KIF22_HUMAN - dbPTM
KIF22_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIF22_HUMAN
UniProt AC Q14807
Protein Name Kinesin-like protein KIF22
Gene Name KIF22
Organism Homo sapiens (Human).
Sequence Length 665
Subcellular Localization Nucleus . Cytoplasm, cytoskeleton .
Protein Description Kinesin family member that is involved in spindle formation and the movements of chromosomes during mitosis and meiosis. Binds to microtubules and to DNA (By similarity). Plays a role in congression of laterally attached chromosomes in NDC80-depleted cells. [PubMed: 25743205]
Protein Sequence MAAGGSTQQRRREMAAASAAAISGAGRCRLSKIGATRRPPPARVRVAVRLRPFVDGTAGASDPPCVRGMDSCSLEIANWRNHQETLKYQFDAFYGERSTQQDIYAGSVQPILRHLLEGQNASVLAYGPTGAGKTHTMLGSPEQPGVIPRALMDLLQLTREEGAEGRPWALSVTMSYLEIYQEKVLDLLDPASGDLVIREDCRGNILIPGLSQKPISSFADFERHFLPASRNRTVGATRLNQRSSRSHAVLLVKVDQRERLAPFRQREGKLYLIDLAGSEDNRRTGNKGLRLKESGAINTSLFVLGKVVDALNQGLPRVPYRDSKLTRLLQDSLGGSAHSILIANIAPERRFYLDTVSALNFAARSKEVINRPFTNESLQPHALGPVKLSQKELLGPPEAKRARGPEEEEIGSPEPMAAPASASQKLSPLQKLSSMDPAMLERLLSLDRLLASQGSQGAPLLSTPKRERMVLMKTVEEKDLEIERLKTKQKELEAKMLAQKAEEKENHCPTMLRPLSHRTVTGAKPLKKAVVMPLQLIQEQAASPNAEIHILKNKGRKRKLESLDALEPEEKAEDCWELQISPELLAHGRQKILDLLNEGSARDLRSLQRIGPKKAQLIVGWRELHGPFSQVEDLERVEGITGKQMESFLKANILGLAAGQRCGAS
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
12DimethylationGSTQQRRREMAAASA
CCHHHHHHHHHHHHH		39.99-
12MethylationGSTQQRRREMAAASA
CCHHHHHHHHHHHHH		39.9924380769
18PhosphorylationRREMAAASAAAISGA
HHHHHHHHHHHHHCC		17.4520068231
23PhosphorylationAASAAAISGAGRCRL
HHHHHHHHCCCCCCC		20.1920068231
27DimethylationAAISGAGRCRLSKIG
HHHHCCCCCCCCCCC		11.23-
27MethylationAAISGAGRCRLSKIG
HHHHCCCCCCCCCCC		11.2324380777
31PhosphorylationGAGRCRLSKIGATRR
CCCCCCCCCCCCCCC		11.6820068231
32SumoylationAGRCRLSKIGATRRP
CCCCCCCCCCCCCCC		50.15-
32UbiquitinationAGRCRLSKIGATRRP
CCCCCCCCCCCCCCC		50.15-
32SumoylationAGRCRLSKIGATRRP
CCCCCCCCCCCCCCC		50.15-
32AcetylationAGRCRLSKIGATRRP
CCCCCCCCCCCCCCC		50.1525953088
36PhosphorylationRLSKIGATRRPPPAR
CCCCCCCCCCCCCCC		23.2320068231
61PhosphorylationVDGTAGASDPPCVRG
CCCCCCCCCCCCCCC		50.1326714015
87UbiquitinationRNHQETLKYQFDAFY
CCCHHHHHHHHHCCC		44.41-
97MethylationFDAFYGERSTQQDIY
HHCCCCCCCCCCCCH		40.41115481207
122PhosphorylationLLEGQNASVLAYGPT
HHCCCCCEEEEECCC		25.8025332170
129PhosphorylationSVLAYGPTGAGKTHT
EEEEECCCCCCCCCC		34.9925332170
133UbiquitinationYGPTGAGKTHTMLGS
ECCCCCCCCCCCCCC		36.28-
134PhosphorylationGPTGAGKTHTMLGSP
CCCCCCCCCCCCCCC		22.9720068231
136PhosphorylationTGAGKTHTMLGSPEQ
CCCCCCCCCCCCCCC		21.2320068231
140PhosphorylationKTHTMLGSPEQPGVI
CCCCCCCCCCCCCCH		22.6928985074
158PhosphorylationLMDLLQLTREEGAEG
HHHHHHHHHHCCCCC		24.0720068231
171PhosphorylationEGRPWALSVTMSYLE
CCCCCCCEEEHHHHH		14.0623401153
173PhosphorylationRPWALSVTMSYLEIY
CCCCCEEEHHHHHHH		9.3123401153
175PhosphorylationWALSVTMSYLEIYQE
CCCEEEHHHHHHHHH		19.7323401153
176PhosphorylationALSVTMSYLEIYQEK
CCEEEHHHHHHHHHH		9.4923401153
180PhosphorylationTMSYLEIYQEKVLDL
EHHHHHHHHHHHHHH		10.9723401153
213UbiquitinationLIPGLSQKPISSFAD
ECCCCCCCCCCCHHH		40.7321906983
233PhosphorylationLPASRNRTVGATRLN
