KIZ_HUMAN - dbPTM
KIZ_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIZ_HUMAN
UniProt AC Q2M2Z5
Protein Name Centrosomal protein kizuna
Gene Name KIZ
Organism Homo sapiens (Human).
Sequence Length 673
Subcellular Localization Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, cilium basal body . Localizes to centrosomes throughout the cell cycle. After centrosome duplication, it usually remains associated only with the mother cen
Protein Description Centrosomal protein required for establishing a robust mitotic centrosome architecture that can endure the forces that converge on the centrosomes during spindle formation. Required for stabilizing the expanded pericentriolar material around the centriole..
Protein Sequence MSRTLASAVPLSSPDYYERLGQLQHGLRDSEKKRLDLEKKLYEYNQSDTCRVKLKYVKLKNYLKEICESEKKAHTRNQEYLKRFERVQAHVVHFTTNTEKLQKLKLEYETQIKKMLCSKDSLGLKEELTDEDREKVAVHEGINSGTAMSRGLYQPATIFMGRQMSAILSMRDFSTEHKSPQPTKNFSIPDPHSHRQTAQSSNVTDSCVVQTSNDTQCLNKSDNIDGKASLQIGEKMPVTASVLSEEEQTHCLEIGSNTRHGKSNLSEGKKSAELNSPLRERLSPENRTTDLKCDSSSGSEGEILTREHIEVEEKRASPPVSPIPVSEYCESENKWSQEKHSPWEGVSDHLAHREPKSQKPFRKMQEEEEESWSTSSDLTISISEDDLILESPEPQPNPGGKMEGEDGIEALKLIHAEQERVALSTEKNCILQTLSSPDSEKESSTNAPTREPGQTPDSDVPRAQVGQHVATLKEHDNSVKEEATALLRKALTEECGRRSAIHSSESSCSLPSILNDNSGIKEAKPAVWLNSVPTREQEVSSGCGDKSKKENVAADIPITETEAYQLLKKATLQDNTNQTENRFQKTDASVSHLSGLNIGSGAFETKTANKIASEASFSSSEGSPLSRHENKKKPVINLKSNALWDESDDSNSEIEAALRPRNHNTDDSDDFYD
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
5 (in isoform 2)Phosphorylation-3.2623663014
7 (in isoform 2)Phosphorylation-32.6723663014
11 (in isoform 5)Phosphorylation-6.7724043423
12PhosphorylationLASAVPLSSPDYYER
HHHCCCCCCHHHHHH		33.4825627689
13 (in isoform 5)Phosphorylation-29.4924043423
13PhosphorylationASAVPLSSPDYYERL
HHCCCCCCHHHHHHH		29.4921815630
16 (in isoform 5)Phosphorylation-15.6024043423
16PhosphorylationVPLSSPDYYERLGQL
CCCCCHHHHHHHHHH		15.6028985074
20 (in isoform 5)Phosphorylation-3.2424043423
24 (in isoform 5)Phosphorylation-22.2524043423
30PhosphorylationLQHGLRDSEKKRLDL
HHHCCCHHHHHHHHH		44.9028555341
42PhosphorylationLDLEKKLYEYNQSDT
HHHHHHHHHCCCCCC		25.83-
56PhosphorylationTCRVKLKYVKLKNYL
CCEEEEEHHHHHHHH		17.1618083107
62PhosphorylationKYVKLKNYLKEICES
EHHHHHHHHHHHHHH		19.9818083107
108PhosphorylationLQKLKLEYETQIKKM
HHHHHHHHHHHHHHH		34.4123403867
110PhosphorylationKLKLEYETQIKKMLC
HHHHHHHHHHHHHHH		34.3923403867
125UbiquitinationSKDSLGLKEELTDED
CCCCCCCCHHCCHHH		47.55-
153PhosphorylationTAMSRGLYQPATIFM
CCHHCCCCCCCEEEE		18.4421955146
157PhosphorylationRGLYQPATIFMGRQM
CCCCCCCEEEECCHH		22.7921955146
165PhosphorylationIFMGRQMSAILSMRD
EEECCHHHHHHHHHC		12.1021955146
169PhosphorylationRQMSAILSMRDFSTE
CHHHHHHHHHCCCCC		12.9821955146
174PhosphorylationILSMRDFSTEHKSPQ
HHHHHCCCCCCCCCC		36.8623312004
175PhosphorylationLSMRDFSTEHKSPQP
HHHHCCCCCCCCCCC		41.9423312004
179PhosphorylationDFSTEHKSPQPTKNF
CCCCCCCCCCCCCCC		30.5826055452
187PhosphorylationPQPTKNFSIPDPHSH
CCCCCCCCCCCCCCC		42.4728985074
193PhosphorylationFSIPDPHSHRQTAQS
CCCCCCCCCCHHCCC		26.2528985074
204PhosphorylationTAQSSNVTDSCVVQT
HCCCCCCCCCEEEEC		26.8430576142
211PhosphorylationTDSCVVQTSNDTQCL
CCCEEEECCCCCCCC		20.2130576142
212PhosphorylationDSCVVQTSNDTQCLN
CCEEEECCCCCCCCC		18.6730576142
263PhosphorylationSNTRHGKSNLSEGKK
CCCCCCCCCCCCCCC		47.82-
266PhosphorylationRHGKSNLSEGKKSAE
CCCCCCCCCCCCHHH		48.86-
271PhosphorylationNLSEGKKSAELNSPL
CCCCCCCHHHCCCHH		30.3829396449
276PhosphorylationKKSAELNSPLRERLS
CCHHHCCCHHHHHCC		37.6329255136
283PhosphorylationSPLRERLSPENRTTD
CHHHHHCCCCCCCCC		36.0723401153
317PhosphorylationEVEEKRASPPVSPIP
EEHHHCCCCCCCCCC		33.5023401153
321PhosphorylationKRASPPVSPIPVSEY
HCCCCCCCCCCHHHH		23.9223401153
