| General information | | DisProt: | DP00428 | | Name: | Serine/threonine-protein kinase PLK1 | | Synonym(s): | PLK1_HUMAN
Polo-like kinase 1
PLK-1
Serine/threonine-protein kinase 13
STPK13
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P53350 | | UniGene: | Hs.592049 | | SwissProt: | PLK1_HUMAN | | TrEMBL: | | | NCBI (GI): | 1709658 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 603 | | Percent disordered: | 9% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
MSAAVTAGKL ARAPADPGKA GVPGVAAPGA PAAAPPAKEI PEVLVDPRSR RRYVRGRFLG - 60
KGGFAKCFEI SDADTKEVFA GKIVPKSLLL KPHQREKMSM EISIHRSLAH QHVVGFHGFF - 120
EDNDFVFVVL ELCRRRSLLE LHKRRKALTE PEARYYLRQI VLGCQYLHRN RVIHRDLKLG - 180
NLFLNEDLEV KIGDFGLATK VEYDGERKKT LCGTPNYIAP EVLSKKGHSF EVDVWSIGCI - 240
MYTLLVGKPP FETSCLKETY LRIKKNEYSI PKHINPVAAS LIQKMLQTDP TARPTINELL - 300
NDEFFTSGYI PARLPITCLT IPPRFSIAPS SLDPSNRKPL TVLNKGLENP LPERPREKEE - 360
PVVRETGEVV DCHLSDMLQQ LHSVNASKPS ERGLVRQEEA EDPACIPIFW VSKWVDYSDK - 420
YGLGYQLCDN SVGVLFNDST RLILYNDGDS LQYIERDGTE SYLTVSSHPN SLMKKITLLK - 480
YFRNYMSEHL LKAGANITPR EGDELARLPY LRTWFRTRSA IILHLSNGSV QINFFQDHTK - 540
LILCPLMAAV TYIDEKRDFR TYRLSLLEEY GCCKELASRL RYARTMVDKL LSSRSASNRL - 600
KAS
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| Functional narrative |
Serine/threonine-protein kinase that performs several important functions throughout M phase of the cell cycle, including the regulation of centrosome maturation and spindle assembly, the removal of cohesins from chromosome arms, the inactivation of APC/C inhibitors, and the regulation of mitotic exit and cytokinesis.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 493 - 507 | | Length: | 15 | | Region sequence: |
AGANITPREGDELAR | | Modification type: | Fragment
| | PDB: | | | Structural/functional type: | Function arises via a disorder to order transition
| | Functional classes: | Entropic chain
| | Functional subclasses: | Flexible linkers/spacers
| Detection methods:
- X-ray crystallography (277 K; Ammonium acetate 0.1 M; PEG 4000 (5-10% (v/v)); protein 10 mg/ml; Sodium citrate (pH 6.0) 0.1 M)
| References:
- Cheng KY, Lowe ED, Sinclair J, Nigg EA, Johnson LN. "The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complex." EMBO J. 2003; 22(21): 5757-68. PubMed: 14592974
| Comments:The fragment used to determine this structure consisted of residues 345-603.
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 345 - 372 | | Length: | 28 | | Region sequence: |
KGLENPLPERPREKEEPVVRETGEVVDC | | Modification type: | Complex
Fragment
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (298 K; MES (pH 6.5) 0.1 M; PEG 20000 (1-10%); Phospho-peptide (Met.Gln.Ser.pThr.Pro.Leu); protein 10 mg/ml)
| References:
- Cheng KY, Lowe ED, Sinclair J, Nigg EA, Johnson LN. "The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complex." EMBO J. 2003; 22(21): 5757-68. PubMed: 14592974
| Comments:The fragment used to determine this structure consisted of residues 345-603.
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| Region 3 | | Type: | Disordered | | Name: | | | Location: | 594 - 603 | | Length: | 10 | | Region sequence: |
RSASNRLKAS | | Modification type: | Complex
Fragment
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography (298 K; MES (pH 6.5) 0.1 M; PEG 20000 (1-10%); Phospho-peptide (Met.Gln.Ser.pThr.Pro.Leu); protein 10 mg/ml)
| References:
- Cheng KY, Lowe ED, Sinclair J, Nigg EA, Johnson LN. "The crystal structure of the human polo-like kinase-1 polo box domain and its phospho-peptide complex." EMBO J. 2003; 22(21): 5757-68. PubMed: 14592974
| Comments:The fragment used to determine this structure consisted of residues 345-603.
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