CCCCCCCCCCCHHCC		27.1722210691
237PhosphorylationRNRTVGATRLNQRSS
CCCCCCCHHCCCCCC		29.7522210691
269UbiquitinationPFRQREGKLYLIDLA
CHHHCCCCEEEEECC		29.25-
287MethylationDNRRTGNKGLRLKES
CCCCCCCCCCCCCCC		61.74116252691
292UbiquitinationGNKGLRLKESGAINT
CCCCCCCCCCCCCCC		43.32-
294PhosphorylationKGLRLKESGAINTSL
CCCCCCCCCCCCCHH		31.7528555341
324UbiquitinationRVPYRDSKLTRLLQD
CCCCCCHHHHHHHHH		59.16-
326PhosphorylationPYRDSKLTRLLQDSL
CCCCHHHHHHHHHHC		24.0220068231
357PhosphorylationRFYLDTVSALNFAAR
CEEHHHHHHHHHHHC		29.1824667141
366UbiquitinationLNFAARSKEVINRPF
HHHHHCCCCHHCCCC		50.91-
387SumoylationPHALGPVKLSQKELL
CCCCCCCCCCHHHHH		45.62-
387SumoylationPHALGPVKLSQKELL
CCCCCCCCCCHHHHH		45.62-
387UbiquitinationPHALGPVKLSQKELL
CCCCCCCCCCHHHHH		45.62-
391UbiquitinationGPVKLSQKELLGPPE
CCCCCCHHHHHCCHH		47.1321890473
400SumoylationLLGPPEAKRARGPEE
HHCCHHHHHCCCCCH		44.95-
400SumoylationLLGPPEAKRARGPEE
HHCCHHHHHCCCCCH		44.95-
400UbiquitinationLLGPPEAKRARGPEE
HHCCHHHHHCCCCCH		44.95-
412PhosphorylationPEEEEIGSPEPMAAP
CCHHHCCCCCCCCCC		31.5825159151
421PhosphorylationEPMAAPASASQKLSP
CCCCCCCCHHHCCCH		27.6523401153
423PhosphorylationMAAPASASQKLSPLQ
CCCCCCHHHCCCHHH		25.9223401153
425UbiquitinationAPASASQKLSPLQKL
CCCCHHHCCCHHHHH		48.7321890473
427PhosphorylationASASQKLSPLQKLSS
CCHHHCCCHHHHHHC		30.5122167270
431UbiquitinationQKLSPLQKLSSMDPA
HCCCHHHHHHCCCHH		59.00-
433PhosphorylationLSPLQKLSSMDPAML
CCHHHHHHCCCHHHH		30.5626074081
434PhosphorylationSPLQKLSSMDPAMLE
CHHHHHHCCCHHHHH		37.3328555341
445PhosphorylationAMLERLLSLDRLLAS
HHHHHHHHHHHHHHH		32.5828450419
452PhosphorylationSLDRLLASQGSQGAP
HHHHHHHHCCCCCCC		34.7417525332
455PhosphorylationRLLASQGSQGAPLLS
HHHHHCCCCCCCCCC		20.1521712546
462PhosphorylationSQGAPLLSTPKRERM
CCCCCCCCCCHHHCE		50.8023401153
463PhosphorylationQGAPLLSTPKRERMV
CCCCCCCCCHHHCEE		32.5729255136
465AcetylationAPLLSTPKRERMVLM
CCCCCCCHHHCEEEE		67.9620167786
465UbiquitinationAPLLSTPKRERMVLM
CCCCCCCHHHCEEEE		67.96-
465SumoylationAPLLSTPKRERMVLM
CCCCCCCHHHCEEEE		67.96-
465SumoylationAPLLSTPKRERMVLM
CCCCCCCHHHCEEEE		67.9628112733
473UbiquitinationRERMVLMKTVEEKDL
HHCEEEEEEHHHHHH		45.30-
474PhosphorylationERMVLMKTVEEKDLE
HCEEEEEEHHHHHHH		21.1329083192
478UbiquitinationLMKTVEEKDLEIERL
EEEEHHHHHHHHHHH		54.85-
478AcetylationLMKTVEEKDLEIERL
EEEEHHHHHHHHHHH		54.8526051181
495UbiquitinationKQKELEAKMLAQKAE
HHHHHHHHHHHHHHH		25.68-
500SumoylationEAKMLAQKAEEKENH
HHHHHHHHHHHHHCC		52.75-
500SumoylationEAKMLAQKAEEKENH
HHHHHHHHHHHHHCC		52.75-
504UbiquitinationLAQKAEEKENHCPTM
HHHHHHHHHCCCCCC		56.15-
510PhosphorylationEKENHCPTMLRPLSH
HHHCCCCCCCCCCCC		33.9429449344
516PhosphorylationPTMLRPLSHRTVTGA
CCCCCCCCCCCCCCC		17.3829449344
524UbiquitinationHRTVTGAKPLKKAVV
CCCCCCCCCCCCHHH		52.83-
528UbiquitinationTGAKPLKKAVVMPLQ
CCCCCCCCHHHHHHH		54.84-
543PhosphorylationLIQEQAASPNAEIHI
HHHHHHCCCCCEEEE		23.0025159151
552UbiquitinationNAEIHILKNKGRKRK
CCEEEEECCCCCCCC		56.8821890473
554UbiquitinationEIHILKNKGRKRKLE
EEEEECCCCCCCCHH		59.51-
559SumoylationKNKGRKRKLESLDAL
CCCCCCCCHHHHCCC		60.69-
559UbiquitinationKNKGRKRKLESLDAL
