KIF2A_HUMAN - dbPTM
KIF2A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIF2A_HUMAN
UniProt AC O00139
Protein Name Kinesin-like protein KIF2A
Gene Name KIF2A
Organism Homo sapiens (Human).
Sequence Length 706
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, spindle. Localized to the spindle microtubules and spindle poles from prophase to metaphase. Efficient targ
Protein Description Plus end-directed microtubule-dependent motor required for normal brain development. May regulate microtubule dynamics during axonal growth. Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate. Required for normal spindle dynamics during mitosis. Promotes spindle turnover. Implicated in formation of bipolar mitotic spindles. Has microtubule depolymerization activity..
Protein Sequence MATANFGKIQIGIYVEIKRSDGRIHQAMVTSLNEDNESVTVEWIENGDTKGKEIDLESIFSLNPDLVPDEEIEPSPETPPPPASSAKVNKIVKNRRTVASIKNDPPSRDNRVVGSARARPSQFPEQSSSAQQNGSVSDISPVQAAKKEFGPPSRRKSNCVKEVEKLQEKREKRRLQQQELREKRAQDVDATNPNYEIMCMIRDFRGSLDYRPLTTADPIDEHRICVCVRKRPLNKKETQMKDLDVITIPSKDVVMVHEPKQKVDLTRYLENQTFRFDYAFDDSAPNEMVYRFTARPLVETIFERGMATCFAYGQTGSGKTHTMGGDFSGKNQDCSKGIYALAARDVFLMLKKPNYKKLELQVYATFFEIYSGKVFDLLNRKTKLRVLEDGKQQVQVVGLQEREVKCVEDVLKLIDIGNSCRTSGQTSANAHSSRSHAVFQIILRRKGKLHGKFSLIDLAGNERGADTSSADRQTRLEGAEINKSLLALKECIRALGRNKPHTPFRASKLTQVLRDSFIGENSRTCMIATISPGMASCENTLNTLRYANRVKELTVDPTAAGDVRPIMHHPPNQIDDLETQWGVGSSPQRDDLKLLCEQNEEEVSPQLFTFHEAVSQMVEMEEQVVEDHRAVFQESIRWLEDEKALLEMTEEVDYDVDSYATQLEAILEQKIDILTELRDKVKSFRAALQEEEQASKQINPKRPRAL
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
20PhosphorylationIYVEIKRSDGRIHQA
EEEEEECCCCCEEEE		39.14-
55PhosphorylationDTKGKEIDLESIFSL
CCCCCEECHHHHHCC		45.5418452278
58PhosphorylationGKEIDLESIFSLNPD
CCEECHHHHHCCCCC		35.9120068231
61PhosphorylationIDLESIFSLNPDLVP
ECHHHHHCCCCCCCC		26.1020068231
75PhosphorylationPDEEIEPSPETPPPP
CCCCCCCCCCCCCCC		23.6830278072
78PhosphorylationEIEPSPETPPPPASS
CCCCCCCCCCCCCCH		44.4730278072
84PhosphorylationETPPPPASSAKVNKI
CCCCCCCCHHHHHHH		36.2819690332
85PhosphorylationTPPPPASSAKVNKIV
CCCCCCCHHHHHHHH		33.9320873877
94 (in isoform 2)Phosphorylation-27.9826434776
97PhosphorylationKIVKNRRTVASIKND
HHHHCCCCEEECCCC		19.7226055452
100PhosphorylationKNRRTVASIKNDPPS
HCCCCEEECCCCCCC		29.7423401153
100 (in isoform 2)Phosphorylation-29.7426434776
101 (in isoform 2)Phosphorylation-3.3126434776
102AcetylationRRTVASIKNDPPSRD
CCCEEECCCCCCCCC		53.4523749302
102 (in isoform 2)Phosphorylation-53.4526434776
107PhosphorylationSIKNDPPSRDNRVVG
ECCCCCCCCCCCCCC		58.6220860994
115PhosphorylationRDNRVVGSARARPSQ
CCCCCCCCEECCHHH		11.7227535140
120PhosphorylationVGSARARPSQFPEQS
CCCEECCHHHCCCCC		31.3419651622
121PhosphorylationGSARARPSQFPEQSS
CCEECCHHHCCCCCC		38.6123312004
127PhosphorylationPSQFPEQSSSAQQNG
HHHCCCCCCCCCCCC		25.2928857561
128PhosphorylationSQFPEQSSSAQQNGS
HHCCCCCCCCCCCCC		29.4128857561
129PhosphorylationQFPEQSSSAQQNGSV
HCCCCCCCCCCCCCH		35.0328857561
135PhosphorylationSSAQQNGSVSDISPV
CCCCCCCCHHHCCHH		26.4630266825
137PhosphorylationAQQNGSVSDISPVQA
CCCCCCHHHCCHHHH		30.8130266825
140PhosphorylationNGSVSDISPVQAAKK
CCCHHHCCHHHHHHH		24.8223401153
147AcetylationSPVQAAKKEFGPPSR
