KLC3_HUMAN - dbPTM
KLC3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KLC3_HUMAN
UniProt AC Q6P597
Protein Name Kinesin light chain 3
Gene Name KLC3
Organism Homo sapiens (Human).
Sequence Length 504
Subcellular Localization Cytoplasm, cytoskeleton . In elongating spermatid tail midpiece, localized in outer dense fibers (ODFs) and associates with mitochondria. Also localizes to the manchette in elongating spermatids.
Protein Description Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport..
Protein Sequence MSVQVAAPGSAGLGPERLSPEELVRQTRQVVQGLEALRAEHHGLAGHLAEALAGQGPAAGLEMLEEKQQVVSHSLEAIELGLGEAQVLLALSAHVGALEAEKQRLRSQARRLAQENVWLREELEETQRRLRASEESVAQLEEEKRHLEFLGQLRQYDPPAESQQSESPPRRDSLASLFPSEEEERKGPEAAGAAAAQQGGYEIPARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATDLLHDALQIREQTLGPEHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVLGADHPDVAKQLNNLALLCQNQGKFEDVERHYARALSIYEALGGPHDPNVAKTKNNLASAYLKQNKYQQAEELYKEILHKEDLPAPLGAPNTGTAGDAEQALRRSSSLSKIRESIRRGSEKLVSRLRGEAAAGAAGMKRAMSLNTLNVDAPRAPGTQFPSWHLDKAPRTLSASTQDLSPH
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
10PhosphorylationVQVAAPGSAGLGPER
CEECCCCCCCCCHHC		20.3624719451
19PhosphorylationGLGPERLSPEELVRQ
CCCHHCCCHHHHHHH		36.1628348404
156PhosphorylationFLGQLRQYDPPAESQ
HHHHHHCCCCCCHHC		24.8023927012
162 (in isoform 2)Phosphorylation-35.3127794612
162PhosphorylationQYDPPAESQQSESPP
CCCCCCHHCCCCCCC		35.3130266825
164 (in isoform 2)Phosphorylation-59.4527794612
165PhosphorylationPPAESQQSESPPRRD
CCCHHCCCCCCCCHH		32.1930266825
166 (in isoform 2)Phosphorylation-64.0327794612
167PhosphorylationAESQQSESPPRRDSL
CHHCCCCCCCCHHHH		45.5130266825
173PhosphorylationESPPRRDSLASLFPS
CCCCCHHHHHHHCCC		24.8323927012
176PhosphorylationPRRDSLASLFPSEEE
CCHHHHHHHCCCHHH		35.5227050516
180PhosphorylationSLASLFPSEEEERKG
HHHHHCCCHHHHHCC		50.7527251275
201PhosphorylationAAAQQGGYEIPARLR
HHHHHCCCCCCHHHH		19.94-
215 (in isoform 3)Phosphorylation-2.6727642862
240PhosphorylationALEDLERSSGHCHPD
HHHHHHHHCCCCCHH		31.1528188228
250PhosphorylationHCHPDVATMLNILAL
CCCHHHHHHHHHHHH		23.2628188228
259PhosphorylationLNILALVYRDQNKYK
HHHHHHHHHCCCCHH		14.8828188228
301PhosphorylationLNNLAVLYGKRGRYR
HHHHHHHHCCCCCCC		17.6324260401
361PhosphorylationRHYARALSIYEALGG
HHHHHHHHHHHHHCC		23.3428857561
363PhosphorylationYARALSIYEALGGPH
HHHHHHHHHHHCCCC		7.5625394399
375 (in isoform 3)Phosphorylation-22.0527642862
377PhosphorylationHDPNVAKTKNNLASA
CCCCHHHHHHHHHHH		29.30-
377 (in isoform 3)Phosphorylation-29.3027642862
383PhosphorylationKTKNNLASAYLKQNK
HHHHHHHHHHHHHCH		22.1723612710
385PhosphorylationKNNLASAYLKQNKYQ
HHHHHHHHHHHCHHH		16.37-
399UbiquitinationQQAEELYKEILHKED
HHHHHHHHHHHCCCC		51.40-
405 (in isoform 3)Phosphorylation-54.7727642862
412 (in isoform 3)Phosphorylation-37.6227642862
418PhosphorylationLGAPNTGTAGDAEQA
CCCCCCCCCCCHHHH		25.9824719451
429PhosphorylationAEQALRRSSSLSKIR
HHHHHHHHHHHHHHH		20.1823312004
430PhosphorylationEQALRRSSSLSKIRE
HHHHHHHHHHHHHHH		33.2223312004
431PhosphorylationQALRRSSSLSKIRES
HHHHHHHHHHHHHHH		37.6023312004
433PhosphorylationLRRSSSLSKIRESIR
HHHHHHHHHHHHHHH		28.1624719451
443PhosphorylationRESIRRGSEKLVSRL
HHHHHHCHHHHHHHH		29.7324719451
462MethylationAAGAAGMKRAMSLNT
HHHHHHHHHHHCCCC		35.77115972179
466PhosphorylationAGMKRAMSLNTLNVD
HHHHHHHCCCCCCCC		19.9223927012
469PhosphorylationKRAMSLNTLNVDAPR
HHHHCCCCCCCCCCC		25.6323927012
480 (in isoform 3)Phosphorylation-26.4421406692
480PhosphorylationDAPRAPGTQFPSWHL
CCCCCCCCCCCCCCC		26.4423090842
484PhosphorylationAPGTQFPSWHLDKAP
CCCCCCCCCCCCCCC		28.5423090842
493PhosphorylationHLDKAPRTLSASTQD
CCCCCCCCCCCCCCC		24.8123927012
495PhosphorylationDKAPRTLSASTQDLS
CCCCCCCCCCCCCCC		21.4028355574
497PhosphorylationAPRTLSASTQDLSPH
CCCCCCCCCCCCCCC		24.1928355574
498PhosphorylationPRTLSASTQDLSPH-
CCCCCCCCCCCCCC-		26.3117525332
502PhosphorylationSASTQDLSPH-----
CCCCCCCCCC-----		29.2617525332
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 KLC3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KLC3_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 KLC3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
1433F_HUMANYWHAHphysical
11969417
KLC3_HUMANKLC3physical
25416956
SPERT_HUMANSPERTphysical
25416956
CE57L_HUMANCEP57L1physical
25416956
IHO1_HUMANCCDC36physical
25416956
CENPP_HUMANCENPPphysical
25416956
KLC3_HUMANKLC3physical
21516116
CE57L_HUMANCEP57L1physical
21516116
CCNB1_HUMANCCNB1physical
26496610
LYST_HUMANLYSTphysical
26496610
ITB4_HUMANITGB4physical
26496610
KINH_HUMANKIF5Bphysical
26496610
KLC1_HUMANKLC1physical
26496610
MYH1_HUMANMYH1physical
26496610
NDUA8_HUMANNDUFA8physical
26496610
NFKB2_HUMANNFKB2physical
26496610
IKBL1_HUMANNFKBIL1physical
26496610
ORC4_HUMANORC4physical
26496610
PIMT_HUMANPCMT1physical
26496610
RBBP6_HUMANRBBP6physical
26496610
SVIL_HUMANSVILphysical
26496610
SF01_HUMANSF1physical
26496610
TRI26_HUMANTRIM26physical
26496610
BAG6_HUMANBAG6physical
26496610
SYMPK_HUMANSYMPKphysical
26496610
EXO1_HUMANEXO1physical
26496610
NOLC1_HUMANNOLC1physical
26496610
CAPON_HUMANNOS1APphysical
26496610
BRE1B_HUMANRNF40physical
26496610
DAPK2_HUMANDAPK2physical
26496610
PPIL2_HUMANPPIL2physical
26496610
NGDN_HUMANNGDNphysical
26496610
ATP5S_HUMANATP5Sphysical
26496610
CC174_HUMANCCDC174physical
26496610
KLC2_HUMANKLC2physical
26496610
BHE41_HUMANBHLHE41physical
26496610
C99L2_HUMANCD99L2physical
26496610
KLC4_HUMANKLC4physical
26496610
ACBD5_HUMANACBD5physical
26496610
CB069_HUMANC2orf69physical
26496610
KI13B_HUMANKIF13Bphysical
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 KLC3_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-466, 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-466, AND MASSSPECTROMETRY.
"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-466 AND SER-502, ANDMASS SPECTROMETRY.

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