KIP2_YEAST - dbPTM
KIP2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KIP2_YEAST
UniProt AC P28743
Protein Name Kinesin-like protein KIP2
Gene Name KIP2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 706
Subcellular Localization Cytoplasm, cytoskeleton .
Protein Description Required for assembly of the mitotic spindle..
Protein Sequence MIQKMSPSLRRPSTRSSSGSSNIPQSPSVRSTSSFSNLTRNSIRSTSNSGSQSISASSTRSNSPLRSVSAKSDPFLHPGRIRIRRSDSINNNSRKNDTYTGSITVTIRPKPRSVGTSRDHVGLKSPRYSQPRSNSHHGSNTFVRDPWFITNDKTIVHEEIGEFKFDHVFASHCTNLEVYERTSKPMIDKLLMGFNATIFAYGMTGSGKTFTMSGNEQELGLIPLSVSYLFTNIMEQSMNGDKKFDVIISYLEIYNERIYDLLESGLEESGSRISTPSRLYMSKSNSNGLGVELKIRDDSQYGVKVIGLTERRCESSEELLRWIAVGDKSRKIGETDYNARSSRSHAIVLIRLTSTNVKNGTSRSSTLSLCDLAGSERATGQQERRKEGSFINKSLLALGTVISKLSADKMNSVGSNIPSPSASGSSSSSGNATNNGTSPSNHIPYRDSKLTRLLQPALSGDSIVTTICTVDTRNDAAAETMNTLRFASRAKNVALHVSKKSIISNGNNDGDKDRTIELLRRQLEEQRRMISELKNRSNIGEPLTKSSNESTYKDIKATGNDGDPNLALMRAENRVLKYKLENCEKLLDKDVVDLQDSEIMEIVEMLPFEVGTLLETKFQGLESQIRQYRKYTQKLEDKIMALEKSGHTAMSLTGCDGTEVIELQKMLERKDKMIEALQSAKRLRDRALKPLINTQQSPHPVVDNDK
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
6Phosphorylation--MIQKMSPSLRRPS
--CCCCCCHHHCCCC		20.5528152593
8PhosphorylationMIQKMSPSLRRPSTR
CCCCCCHHHCCCCCC		27.4830377154
16PhosphorylationLRRPSTRSSSGSSNI
HCCCCCCCCCCCCCC		29.0121126336
18PhosphorylationRPSTRSSSGSSNIPQ
CCCCCCCCCCCCCCC		43.8925752575
26PhosphorylationGSSNIPQSPSVRSTS
CCCCCCCCCCCCCCC		17.4921082442
28PhosphorylationSNIPQSPSVRSTSSF
CCCCCCCCCCCCCCC		35.1028889911
31PhosphorylationPQSPSVRSTSSFSNL
CCCCCCCCCCCCCCC		30.4122369663
32PhosphorylationQSPSVRSTSSFSNLT
CCCCCCCCCCCCCCC		20.1622369663
33PhosphorylationSPSVRSTSSFSNLTR
CCCCCCCCCCCCCCH		30.5422369663
34PhosphorylationPSVRSTSSFSNLTRN
CCCCCCCCCCCCCHH		32.5522369663
36PhosphorylationVRSTSSFSNLTRNSI
CCCCCCCCCCCHHHC		32.6422369663
39PhosphorylationTSSFSNLTRNSIRST
CCCCCCCCHHHCCCC		31.8628889911
51PhosphorylationRSTSNSGSQSISASS
CCCCCCCCCCCCCCC		22.1522369663
53PhosphorylationTSNSGSQSISASSTR
CCCCCCCCCCCCCCC		21.8719779198
