NEK2_MOUSE - dbPTM
NEK2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NEK2_MOUSE
UniProt AC O35942
Protein Name Serine/threonine-protein kinase Nek2
Gene Name Nek2
Organism Mus musculus (Mouse).
Sequence Length 443
Subcellular Localization Nucleus . Nucleus, nucleolus . Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle pole. Chromosome, centromere, kinetochore. Chromosome, centromere . STK3/MST2 and SAV1 are required for it
Protein Description Protein kinase which is involved in the control of centrosome separation and bipolar spindle formation in mitotic cells and chromatin condensation in meiotic cells. Regulates centrosome separation (essential for the formation of bipolar spindles and high-fidelity chromosome separation) by phosphorylating centrosomal proteins such as CROCC, CEP250 and NINL, resulting in their displacement from the centrosomes. Regulates kinetochore microtubule attachment stability in mitosis via phosphorylation of NDC80. Involved in regulation of mitotic checkpoint protein complex via phosphorylation of CDC20 and MAD2L1. Plays an active role in chromatin condensation during the first meiotic division through phosphorylation of HMGA2. Phosphorylates: PPP1CC; SGO1; NECAB3 and NPM1. Essential for localization of MAD2L1 to kinetochore and MAPK1 and NPM1 to the centrosome. Phosphorylates CEP68 and CNTLN directly or indirectly (By similarity). NEK2-mediated phosphorylation of CEP68 promotes CEP68 dissociation from the centrosome and its degradation at the onset of mitosis (By similarity). Phosphorylates and activates NEK11 in G1/S-arrested cells. Involved in the regulation of centrosome disjunction (By similarity)..
Protein Sequence MPSRVEDYEVLHSIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEVEKQMLVSEVNLLRELKHPNIVSYYDRIIDRTNTTLYIVMEYCEGGDLASVISKGTKDRQYLEEEFVLRVMTQLTLALKECHRRSDGGHTVLHRDLKPANVFLDSKHNVKLGDFGLARILNHDTSFAKTFVGTPYYMSPEQMSCLSYNEKSDIWSLGCLLYELCALMPPFTAFNQKELAGKIREGRFRRIPYRYSDGLNDLITRMLNLKDYHRPSVEEILESPLIADLVAEEQRRNLERRGRRSGEPSKLPDSSPVLSELKLKERQLQDREQALRAREDILEQKERELCIRERLAEDKLARAESLMKNYSLLKEHRLLCLAGGPELDLPSSAMKKKVHFHGESKENTARSENSESYLAKSKCRDLKKRLHAAQLRAQALADIEKNYQLKSRQILGMR
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
41PhosphorylationLVWKELDYGSMTEVE
EEEEECCCCCCCHHH
24.5928059163
45PhosphorylationELDYGSMTEVEKQML
ECCCCCCCHHHHHHH
38.2828059163
170PhosphorylationARILNHDTSFAKTFV
HHHHCCCCCHHHHCC
20.42-
171PhosphorylationRILNHDTSFAKTFVG
HHHCCCCCHHHHCCC
29.30-
175PhosphorylationHDTSFAKTFVGTPYY
CCCCHHHHCCCCCCC
21.81-
179PhosphorylationFAKTFVGTPYYMSPE
HHHHCCCCCCCCCHH
11.65-
184PhosphorylationVGTPYYMSPEQMSCL
CCCCCCCCHHHHHCC
14.79-
238PhosphorylationGRFRRIPYRYSDGLN
CCCCCCCCCCCCCHH
21.5824719451
240PhosphorylationFRRIPYRYSDGLNDL
CCCCCCCCCCCHHHH
12.7924719451
241PhosphorylationRRIPYRYSDGLNDLI
CCCCCCCCCCHHHHH
19.0624719451
290PhosphorylationLERRGRRSGEPSKLP
HHHHCCCCCCCCCCC
46.2622067460
294PhosphorylationGRRSGEPSKLPDSSP
CCCCCCCCCCCCCCH
42.3922067460
299PhosphorylationEPSKLPDSSPVLSEL
CCCCCCCCCHHHHHH
34.3028066266
300PhosphorylationPSKLPDSSPVLSELK
CCCCCCCCHHHHHHH
26.8028066266
356PhosphorylationESLMKNYSLLKEHRL
HHHHHHHHHHHHCCC
36.30-
389PhosphorylationKVHFHGESKENTARS
CEEECCCCCCCCCCC
50.27-
396PhosphorylationSKENTARSENSESYL
CCCCCCCCCCHHHHH
38.37-
401PhosphorylationARSENSESYLAKSKC
CCCCCHHHHHHHHHH
25.85-
436PhosphorylationEKNYQLKSRQILGMR
HHHHHCHHHHHHCCC
37.70-

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
356SPhosphorylationKinaseMST2Q9JI10
Uniprot
436SPhosphorylationKinaseMST2Q9JI10
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NEK2_MOUSE !!

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 NEK2_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IPP2_HUMANPPP1R2physical
12221103
NEK2_HUMANNEK2physical
20360068
ACAD8_HUMANACAD8physical
20360068
CDC27_HUMANCDC27physical
26496610
CATC_HUMANCTSCphysical
26496610
FOXM1_HUMANFOXM1physical
26496610
FLNA_HUMANFLNAphysical
26496610
PDIA3_HUMANPDIA3physical
26496610
KIFC1_HUMANKIFC1physical
26496610
KAP2_HUMANPRKAR2Aphysical
26496610
PSMD5_HUMANPSMD5physical
26496610
PRP18_HUMANPRPF18physical
26496610
MKNK1_HUMANMKNK1physical
26496610
CDC23_HUMANCDC23physical
26496610
CDC16_HUMANCDC16physical
26496610
WDR46_HUMANWDR46physical
26496610
ITM2B_HUMANITM2Bphysical
26496610
DNM1L_HUMANDNM1Lphysical
26496610
MTDC_HUMANMTHFD2physical
26496610
DLGP4_HUMANDLGAP4physical
26496610
LTN1_HUMANLTN1physical
26496610
FZR1_HUMANFZR1physical
26496610
APC7_HUMANANAPC7physical
26496610
DEP1A_HUMANDEPDC1physical
26496610
SYIM_HUMANIARS2physical
26496610
HMCES_HUMANHMCESphysical
26496610
BBX_HUMANBBXphysical
26496610
KNL1_HUMANCASC5physical
26496610
DEFM_HUMANPDFphysical
26496610
TFB2M_HUMANTFB2Mphysical
26496610
APC1_HUMANANAPC1physical
26496610
CDCA3_HUMANCDCA3physical
26496610
K2013_HUMANKIAA2013physical
26496610
RRFM_HUMANMRRFphysical
26496610
EME1_HUMANEME1physical
26496610
CDC26_HUMANCDC26physical
26496610
KIF24_HUMANKIF24physical
26496610

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NEK2_MOUSE

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Related Literatures of Post-Translational Modification

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