KIF2C_HUMAN - dbPTM
KIF2C_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIF2C_HUMAN
UniProt AC Q99661
Protein Name Kinesin-like protein KIF2C
Gene Name KIF2C
Organism Homo sapiens (Human).
Sequence Length 725
Subcellular Localization Cytoplasm, cytoskeleton . Nucleus . Chromosome, centromere . Chromosome, centromere, kinetochore . Associates with the microtubule network at the growing distal tip (the plus-end) of microtubules, probably through interaction with MTUS2/TIP150 and MA
Protein Description In complex with KIF18B, constitutes the major microtubule plus-end depolymerizing activity in mitotic cells. [PubMed: 21820309 Regulates the turnover of microtubules at the kinetochore and functions in chromosome segregation during mitosis]
Protein Sequence MAMDSSLQARLFPGLAIKIQRSNGLIHSANVRTVNLEKSCVSVEWAEGGATKGKEIDFDDVAAINPELLQLLPLHPKDNLPLQENVTIQKQKRRSVNSKIPAPKESLRSRSTRMSTVSELRITAQENDMEVELPAAANSRKQFSVPPAPTRPSCPAVAEIPLRMVSEEMEEQVHSIRGSSSANPVNSVRRKSCLVKEVEKMKNKREEKKAQNSEMRMKRAQEYDSSFPNWEFARMIKEFRATLECHPLTMTDPIEEHRICVCVRKRPLNKQELAKKEIDVISIPSKCLLLVHEPKLKVDLTKYLENQAFCFDFAFDETASNEVVYRFTARPLVQTIFEGGKATCFAYGQTGSGKTHTMGGDLSGKAQNASKGIYAMASRDVFLLKNQPCYRKLGLEVYVTFFEIYNGKLFDLLNKKAKLRVLEDGKQQVQVVGLQEHLVNSADDVIKMIDMGSACRTSGQTFANSNSSRSHACFQIILRAKGRMHGKFSLVDLAGNERGADTSSADRQTRMEGAEINKSLLALKECIRALGQNKAHTPFRESKLTQVLRDSFIGENSRTCMIATISPGISSCEYTLNTLRYADRVKELSPHSGPSGEQLIQMETEEMEACSNGALIPGNLSKEEEELSSQMSSFNEAMTQIRELEEKAMEELKEIIQQGPDWLELSEMTEQPDYDLETFVNKAESALAQQAKHFSALRDVIKALRLAMQLEEQASRQISSKKRPQ
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
2Acetylation------MAMDSSLQA
------CCCCHHHHH
15.5322814378
5Phosphorylation---MAMDSSLQARLF
---CCCCHHHHHHHC
21.6220860994
6Phosphorylation--MAMDSSLQARLFP
--CCCCHHHHHHHCC
21.8925159151
18AcetylationLFPGLAIKIQRSNGL
HCCCEEEEEEECCCC
27.4625953088
18UbiquitinationLFPGLAIKIQRSNGL
HCCCEEEEEEECCCC
27.46-
22PhosphorylationLAIKIQRSNGLIHSA
EEEEEEECCCCEEEC
20.9030266825
28PhosphorylationRSNGLIHSANVRTVN
ECCCCEEECEEEEEE
17.9730266825
33PhosphorylationIHSANVRTVNLEKSC
EEECEEEEEECCCCE
14.95-
36 (in isoform 2)Ubiquitination-8.3521890473
52UbiquitinationWAEGGATKGKEIDFD
EECCCCCCCCCCCHH
68.41-
54UbiquitinationEGGATKGKEIDFDDV
CCCCCCCCCCCHHHH
53.72-
77UbiquitinationQLLPLHPKDNLPLQE
HHCCCCCCCCCCCCC
48.80-
87PhosphorylationLPLQENVTIQKQKRR
CCCCCCCCCCCHHHH
29.3130576142
90UbiquitinationQENVTIQKQKRRSVN
CCCCCCCCHHHHCCC
54.6721906983
90 (in isoform 1)Ubiquitination-54.6721890473
95PhosphorylationIQKQKRRSVNSKIPA
CCCHHHHCCCCCCCC
29.6821712546
98PhosphorylationQKRRSVNSKIPAPKE
HHHHCCCCCCCCCHH
29.7926434776
99AcetylationKRRSVNSKIPAPKES
HHHCCCCCCCCCHHH
47.7225953088
99UbiquitinationKRRSVNSKIPAPKES
HHHCCCCCCCCCHHH
47.72-
104UbiquitinationNSKIPAPKESLRSRS
