KLC3_MOUSE - dbPTM
KLC3_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KLC3_MOUSE
UniProt AC Q91W40
Protein Name Kinesin light chain 3
Gene Name Klc3
Organism Mus musculus (Mouse).
Sequence Length 508
Subcellular Localization Cytoplasm, cytoskeleton . In elongating spermatid tail midpiece, localized in outer dense fibers (ODFs) and associates with mitochondria (By similarity). Also localizes to the manchette in elongating spermatids (PubMed:28003339).
Protein Description Kinesin is a microtubule-associated force-producing protein that may play a role in organelle transport..
Protein Sequence MSVQVAAPGSTGLGPERLNPEELVRQTRQVVQGLEALRAEHHSLAGHLAEALAGPGPVAGVELLEEKQQVVNHSLEAIELGLGEAQVLLALSAHVSVLEAEKQRLRAQARRLAQENTWLREELEETQRRLRASEEAVAQLEEEKSHLQFLGQLRQYDPPEESQRPESPPRRDSLASLFPSEEEEKKGPEAAGAAAAQQGGYEIPARLRTLHNLVIQYAGQGRYEVAVPLCRQALEDLERSSGHCHPDVATMLNILALVYRDQNKYKEATELLHDALQIREQTLGPEHPAVAATLNNLAVLYGKRGRYREAEPLCQRALEIREKVLGADHPDVAKQLNNLALLCQNQGKFQDVERHYARALSIYEALGGPQDPNVAKTKNNLASAYLKQNKYQQAEELYKEILSQEALPAPLGAPQGGTAGDTQQQVLRRSSSFSKLRESIRRGSEKLVSRLRGEGMAGAAGMKRAMSLNMLNVDGPRAARTQLSQLSTRHLSEAPRTLSISTQDLSPR
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------MSVQVAAPG
------CCCEECCCC		22.66-
126PhosphorylationLREELEETQRRLRAS
HHHHHHHHHHHHHHC		20.2830165576
162PhosphorylationQYDPPEESQRPESPP
CCCCCHHHCCCCCCC		29.8128066266
167PhosphorylationEESQRPESPPRRDSL
HHHCCCCCCCCCHHH		42.7726824392
173PhosphorylationESPPRRDSLASLFPS
CCCCCCHHHHHHCCC		24.8326824392
176PhosphorylationPRRDSLASLFPSEEE
CCCHHHHHHCCCHHH		35.5228833060
180PhosphorylationSLASLFPSEEEEKKG
HHHHHCCCHHHHHHC		50.7527149854
418PhosphorylationLGAPQGGTAGDTQQQ
CCCCCCCCCCHHHHH		34.0026643407
422PhosphorylationQGGTAGDTQQQVLRR
CCCCCCHHHHHHHHH		27.6226643407
430PhosphorylationQQQVLRRSSSFSKLR
HHHHHHHCCCHHHHH		24.7326643407
431PhosphorylationQQVLRRSSSFSKLRE
HHHHHHCCCHHHHHH		33.3226643407
432PhosphorylationQVLRRSSSFSKLRES
HHHHHCCCHHHHHHH		34.4827149854
434PhosphorylationLRRSSSFSKLRESIR
HHHCCCHHHHHHHHH		32.5026643407
439PhosphorylationSFSKLRESIRRGSEK
CHHHHHHHHHHCCHH		18.2426824392
444PhosphorylationRESIRRGSEKLVSRL
HHHHHHCCHHHHHHH		29.73-
467PhosphorylationAGMKRAMSLNMLNVD
HHHHHHHHCCCCCCC		18.6625521595
484PhosphorylationRAARTQLSQLSTRHL
HHHHHHHHHHHHHHH		21.1829514104
487PhosphorylationRTQLSQLSTRHLSEA
HHHHHHHHHHHHHCC		18.7629514104
492PhosphorylationQLSTRHLSEAPRTLS
HHHHHHHHCCCCEEE		26.1127600695
497PhosphorylationHLSEAPRTLSISTQD
HHHCCCCEEEEECCC		24.6525619855
499PhosphorylationSEAPRTLSISTQDLS
HCCCCEEEEECCCCC		17.5522942356
501PhosphorylationAPRTLSISTQDLSPR
CCCEEEEECCCCCCC		19.3527087446
502PhosphorylationPRTLSISTQDLSPR-
CCEEEEECCCCCCC-		25.1625521595
506PhosphorylationSISTQDLSPR-----
EEECCCCCCC-----		27.2426824392
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_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KLC3_MOUSE !!
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_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KIF5C_MOUSEKif5cphysical
11319135
CROCC_MOUSECroccphysical
16018997
KINH_HUMANKIF5Bphysical
26496610
KLC1_HUMANKLC1physical
26496610
NCBP1_HUMANNCBP1physical
26496610
FXR1_HUMANFXR1physical
26496610
OASL_HUMANOASLphysical
26496610
RB11A_HUMANRAB11Aphysical
26496610
RFIP2_HUMANRAB11FIP2physical
26496610
ZC3H3_HUMANZC3H3physical
26496610
TLS1_HUMANC9orf78physical
26496610
WDR70_HUMANWDR70physical
26496610
ZCCHV_HUMANZC3HAV1physical
26496610
KLC2_HUMANKLC2physical
26496610
RFIP1_HUMANRAB11FIP1physical
26496610
KLC4_HUMANKLC4physical
26496610
TOE1_HUMANTOE1physical
26496610
LYSM2_HUMANLYSMD2physical
26496610
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KLC3_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND MASSSPECTROMETRY.

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