Q99LS3 (SERB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoserine phosphatase
Short name=PSP
Short name=PSPase
EC=3.1.3.3

Alternative name(s):
O-phosphoserine phosphohydrolase

Gene names

Name:

Psph

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	225 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Catalytic activity	O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Pathway	Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the serB family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Serine biosynthesis
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	L-serine biosynthetic process Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular component	cytoplasm Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	calcium ion binding Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion binding Inferred from sequence or structural similarity. Source: UniProtKB phosphoserine phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 225	225	Phosphoserine phosphatase		PRO_0000156880
Regions
	Region	109 – 110	2	Substrate binding By similarity
Sites
	Active site	20	1	Nucleophile By similarity
	Active site	22	1	Proton donor By similarity
	Metal binding	20	1	Magnesium By similarity
	Metal binding	22	1	Magnesium; via carbonyl oxygen By similarity
	Metal binding	179	1	Magnesium By similarity
	Binding site	29	1	Substrate By similarity
	Binding site	65	1	Substrate By similarity
	Binding site	158	1	Substrate By similarity
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q99LS3 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: CCEE55B48787D10A	FASTA	225	25,096
	10 20 30 40 50 60 MVSHSELRKL FCSADAVCFD VDSTVIREEG IDELAKFCGV EAAVSEMTRR AMGGALPFKD 70 80 90 100 110 120 ALTQRLALIQ PSRDQVQRLL AEHPPHLTPG IRELVSRLQE RNVQVFLISG GFRSIVEHVA 130 140 150 160 170 180 AKLNIPTTNV FANRLKFYFN GEYAGFDEMQ PTAESGGKGK VIRFLKEKFH FKKIIMIGDG 190 200 210 220 ATDMEACPPA DAFIGFGGNV IRQQVKDNAK WYITDFVELL GELEE

References

[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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: BALB/c 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II. Tissue: Mammary tumor.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK088865 mRNA. Translation: BAC40622.1. AK168048 mRNA. Translation: BAE40030.1. BC002251 mRNA. Translation: AAH02251.1.
IPI	IPI00117146.
RefSeq	NP_598661.1. NM_133900.4.
UniGene	Mm.271784.
3D structure databases
ProteinModelPortal	Q99LS3.
SMR	Q99LS3. Positions 4-225.
ModBase	Search...
Protein-protein interaction databases
STRING	Q99LS3.
PTM databases
PhosphoSite	Q99LS3.
2D gel databases
UCD-2DPAGE	Q99LS3.
Proteomic databases
PRIDE	Q99LS3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	100678.
KEGG	mmu:100678.
UCSC	uc008zth.2. mouse.
Organism-specific databases
CTD	5723.
MGI	MGI:97788. Psph.
Phylogenomic databases
eggNOG	maNOG12671.
GeneTree	ENSGT00390000003115.
HOGENOM	HBG482410.
HOVERGEN	HBG057486.
InParanoid	Q99LS3.
OrthoDB	EOG4NVZM5.
PhylomeDB	Q99LS3.
Gene expression databases
ArrayExpress	Q99LS3.
Bgee	Q99LS3.
CleanEx	MM_PSPH.
Genevestigator	Q99LS3.
GermOnline	ENSMUSG00000029446. Mus musculus.
Family and domain databases
InterPro	IPR005834. Dehalogen-like_hydro. IPR023214. HAD-like_dom. IPR006383. HAD-SF_hydro_IB_PSP-like. IPR023190. Pser_Pase_dom_2. IPR004469. SerB. [Graphical view]
Gene3D	G3DSA:3.40.50.1000. HAD-like_dom. 2 hits. G3DSA:1.10.150.210. Pser_Pase_dom_2. 1 hit.
KO	K01079.
Pfam	PF00702. Hydrolase. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01488. HAD-SF-IB. 1 hit. TIGR00338. SerB. 1 hit.
ProtoNet	Search...
Other
NextBio	354580.
SOURCE	Search...

Entry information

Entry name

SERB_MOUSE

Accession

Primary (citable) accession number: Q99LS3
Secondary accession number(s): Q3TI16, Q5XHW3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	June 1, 2001
Last modified:	November 16, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program