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Q9BVG9 (PTSS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphatidylserine synthase 2

Short name=PSS-2
Short name=PtdSer synthase 2
EC=2.7.8.29
Alternative name(s):
Serine-exchange enzyme II
Gene names
Name:PTDSS2
Synonyms:PSS2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length487 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. PTDSS2 is specific for phosphatatidylethanolamine and does not act on phosphatidylcholine.

Catalytic activity

L-1-phosphatidylethanolamine + L-serine = L-1-phosphatidylserine + ethanolamine.

Enzyme regulation

Inhibited in both the MAM and the ER per se by ethanolamine. Requires calcium ions. Ref.8

Pathway

Phospholipid metabolism; phosphatidylserine biosynthesis.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein By similarity. Note: Highly enriched in the mitochondria-associated membrane (MAM) By similarity.

Sequence similarities

Belongs to the phosphatidyl serine synthase family.

Biophysicochemical properties

Kinetic parameters:

KM=120 µM for serine (in the presence of 1 mM PE) Ref.8

Vmax=0.57 mmol/h/mg enzyme

pH dependence:

Optimum pH is around 7.5.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 487487Phosphatidylserine synthase 2
PRO_0000056832

Regions

Topological domain1 – 6262Cytoplasmic Potential
Transmembrane63 – 8321Helical; Potential
Topological domain84 – 9613Lumenal Potential
Transmembrane97 – 11721Helical; Potential
Topological domain118 – 1269Cytoplasmic Potential
Transmembrane127 – 14721Helical; Potential
Topological domain148 – 313166Lumenal Potential
Transmembrane314 – 33421Helical; Potential
Topological domain3351Cytoplasmic Potential
Transmembrane336 – 35621Helical; Potential
Topological domain357 – 37620Lumenal Potential
Transmembrane377 – 39721Helical; Potential
Topological domain398 – 4036Cytoplasmic Potential
Transmembrane404 – 42421Helical; Potential
Topological domain425 – 48763Lumenal Potential

Amino acid modifications

Modified residue161Phosphoserine Ref.4 Ref.5 Ref.6 Ref.10 Ref.11 Ref.12
Modified residue4851Phosphothreonine Ref.6
Glycosylation1811N-linked (GlcNAc...) Ref.9

Sequences

Sequence LengthMass (Da)Tools
Q9BVG9 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: E02508F894841A4F

FASTA48756,253
        10         20         30         40         50         60 
MRRGERRDAG GPRPESPVPA GRASLEEPPD GPSAGQATGP GEGRRSTESE VYDDGTNTFF 

        70         80         90        100        110        120 
WRAHTLTVLF ILTCTLGYVT LLEETPQDTA YNTKRGIVAS ILVFLCFGVT QAKDGPFSRP 

       130        140        150        160        170        180 
HPAYWRFWLC VSVVYELFLI FILFQTVQDG RQFLKYVDPK LGVPLPERDY GGNCLIYDPD 

       190        200        210        220        230        240 
NETDPFHNIW DKLDGFVPAH FLGWYLKTLM IRDWWMCMII SVMFEFLEYS LEHQLPNFSE 

       250        260        270        280        290        300 
CWWDHWIMDV LVCNGLGIYC GMKTLEWLSL KTYKWQGLWN IPTYKGKMKR IAFQFTPYSW 

       310        320        330        340        350        360 
VRFEWKPASS LRRWLAVCGI ILVFLLAELN TFYLKFVLWM PPEHYLVLLR LVFFVNVGGV 

       370        380        390        400        410        420 
AMREIYDFMD DPKPHKKLGP QAWLVAAITA TELLIVVKYD PHTLTLSLPF YISQCWTLGS 

       430        440        450        460        470        480 
VLALTWTVWR FFLRDITLRY KETRWQKWQN KDDQGSTVGN GDQHPLGLDE DLLGPGVAEG 


EGAPTPN 

« Hide

References

« Hide 'large scale' references
[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[2]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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].
Tissue: Brain.
[4]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[6]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND THR-485, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Purification and characterization of human phosphatidylserine synthases 1 and 2."
Tomohiro S., Kawaguti A., Kawabe Y., Kitada S., Kuge O.
Biochem. J. 418:421-429(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[9]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-181.
Tissue: Liver.
[10]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL834357 mRNA. Translation: CAD39022.1.
AC137894 Genomic DNA. No translation available.
AC138230 Genomic DNA. No translation available.
BC001210 mRNA. Translation: AAH01210.1.
CCDSCCDS7696.1.
RefSeqNP_110410.1. NM_030783.1.
UniGeneHs.731700.

3D structure databases

ProteinModelPortalQ9BVG9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123499. 3 interactions.
STRING9606.ENSP00000308258.

Chemistry

DrugBankDB00144. Phosphatidylserine.

PTM databases

PhosphoSiteQ9BVG9.

Polymorphism databases

DMDM49036457.

Proteomic databases

MaxQBQ9BVG9.
PaxDbQ9BVG9.
PRIDEQ9BVG9.

Protocols and materials databases

DNASU81490.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308020; ENSP00000308258; ENSG00000174915.
GeneID81490.
KEGGhsa:81490.
UCSCuc001lpj.3. human.

Organism-specific databases

CTD81490.
GeneCardsGC11P000440.
H-InvDBHIX0026263.
HGNCHGNC:15463. PTDSS2.
HPAHPA038928.
HPA038929.
MIM612793. gene.
neXtProtNX_Q9BVG9.
PharmGKBPA33940.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG264399.
HOGENOMHOG000005791.
HOVERGENHBG053766.
InParanoidQ9BVG9.
KOK08730.
OMAKPHKKLG.
OrthoDBEOG7CNZGB.
PhylomeDBQ9BVG9.
TreeFamTF300012.

Enzyme and pathway databases

BioCycMetaCyc:HS10846-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00948.

Gene expression databases

ArrayExpressQ9BVG9.
BgeeQ9BVG9.
CleanExHS_PTDSS2.
GenevestigatorQ9BVG9.

Family and domain databases

InterProIPR004277. PSS.
[Graphical view]
PANTHERPTHR12615. PTHR12615. 1 hit.
PfamPF03034. PSS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi81490.
NextBio71722.
PROQ9BVG9.
SOURCESearch...

Entry information

Entry namePTSS2_HUMAN
AccessionPrimary (citable) accession number: Q9BVG9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

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

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM