NEK9_MOUSE - dbPTM
NEK9_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NEK9_MOUSE
UniProt AC Q8K1R7
Protein Name Serine/threonine-protein kinase Nek9
Gene Name Nek9
Organism Mus musculus (Mouse).
Sequence Length 984
Subcellular Localization Cytoplasm. Nucleus.
Protein Description Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation. Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2. Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues Important for G1/S transition and S phase progression. Phosphorylates NEK6 and NEK7 and stimulates their activity by releasing the autoinhibitory functions of Tyr-108 and Tyr-97 respectively (By similarity)..
Protein Sequence MSVLGEYERHCDSINSDFGSESGGGGDSGPGPSAVPGPRAGGGAAEQEELHYIPIRVLGRGAFGEATLYRRTEDDSLVVWKEVDLTRLSEKERRDALNEIVILALLQHDNIIAYYNHFMDNTTLLIELEYCNGGNLYDKILRQKDKLFEEEMVVWYLFQIVSAVSCIHKAGILHRDIKTLNIFLTKANLIKLGDYGLAKKLNSEYSMAETLVGTPYYMSPELCQGVKYNFKSDIWAVGCVIFELLTLKRTFDATNPLNLCVKIVQGIRAMEVDSSQYSLELIQLVHACLDQDPEQRPAADALLDLPLLRTRRREMEEKVTLLNAPTKRPRSSTVTEAPIAVVTSRTSEVYVWGGGKSTPQKLDVIKSGCSARQVCAGNTHFAVVTVEKELYTWVNMQGGTKLHGQLGHGDKASYRQPKHVEKLQGKAIHQVSCGDDFTVCVTDEGQLYAFGSDYYGCMGVDKVSGPEVLEPMQLNFFLSNPVEQVSCGDNHVVVLTRNKEVYSWGCGEYGRLGLDSEEDYYTPQRVDVPKALIIVAVQCGCDGTFLLTQSGKVLACGLNEFNKLGLNQCMSGIINHEAYHEVPYTTSFTLAKQLSFYKIRTIAPGKTHTAAIDERGRLLTFGCNKCGQLGVGNYKKRLGINLLGGPLGGKQVIRVSCGDEFTIAATDDNHIFAWGNGGNGRLAMTPTERPHGSDICTSWPRPIFGSLHHVPDLSCRGWHTILIVEKVLNSKTIRSNSSGLSIGTVVQSSSPGGGIGGGGGGGGGGGGEEEDSQQESETPDPSGGFRGTMEADRGMEGLISPTEAVGNSCGASSSCPGWLRKELENAEFIPMPDSPAPLSAAFSQSEKDTLPYEELQGLKVASEVPPEPQRAAGAWPPRLDPAVPCVGKALTSAACACSALQVEVDRLQALVLKCLEEQQKLQQENLQMFTQLQKLNKKLEGGQQVGMHSRGTQTAKEEMEMDPKPDLDSESWCLLGTDSCRPSL
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------MSVLGEYER
------CCCCCCHHH
26.50-
2Phosphorylation------MSVLGEYER
------CCCCCCHHH
26.5026824392
13PhosphorylationEYERHCDSINSDFGS
CHHHHHCCCCCCCCC
29.1230352176
16PhosphorylationRHCDSINSDFGSESG
HHHCCCCCCCCCCCC
32.4223684622
20PhosphorylationSINSDFGSESGGGGD
CCCCCCCCCCCCCCC
28.6930352176
22PhosphorylationNSDFGSESGGGGDSG
CCCCCCCCCCCCCCC
44.4230352176
28PhosphorylationESGGGGDSGPGPSAV
CCCCCCCCCCCCCCC
50.6023684622
52PhosphorylationAEQEELHYIPIRVLG
CCCCCCEEEEEEEEC
22.48-
76PhosphorylationYRRTEDDSLVVWKEV
EEECCCCCEEEEEEE
35.0725338131
206PhosphorylationKKLNSEYSMAETLVG
HHHCCCCCHHHHHCC
13.8925338131
210PhosphorylationSEYSMAETLVGTPYY
CCCCHHHHHCCCCCC
19.7325338131
250PhosphorylationELLTLKRTFDATNPL
HHHHCHHHCCCCCCH
25.0429472430
254PhosphorylationLKRTFDATNPLNLCV
CHHHCCCCCCHHHHH
38.9329472430
262UbiquitinationNPLNLCVKIVQGIRA
CCHHHHHHHHHHCCE
35.84-
318AcetylationRRREMEEKVTLLNAP
HHHHHHHHHHHHCCC
27.497385623
331PhosphorylationAPTKRPRSSTVTEAP
CCCCCCCCCCCCCCC
32.8025521595
332PhosphorylationPTKRPRSSTVTEAPI
CCCCCCCCCCCCCCE
28.3325521595
333PhosphorylationTKRPRSSTVTEAPIA
CCCCCCCCCCCCCEE
32.4725521595
335PhosphorylationRPRSSTVTEAPIAVV
CCCCCCCCCCCEEEE
26.9023684622
343PhosphorylationEAPIAVVTSRTSEVY
CCCEEEEEECCCEEE
13.0925619855
344PhosphorylationAPIAVVTSRTSEVYV
CCEEEEEECCCEEEE
23.1925619855
358PhosphorylationVWGGGKSTPQKLDVI
EECCCCCCCHHHHHH
32.97-
367PhosphorylationQKLDVIKSGCSARQV
HHHHHHHCCCCCCHH
33.63-
370PhosphorylationDVIKSGCSARQVCAG
HHHHCCCCCCHHHCC
29.97-
379PhosphorylationRQVCAGNTHFAVVTV
CHHHCCCCEEEEEEE
19.90-
509PhosphorylationYSWGCGEYGRLGLDS
EEECCCCCCCCCCCC
7.8822817900
685PhosphorylationGNGRLAMTPTERPHG
CCCCCCCCCCCCCCC
22.8121930439
693PhosphorylationPTERPHGSDICTSWP
CCCCCCCCCCCCCCC
22.2921930439
697PhosphorylationPHGSDICTSWPRPIF
CCCCCCCCCCCCCCC
33.8721930439
698PhosphorylationHGSDICTSWPRPIFG
CCCCCCCCCCCCCCC
30.5821930439
731UbiquitinationVEKVLNSKTIRSNSS
EEEHHHCCCHHCCCC
47.07-
735PhosphorylationLNSKTIRSNSSGLSI
HHCCCHHCCCCCCEE
36.8925338131
741PhosphorylationRSNSSGLSIGTVVQS
HCCCCCCEEEEEEEC
23.6122942356
748PhosphorylationSIGTVVQSSSPGGGI
EEEEEEECCCCCCCC
22.6025338131
788PhosphorylationPSGGFRGTMEADRGM
CCCCCCCCCCCCCCC
13.9526745281
800PhosphorylationRGMEGLISPTEAVGN
CCCCCCCCCHHHCCC
30.7126745281
802PhosphorylationMEGLISPTEAVGNSC
CCCCCCCHHHCCCCC
29.7726745281
808PhosphorylationPTEAVGNSCGASSSC
CHHHCCCCCCCCCCC
14.1722942356
809GlutathionylationTEAVGNSCGASSSCP
HHHCCCCCCCCCCCC
6.4724333276
812PhosphorylationVGNSCGASSSCPGWL
CCCCCCCCCCCCCHH
14.2025777480
813PhosphorylationGNSCGASSSCPGWLR
CCCCCCCCCCCCHHH
35.1125777480
814PhosphorylationNSCGASSSCPGWLRK
CCCCCCCCCCCHHHH
23.1025777480
815GlutathionylationSCGASSSCPGWLRKE
CCCCCCCCCCHHHHH
3.7924333276
834PhosphorylationEFIPMPDSPAPLSAA
CCCCCCCCCCCHHHC
19.6627180971
839PhosphorylationPDSPAPLSAAFSQSE
CCCCCCHHHCCCCCC
19.2527180971
843PhosphorylationAPLSAAFSQSEKDTL
CCHHHCCCCCCCCCC
28.2428066266
845PhosphorylationLSAAFSQSEKDTLPY
HHHCCCCCCCCCCCH
45.4728066266
852PhosphorylationSEKDTLPYEELQGLK
CCCCCCCHHHHCCCE
25.7529514104
862PhosphorylationLQGLKVASEVPPEPQ
HCCCEEECCCCCCCC
41.9625177544
891PhosphorylationPCVGKALTSAACACS
CCCHHHHHHHHHHHH
22.60-
949PhosphorylationGQQVGMHSRGTQTAK
CCCCCCCCCCCHHHH
24.4227841257
983PhosphorylationGTDSCRPSL------
CCCCCCCCC------
100.0025159016

