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Reviewed, UniProtKB/Swiss-Prot P78330 (SERB_HUMAN)

Last modified February 9, 2010. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoserine phosphatase
      Short name=PSPase
      Short name=PSP
    EC=3.1.3.3
Alternative name(s):
    O-phosphoserine phosphohydrolase
    L-3-phosphoserine phosphatase
Gene names
Name: PSPH
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length225 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Catalytic activity

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

Cofactor

Magnesium.

Pathway

Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 3/3.

Subunit structure

Homodimer.

Involvement in disease

Defects in PSPH are the cause of 3-phosphoserine phosphatase deficiency (PSPHD)[MIM:172480]. Affected individuals have pre- and postnatal growth retardation, moderate psychomotor retardation and facial features suggestive of Williams syndrome. Ref.8

Sequence similarities

Belongs to the serB family.

Ontologies

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 225225Phosphoserine phosphatase
PRO_0000156879

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7

Natural variations

Natural variant321D → N in PSPHD. dbSNP rs28933976. Ref.8
VAR_022378
Natural variant521M → T in PSPHD. Ref.8
VAR_022379

Experimental info

Sequence conflict21V → I in CAA71318. Ref.1

Secondary structure

........................................... 225
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P78330-1 [UniParc].

Last modified April 26, 2005. Version 2.
Checksum: BD5D72697747FA30

FASTA22525,008
        10         20         30         40         50         60 
MVSHSELRKL FYSADAVCFD VDSTVIREEG IDELAKICGV EDAVSEMTRR AMGGAVPFKA 

        70         80         90        100        110        120 
ALTERLALIQ PSREQVQRLI AEQPPHLTPG IRELVSRLQE RNVQVFLISG GFRSIVEHVA 

       130        140        150        160        170        180 
SKLNIPATNV FANRLKFYFN GEYAGFDETQ PTAESGGKGK VIKLLKEKFH FKKIIMIGDG 

       190        200        210        220 
ATDMEACPPA DAFIGFGGNV IRQQVKDNAK WYITDFVELL GELEE 

« Hide

References

« Hide 'large scale' references
[1]"Human L-3-phosphoserine phosphatase: sequence, expression and evidence for a phosphoenzyme intermediate."
Collet J.-F., Gerin I., Rider M.H., Veiga-Da-Cunha M., Van Schaftingen E.
FEBS Lett. 408:281-284(1997) [PubMed: 9188776] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Endometrial tumor.
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
[6]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY.
[8]"Mutations responsible for 3-phosphoserine phosphatase deficiency."
Veiga-da-Cunha M., Collet J.F., Prieur B., Jaeken J., Peeraer Y., Rabbijns A., Van Schaftingen E.
Eur. J. Hum. Genet. 12:163-166(2004) [PubMed: 14673469] [Abstract]
Cited for: VARIANTS PSPHD ASN-32 AND THR-52.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y10275 mRNA. Translation: CAA71318.1.
AK315235 mRNA. Translation: BAG37662.1.
BX537439 mRNA. Translation: CAD97681.1.
CH471140 Genomic DNA. Translation: EAX07968.1.
BC063614 mRNA. Translation: AAH63614.1.
IPIIPI00019178.
RefSeqNP_004568.2.
UniGeneHs.512656

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1L8LX-ray2.51A/B3-225[»]
1L8OX-ray2.80A/B3-225[»]
1NNLX-ray1.53A/B3-225[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP78330. 16 interactions.
STRINGP78330.

PTM databases

PhosphoSiteP78330.

Proteomic databases

PeptideAtlasP78330.
PRIDEP78330.

Genome annotation databases

EnsemblENST00000275605; ENSP00000275605; ENSG00000146733; Homo sapiens. [Genome view]
ENST00000395471; ENSP00000378854; ENSG00000146733; Homo sapiens. [Genome view]
ENST00000437355; ENSP00000401639; ENSG00000146733; Homo sapiens. [Genome view]
GeneID5723.
KEGGhsa:5723.
UCSCuc003trg.1. human.

Organism-specific databases

CTD5723.
GeneCardsGC07M056046.
H-InvDBHIX0021579.
HIX0058416.
HGNCHGNC:9577. PSPH.
HPAHPA020376.
MIM172480. gene+phenotype.
Orphanet35705. Neurometabolic disorder due to serine deficiency.
PharmGKBPA33928.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG17027.
HOGENOMHBG482410.
HOVERGENP78330.
InParanoidP78330.
OMAPATNVFA.
OrthoDBEOG95TG6X.
PhylomeDBP78330.

Enzyme and pathway databases

BRENDA3.1.3.3. 247.

Gene expression databases

ArrayExpressP78330.
BgeeP78330.
CleanExHS_PSPH.
GenevestigatorP78330.
GermOnlineENSG00000146733. Homo sapiens.

Family and domain databases

InterProIPR005834. Dehalogen-like_hydro.
IPR006383. HAD-SF_hydro_IB_PSP-like.
IPR004469. SerB.
[Graphical view]
PfamPF00702. Hydrolase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01488. HAD-SF-IB. 1 hit.
TIGR00338. serB. 1 hit.
ProtoNetSearch...

Other Resources

NextBio22244.
SOURCESearch...

Entry information

Entry nameSERB_HUMAN
AccessionPrimary (citable) accession number: P78330
Secondary accession number(s): B2RCR5, Q7Z3S5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 26, 2005
Last modified: February 9, 2010
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents