| General information | | DisProt: | DP00365 | | Name: | Serine/threonine protein phosphatase 5 | | Synonym(s): | PP5
PPT
PP-T
Protein phosphatase T
PPP5_HUMAN
| | First appeared in release: | Release 3.0 (02/17/2006) | | UniProt: | P53041 | | UniGene: | | | SwissProt: | PPP5_HUMAN | | TrEMBL: | | | NCBI (GI): | 1709744 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 499 | | Percent disordered: | 26% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MAMAEGERTE CAEPPRDEPP ADGALKRAEE LKTQANDYFK AKDYENAIKF YSQAIELNPS - 60
NAIYYGNRSL AYLRTECYGY ALGDATRAIE LDKKYIKGYY RRAASNMALG KFRAALRDYE - 120
TVVKVKPHDK DAKMKYQECN KIVKQKAFER AIAGDEHKRS VVDSLDIESM TIEDEYSGPK - 180
LEDGKVTISF MKELMQWYKD QKKLHRKCAY QILVQVKEVL SKLSTLVETT LKETEKITVC - 240
GDTHGQFYDL LNIFELNGLP SETNPYIFNG DFVDRGSFSV EVILTLFGFK LLYPDHFHLL - 300
RGNHETDNMN QIYGFEGEVK AKYTAQMYEL FSEVFEWLPL AQCINGKVLI MHGGLFSEDG - 360
VTLDDIRKIE RNRQPPDSGP MCDLLWSDPQ PQNGRSISKR GVSCQFGPDV TKAFLEENNL - 420
DYIIRSHEVK AEGYEVAHGG RCVTVFSAPN YCDQMGNKAS YIHLQGSDLR PQFHQFTAVP - 480
HPNVKPMAYA NTLLQLGMM
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| Functional narrative |
"Protein phosphatase 5 (PP5) is a threonine-serine phosphatase that is targeted to the Hsp90 complex via its N-terminal TPR domain. In isolation, PP5 has a low level of enzymatic activity, which can be enhanced by removal of its TPR domain. The enzyme can be activated by the addition of the 12 kDa C-terminal domain of Hsp90 or long-chain fatty acids to the full-length protein. It has been shown that residues in the TPR domain are essential for modulation of activity by these physiological activators. The TPR domain is consequently thought to act as an inhibitor/regulator of the protein phosphatase in addition to specifically binding to the Hsp90 C terminus." (Cliff et al. 2005)
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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: | TPR domain | | Location: | 19 - 147 | | Length: | 129 | | Region sequence: |
PPADGALKRAEELKTQANDYFKAKDYENAIKFYSQAIELNPSNAIYYGNRSLAYLRTECY
GYALGDATRAIELDKKYIKGYYRRAASNMALGKFRAALRDYETVVKVKPHDKDAKMKYQE
CNKIVKQKA | | Modification type: | Native
| | PDB: | 1A17:A | | Structural/functional type: | Function arises via a molten globule to order transition
| | Functional classes: | Molecular assembly
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (298 K; pH: 7.5; )
- Circular dichroism (CD) spectroscopy, far-UV (pH: 6; )
| References:
- Cliff MJ, Williams MA, Brooke-Smith J, Barford D, Ladbury JE. "Molecular recognition via coupled folding and binding in a TPR domain." J Mol Biol. 2005; 346(3): 717-32. PubMed: 15713458
| Comments:
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| References |
- Chinkers M. "Protein phosphatase 5 in signal transduction." Trends Endocrinol Metab. 2001; 12(1): 28-32. PubMed: 11137038
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