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Protein

Phosphoserine phosphatase

Gene

Psph

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates (By similarity).By similarity

Catalytic activityi

O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate.

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

Pathwayi: L-serine biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes L-serine from 3-phospho-D-glycerate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. D-3-phosphoglycerate dehydrogenase (Phgdh)
  2. Phosphoserine aminotransferase (Psat1), Phosphoserine aminotransferase (Psat1), Phosphoserine aminotransferase (Psat1), Phosphoserine aminotransferase (Psat1), Phosphoserine aminotransferase (Psat1)
  3. Phosphoserine phosphatase (Psph)
This subpathway is part of the pathway L-serine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-serine from 3-phospho-D-glycerate, the pathway L-serine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei20 – 201NucleophileBy similarity
Metal bindingi20 – 201MagnesiumBy similarity
Active sitei22 – 221Proton donorBy similarity
Metal bindingi22 – 221Magnesium; via carbonyl oxygenBy similarity
Binding sitei29 – 291SubstrateBy similarity
Binding sitei65 – 651SubstrateBy similarity
Binding sitei158 – 1581SubstrateBy similarity
Metal bindingi179 – 1791MagnesiumBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Amino-acid biosynthesis, Serine biosynthesis

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.3.3. 3474.
ReactomeiR-MMU-977347. Serine biosynthesis.
UniPathwayiUPA00135; UER00198.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoserine phosphatase (EC:3.1.3.3)
Short name:
PSP
Short name:
PSPase
Alternative name(s):
O-phosphoserine phosphohydrolase
Gene namesi
Name:Psph
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:97788. Psph.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 225225Phosphoserine phosphatasePRO_0000156880Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ99LS3.
MaxQBiQ99LS3.
PaxDbiQ99LS3.
PeptideAtlasiQ99LS3.
PRIDEiQ99LS3.

2D gel databases

UCD-2DPAGEQ99LS3.

PTM databases

iPTMnetiQ99LS3.
PhosphoSiteiQ99LS3.

Expressioni

Gene expression databases

BgeeiQ99LS3.
CleanExiMM_PSPH.
ExpressionAtlasiQ99LS3. baseline and differential.
GenevisibleiQ99LS3. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi221509. 1 interaction.
IntActiQ99LS3. 2 interactions.
MINTiMINT-4124330.
STRINGi10090.ENSMUSP00000031399.

Structurei

3D structure databases

ProteinModelPortaliQ99LS3.
SMRiQ99LS3. Positions 4-225.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni109 – 1102Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the SerB family.Curated

Phylogenomic databases

eggNOGiKOG1615. Eukaryota.
COG0560. LUCA.
GeneTreeiENSGT00390000003115.
HOGENOMiHOG000231116.
HOVERGENiHBG057486.
InParanoidiQ99LS3.
KOiK01079.
OMAiTDLEACP.
PhylomeDBiQ99LS3.
TreeFamiTF315024.

Family and domain databases

Gene3Di1.10.150.210. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006383. HAD-SF_hydro_IB_PSP-like.
IPR023190. Pser_Pase_dom_2.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01488. HAD-SF-IB. 1 hit.

Sequencei

Sequence statusi: Complete.

Q99LS3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSHSELRKL FCSADAVCFD VDSTVIREEG IDELAKFCGV EAAVSEMTRR
60 70 80 90 100
AMGGALPFKD ALTQRLALIQ PSRDQVQRLL AEHPPHLTPG IRELVSRLQE
110 120 130 140 150
RNVQVFLISG GFRSIVEHVA AKLNIPTTNV FANRLKFYFN GEYAGFDEMQ
160 170 180 190 200
PTAESGGKGK VIRFLKEKFH FKKIIMIGDG ATDMEACPPA DAFIGFGGNV
210 220
IRQQVKDNAK WYITDFVELL GELEE
Length:225
Mass (Da):25,096
Last modified:June 1, 2001 - v1
Checksum:iCCEE55B48787D10A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK088865 mRNA. Translation: BAC40622.1.
AK168048 mRNA. Translation: BAE40030.1.
BC002251 mRNA. Translation: AAH02251.1.
CCDSiCCDS19699.1.
RefSeqiNP_598661.1. NM_133900.4.
XP_006504337.1. XM_006504274.2.
UniGeneiMm.271784.

Genome annotation databases

EnsembliENSMUST00000031399; ENSMUSP00000031399; ENSMUSG00000029446.
GeneIDi100678.
KEGGimmu:100678.
UCSCiuc008zth.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK088865 mRNA. Translation: BAC40622.1.
AK168048 mRNA. Translation: BAE40030.1.
BC002251 mRNA. Translation: AAH02251.1.
CCDSiCCDS19699.1.
RefSeqiNP_598661.1. NM_133900.4.
XP_006504337.1. XM_006504274.2.
UniGeneiMm.271784.

3D structure databases

ProteinModelPortaliQ99LS3.
SMRiQ99LS3. Positions 4-225.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi221509. 1 interaction.
IntActiQ99LS3. 2 interactions.
MINTiMINT-4124330.
STRINGi10090.ENSMUSP00000031399.

PTM databases

iPTMnetiQ99LS3.
PhosphoSiteiQ99LS3.

2D gel databases

UCD-2DPAGEQ99LS3.

Proteomic databases

EPDiQ99LS3.
MaxQBiQ99LS3.
PaxDbiQ99LS3.
PeptideAtlasiQ99LS3.
PRIDEiQ99LS3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031399; ENSMUSP00000031399; ENSMUSG00000029446.
GeneIDi100678.
KEGGimmu:100678.
UCSCiuc008zth.2. mouse.

Organism-specific databases

CTDi5723.
MGIiMGI:97788. Psph.

Phylogenomic databases

eggNOGiKOG1615. Eukaryota.
COG0560. LUCA.
GeneTreeiENSGT00390000003115.
HOGENOMiHOG000231116.
HOVERGENiHBG057486.
InParanoidiQ99LS3.
KOiK01079.
OMAiTDLEACP.
PhylomeDBiQ99LS3.
TreeFamiTF315024.

Enzyme and pathway databases

UniPathwayiUPA00135; UER00198.
BRENDAi3.1.3.3. 3474.
ReactomeiR-MMU-977347. Serine biosynthesis.

Miscellaneous databases

PROiQ99LS3.
SOURCEiSearch...

Gene expression databases

BgeeiQ99LS3.
CleanExiMM_PSPH.
ExpressionAtlasiQ99LS3. baseline and differential.
GenevisibleiQ99LS3. MM.

Family and domain databases

Gene3Di1.10.150.210. 1 hit.
3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006383. HAD-SF_hydro_IB_PSP-like.
IPR023190. Pser_Pase_dom_2.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01488. HAD-SF-IB. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/cJ and NOD.
    Tissue: Thymus.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Mammary tumor.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas and Testis.

Entry informationi

Entry nameiSERB_MOUSE
AccessioniPrimary (citable) accession number: Q99LS3
Secondary accession number(s): Q3TI16, Q5XHW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.