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P48651

- PTSS1_HUMAN

UniProt

P48651 - PTSS1_HUMAN

Protein

Phosphatidylserine synthase 1

Gene

PTDSS1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. In membranes, PTDSS1 catalyzes mainly the conversion of phosphatidylcholine. Also converts, in vitro and to a lesser extent, phosphatidylethanolamine.

    Catalytic activityi

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

    Enzyme regulationi

    Requires calcium ions. Activated by exogenous phosphatidylethanolamine.2 Publications

    Kineticsi

    1. KM=67 µM for serine (in the presence of 2 mM PC)1 Publication
    2. KM=24 µM for serine (in the presence of 1 mM PE)1 Publication

    pH dependencei

    Optimum pH for both PC and PE is between 7.0 and 7.5.1 Publication

    Pathwayi

    GO - Molecular functioni

    1. transferase activity Source: UniProtKB-KW

    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

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:HS08129-MONOMER.
    ReactomeiREACT_120823. Synthesis of PS.
    UniPathwayiUPA00948.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylserine synthase 1 (EC:2.7.8.29)
    Short name:
    PSS-1
    Short name:
    PtdSer synthase 1
    Alternative name(s):
    Serine-exchange enzyme I
    Gene namesi
    Name:PTDSS1
    Synonyms:KIAA0024, PSSA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:9587. PTDSS1.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Lenz-Majewski hyperostotic dwarfism (LMHD) [MIM:151050]: A syndrome of intellectual disability and multiple congenital anomalies that features generalized craniotubular hyperostosis. LMHD is characterized by the combination of sclerosing bone dysplasia, intellectual disability and distinct craniofacial, dental, cutaneous and distal limb anomalies. The progressive generalized hyperostosis associated with this syndrome affects the cranium, the vertebrae and the diaphyses of tubular bones, leading to severe growth restriction.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti265 – 2651L → P in LMHD; does not affect protein levels; increases the rate of phosphatidylserine synthesis; profoundly impairs negative feedback enzyme regulation by phosphatidylserine. 1 Publication
    VAR_070987
    Natural varianti269 – 2691P → S in LMHD; does not affect protein levels; increases the rate of phosphatidylserine synthesis; profoundly impairs negative feedback enzyme regulation by phosphatidylserine. 1 Publication
    VAR_070988
    Natural varianti353 – 3531Q → R in LMHD; does not affect protein levels; increases the rate of phosphatidylserine synthesis; profoundly impairs negative feedback enzyme regulation by phosphatidylserine. 1 Publication
    VAR_070989

    Keywords - Diseasei

    Disease mutation, Dwarfism, Mental retardation

    Organism-specific databases

    MIMi151050. phenotype.
    Orphaneti2658. Lenz-Majewski hyperostotic dwarfism.
    PharmGKBiPA33939.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 473473Phosphatidylserine synthase 1PRO_0000056829Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei417 – 4171Phosphoserine1 Publication
    Modified residuei425 – 4251Phosphoserine1 Publication
    Modified residuei442 – 4421Phosphoserine3 Publications
    Modified residuei454 – 4541Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP48651.
    PaxDbiP48651.
    PeptideAtlasiP48651.
    PRIDEiP48651.

    PTM databases

    PhosphoSiteiP48651.

    Expressioni

    Gene expression databases

    ArrayExpressiP48651.
    BgeeiP48651.
    CleanExiHS_PTDSS1.
    GenevestigatoriP48651.

    Organism-specific databases

    HPAiHPA016852.

    Interactioni

    Protein-protein interaction databases

    BioGridi115135. 3 interactions.
    IntActiP48651. 1 interaction.
    STRINGi9606.ENSP00000337331.

    Structurei

    3D structure databases

    ProteinModelPortaliP48651.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3535CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini57 – 7216LumenalSequence AnalysisAdd
    BLAST
    Topological domaini94 – 1029CytoplasmicSequence Analysis
    Topological domaini124 – 18663LumenalSequence AnalysisAdd
    BLAST
    Topological domaini208 – 2169CytoplasmicSequence Analysis
    Topological domaini238 – 28649LumenalSequence AnalysisAdd
    BLAST
    Topological domaini308 – 31912CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini343 – 35513LumenalSequence AnalysisAdd
    BLAST
    Topological domaini377 – 3837CytoplasmicSequence Analysis
    Topological domaini405 – 47369LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei36 – 5621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei73 – 9321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei103 – 12321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei187 – 20721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei217 – 23721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei287 – 30721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei320 – 34223HelicalSequence AnalysisAdd
    BLAST
    Transmembranei356 – 37621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei384 – 40421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG264399.
    HOVERGENiHBG053765.
    InParanoidiP48651.
    KOiK08729.
    OMAiSGNNESH.
    OrthoDBiEOG7CRTQC.
    PhylomeDBiP48651.
    TreeFamiTF300012.