55PhosphorylationNSGSQSISASSTRSN
CCCCCCCCCCCCCCC		27.6122369663
57PhosphorylationGSQSISASSTRSNSP
CCCCCCCCCCCCCCC		26.0022369663
58PhosphorylationSQSISASSTRSNSPL
CCCCCCCCCCCCCCC		27.7922369663
59PhosphorylationQSISASSTRSNSPLR
CCCCCCCCCCCCCCC		35.3022369663
63PhosphorylationASSTRSNSPLRSVSA
CCCCCCCCCCCCCCC		26.9319779198
67PhosphorylationRSNSPLRSVSAKSDP
CCCCCCCCCCCCCCC		28.2728889911
69PhosphorylationNSPLRSVSAKSDPFL
CCCCCCCCCCCCCCC		31.0919779198
72PhosphorylationLRSVSAKSDPFLHPG
CCCCCCCCCCCCCCC		50.6728889911
86PhosphorylationGRIRIRRSDSINNNS
CCEEEEECCCCCCCC		26.3428889911
88PhosphorylationIRIRRSDSINNNSRK
EEEEECCCCCCCCCC		28.5821082442
93PhosphorylationSDSINNNSRKNDTYT
CCCCCCCCCCCCEEE		46.9128889911
124AcetylationSRDHVGLKSPRYSQP
CCCCCCCCCCCCCCC		53.1122865919
125PhosphorylationRDHVGLKSPRYSQPR
CCCCCCCCCCCCCCC		21.4728889911
228PhosphorylationLIPLSVSYLFTNIME
EEEHHHHHHHHHHHH		12.0428132839
264PhosphorylationRIYDLLESGLEESGS
HHHHHHHCCCCCCCC		48.9627017623
269PhosphorylationLESGLEESGSRISTP
HHCCCCCCCCCCCCC		32.4723749301
271PhosphorylationSGLEESGSRISTPSR
CCCCCCCCCCCCCCE		35.4027017623
274PhosphorylationEESGSRISTPSRLYM
CCCCCCCCCCCEEEE		32.9127017623
275PhosphorylationESGSRISTPSRLYMS
CCCCCCCCCCEEEEE		23.9423749301
362PhosphorylationTNVKNGTSRSSTLSL
CCCCCCCCCCCEEEH		31.4024930733
364PhosphorylationVKNGTSRSSTLSLCD
CCCCCCCCCEEEHHH		27.6925005228
365PhosphorylationKNGTSRSSTLSLCDL
CCCCCCCCEEEHHHH		32.0524930733
531PhosphorylationEEQRRMISELKNRSN
HHHHHHHHHHHHCCC		27.7727017623
537PhosphorylationISELKNRSNIGEPLT
HHHHHHCCCCCCCCC		42.0427017623
544PhosphorylationSNIGEPLTKSSNEST
CCCCCCCCCCCCCCC		39.3327017623
556UbiquitinationESTYKDIKATGNDGD
CCCHHHHHHHCCCCC		50.4524961812
694PhosphorylationALKPLINTQQSPHPV
CHHHHCCCCCCCCCC		22.4624961812
697PhosphorylationPLINTQQSPHPVVDN
HHCCCCCCCCCCCCC		18.5023749301
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

Oops, there are no upstream regulatory protein records of KIP2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KIP2_YEAST !!
