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Protein

Phosphatidylserine synthase 2

Gene

PTDSS2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Enzyme regulationi

Inhibited in both the MAM and the ER per se by ethanolamine. Requires calcium ions.1 Publication

Kineticsi

  1. KM=120 µM for serine (in the presence of 1 mM PE)1 Publication
  1. Vmax=0.57 mmol/h/mg enzyme1 Publication

pH dependencei

Optimum pH is around 7.5.1 Publication

Pathway: phosphatidylserine biosynthesis

This protein is involved in the pathway phosphatidylserine biosynthesis, which is part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the pathway phosphatidylserine biosynthesis and in Phospholipid metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS10846-MONOMER.
BRENDAi2.7.8.29. 2681.
ReactomeiREACT_120823. Synthesis of PS.
UniPathwayiUPA00948.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidylserine synthase 2 (EC:2.7.8.29)
Short name:
PSS-2
Short name:
PtdSer synthase 2
Alternative name(s):
Serine-exchange enzyme II
Gene namesi
Name:PTDSS2
Synonyms:PSS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:15463. PTDSS2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6262CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei63 – 8321HelicalSequence AnalysisAdd
BLAST
Topological domaini84 – 9613LumenalSequence AnalysisAdd
BLAST
Transmembranei97 – 11721HelicalSequence AnalysisAdd
BLAST
Topological domaini118 – 1269CytoplasmicSequence Analysis
Transmembranei127 – 14721HelicalSequence AnalysisAdd
BLAST
Topological domaini148 – 313166LumenalSequence AnalysisAdd
BLAST
Transmembranei314 – 33421HelicalSequence AnalysisAdd
BLAST
Topological domaini335 – 3351CytoplasmicSequence Analysis
Transmembranei336 – 35621HelicalSequence AnalysisAdd
BLAST
Topological domaini357 – 37620LumenalSequence AnalysisAdd
BLAST
Transmembranei377 – 39721HelicalSequence AnalysisAdd
BLAST
Topological domaini398 – 4036CytoplasmicSequence Analysis
Transmembranei404 – 42421HelicalSequence AnalysisAdd
BLAST
Topological domaini425 – 48763LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33940.

Chemistry

DrugBankiDB00144. Phosphatidylserine.

Polymorphism and mutation databases

BioMutaiPTDSS2.
DMDMi49036457.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 487487Phosphatidylserine synthase 2PRO_0000056832Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161Phosphoserine7 Publications
Modified residuei24 – 241Phosphoserine1 Publication
Glycosylationi181 – 1811N-linked (GlcNAc...)1 Publication
Modified residuei485 – 4851Phosphothreonine1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9BVG9.
PaxDbiQ9BVG9.
PRIDEiQ9BVG9.

PTM databases

PhosphoSiteiQ9BVG9.

Expressioni

Gene expression databases

BgeeiQ9BVG9.
CleanExiHS_PTDSS2.
ExpressionAtlasiQ9BVG9. baseline and differential.
GenevisibleiQ9BVG9. HS.

Organism-specific databases

HPAiHPA038928.
HPA038929.

Interactioni

Protein-protein interaction databases

BioGridi123499. 3 interactions.
STRINGi9606.ENSP00000308258.

Structurei

3D structure databases

ProteinModelPortaliQ9BVG9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG264399.
GeneTreeiENSGT00530000063576.
HOGENOMiHOG000005791.
HOVERGENiHBG053766.
InParanoidiQ9BVG9.
KOiK08730.
OMAiKPHKKLG.
OrthoDBiEOG7CNZGB.
PhylomeDBiQ9BVG9.
TreeFamiTF300012.