CHHHHHHHHHCCCCC		54.2530589725
147MethylationSPVQAAKKEFGPPSR
CHHHHHHHHHCCCCC		54.2530589725
153PhosphorylationKKEFGPPSRRKSNCV
HHHHCCCCCCCCHHH		48.1027535140
157PhosphorylationGPPSRRKSNCVKEVE
CCCCCCCCHHHHHHH		33.3826074081
161MethylationRRKSNCVKEVEKLQE
CCCCHHHHHHHHHHH		59.2423644510
165AcetylationNCVKEVEKLQEKREK
HHHHHHHHHHHHHHH		61.7225953088
169MethylationEVEKLQEKREKRRLQ
HHHHHHHHHHHHHHH		53.5523644510
195PhosphorylationVDATNPNYEIMCMIR
CCCCCCCCEEEEEEE		14.2120736484
199GlutathionylationNPNYEIMCMIRDFRG
CCCCEEEEEEECCCC		2.2322555962
207PhosphorylationMIRDFRGSLDYRPLT
EEECCCCCCCCCCCC		17.5130576142
210PhosphorylationDFRGSLDYRPLTTAD
CCCCCCCCCCCCCCC		21.3029978859
214PhosphorylationSLDYRPLTTADPIDE
CCCCCCCCCCCCCCC		23.7129978859
215PhosphorylationLDYRPLTTADPIDEH
CCCCCCCCCCCCCCC		36.4229978859
250PhosphorylationLDVITIPSKDVVMVH
CCEEEECCCCEEEEC		37.3224719451
251AcetylationDVITIPSKDVVMVHE
CEEEECCCCEEEECC		49.5426051181
278PhosphorylationNQTFRFDYAFDDSAP
CCEEEEEEEECCCCC		13.37-
283PhosphorylationFDYAFDDSAPNEMVY
EEEEECCCCCCCEEE		47.6820068231
290PhosphorylationSAPNEMVYRFTARPL
CCCCCEEEEEECHHH		9.9420068231
312PhosphorylationGMATCFAYGQTGSGK
CCEEEEEECCCCCCC		6.9029496907
328PhosphorylationHTMGGDFSGKNQDCS
EECCCCCCCCCCCHH		54.3122210691
330UbiquitinationMGGDFSGKNQDCSKG
CCCCCCCCCCCHHHH		50.68-
330 (in isoform 4)Ubiquitination-50.68-
330AcetylationMGGDFSGKNQDCSKG
CCCCCCCCCCCHHHH		50.6826051181
335PhosphorylationSGKNQDCSKGIYALA
CCCCCCHHHHHHHHH		42.0522210691
336MalonylationGKNQDCSKGIYALAA
CCCCCHHHHHHHHHH		56.5126320211
336AcetylationGKNQDCSKGIYALAA
CCCCCHHHHHHHHHH		56.5126051181
345 (in isoform 2)Ubiquitination-30.6921906983
371 (in isoform 1)Ubiquitination-37.4921906983
391 (in isoform 4)Ubiquitination-50.2921906983
391AcetylationLRVLEDGKQQVQVVG
EEEECCCCCEEEEEE		50.2926051181
391 (in isoform 3)Ubiquitination-50.2921906983
391MethylationLRVLEDGKQQVQVVG
EEEECCCCCEEEEEE		50.29116251817
391UbiquitinationLRVLEDGKQQVQVVG
EEEECCCCCEEEEEE		50.292190698
432PhosphorylationQTSANAHSSRSHAVF
CCCCCCCCCHHHHHH		25.6527732954
433PhosphorylationTSANAHSSRSHAVFQ
CCCCCCCCHHHHHHH		28.1227732954
483 (in isoform 4)Ubiquitination-48.41-
483UbiquitinationLEGAEINKSLLALKE
HCHHHHHHHHHHHHH		48.41-
484PhosphorylationEGAEINKSLLALKEC
CHHHHHHHHHHHHHH		24.9121712546
489 (in isoform 4)Ubiquitination-44.95-
489AcetylationNKSLLALKECIRALG
HHHHHHHHHHHHHHC		44.9525953088
491GlutathionylationSLLALKECIRALGRN
HHHHHHHHHHHHCCC		2.1422555962
508 (in isoform 4)Ubiquitination-55.35-
508UbiquitinationHTPFRASKLTQVLRD
CCCCHHHHHHHHHHH		55.35-
508AcetylationHTPFRASKLTQVLRD
CCCCHHHHHHHHHHH		55.3525953088
514MethylationSKLTQVLRDSFIGEN
HHHHHHHHHHCCCCC		38.38-
516PhosphorylationLTQVLRDSFIGENSR
HHHHHHHHCCCCCCC		16.6023186163
546PhosphorylationNTLNTLRYANRVKEL
HHHHHHHHHHCCEEE		16.0222817900
554PhosphorylationANRVKELTVDPTAAG
HHCCEEEECCCCCCC		24.7720873877
556 (in isoform 4)Phosphorylation-29.60-
558PhosphorylationKELTVDPTAAGDVRP
EEEECCCCCCCCCCC		25.3620873877
573 (in isoform 4)Phosphorylation-46.3824076635
575 (in isoform 4)Phosphorylation-44.6827732954
578 (in isoform 4)Phosphorylation-46.0427732954
579PhosphorylationNQIDDLETQWGVGSS
CCCCCCHHCCCCCCC		36.6030108239