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 KIP2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BIM1_YEASTBIM1genetic
14764870
KAR9_YEASTKAR9genetic
14764870
ATC3_YEASTDRS2genetic
14764870
PFD2_YEASTGIM4genetic
14764870
CIN8_YEASTCIN8genetic
14764870
PFD3_YEASTPAC10genetic
14764870
DBF2_YEASTDBF2genetic
14764870
PFD6_YEASTYKE2genetic
14764870
PFD5_YEASTGIM5genetic
14764870
TBA3_YEASTTUB3genetic
14764870
PFD4_YEASTGIM3genetic
14764870
BIK1_YEASTBIK1physical
15177030
KAR9_YEASTKAR9physical
12554645
SPC29_YEASTSPC29physical
11087867
BIK1_YEASTBIK1physical
11087867
KIP2_YEASTKIP2physical
11087867
SMC1_YEASTSMC1physical
16554755
KEL1_YEASTKEL1physical
16554755
LSP1_YEASTLSP1physical
16554755
PFD4_YEASTGIM3genetic
17314980
BIM1_YEASTBIM1genetic
17314980
ASE1_YEASTASE1genetic
17314980
PFD3_YEASTPAC10genetic
17314980
CIN1_YEASTCIN1genetic
17314980
CCS1_YEASTCCS1genetic
17314980
CIN8_YEASTCIN8genetic
17314980
BUD6_YEASTBUD6genetic
17615297
LIC4_YEASTATC1genetic
17615297
MSL1_YEASTMSL1genetic
17615297
BIM1_YEASTBIM1genetic
18931302
PFD6_YEASTYKE2genetic
18931302
PFD4_YEASTGIM3genetic
18931302
PFD2_YEASTGIM4genetic
18931302
ASE1_YEASTASE1genetic
18931302
PFD3_YEASTPAC10genetic
18931302
ADPP_YEASTYSA1genetic
20093466
NRG1_YEASTNRG1genetic
20093466
EMI1_YEASTEMI1genetic
20093466
DBF2_YEASTDBF2genetic
20093466
ASK10_YEASTASK10genetic
20093466
YIT6_YEASTYIR016Wgenetic
20093466
PFD6_YEASTYKE2genetic
20093466
JNM1_YEASTJNM1genetic
20093466
PFD4_YEASTGIM3genetic
20093466
TPM1_YEASTTPM1genetic
20093466
ASE1_YEASTASE1genetic
20093466
DGK1_YEASTDGK1genetic
20093466
CIN1_YEASTCIN1genetic
20093466
QCR2_YEASTQCR2genetic
20093466
KIP3_YEASTKIP3genetic
9281582
DYHC_YEASTDYN1genetic
9281582
PAC2_YEASTPAC2genetic
14764870
ASE1_YEASTASE1genetic
14764870
CIN1_YEASTCIN1genetic
14764870
TBCC_YEASTCIN2genetic
14764870
ATC3_YEASTDRS2genetic
21987634
NUM1_YEASTNUM1genetic
21987634
PFD2_YEASTGIM4genetic
21987634
CIN8_YEASTCIN8genetic
21987634
PFD3_YEASTPAC10genetic
21987634
PFD6_YEASTYKE2genetic
21987634
PFD5_YEASTGIM5genetic
21987634
PFD4_YEASTGIM3genetic
21987634
CIN1_YEASTCIN1genetic
21987634
ATG21_YEASTATG21genetic
21987634
SPC72_YEASTSPC72physical
22875988
BIK1_YEASTBIK1physical
22875988
TBA1C_BOVINTUBA1Cphysical
24916158
TBA1_YEASTTUB1physical
23142046
TBB_YEASTTUB2physical
23142046
ASK10_YEASTASK10genetic
27708008
ADPP_YEASTYSA1genetic
27708008
IMG2_YEASTIMG2genetic
27708008
GPR1_YEASTGPR1genetic
27708008
PEX5_YEASTPEX5genetic
27708008
MRM2_YEASTMRM2genetic
27708008
PFD3_YEASTPAC10genetic
27708008
SNF6_YEASTSNF6genetic
27708008
CBT1_YEASTCBT1genetic
27708008
ACE2_YEASTACE2genetic
27708008
PFD6_YEASTYKE2genetic
27708008
PET8_YEASTPET8genetic
27708008
EFM6_YEASTYNL024Cgenetic
27708008
TPM1_YEASTTPM1genetic
27708008
LSM7_YEASTLSM7genetic
27708008
PFD4_YEASTGIM3genetic
27708008
ASE1_YEASTASE1genetic
27708008
GYP1_YEASTGYP1genetic
27708008
CIN1_YEASTCIN1genetic
27708008
MSS18_YEASTMSS18genetic
27708008
SUE1_YEASTSUE1genetic
27708008
QCR2_YEASTQCR2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KIP2_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND SER-88, AND MASSSPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND MASSSPECTROMETRY.

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