CCCCCCCCHHHHCCC		60.69-
559SumoylationKNKGRKRKLESLDAL
CCCCCCCCHHHHCCC		60.69-
562PhosphorylationGRKRKLESLDALEPE
CCCCCHHHHCCCCHH		41.8230266825
581PhosphorylationDCWELQISPELLAHG
HHHHCCCCHHHHHCC		10.2030266825
591UbiquitinationLLAHGRQKILDLLNE
HHHCCHHHHHHHHHC		43.8221890473
591UbiquitinationLLAHGRQKILDLLNE
HHHCCHHHHHHHHHC		43.8221890473
600PhosphorylationLDLLNEGSARDLRSL
HHHHHCCCHHHHHHH		17.6026074081
643UbiquitinationRVEGITGKQMESFLK
HHCCCCHHHHHHHHH		37.51-
647PhosphorylationITGKQMESFLKANIL
CCHHHHHHHHHHHHH		30.4524719451
650UbiquitinationKQMESFLKANILGLA
HHHHHHHHHHHHHHH		37.06-
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
427SPhosphorylationKinaseCDK1P06493
PSP
463TPhosphorylationKinaseCDK1P06493
PSP
-KUbiquitinationE3 ubiquitin ligaseCHFRQ96EP1
PMID:19321445
-KUbiquitinationE3 ubiquitin ligaseSIAH1Q8IUQ4
PMID:20144232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KIF22_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 KIF22_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GDF9_HUMANGDF9physical
16169070
MIC60_HUMANIMMTphysical
16169070
PJA1_HUMANPJA1physical
16169070
SIAH1_HUMANSIAH1physical
11146551
CHFR_HUMANCHFRphysical
19321445
CO4A_HUMANC4Aphysical
26496610
CCNB1_HUMANCCNB1physical
26496610
FUS_HUMANFUSphysical
26496610
SP110_HUMANSP110physical
26496610
IMA4_HUMANKPNA3physical
26496610
IMA3_HUMANKPNA4physical
26496610
LIMS1_HUMANLIMS1physical
26496610
PSN2_HUMANPSEN2physical
26496610
STAT6_HUMANSTAT6physical
26496610
TAF12_HUMANTAF12physical
26496610
MPDZ_HUMANMPDZphysical
26496610
COX5A_HUMANCOX5Aphysical
26496610
CE350_HUMANCEP350physical
26496610
B2L11_HUMANBCL2L11physical
26496610
HMGX4_HUMANHMGXB4physical
26496610
MARH6_HUMANMARCH6physical
26496610
CEPT1_HUMANCEPT1physical
26496610
CD2B2_HUMANCD2BP2physical
26496610
CKAP2_HUMANCKAP2physical
26496610
PF21A_HUMANPHF21Aphysical
26496610
SMBT1_HUMANSFMBT1physical
26496610
E41LB_HUMANEPB41L4Bphysical
26496610
BIRC6_HUMANBIRC6physical
26496610
ZN668_HUMANZNF668physical
26496610
WDCP_HUMANC2orf44physical
26496610
CCNL2_HUMANCCNL2physical
26496610
CR021_HUMANC18orf21physical
26496610
UTP23_HUMANUTP23physical
26496610
PSRC1_HUMANPSRC1physical
26496610
UTP4_HUMANCIRH1Aphysical
26496610
SKAP_HUMANKNSTRNphysical
26496610
PGM2L_HUMANPGM2L1physical
26496610
TBC15_HUMANTBC1D15physical
28514442
IMA3_HUMANKPNA4physical
28514442
IMA4_HUMANKPNA3physical
28514442
UBP47_HUMANUSP47physical
28514442
ZY11B_HUMANZYG11Bphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
603546Spondyloepimetaphyseal dysplasia with joint laxity, 2 (SEMDJL2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KIF22_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-412 AND SER-427, 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-412 AND SER-427, 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-412; SER-427 ANDSER-543, 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-452, AND MASSSPECTROMETRY.
"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 SER-543; SER-562 ANDSER-581, AND MASS SPECTROMETRY.

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