CCCCCCCHHHHHCCC
63.14-
106PhosphorylationKIPAPKESLRSRSTR
CCCCCHHHHHCCCCC
34.9030266825
109PhosphorylationAPKESLRSRSTRMST
CCHHHHHCCCCCCCE
35.5622817900
111PhosphorylationKESLRSRSTRMSTVS
HHHHHCCCCCCCEEE
22.9325159151
112PhosphorylationESLRSRSTRMSTVSE
HHHHCCCCCCCEEEE
29.3122199227
114SulfoxidationLRSRSTRMSTVSELR
HHCCCCCCCEEEEEE
3.8921406390
115PhosphorylationRSRSTRMSTVSELRI
HCCCCCCCEEEEEEE
23.5129255136
116PhosphorylationSRSTRMSTVSELRIT
CCCCCCCEEEEEEEE
20.7829255136
118PhosphorylationSTRMSTVSELRITAQ
CCCCCEEEEEEEEEE
30.8822199227
129SulfoxidationITAQENDMEVELPAA
EEEECCCEEEECCCC
10.5521406390
139PhosphorylationELPAAANSRKQFSVP
ECCCCCCCCCCCCCC
35.8128985074
141UbiquitinationPAAANSRKQFSVPPA
CCCCCCCCCCCCCCC
56.36-
144PhosphorylationANSRKQFSVPPAPTR
CCCCCCCCCCCCCCC
31.0822210691
150PhosphorylationFSVPPAPTRPSCPAV
CCCCCCCCCCCCCCC
58.2725159151
153PhosphorylationPPAPTRPSCPAVAEI
CCCCCCCCCCCCEEC
29.4625159151
166PhosphorylationEIPLRMVSEEMEEQV
ECCHHHCCHHHHHHH
20.6322617229
175PhosphorylationEMEEQVHSIRGSSSA
HHHHHHHHHCCCCCC
18.3525159151
177MethylationEEQVHSIRGSSSANP
HHHHHHHCCCCCCCC
41.79115481249
179PhosphorylationQVHSIRGSSSANPVN
HHHHHCCCCCCCCCH
15.9825159151
180PhosphorylationVHSIRGSSSANPVNS
HHHHCCCCCCCCCHH
35.9725262027
181PhosphorylationHSIRGSSSANPVNSV
HHHCCCCCCCCCHHH
33.4929396449
187PhosphorylationSSANPVNSVRRKSCL
CCCCCCHHHHHHHHH
19.7523401153
192PhosphorylationVNSVRRKSCLVKEVE
CHHHHHHHHHHHHHH
15.7529496963
196AcetylationRRKSCLVKEVEKMKN
HHHHHHHHHHHHHHC
42.9926051181
196UbiquitinationRRKSCLVKEVEKMKN
HHHHHHHHHHHHHHC
42.99-
223PhosphorylationRMKRAQEYDSSFPNW
HHHHHHHHHCCCCCH
14.7228796482
234MethylationFPNWEFARMIKEFRA
CCCHHHHHHHHHHHH
32.45115481259
237UbiquitinationWEFARMIKEFRATLE
HHHHHHHHHHHHHHE
41.27-
270UbiquitinationVRKRPLNKQELAKKE
EECCCCCHHHHHHHC
53.48-
275AcetylationLNKQELAKKEIDVIS
CCHHHHHHHCCCEEE
64.6628734223
276AcetylationNKQELAKKEIDVISI
CHHHHHHHCCCEEEE
55.0526051181
276UbiquitinationNKQELAKKEIDVISI
CHHHHHHHCCCEEEE
55.05-
285PhosphorylationIDVISIPSKCLLLVH
CCEEEECCCCEEEEC
34.0424719451
286UbiquitinationDVISIPSKCLLLVHE
CEEEECCCCEEEECC
24.44-
287GlutathionylationVISIPSKCLLLVHEP
EEEECCCCEEEECCC
3.6722555962
295AcetylationLLLVHEPKLKVDLTK
EEEECCCCCEEEHHH
58.9426051181
295UbiquitinationLLLVHEPKLKVDLTK
EEEECCCCCEEEHHH
58.94-
297UbiquitinationLVHEPKLKVDLTKYL
EECCCCCEEEHHHHH
39.57-
301PhosphorylationPKLKVDLTKYLENQA
CCCEEEHHHHHHHCC
17.1221857030
311 (in isoform 2)Ubiquitination-7.5621890473
328PhosphorylationNEVVYRFTARPLVQT
CCEEEEEECCCHHHH
16.8628674151
341UbiquitinationQTIFEGGKATCFAYG
HHHHCCCEEEEEEEC
51.91-
347PhosphorylationGKATCFAYGQTGSGK
CEEEEEEECCCCCCC
6.9029496907
354UbiquitinationYGQTGSGKTHTMGGD
ECCCCCCCCEECCCC
38.54-
