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Q9BVG9

- PTSS2_HUMAN

UniProt

Q9BVG9 - PTSS2_HUMAN

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Protein
Phosphatidylserine synthase 2
Gene
PTDSS2, PSS2
Organism
Homo sapiens (Human)
Status
Reviewed - 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

Vmax=0.57 mmol/h/mg enzyme

pH dependencei

Optimum pH is around 7.5.

Pathwayi

GO - Molecular functioni

  1. CDP-diacylglycerol-serine O-phosphatidyltransferase activity Source: Ensembl
Complete GO annotation...

GO - Biological processi

  1. glycerophospholipid biosynthetic process Source: Reactome
  2. phosphatidylserine biosynthetic process Source: Reactome
  3. phospholipid metabolic process Source: Reactome
  4. small molecule metabolic process Source: Reactome
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.
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: Chromosome 11

Organism-specific databases

HGNCiHGNC:15463. PTDSS2.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6262Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei63 – 8321Helical; Reviewed prediction
Add
BLAST
Topological domaini84 – 9613Lumenal Reviewed prediction
Add
BLAST
Transmembranei97 – 11721Helical; Reviewed prediction
Add
BLAST
Topological domaini118 – 1269Cytoplasmic Reviewed prediction
Transmembranei127 – 14721Helical; Reviewed prediction
Add
BLAST
Topological domaini148 – 313166Lumenal Reviewed prediction
Add
BLAST
Transmembranei314 – 33421Helical; Reviewed prediction
Add
BLAST
Topological domaini335 – 3351Cytoplasmic Reviewed prediction
Transmembranei336 – 35621Helical; Reviewed prediction
Add
BLAST
Topological domaini357 – 37620Lumenal Reviewed prediction
Add
BLAST
Transmembranei377 – 39721Helical; Reviewed prediction
Add
BLAST
Topological domaini398 – 4036Cytoplasmic Reviewed prediction
Transmembranei404 – 42421Helical; Reviewed prediction
Add
BLAST
Topological domaini425 – 48763Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
  3. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33940.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161Phosphoserine6 Publications
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

ArrayExpressiQ9BVG9.
BgeeiQ9BVG9.
CleanExiHS_PTDSS2.
GenevestigatoriQ9BVG9.

Organism-specific databases

HPAiHPA038928.
HPA038929.

Interactioni

Protein-protein interaction databases

BioGridi123499. 3 interactions.
STRINGi9606.ENSP00000308258.

Structurei

3D structure databases

ProteinModelPortaliQ9BVG9.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG264399.
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

MRRGERRDAG GPRPESPVPA GRASLEEPPD GPSAGQATGP GEGRRSTESE    50
VYDDGTNTFF WRAHTLTVLF ILTCTLGYVT LLEETPQDTA YNTKRGIVAS 100
ILVFLCFGVT QAKDGPFSRP HPAYWRFWLC VSVVYELFLI FILFQTVQDG 150
RQFLKYVDPK LGVPLPERDY GGNCLIYDPD NETDPFHNIW DKLDGFVPAH 200
FLGWYLKTLM IRDWWMCMII SVMFEFLEYS LEHQLPNFSE CWWDHWIMDV 250
LVCNGLGIYC GMKTLEWLSL KTYKWQGLWN IPTYKGKMKR IAFQFTPYSW 300
VRFEWKPASS LRRWLAVCGI ILVFLLAELN TFYLKFVLWM PPEHYLVLLR 350
LVFFVNVGGV AMREIYDFMD DPKPHKKLGP QAWLVAAITA TELLIVVKYD 400
PHTLTLSLPF YISQCWTLGS VLALTWTVWR FFLRDITLRY KETRWQKWQN 450
KDDQGSTVGN GDQHPLGLDE DLLGPGVAEG EGAPTPN 487
Length:487
Mass (Da):56,253
Last modified:June 1, 2001 - v1
Checksum:iE02508F894841A4F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Polymorphism databases

DMDMi49036457.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL834357 mRNA. Translation: CAD39022.1 .
AC137894 Genomic DNA. No translation available.
AC138230 Genomic DNA. No translation available.
BC001210 mRNA. Translation: AAH01210.1 .
CCDSi CCDS7696.1.
RefSeqi NP_110410.1. NM_030783.1.
UniGenei Hs.731700.

3D structure databases

ProteinModelPortali Q9BVG9.
ModBasei Search...

Protein-protein interaction databases

BioGridi 123499. 3 interactions.
STRINGi 9606.ENSP00000308258.

Chemistry

DrugBanki DB00144. Phosphatidylserine.

PTM databases

PhosphoSitei Q9BVG9.

Polymorphism databases

DMDMi 49036457.

Proteomic databases

MaxQBi Q9BVG9.
PaxDbi Q9BVG9.
PRIDEi Q9BVG9.

Protocols and materials databases

DNASUi 81490.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000308020 ; ENSP00000308258 ; ENSG00000174915 .
GeneIDi 81490.
KEGGi hsa:81490.
UCSCi uc001lpj.3. human.

Organism-specific databases

CTDi 81490.
GeneCardsi GC11P000440.
H-InvDB HIX0026263.
HGNCi HGNC:15463. PTDSS2.
HPAi HPA038928.
HPA038929.
MIMi 612793. gene.
neXtProti NX_Q9BVG9.
PharmGKBi PA33940.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG264399.
HOGENOMi HOG000005791.
HOVERGENi HBG053766.
InParanoidi Q9BVG9.
KOi K08730.
OMAi KPHKKLG.
OrthoDBi EOG7CNZGB.
PhylomeDBi Q9BVG9.
TreeFami TF300012.

Enzyme and pathway databases

UniPathwayi UPA00948 .
BioCyci MetaCyc:HS10846-MONOMER.
Reactomei REACT_120823. Synthesis of PS.

Miscellaneous databases

GenomeRNAii 81490.
NextBioi 71722.
PROi Q9BVG9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9BVG9.
Bgeei Q9BVG9.
CleanExi HS_PTDSS2.
Genevestigatori Q9BVG9.

Family and domain databases

InterProi IPR004277. PSS.
[Graphical view ]
PANTHERi PTHR12615. PTHR12615. 1 hit.
Pfami PF03034. PSS. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].

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: September 3, 2014
This is version 96 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

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