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 NEK9_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
210TPhosphorylation

-
210TPhosphorylation

-

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 NEK9_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDB1_HUMANDDB1physical
20360068
NEK9_HUMANNEK9physical
20360068
ELOC_HUMANTCEB1physical
20360068
AURKA_HUMANAURKAphysical
20360068
COG7_HUMANCOG7physical
20360068
DYL1_HUMANDYNLL1physical
20360068
AMRA1_HUMANAMBRA1physical
20360068
DDA1_HUMANDDA1physical
20360068
DYL2_HUMANDYNLL2physical
20360068
RFA2_HUMANRPA2physical
20360068
COG5_HUMANCOG5physical
20360068
EMAL1_HUMANEML1physical
26496610
UTRO_HUMANUTRNphysical
26496610
DYL1_HUMANDYNLL1physical
26496610
TBB4B_HUMANTUBB4Bphysical
26496610
EMAL2_HUMANEML2physical
26496610
EMAL4_HUMANEML4physical
26496610
NBEL1_HUMANNBEAL1physical
26496610
TBA1C_HUMANTUBA1Cphysical
26496610
RRP36_HUMANRRP36physical
26496610
NEK7_HUMANNEK7physical
26496610
STT3B_HUMANSTT3Bphysical
26496610
TBB5_HUMANTUBBphysical
26496610
EMAL3_HUMANEML3physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NEK9_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-333, AND MASSSPECTROMETRY.

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