361 (in isoform 2)Ubiquitination-31.7521890473
365MethylationMGGDLSGKAQNASKG
CCCCCCCCCCHHHCC
43.3442355277
365UbiquitinationMGGDLSGKAQNASKG
CCCCCCCCCCHHHCC
43.3421906983
365 (in isoform 1)Ubiquitination-43.3421890473
371UbiquitinationGKAQNASKGIYAMAS
CCCCHHHCCHHEEEC
47.09-
372 (in isoform 2)Ubiquitination-18.6821890473
374PhosphorylationQNASKGIYAMASRDV
CHHHCCHHEEECCCE
10.0527642862
385AcetylationSRDVFLLKNQPCYRK
CCCEEEECCCHHHHH
56.5426051181
385UbiquitinationSRDVFLLKNQPCYRK
CCCEEEECCCHHHHH
56.54-
398PhosphorylationRKLGLEVYVTFFEIY
HHCCCEEEEEEEEEE
5.61-
405PhosphorylationYVTFFEIYNGKLFDL
EEEEEEEECCCHHHH
15.63-
415AcetylationKLFDLLNKKAKLRVL
CHHHHHCCCCCEEEE
54.8225953088
415UbiquitinationKLFDLLNKKAKLRVL
CHHHHHCCCCCEEEE
54.8221906983
415 (in isoform 1)Ubiquitination-54.8221890473
416UbiquitinationLFDLLNKKAKLRVLE
HHHHHCCCCCEEEEC
50.08-
426UbiquitinationLRVLEDGKQQVQVVG
EEEECCCCCEEEEEE
50.2921906983
426 (in isoform 1)Ubiquitination-50.2921890473
453PhosphorylationIKMIDMGSACRTSGQ
HHHHCCCCCHHCCCC
19.9822199227
457PhosphorylationDMGSACRTSGQTFAN
CCCCCHHCCCCCCCC
36.7728450419
458PhosphorylationMGSACRTSGQTFANS
CCCCHHCCCCCCCCC
15.0028450419
461PhosphorylationACRTSGQTFANSNSS
CHHCCCCCCCCCCCC
28.3928450419
464 (in isoform 2)Ubiquitination-37.2221890473
487UbiquitinationAKGRMHGKFSLVDLA
HCCCCCCEEEEEECC
19.66-
489PhosphorylationGRMHGKFSLVDLAGN
CCCCCEEEEEECCCC
30.85-
498MethylationVDLAGNERGADTSSA
EECCCCCCCCCCCHH
49.99115481229
518UbiquitinationMEGAEINKSLLALKE
HCHHHHHHHHHHHHH
48.4121890473
518 (in isoform 1)Ubiquitination-48.4121890473
519PhosphorylationEGAEINKSLLALKEC
CHHHHHHHHHHHHHH
24.9123401153
524UbiquitinationNKSLLALKECIRALG
HHHHHHHHHHHHHHC
44.95-
526GlutathionylationSLLALKECIRALGQN
HHHHHHHHHHHHCCC
2.1422555962
534UbiquitinationIRALGQNKAHTPFRE
HHHHCCCCCCCCCCH
33.39-
537PhosphorylationLGQNKAHTPFRESKL
HCCCCCCCCCCHHHH
29.0522817900
543AcetylationHTPFRESKLTQVLRD
CCCCCHHHHHHHHHH
51.2925953088
543UbiquitinationHTPFRESKLTQVLRD
CCCCCHHHHHHHHHH
51.29-
549MethylationSKLTQVLRDSFIGEN
HHHHHHHHHHCCCCC
38.38-
551PhosphorylationLTQVLRDSFIGENSR
HHHHHHHHCCCCCCC
16.6023186163
589PhosphorylationADRVKELSPHSGPSG
HHHHHHCCCCCCCCH
22.9726074081
592PhosphorylationVKELSPHSGPSGEQL
HHHCCCCCCCCHHHE
56.6426074081
595PhosphorylationLSPHSGPSGEQLIQM
CCCCCCCCHHHEEEE
59.4926074081
604PhosphorylationEQLIQMETEEMEACS
HHEEEECHHHHHHHH
31.7220068231
611PhosphorylationTEEMEACSNGALIPG
HHHHHHHHCCCCCCC
45.4020068231
621PhosphorylationALIPGNLSKEEEELS
CCCCCCCCHHHHHHH
41.8620068231
628PhosphorylationSKEEEELSSQMSSFN
CHHHHHHHHHHHHHH
23.0822199227
629PhosphorylationKEEEELSSQMSSFNE
HHHHHHHHHHHHHHH
42.3917525332
632PhosphorylationEELSSQMSSFNEAMT
HHHHHHHHHHHHHHH
24.9225159151
633PhosphorylationELSSQMSSFNEAMTQ
