Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Kinesin-like protein KIF2C  

UniProtKB / Swiss-Prot ID :  KIF2C_HUMAN

Gene Name (Synonyms) : 
KIF2C, KNSL6  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm, cytoskeleton (By similarity). Nucleus (By similarity). Chromosome, centromere. Chromosome, centromere, kinetochore. Note=Associates with the microtubule network at the growing distal tip (the plus-end) of microtubules, probably through interac 

Protein Function :  In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells. Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis. 

Protein Sequence MAMDSSLQARLFPGLAIKIQRSNGLIHSANVRTVNLEKSCVSVEWAEGGATKGKEIDFDDVAAINPELLQ...
Predicted Secondary Structure CCCHHHHHHHHCCCEEEEEEECCCEEEEEEEEEEEECCCEEEEEEEECCCCCCCEECHHHHHHCCHHHHH...
Protein Variant
LocationDescription
449I -> L (in dbSNP:rs4342887). VAR_049683
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
22PhosphoserineKIQRSNGLI
EEEECCCEE
20.90HPRD
Link-
22PhosphoserineKIQRSNGLI
EEEECCCEE
20.90Phosphositeplus
Link-
90Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VTIQKQKRR
CCCCCCCCC
54.67Phosphositeplus
Link-
95PhosphoserineQKRRSVNSK
CCCCCCCCC
29.68Phosphositeplus
Link-
95Phosphoserine (Aurora B)QKRRSVNSK
CCCCCCCCC
29.68PhosphoELM
Link-
95Phosphoserine; by AURKB.QKRRSVNSK
CCCCCCCCC
29.68UniProtKB
Link-
106PhosphoserineAPKESLRSR
CCCCCCCCC
34.90HPRD
Link-
106PhosphoserineAPKESLRSR
CCCCCCCCC
34.90PhosphoELM
Link-
106PhosphoserineAPKESLRSR
CCCCCCCCC
34.90Phosphositeplus
Link-
106Phosphoserine.APKESLRSR
CCCCCCCCC
34.90UniProtKB
Link-
109PhosphoserineESLRSRSTR
CCCCCCCCH
35.56Phosphositeplus
Link-
111PhosphoserineLRSRSTRMS
CCCCCCHHE
22.93HPRD
Link-
111PhosphoserineLRSRSTRMS
CCCCCCHHE
22.93Phosphositeplus
Link-
115PhosphoserineSTRMSTVSE
CCHHEECCC
23.51HPRD
Link-
115Phosphoserine.STRMSTVSE
CCHHEECCC
23.51UniProtKB
Link-
116PhosphothreonineTRMSTVSEL
CHHEECCCC
20.78HPRD
Link-
166PhosphoserineLRMVSEEME
HCCCCHHHH
20.63HPRD
Link-
166PhosphoserineLRMVSEEME
HCCCCHHHH
20.63PhosphoELM
Link-
166PhosphoserineLRMVSEEME
HCCCCHHHH
20.63Phosphositeplus
Link-
166Phosphoserine.LRMVSEEME
HCCCCHHHH
20.63UniProtKB
Link-
179PhosphoserineSIRGSSSAN
CCCCCCCCC
15.98HPRD
Link-
179Phosphoserine.SIRGSSSAN
CCCCCCCCC
15.98UniProtKB
Link-
187PhosphoserineNPVNSVRRK
CCCCCCCCC
19.75Phosphositeplus
Link-
223PhosphotyrosineRAQEYDSSF
HHHHHCCCC
14.72Phosphositeplus
Link-
275N6-acetyllysineQELAKKEID
HHHHCCCCC
64.66Phosphositeplus
Link
276N6-acetyllysineELAKKEIDV
HHHCCCCCE
55.05Phosphositeplus
Link
365Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DLSGKAQNA
CCCCCCCCC
43.34Phosphositeplus
Link-
415Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DLLNKKAKL
HHCCCCCCC
54.82Phosphositeplus
Link
426Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LEDGKQQVQ
EECCCCCEE
50.29Phosphositeplus
Link
518Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AEINKSLLA
HHHHHHHHH
48.41Phosphositeplus
Link
519PhosphoserineEINKSLLAL
HHHHHHHHH
24.91HPRD
Link
519PhosphoserineEINKSLLAL
HHHHHHHHH
24.91Phosphositeplus
Link
604PhosphothreonineIQMETEEME
HHHHHHHHH
31.72HPRD
Link-
611PhosphoserineMEACSNGAL
HHCCCCCCC
45.40PhosphoELM
Link-
611PhosphoserineMEACSNGAL
HHCCCCCCC
45.40Phosphositeplus
Link-
621PhosphoserinePGNLSKEEE
CCCCHHHHH
41.86HPRD
Link-
621PhosphoserinePGNLSKEEE
CCCCHHHHH
41.86Phosphositeplus
Link-
628PhosphoserineEEELSSQMS
HHHHHHHHH
23.08HPRD
Link-
628PhosphoserineEEELSSQMS
HHHHHHHHH
23.08PhosphoELM
Link-
628Phosphoserine.EEELSSQMS
HHHHHHHHH
23.08UniProtKB
Link-
629PhosphoserineEELSSQMSS
HHHHHHHHH
42.39HPRD
Link-
629PhosphoserineEELSSQMSS
HHHHHHHHH
42.39PhosphoELM
Link-
629PhosphoserineEELSSQMSS
HHHHHHHHH
42.39Phosphositeplus
Link-
629Phosphoserine.EELSSQMSS
HHHHHHHHH
42.39UniProtKB
Link-
632PhosphoserineSSQMSSFNE
HHHHHHHHH
24.92HPRD
Link-
632PhosphoserineSSQMSSFNE
HHHHHHHHH
24.92PhosphoELM
Link-
632Phosphoserine.SSQMSSFNE
HHHHHHHHH
24.92UniProtKB
Link-
633PhosphoserineSQMSSFNEA
HHHHHHHHH
27.09HPRD
Link-
633PhosphoserineSQMSSFNEA
HHHHHHHHH
27.09PhosphoELM
Link-
633PhosphoserineSQMSSFNEA
HHHHHHHHH
27.09Phosphositeplus
Link-
633Phosphoserine.SQMSSFNEA
HHHHHHHHH
27.09UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CENPH_HUMANin vitroHPRD:05172HPRD11092768
KIF2C_HUMANin vivo
yeast 2-hybrid
HPRD:05172HPRD11466324
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Aurora B regulates MCAK at the mitotic centromere.";
Andrews P.D., Ovechkina Y., Morrice N., Wagenbach M., Duncan K.,Wordeman L., Swedlow J.R.;
Dev. Cell 6:253-268(2004).
Cited for: PHOSPHORYLATION AT SER-95 BY AURKB, AND SUBCELLULAR LOCATION.
"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-628; SER-629; SER-632AND SER-633, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115 AND SER-179, 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-106 AND SER-166, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures