Protein:NEK2 |
Protein Summary |
 Gene summary |
| Gene name: NEK2 | ASpdb.0 ID: 4751 | Gene | Gene symbol | NEK2 | Gene ID | 4751 |
| Gene name | NIMA related kinase 2 |
| Synonyms | HsPK21|NEK2A|NLK1|PPP1R111|RP67 |
| Cytomap | 1q32.3 |
| Type of gene | protein-coding |
| Description | serine/threonine-protein kinase Nek2NIMA (never in mitosis gene a)-related kinase 2nimA-like protein kinase 1nimA-related protein kinase 2protein phosphatase 1, regulatory subunit 111 |
| Modification date | 20240323 |
| UniProtAcc | P51955 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | NEK2 | GO:0000776 | kinetochore | 17621308 |
| Gene | NEK2 | GO:0000776 | kinetochore | 14978040 |
| Gene | NEK2 | GO:0004672 | protein kinase activity | 10880350|18086858|26220856 |
| Gene | NEK2 | GO:0005654 | nucleoplasm | - |
| Gene | NEK2 | GO:0005813 | centrosome | 21399614|26220856 |
| Gene | NEK2 | GO:0006468 | protein phosphorylation | 21076410 |
| Gene | NEK2 | GO:0007059 | chromosome segregation | 14978040 |
| Gene | NEK2 | GO:0046777 | protein autophosphorylation | 17626005 |
| Gene | NEK2 | GO:0051299 | centrosome separation | 18086858 |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| P51955-1 | P51955-1_2w5a_A.pdb | 2W5A | X-ray | 1.55 | A | 3 | 271 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| P51955 | NEK2 | P51955-1 | P51955-2 | 445 | 384 | 371 | 384 | Substitution | ELLNLPSSVIKKKV | GMRINLVNRSWCYK | 371 | 384 |
| P51955 | NEK2 | P51955-1 | P51955-2 | 445 | 384 | 385 | 445 | Deletion | none | none | 384 | 384 |
| P51955 | NEK2 | P51955-1 | P51955-3 | 445 | 326 | 323 | 326 | Substitution | REER | KKKK | 323 | 326 |
| P51955 | NEK2 | P51955-1 | P51955-3 | 445 | 326 | 327 | 445 | Deletion | none | none | 326 | 326 |
| P51955 | NEK2 | P51955-1 | P51955-4 | 445 | 437 | 371 | 378 | Deletion | none | none | 370 | 370 |
| Multiple sequence alignment of our canonical and alternatively spliced NEK2 |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of NEK2 |
| UniProt-id | ENSG | ENST | ENSP |
| P51955-1 | ENSG00000117650.13 | ENST00000366999.9 | ENSP00000355966.4 |
| P51955-2 | ENSG00000117650.13 | ENST00000366998.4 | ENSP00000355965.3 |
| UniProt-id | NM ID | NP ID |
| P51955-1 | NM_002497.3 | NP_002488.1 |
| P51955-2 | NM_001204183.1 | NP_001191112.1 |
| Amino acid sequences of our canonical and alternatively spliced NEK2 |
| accession_id | Protein sequence |
| P51955-1 | MPSRAEDYEVLYTIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEAEKQMLVSEVNLLRELKHPNIVRYYDRIIDRTNTTLYIVMEYCE GGDLASVITKGTKERQYLDEEFVLRVMTQLTLALKECHRRSDGGHTVLHRDLKPANVFLDGKQNVKLGDFGLARILNHDTSFAKTFVGTP YYMSPEQMNRMSYNEKSDIWSLGCLLYELCALMPPFTAFSQKELAGKIREGKFRRIPYRYSDELNEIITRMLNLKDYHRPSVEEILENPL IADLVADEQRRNLERRGRQLGEPEKSQDSSPVLSELKLKEIQLQERERALKAREERLEQKEQELCVRERLAEDKLARAENLLKNYSLLKE |
| P51955-2 | MPSRAEDYEVLYTIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEAEKQMLVSEVNLLRELKHPNIVRYYDRIIDRTNTTLYIVMEYCE GGDLASVITKGTKERQYLDEEFVLRVMTQLTLALKECHRRSDGGHTVLHRDLKPANVFLDGKQNVKLGDFGLARILNHDTSFAKTFVGTP YYMSPEQMNRMSYNEKSDIWSLGCLLYELCALMPPFTAFSQKELAGKIREGKFRRIPYRYSDELNEIITRMLNLKDYHRPSVEEILENPL IADLVADEQRRNLERRGRQLGEPEKSQDSSPVLSELKLKEIQLQERERALKAREERLEQKEQELCVRERLAEDKLARAENLLKNYSLLKE |
| P51955-3 | MPSRAEDYEVLYTIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEAEKQMLVSEVNLLRELKHPNIVRYYDRIIDRTNTTLYIVMEYCE GGDLASVITKGTKERQYLDEEFVLRVMTQLTLALKECHRRSDGGHTVLHRDLKPANVFLDGKQNVKLGDFGLARILNHDTSFAKTFVGTP YYMSPEQMNRMSYNEKSDIWSLGCLLYELCALMPPFTAFSQKELAGKIREGKFRRIPYRYSDELNEIITRMLNLKDYHRPSVEEILENPL |
| P51955-4 | MPSRAEDYEVLYTIGTGSYGRCQKIRRKSDGKILVWKELDYGSMTEAEKQMLVSEVNLLRELKHPNIVRYYDRIIDRTNTTLYIVMEYCE GGDLASVITKGTKERQYLDEEFVLRVMTQLTLALKECHRRSDGGHTVLHRDLKPANVFLDGKQNVKLGDFGLARILNHDTSFAKTFVGTP YYMSPEQMNRMSYNEKSDIWSLGCLLYELCALMPPFTAFSQKELAGKIREGKFRRIPYRYSDELNEIITRMLNLKDYHRPSVEEILENPL IADLVADEQRRNLERRGRQLGEPEKSQDSSPVLSELKLKEIQLQERERALKAREERLEQKEQELCVRERLAEDKLARAENLLKNYSLLKE |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| NEK2 (go to UniProt):P51955 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| P51955 | Region | 264 | 445 | Note=Interaction with PCNT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20599736;Dbxref=PMID:20599736 | Type=Substitution;Start=371;End=384 |