HHHHHHHHHHHHHHH
27.0925159151
639PhosphorylationSSFNEAMTQIRELEE
HHHHHHHHHHHHHHH
28.0829523821
647UbiquitinationQIRELEEKAMEELKE
HHHHHHHHHHHHHHH
43.59-
692AcetylationSALAQQAKHFSALRD
HHHHHHHHHHHHHHH
40.6225953088
692UbiquitinationSALAQQAKHFSALRD
HHHHHHHHHHHHHHH
40.62-
702AcetylationSALRDVIKALRLAMQ
HHHHHHHHHHHHHHH
41.0125953088
702UbiquitinationSALRDVIKALRLAMQ
HHHHHHHHHHHHHHH
41.01-
715PhosphorylationMQLEEQASRQISSKK
HHHHHHHHHHHHHCC
25.1430266825
719PhosphorylationEQASRQISSKKRPQ-
HHHHHHHHHCCCCC-
27.97-

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
95SPhosphorylationKinaseAURBQ96GD4
PSP
109SPhosphorylationKinaseAURKBQ96GD4
GPS
111SPhosphorylationKinaseAURKBQ96GD4
GPS
111SPhosphorylationKinasePAK1Q13153
PSP
115SPhosphorylationKinaseAURKBQ96GD4
GPS
192SPhosphorylationKinaseAURKBQ96GD4
GPS
192SPhosphorylationKinasePAK1Q13153
PSP
537TPhosphorylationKinaseCDK1P06493
PSP
621SPhosphorylationKinasePLK1P53350
PSP
632SPhosphorylationKinasePLK1P53350
PSP
633SPhosphorylationKinasePLK1P53350
PSP
715SPhosphorylationKinasePLK1P53350
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KIF2C_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 KIF2C_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KIF2C_HUMANKIF2Cphysical
11466324
A4_HUMANAPPphysical
21832049
ZN566_HUMANZNF566physical
21988832
PLK1_HUMANPLK1physical
24931513
AATC_HUMANGOT1physical
26344197
HSP7E_HUMANHSPA14physical
26344197
PCBP2_HUMANPCBP2physical
26344197
WDR5_HUMANWDR5physical
26344197
CENPB_HUMANCENPBphysical
26496610
T2FA_HUMANGTF2F1physical
26496610
KIF2A_HUMANKIF2Aphysical
26496610
MBD1_HUMANMBD1physical
26496610
RL5_HUMANRPL5physical
26496610
RL7_HUMANRPL7physical
26496610
RL9_HUMANRPL9physical
26496610
RS25_HUMANRPS25physical
26496610
BRPF1_HUMANBRPF1physical
26496610
ADAM9_HUMANADAM9physical
26496610
ESPL1_HUMANESPL1physical
26496610
CE170_HUMANCEP170physical
26496610
SRGP3_HUMANSRGAP3physical
26496610
POP1_HUMANPOP1physical
26496610
RRP12_HUMANRRP12physical
26496610
CAB45_HUMANSDF4physical
26496610
TBCD7_HUMANTBC1D7physical
26496610
TEX10_HUMANTEX10physical
26496610
BOREA_HUMANCDCA8physical
26496610
BCCIP_HUMANBCCIPphysical
26496610
WDR18_HUMANWDR18physical
26496610
ZN668_HUMANZNF668physical
26496610
PCGF5_HUMANPCGF5physical
26496610
RM52_HUMANMRPL52physical
26496610
SMS2_HUMANSGMS2physical
26496610
WDR62_HUMANWDR62physical
26496610
K2C79_HUMANKRT79physical
26496610
MARE1_HUMANMAPRE1physical
27173435
MARE3_HUMANMAPRE3physical
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 KIF2C_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.
"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.

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