphorylationTVNTTLRSLGALYRR
CHHHHHHHHHHHHHH		33.9828555341
459PhosphorylationLRSLGALYRRQGKLE
HHHHHHHHHHCCCHH		11.83-
462PhosphorylationLGALYRRQGKLEAAH
HHHHHHHCCCHHHCH		44.3632142685
464AcetylationALYRRQGKLEAAHTL
HHHHHCCCHHHCHHH		34.5125953088
470PhosphorylationGKLEAAHTLEDCASR
CCHHHCHHHHHHHHC		27.4128857561
479PhosphorylationEDCASRNRKQGLDPA
HHHHHCCHHHCCCHH		31.4032142685
480PhosphorylationDCASRNRKQGLDPAS
HHHHCCHHHCCCHHH		52.8732142685
487PhosphorylationKQGLDPASQTKVVEL
HHCCCHHHHHHHHHH		43.7125159151
499PhosphorylationVELLKDGSGRRGDRR
HHHHHCCCCCCCCCC		38.9826434776
505PhosphorylationGSGRRGDRRSSRDMA
CCCCCCCCCCCCCCC		43.1132142685
507PhosphorylationGRRGDRRSSRDMAGG
CCCCCCCCCCCCCCC		30.5323927012
508PhosphorylationRRGDRRSSRDMAGGA
CCCCCCCCCCCCCCC		30.4123927012
512PhosphorylationRRSSRDMAGGAGPRS
CCCCCCCCCCCCCCC		19.9833259812
519PhosphorylationAGGAGPRSESDLEDV
CCCCCCCCHHHHHHC		44.5829978859
521PhosphorylationGAGPRSESDLEDVGP
CCCCCCHHHHHHCCC		49.0629978859
529PhosphorylationDLEDVGPTAEWNGDG
HHHHCCCCCCCCCCC		31.1423186163
533PhosphorylationVGPTAEWNGDGSGSL
CCCCCCCCCCCCCCC		30.1332645325
537PhosphorylationAEWNGDGSGSLRRSG
CCCCCCCCCCCCCCC		29.9229507054
539PhosphorylationWNGDGSGSLRRSGSF
CCCCCCCCCCCCCCH		22.0230576142
543PhosphorylationGSGSLRRSGSFGKLR
CCCCCCCCCCHHHHH		32.1530266825
545PhosphorylationGSLRRSGSFGKLRDA
CCCCCCCCHHHHHHH		31.8823401153
556PhosphorylationLRDALRRSSEMLVKK
HHHHHHHCHHHHHHH		24.9830266825
557PhosphorylationRDALRRSSEMLVKKL
HHHHHHCHHHHHHHH		25.8027273156
568PhosphorylationVKKLQGGTPQEPPNP
HHHHCCCCCCCCCCH		28.7321815630
581PhosphorylationNPRMKRASSLNFLNK
CHHHHHHHHHCCCCC		39.1222167270
582PhosphorylationPRMKRASSLNFLNKS
HHHHHHHHHCCCCCC		26.7519664994
589PhosphorylationSLNFLNKSVEEPTQP
HHCCCCCCCCCCCCC		33.4223927012
594PhosphorylationNKSVEEPTQPGGTGL
CCCCCCCCCCCCCCC		51.1530266825
599PhosphorylationEPTQPGGTGLSDSRT
CCCCCCCCCCCCCCC		40.6430266825
602PhosphorylationQPGGTGLSDSRTLSS
CCCCCCCCCCCCCCC		34.5827273156
604PhosphorylationGGTGLSDSRTLSSSS
CCCCCCCCCCCCCCC		24.6421815630
606PhosphorylationTGLSDSRTLSSSSMD
CCCCCCCCCCCCCCC		34.6425159151
608PhosphorylationLSDSRTLSSSSMDLS
CCCCCCCCCCCCCHH		27.7923927012
609PhosphorylationSDSRTLSSSSMDLSR
CCCCCCCCCCCCHHH		29.5523927012
610PhosphorylationDSRTLSSSSMDLSRR
CCCCCCCCCCCHHHH		26.7225159151
611PhosphorylationSRTLSSSSMDLSRRS
CCCCCCCCCCHHHHH		20.4723927012
612SulfoxidationRTLSSSSMDLSRRSS
CCCCCCCCCHHHHHH		6.9321406390
615PhosphorylationSSSSMDLSRRSSLVG
CCCCCCHHHHHHCCC		22.7623927012
618PhosphorylationSMDLSRRSSLVG---
CCCHHHHHHCCC---		27.2427273156
619PhosphorylationMDLSRRSSLVG----
CCHHHHHHCCC----		25.8427273156
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
545SPhosphorylationKinasePRKAA1Q13131
GPS
582SPhosphorylationKinasePRKAA1Q13131
GPS
608SPhosphorylationKinaseGSK3BP49841
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KLC2_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 KLC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KINH_HUMANKIF5Bphysical
9624122
KIF5C_HUMANKIF5Cphysical
9624122
KIF5A_HUMANKIF5Aphysical
10491391
KINH_HUMANKIF5Bphysical
10491391
A4_HUMANAPPphysical
21832049
PATL1_HUMANPATL1physical
22939629
SLAI2_HUMANSLAIN2physical
22939629
SEPT2_HUMANSEPT2physical
22939629
PYGO2_HUMANPYGO2physical
22939629
ZPR1_HUMANZPR1physical
22939629
RBBP5_HUMANRBBP5physical
22939629
KINH_HUMANKIF5Bphysical
22863883
KLC1_HUMANKLC1physical
22863883
PTN23_HUMANPTPN23physical
22863883
P4R3B_HUMANSMEK2physical
22863883
KINH_HUMANKIF5Bphysical
26344197
KIF5C_HUMANKIF5Cphysical
26344197
LSM3_HUMANLSM3physical
26344197
LSM7_HUMANLSM7physical
26344197
LSMD1_HUMANNAA38physical
26344197
KINH_HUMANKIF5Bphysical
26496610
KLC1_HUMANKLC1physical
26496610
LYN_HUMANLYNphysical
26496610
SRP14_HUMANSRP14physical
26496610
AP3D1_HUMANAP3D1physical
26496610
PPIL2_HUMANPPIL2physical
26496610
TIM8B_HUMANTIMM8Bphysical
26496610
GPKOW_HUMANGPKOWphysical
26496610
RT02_HUMANMRPS2physical
26496610
KLC4_HUMANKLC4physical
26496610
CCD84_HUMANCCDC84physical
26496610
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 KLC2_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-582 AND SER-610, 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-445; SER-582 ANDSER-589, 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-445; SER-582 ANDSER-589, AND MASS SPECTROMETRY.
"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-445, 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-445, 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-507; SER-508 ANDSER-582, AND MASS 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-582, AND MASSSPECTROMETRY.

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