326PhosphorylationPVSPIPVSEYCESEN
CCCCCCHHHHCCCCC		19.9323663014
328PhosphorylationSPIPVSEYCESENKW
CCCCHHHHCCCCCCC		8.2623663014
331PhosphorylationPVSEYCESENKWSQE
CHHHHCCCCCCCCCC		42.8023663014
336PhosphorylationCESENKWSQEKHSPW
CCCCCCCCCCCCCCC		30.0328450419
379PhosphorylationWSTSSDLTISISEDD
CCCCCCCEEEECCCC		20.0516980960
433PhosphorylationEKNCILQTLSSPDSE
CCCEEEEECCCCCCC		25.7622199227
435PhosphorylationNCILQTLSSPDSEKE
CEEEEECCCCCCCCC		43.1221815630
436PhosphorylationCILQTLSSPDSEKES
EEEEECCCCCCCCCC		35.5230576142
439PhosphorylationQTLSSPDSEKESSTN
EECCCCCCCCCCCCC		54.6925850435
455PhosphorylationPTREPGQTPDSDVPR
CCCCCCCCCCCCCCH		34.6728450419
458PhosphorylationEPGQTPDSDVPRAQV
CCCCCCCCCCCHHHC		41.5328450419
478PhosphorylationTLKEHDNSVKEEATA
HHHHCCCHHHHHHHH		40.3920873877
484PhosphorylationNSVKEEATALLRKAL
CHHHHHHHHHHHHHH		22.5523312004
499PhosphorylationTEECGRRSAIHSSES
HHHHCCHHHCCCCCC		30.1625627689
503PhosphorylationGRRSAIHSSESSCSL
CCHHHCCCCCCCCCC		29.6823186163
504PhosphorylationRRSAIHSSESSCSLP
CHHHCCCCCCCCCCC		27.6023186163
506PhosphorylationSAIHSSESSCSLPSI
HHCCCCCCCCCCCHH		38.3023186163
507PhosphorylationAIHSSESSCSLPSIL
HCCCCCCCCCCCHHH		12.0423186163
540PhosphorylationPTREQEVSSGCGDKS
CCCHHHHHCCCCCHH		21.9129083192
541PhosphorylationTREQEVSSGCGDKSK
CCHHHHHCCCCCHHH		43.1929083192
564PhosphorylationPITETEAYQLLKKAT
CCCHHHHHHHHHHHH		8.0827642862
594PhosphorylationDASVSHLSGLNIGSG
CCCHHHHCCCCCCCC		35.49-
600PhosphorylationLSGLNIGSGAFETKT
HCCCCCCCCCCCCCC		24.13-
605PhosphorylationIGSGAFETKTANKIA
CCCCCCCCCCHHHHH		27.52-
607PhosphorylationSGAFETKTANKIASE
CCCCCCCCHHHHHHH		42.7724114839
613PhosphorylationKTANKIASEASFSSS
CCHHHHHHHHCCCCC		36.8523403867
616PhosphorylationNKIASEASFSSSEGS
HHHHHHHCCCCCCCC		22.9323663014
618PhosphorylationIASEASFSSSEGSPL
HHHHHCCCCCCCCCC		30.3823663014
619PhosphorylationASEASFSSSEGSPLS
HHHHCCCCCCCCCCC		30.3323663014
620PhosphorylationSEASFSSSEGSPLSR
HHHCCCCCCCCCCCC		44.7923663014
623PhosphorylationSFSSSEGSPLSRHEN
CCCCCCCCCCCCCCC		20.7230266825
626PhosphorylationSSEGSPLSRHENKKK
CCCCCCCCCCCCCCC		34.6723663014
640PhosphorylationKPVINLKSNALWDES
CCCEECCCCCCCCCC		30.4228450419
647PhosphorylationSNALWDESDDSNSEI
CCCCCCCCCCCCHHH		44.2223927012
650PhosphorylationLWDESDDSNSEIEAA
CCCCCCCCCHHHHHH		47.4425159151
652PhosphorylationDESDDSNSEIEAALR
CCCCCCCHHHHHHHC		43.8523927012
665PhosphorylationLRPRNHNTDDSDDFY
HCCCCCCCCCCCCCC		33.3624501219
668PhosphorylationRNHNTDDSDDFYD--
CCCCCCCCCCCCC--		41.7230177828
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
379TPhosphorylationKinasePLK1P53350
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
379TPhosphorylation

16980960
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 KIZ_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SCLT1_HUMANSCLT1physical
28514442
DPYL3_HUMANDPYSL3physical
28514442
BMX_HUMANBMXphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615780Retinitis pigmentosa 69 (RP69)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KIZ_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-616, AND MASSSPECTROMETRY.
"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-317; SER-321; SER-647;SER-650 AND SER-652, AND MASS SPECTROMETRY.
"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-317 AND SER-321, ANDMASS SPECTROMETRY.
"The Plk1 target Kizuna stabilizes mitotic centrosomes to ensurespindle bipolarity.";
Oshimori N., Ohsugi M., Yamamoto T.;
Nat. Cell Biol. 8:1095-1101(2006).
Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-379,MUTAGENESIS OF THR-249 AND THR-379, AND INTERACTION WITH AKAP9; ODF2;PCNT AND TUBGCP2.

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