| Tag |
Content |
LipidDB ID |
LipidDB-559292-01175 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
9.37 |
Molecular Weight |
78491.59 |
Genbank Protein ID |
|
Genbank Nucleotide ID |
|
Protein Name |
Serine/threonine-protein phosphatase PP-Z2 |
Protein Synonyms/Alias |
3.1.3.16; |
Gene Name |
PPZ2 |
Gene Synonyms/Alias |
YDR436W; D9461.22; |
Created Date |
01-FEB-1994 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
2 | Canonical | ******MGNSGSKQH | [1] | N-Myristoylation |
|
Organism |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID |
559292 |
Reference |
[1] Resh MD. Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins. Biochim Biophys Acta. 1999 Aug12;1451(1):1-16. Review.[ PMID:10446384]
|
Functional Description |
Essential for the maintenance of cell size and integrity in response to osmotic stress. |
Sequence Annotation |
Active site: 515 515 Proton donor.
Metal binding site: 454 454 Manganese 1.
Metal binding site: 456 456 Manganese 1.
Metal binding site: 482 482 Manganese 1.
Metal binding site: 482 482 Manganese 2.
Metal binding site: 514 514 Manganese 2.
Metal binding site: 563 563 Manganese 2.
Metal binding site: 638 638 Manganese 2.
Modified residue: 71 71 Phosphoserine.
Modified residue: 203 203 Phosphoserine.
Modified residue: 224 224 Phosphoserine.
Modified residue: 310 310 Phosphoserine.
|
Protein Length |
710 AA. |
Protein Sequence
(Canonical) |
MGNSGSKQHT KHNSKKDDHD GDRKKTLDLP PLTKSDTTHS LKSSRSLRSL RSKRSEASLA 60
SNVQAQTQPL SRRSSTLGNG NRNHRRSNNA PITPPNNHYL TSHPSSSRRL SSSSRRSSMG 120
NNNNSELPPS MIQMEPKSPI LKNSTSMHST SSFNSYENAL TDDDDDRGDD GGESPSMAKV 180
TRINTSSSAD RGSKRTPLRR HNSLQPEKGV TGFSSTSSKL RRRSDNTLPA SYPLNAEAGG 240
NGSDYFSNRS NSHASSRKSS FGSTGNTAYS TPLHSPALRK MSSRDNDDSG DNVNGRGTSP 300
IPNLNIDKPS PSASSASKRE YLSAYPTLAH RDSSSSLSPR GKGQRSSSSS SSSQRIYVSP 360
PSPTGDFVHG SCADGDNGSR TNTMVEMKRK KPVRPVDIDE IIQRLLDAGY AAKRTKNVCL 420
KNSEIIQICH KARELFLAQP ALLELSPSVK IVGDVHGQYA DLLRLFTKCG FPPMANYLFL 480
GDYVDRGKQS LETILLLLCY KIKYPENFFL LRGNHECANV TRVYGFYDEC KRRCNIKIWK 540
TFVDTFNTLP LAAIVTGKIF CVHGGLSPVL NSMDEIRHVS RPTDVPDFGL INDLLWSDPT 600
DSSNEWEDNE RGVSFCYNKV AINKFLNKFG FDLVCRAHMV VEDGYEFFND RSLVTVFSAP 660
NYCGEFDNWG AVMTVSEGLL CSFELLDPLD STALKQVMKK GRQERKLANR 710
|
FASTA
(Canonical) |
>LipidDB-559292-01175|P33329
MGNSGSKQHTKHNSKKDDHDGDRKKTLDLPPLTKSDTTHSLKSSRSLRSLRSKRSEASLA
SNVQAQTQPLSRRSSTLGNGNRNHRRSNNAPITPPNNHYLTSHPSSSRRLSSSSRRSSMG
NNNNSELPPSMIQMEPKSPILKNSTSMHSTSSFNSYENALTDDDDDRGDDGGESPSMAKV
TRINTSSSADRGSKRTPLRRHNSLQPEKGVTGFSSTSSKLRRRSDNTLPASYPLNAEAGG
NGSDYFSNRSNSHASSRKSSFGSTGNTAYSTPLHSPALRKMSSRDNDDSGDNVNGRGTSP
IPNLNIDKPSPSASSASKREYLSAYPTLAHRDSSSSLSPRGKGQRSSSSSSSSQRIYVSP
PSPTGDFVHGSCADGDNGSRTNTMVEMKRKKPVRPVDIDEIIQRLLDAGYAAKRTKNVCL
KNSEIIQICHKARELFLAQPALLELSPSVKIVGDVHGQYADLLRLFTKCGFPPMANYLFL
GDYVDRGKQSLETILLLLCYKIKYPENFFLLRGNHECANVTRVYGFYDECKRRCNIKIWK
TFVDTFNTLPLAAIVTGKIFCVHGGLSPVLNSMDEIRHVSRPTDVPDFGLINDLLWSDPT
DSSNEWEDNERGVSFCYNKVAINKFLNKFGFDLVCRAHMVVEDGYEFFNDRSLVTVFSAP
NYCGEFDNWGAVMTVSEGLLCSFELLDPLDSTALKQVMKKGRQERKLANR
|
Gene Ontology |
GO:0048037; F:cofactor binding; IEA:InterPro GO:0004724; F:magnesium-dependent protein serine/threonine phosphatase activity; IEA:InterPro GO:0046872; F:metal ion binding; IEA:UniProtKB-KW GO:0004722; F:protein serine/threonine phosphatase activity; ISS:SGD GO:0006883; P:cellular sodium ion homeostasis; IMP:SGD GO:0016311; P:dephosphorylation; ISS:GOC |
Interpro |
|
Pfam |
|
SMART |
|
PROSITE |
PROSITE; PS00125; SER_THR_PHOSPHATASE; |
PRINTS |
|