582 (in isoform 4)Phosphorylation-12.2327732954
584 (in isoform 4)Phosphorylation-20.6127732954
585PhosphorylationETQWGVGSSPQRDDL
HHCCCCCCCCCHHHH		36.1230266825
586 (in isoform 4)Phosphorylation-21.0827732954
586PhosphorylationTQWGVGSSPQRDDLK
HCCCCCCCCCHHHHH		21.0830266825
604PhosphorylationEQNEEEVSPQLFTFH
HCCCCCCCHHHHHHH		15.3725159151
609PhosphorylationEVSPQLFTFHEAVSQ
CCCHHHHHHHHHHHH		32.4527174698
615PhosphorylationFTFHEAVSQMVEMEE
HHHHHHHHHHHHHHH		21.43-
624PhosphorylationMVEMEEQVVEDHRAV
HHHHHHHHHHHHHHH		6.0327251275
635PhosphorylationHRAVFQESIRWLEDE
HHHHHHHHHHHHHHH		13.4830266825
675PhosphorylationEQKIDILTELRDKVK
HHHCHHHHHHHHHHH		33.0519007248
680AcetylationILTELRDKVKSFRAA
HHHHHHHHHHHHHHH		45.1626051181
683PhosphorylationELRDKVKSFRAALQE
HHHHHHHHHHHHHHH		23.97-
695PhosphorylationLQEEEQASKQINPKR
HHHHHHHHHHCCCCC		25.4528857561
696UbiquitinationQEEEQASKQINPKRP
HHHHHHHHHCCCCCC		59.21-
696AcetylationQEEEQASKQINPKRP
HHHHHHHHHCCCCCC		59.2126051181
734 (in isoform 4)Ubiquitination--
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
135SPhosphorylationKinaseTTBK2Q6IQ55
PSP
554TPhosphorylationKinasePLK1P53350
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KIF2A_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 KIF2A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KIF2A_HUMANKIF2Aphysical
25416956
LAR1B_HUMANLARP1Bphysical
25416956
RM53_HUMANMRPL53physical
25416956
FA13C_HUMANFAM13Cphysical
25416956
RAE1_HUMANCHMphysical
26344197
LAR1B_HUMANLARP1Bphysical
21516116
ACADV_HUMANACADVLphysical
26496610
AL7A1_HUMANALDH7A1physical
26496610
KC1E_HUMANCSNK1Ephysical
26496610
GNS_HUMANGNSphysical
26496610
MTRR_HUMANMTRRphysical
26496610
IKBL1_HUMANNFKBIL1physical
26496610
KPCA_HUMANPRKCAphysical
26496610
ROBO2_HUMANROBO2physical
26496610
TIAR_HUMANTIAL1physical
26496610
BAG6_HUMANBAG6physical
26496610
UBL4A_HUMANUBL4Aphysical
26496610
EIF3F_HUMANEIF3Fphysical
26496610
CE170_HUMANCEP170physical
26496610
TRAP1_HUMANTRAP1physical
26496610
CELF1_HUMANCELF1physical
26496610
KIF2C_HUMANKIF2Cphysical
26496610
TARA_HUMANTRIOBPphysical
26496610
EXOC3_HUMANEXOC3physical
26496610
MTF2_HUMANMTF2physical
26496610
K0556_HUMANKIAA0556physical
26496610
ATP5S_HUMANATP5Sphysical
26496610
UBR5_HUMANUBR5physical
26496610
GET4_HUMANGET4physical
26496610
WDR35_HUMANWDR35physical
26496610
TMPS3_HUMANTMPRSS3physical
26496610
ZMYM1_HUMANZMYM1physical
26496610
S35E1_HUMANSLC35E1physical
26496610
WDCP_HUMANC2orf44physical
26496610
FIP1_HUMANFIP1L1physical
26496610
C99L2_HUMANCD99L2physical
26496610
G45IP_HUMANGADD45GIP1physical
26496610
C170B_HUMANCEP170Bphysical
26496610
TSNAX_HUMANTSNAXgenetic
20506231
RHPN1_HUMANRHPN1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615411Cortical dysplasia, complex, with other brain malformations 3 (CDCBM3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KIF2A_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-75 AND THR-78, 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-140 AND SER-695, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-78 AND SER-140, AND MASSSPECTROMETRY.

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