Family and domain databases

InterProiIPR004277. PSS.
[Graphical view]
PANTHERiPTHR12615. PTHR12615. 1 hit.
PfamiPF03034. PSS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BVG9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRGERRDAG GPRPESPVPA GRASLEEPPD GPSAGQATGP GEGRRSTESE
60 70 80 90 100
VYDDGTNTFF WRAHTLTVLF ILTCTLGYVT LLEETPQDTA YNTKRGIVAS
110 120 130 140 150
ILVFLCFGVT QAKDGPFSRP HPAYWRFWLC VSVVYELFLI FILFQTVQDG
160 170 180 190 200
RQFLKYVDPK LGVPLPERDY GGNCLIYDPD NETDPFHNIW DKLDGFVPAH
210 220 230 240 250
FLGWYLKTLM IRDWWMCMII SVMFEFLEYS LEHQLPNFSE CWWDHWIMDV
260 270 280 290 300
LVCNGLGIYC GMKTLEWLSL KTYKWQGLWN IPTYKGKMKR IAFQFTPYSW
310 320 330 340 350
VRFEWKPASS LRRWLAVCGI ILVFLLAELN TFYLKFVLWM PPEHYLVLLR
360 370 380 390 400
LVFFVNVGGV AMREIYDFMD DPKPHKKLGP QAWLVAAITA TELLIVVKYD
410 420 430 440 450
PHTLTLSLPF YISQCWTLGS VLALTWTVWR FFLRDITLRY KETRWQKWQN
460 470 480
KDDQGSTVGN GDQHPLGLDE DLLGPGVAEG EGAPTPN
Length:487
Mass (Da):56,253
Last modified:June 1, 2001 - v1
Checksum:iE02508F894841A4F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL834357 mRNA. Translation: CAD39022.1.
AC137894 Genomic DNA. No translation available.
AC138230 Genomic DNA. No translation available.
BC001210 mRNA. Translation: AAH01210.1.
CCDSiCCDS7696.1.
RefSeqiNP_110410.1. NM_030783.1.
UniGeneiHs.731700.

Genome annotation databases

EnsembliENST00000308020; ENSP00000308258; ENSG00000174915.
GeneIDi81490.
KEGGihsa:81490.
UCSCiuc001lpj.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL834357 mRNA. Translation: CAD39022.1.
AC137894 Genomic DNA. No translation available.
AC138230 Genomic DNA. No translation available.
BC001210 mRNA. Translation: AAH01210.1.
CCDSiCCDS7696.1.
RefSeqiNP_110410.1. NM_030783.1.
UniGeneiHs.731700.

3D structure databases

ProteinModelPortaliQ9BVG9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123499. 3 interactions.
STRINGi9606.ENSP00000308258.

Chemistry

DrugBankiDB00144. Phosphatidylserine.

PTM databases

PhosphoSiteiQ9BVG9.

Polymorphism and mutation databases

BioMutaiPTDSS2.
DMDMi49036457.

Proteomic databases

MaxQBiQ9BVG9.
PaxDbiQ9BVG9.
PRIDEiQ9BVG9.

Protocols and materials databases

DNASUi81490.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308020; ENSP00000308258; ENSG00000174915.
GeneIDi81490.
KEGGihsa:81490.
UCSCiuc001lpj.3. human.

Organism-specific databases

CTDi81490.
GeneCardsiGC11P000440.
H-InvDBHIX0026263.
HGNCiHGNC:15463. PTDSS2.
HPAiHPA038928.
HPA038929.
MIMi612793. gene.
neXtProtiNX_Q9BVG9.
PharmGKBiPA33940.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG264399.
GeneTreeiENSGT00530000063576.
HOGENOMiHOG000005791.
HOVERGENiHBG053766.
InParanoidiQ9BVG9.
KOiK08730.
OMAiKPHKKLG.
OrthoDBiEOG7CNZGB.
PhylomeDBiQ9BVG9.
TreeFamiTF300012.

Enzyme and pathway databases

UniPathwayiUPA00948.
BioCyciMetaCyc:HS10846-MONOMER.
BRENDAi2.7.8.29. 2681.
ReactomeiREACT_120823. Synthesis of PS.

Miscellaneous databases

GenomeRNAii81490.
NextBioi71722.
PROiQ9BVG9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BVG9.
CleanExiHS_PTDSS2.
ExpressionAtlasiQ9BVG9. baseline and differential.
GenevisibleiQ9BVG9. HS.

Family and domain databases

InterProiIPR004277. PSS.
[Graphical view]
PANTHERiPTHR12615. PTHR12615. 1 hit.
PfamiPF03034. PSS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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. 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. 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. 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].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-24, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPTSS2_HUMAN
AccessioniPrimary (citable) accession number: Q9BVG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.