| P51955 | Region | 264 | 445 | Note=Interaction with PCNT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20599736;Dbxref=PMID:20599736 | Type=Deletion;Start=385;End=445 |
| P51955 | Region | 264 | 445 | Note=Interaction with PCNT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20599736;Dbxref=PMID:20599736 | Type=Substitution;Start=323;End=326 |
| P51955 | Region | 264 | 445 | Note=Interaction with PCNT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20599736;Dbxref=PMID:20599736 | Type=Deletion;Start=327;End=445 |
| P51955 | Region | 264 | 445 | Note=Interaction with PCNT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20599736;Dbxref=PMID:20599736 | Type=Deletion;Start=371;End=378 |
| P51955 | Region | 301 | 445 | Note=Interaction with CEP85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26220856;Dbxref=PMID:26220856 | Type=Substitution;Start=371;End=384 |
| P51955 | Region | 301 | 445 | Note=Interaction with CEP85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26220856;Dbxref=PMID:26220856 | Type=Deletion;Start=385;End=445 |
| P51955 | Region | 301 | 445 | Note=Interaction with CEP85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26220856;Dbxref=PMID:26220856 | Type=Substitution;Start=323;End=326 |
| P51955 | Region | 301 | 445 | Note=Interaction with CEP85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26220856;Dbxref=PMID:26220856 | Type=Deletion;Start=327;End=445 |
| P51955 | Region | 301 | 445 | Note=Interaction with CEP85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26220856;Dbxref=PMID:26220856 | Type=Deletion;Start=371;End=378 |
| P51955 | Region | 306 | 334 | Note=Leucine-zipper | Type=Substitution;Start=323;End=326 |
| P51955 | Region | 306 | 334 | Note=Leucine-zipper | Type=Deletion;Start=327;End=445 |
| P51955 | Region | 329 | 445 | Note=Necessary for interaction with MAD1L1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14978040;Dbxref=PMID:14978040 | Type=Substitution;Start=371;End=384 |
| P51955 | Region | 329 | 445 | Note=Necessary for interaction with MAD1L1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14978040;Dbxref=PMID:14978040 | Type=Deletion;Start=385;End=445 |
| P51955 | Region | 329 | 445 | Note=Necessary for interaction with MAD1L1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14978040;Dbxref=PMID:14978040 | Type=Deletion;Start=327;End=445 |
| P51955 | Region | 329 | 445 | Note=Necessary for interaction with MAD1L1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14978040;Dbxref=PMID:14978040 | Type=Deletion;Start=371;End=378 |
| P51955 | Region | 333 | 370 | Note=Required for microtubule binding and for localization to the centrosomes | Type=Deletion;Start=327;End=445 |
| P51955 | Region | 403 | 439 | Note=Interaction with SAV1 and STK3/MST2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21076410;Dbxref=PMID:21076410 | Type=Deletion;Start=385;End=445 |
| P51955 | Region | 403 | 439 | Note=Interaction with SAV1 and STK3/MST2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21076410;Dbxref=PMID:21076410 | Type=Deletion;Start=327;End=445 |
| P51955 | Coiled coil | 303 | 362 | Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=323;End=326 |
| P51955 | Coiled coil | 303 | 362 | Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=327;End=445 |
| P51955 | Coiled coil | 406 | 430 | Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=385;End=445 |
| P51955 | Coiled coil | 406 | 430 | Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=327;End=445 |
Gene Isoform Structures and Expression Levels for NEK2 |
| Gene structures of our canonical and alternative spliced genes of NEK2 * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
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| Expression levels of gene isoforms across TCGA. |
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Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of P51955-1 |
| 3D view using mol* of P51955-2 |
| 3D view using mol* of P51955-3 |
| 3D view using mol* of P51955-4 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of P51955-1 |
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| pLDDT distribution across the protein length of P51955-2 |
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| pLDDT distribution across the protein length of P51955-3 |
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| pLDDT distribution across the protein length of P51955-4 |
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Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of P51955-1 |
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| Ramachandran plot of P51955-3 |
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Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| P51955-1 | 1.02 | 378 | 1.044 | 1235.143 | 0.577 | 0.716 | 0.888 | 0.529 | 0.999 | 0.53 | 0.841 | 12,14,15,17,18,19,20,22,35,37,38,39,50,51,53,54,55 ,57,58,60,61,68,73,86,87,88,89,92,93,127,129,130,1 31,132,133,134,135,136,137,138,139,140,141,142,143 ,145,146,148,158,159,160,161,162,163,164,166,167,1 71,174,175,178,179,180,181,182,183,187,188,190,193 ,201,221,225,229,317,320,321,323,324,327,328,331 |
| P51955-2 | 1.048 | 239 | 1.077 | 796.103 | 0.555 | 0.742 | 0.934 | 0.828 | 0.946 | 0.876 | 0.82 | 14,15,17,18,19,20,22,35,37,38,39,68,86,87,88,89,92 ,139,140,141,142,143,145,146,148,159,160,161,162,1 63,164,166,167,171,174,175,178,179,180,181,182,183 ,187,188,190,191,192,193,201 |
| P51955-3 | 1.04 | 339 | 1.06 | 1077.02 | 0.529 | 0.747 | 0.968 | 0.71 | 1.007 | 0.706 | 1.041 | 12,14,15,17,18,19,20,21,22,35,37,38,39,54,55,58,61 ,62,63,68,86,87,88,89,90,92,126,127,129,130,131,13 4,135,136,137,138,139,140,141,142,143,145,146,148, 158,159,160,161,162,163,164,166,167,168,171,172,17 4,175,176,178,180,182,183,187,188,189,190,193,198, 201,229 |
| P51955-4 | 1.027 | 418 | 1.053 | 1228.626 | 0.552 | 0.718 | 0.913 | 0.706 | 0.974 | 0.725 | 0.978 | 12,14,17,18,19,20,21,22,35,37,38,39,55,58,61,62,68 ,86,87,88,89,92,93,126,127,128,129,130,131,132,133 ,134,135,136,137,138,139,140,141,142,143,145,146,1 48,158,159,160,161,162,163,164,166,167,174,175,178 ,179,180,181,182,183,187,188,190,192,193,194,195,2 01,221,317,320,321,324,325,328 |
Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of P51955-1_P51955-1_2w5a_A.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P51955-1_2w5a_A_P51955-2.pdb |
| 3D view using mol* of P51955-1_2w5a_A_P51955-3.pdb |
| 3D view using mol* of P51955-1_2w5a_A_P51955-4.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P51955-1_P51955-2.pdb |
| 3D view using mol* of P51955-1_P51955-3.pdb |
| 3D view using mol* of P51955-1_P51955-4.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/P51955-1_vs_P51955-2.png |
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| ./stats/secondary_structure/figure/P51955-1_vs_P51955-3.png |
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| ./stats/secondary_structure/figure/P51955-1_vs_P51955-4.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/P51955-1_vs_P51955-2.png |
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| ./stats/relative_asa/P51955-1_vs_P51955-3.png |
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| ./stats/relative_asa/P51955-1_vs_P51955-4.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| P51955 | Region | 264 | 445 | Note=Interaction with PCNT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20599736;Dbxref=PMID:20599736 | Type=Substitution;Start=371;End=384 |
| P51955 | Region | 264 | 445 | Note=Interaction with PCNT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20599736;Dbxref=PMID:20599736 | Type=Deletion;Start=385;End=445 |
| P51955 | Region | 264 | 445 | Note=Interaction with PCNT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20599736;Dbxref=PMID:20599736 | Type=Substitution;Start=323;End=326 |
| P51955 | Region | 264 | 445 | Note=Interaction with PCNT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20599736;Dbxref=PMID:20599736 | Type=Deletion;Start=327;End=445 |
| P51955 | Region | 264 | 445 | Note=Interaction with PCNT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:20599736;Dbxref=PMID:20599736 | Type=Deletion;Start=371;End=378 |
| P51955 | Region | 301 | 445 | Note=Interaction with CEP85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26220856;Dbxref=PMID:26220856 | Type=Substitution;Start=371;End=384 |
| P51955 | Region | 301 | 445 | Note=Interaction with CEP85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26220856;Dbxref=PMID:26220856 | Type=Deletion;Start=385;End=445 |
| P51955 | Region | 301 | 445 | Note=Interaction with CEP85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26220856;Dbxref=PMID:26220856 | Type=Substitution;Start=323;End=326 |
| P51955 | Region | 301 | 445 | Note=Interaction with CEP85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26220856;Dbxref=PMID:26220856 | Type=Deletion;Start=327;End=445 |
| P51955 | Region | 301 | 445 | Note=Interaction with CEP85;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26220856;Dbxref=PMID:26220856 | Type=Deletion;Start=371;End=378 |
| P51955 | Region | 329 | 445 | Note=Necessary for interaction with MAD1L1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14978040;Dbxref=PMID:14978040 | Type=Substitution;Start=371;End=384 |
| P51955 | Region | 329 | 445 | Note=Necessary for interaction with MAD1L1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14978040;Dbxref=PMID:14978040 | Type=Deletion;Start=385;End=445 |
| P51955 | Region | 329 | 445 | Note=Necessary for interaction with MAD1L1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14978040;Dbxref=PMID:14978040 | Type=Deletion;Start=327;End=445 |
| P51955 | Region | 329 | 445 | Note=Necessary for interaction with MAD1L1;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:14978040;Dbxref=PMID:14978040 | Type=Deletion;Start=371;End=378 |
| P51955 | Region | 403 | 439 | Note=Interaction with SAV1 and STK3/MST2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21076410;Dbxref=PMID:21076410 | Type=Deletion;Start=385;End=445 |
| P51955 | Region | 403 | 439 | Note=Interaction with SAV1 and STK3/MST2;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:21076410;Dbxref=PMID:21076410 | Type=Deletion;Start=327;End=445 |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to NEK2 |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| P51955 | NEK2 | DB12010 | Fostamatinib | approved, investigational | inhibitor |
| P51955 | NEK2 | DB07180 | 5-[(Z)-(5-Chloro-2-oxo-1,2-dihydro-3H-indol-3-ylidene)methyl]-N,2,4-trimethyl-1H-pyrrole-3-carboxamide | experimental |
Related Diseases to NEK2 |
| Previous studies relating to the alternative splicing of NEK2 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
| NEK2 | 15659832 | Alternatively spliced protein variants as potential therapeutic targets for male infertility and contraception. | Mammalian sperm were previously shown to express the PP1gamma2 isoform of protein phosphatase 1 (PP1) as well as its regulatory proteins inhibitor 2 and glycogen synthase kinase 3. Furthermore, the development of sperm motility during transit through the epididymis correlates with changes in PP1 activity. Thus, since PP1 cellular activity is determined by the partners it binds, we embarked on a study aimed at defining the specific interactomes of PP1gamma1 and PP1gamma2 (the two known alternatively spliced variants of PP1gamma). To this end, exhaustive screens were performed on a human testis cDNA library using the yeast two-hybrid method. Among the various proteins detected, the most abundant interactors with PP1gamma2 were Nek2A and R15B. Closer sequence analysis revealed novel alternatively spliced variants of Nek2A and NIPP1, which we designated Nek2A-T and NIPP1-T, respectively. They were shown to be highly expressed in rat and human testis by Northern analysis and to result from alternative splicing events by RT-PCR. Thus, both the previously known Nek2A isoform and the novel Nek2A-T and NIPP1-T variants appear to bind PP1gamma2 in vitro (blot overlays) and in vivo by coexpression in yeast. The usefulness of testis-specific alternatively spliced proteins as targets for the development of novel therapeutic strategies for male infertility and contraception is discussed. PP1gamma2, Nek2A-T, and NIPP1-T are currently being investigated as alternatively spliced targets for signal transduction therapeutics. | D007248 | Infertility, Male |
Clinically important variants in NEK2 |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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