    Family and domain databases

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

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P48651-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASCVGSRTL SKDDVNYKMH FRMINEQQVE DITIDFFYRP HTITLLSFTI    50
    VSLMYFAFTR DDSVPEDNIW RGILSVIFFF LIISVLAFPN GPFTRPHPAL 100
    WRMVFGLSVL YFLFLVFLLF LNFEQVKSLM YWLDPNLRYA TREADVMEYA 150
    VNCHVITWER IISHFDIFAF GHFWGWAMKA LLIRSYGLCW TISITWELTE 200
    LFFMHLLPNF AECWWDQVIL DILLCNGGGI WLGMVVCRFL EMRTYHWASF 250
    KDIHTTTGKI KRAVLQFTPA SWTYVRWFDP KSSFQRVAGV YLFMIIWQLT 300
    ELNTFFLKHI FVFQASHPLS WGRILFIGGI TAPTVRQYYA YLTDTQCKRV 350
    GTQCWVFGVI GFLEAIVCIK FGQDLFSKTQ ILYVVLWLLC VAFTTFLCLY 400
    GMIWYAEHYG HREKTYSECE DGTYSPEISW HHRKGTKGSE DSPPKHAGNN 450
    ESHSSRRRNR HSKSKVTNGV GKK 473
    Length:473
    Mass (Da):55,528
    Last modified:February 1, 1996 - v1
    Checksum:iCFC8F50A33CE038D
    GO
    Isoform 2 (identifier: P48651-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-146: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:327
    Mass (Da):38,273
    Checksum:i6F14EC0246926405
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti265 – 2651L → P in LMHD; does not affect protein levels; increases the rate of phosphatidylserine synthesis; profoundly impairs negative feedback enzyme regulation by phosphatidylserine. 1 Publication
    VAR_070987
    Natural varianti269 – 2691P → S in LMHD; does not affect protein levels; increases the rate of phosphatidylserine synthesis; profoundly impairs negative feedback enzyme regulation by phosphatidylserine. 1 Publication
    VAR_070988
    Natural varianti353 – 3531Q → R in LMHD; does not affect protein levels; increases the rate of phosphatidylserine synthesis; profoundly impairs negative feedback enzyme regulation by phosphatidylserine. 1 Publication
    VAR_070989
    Natural varianti423 – 4231T → N.
    Corresponds to variant rs7835798 [ dbSNP | Ensembl ].
    VAR_048735

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 146146Missing in isoform 2. 1 PublicationVSP_055980Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14694 mRNA. Translation: BAA03520.1.
    AP003465 Genomic DNA. No translation available.
    BC004192 mRNA. Translation: AAH04192.1.
    BC002376 mRNA. Translation: AAH02376.2.
    BC004390 mRNA. Translation: AAH04390.1.
    CCDSiCCDS6271.1.
    RefSeqiNP_001277154.1. NM_001290225.1.
    NP_055569.1. NM_014754.2.
    UniGeneiHs.292579.

    Genome annotation databases

    EnsembliENST00000455950; ENSP00000401248; ENSG00000156471.
    ENST00000517309; ENSP00000430548; ENSG00000156471.
    GeneIDi9791.
    KEGGihsa:9791.
    UCSCiuc003yht.1. human.

    Polymorphism databases

    DMDMi1346881.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D14694 mRNA. Translation: BAA03520.1 .
    AP003465 Genomic DNA. No translation available.
    BC004192 mRNA. Translation: AAH04192.1 .
    BC002376 mRNA. Translation: AAH02376.2 .
    BC004390 mRNA. Translation: AAH04390.1 .
    CCDSi CCDS6271.1.
    RefSeqi NP_001277154.1. NM_001290225.1.
    NP_055569.1. NM_014754.2.
    UniGenei Hs.292579.

    3D structure databases

    ProteinModelPortali P48651.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115135. 3 interactions.
    IntActi P48651. 1 interaction.
    STRINGi 9606.ENSP00000337331.

    Chemistry

    DrugBanki DB00144. Phosphatidylserine.

    PTM databases

    PhosphoSitei P48651.

    Polymorphism databases

    DMDMi 1346881.

    Proteomic databases

    MaxQBi P48651.
    PaxDbi P48651.
    PeptideAtlasi P48651.
    PRIDEi P48651.

    Protocols and materials databases

    DNASUi 9791.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000455950 ; ENSP00000401248 ; ENSG00000156471 .
    ENST00000517309 ; ENSP00000430548 ; ENSG00000156471 .
    GeneIDi 9791.
    KEGGi hsa:9791.
    UCSCi uc003yht.1. human.

    Organism-specific databases

    CTDi 9791.
    GeneCardsi GC08P097343.
    HGNCi HGNC:9587. PTDSS1.
    HPAi HPA016852.
    MIMi 151050. phenotype.
    612792. gene.
    neXtProti NX_P48651.
    Orphaneti 2658. Lenz-Majewski hyperostotic dwarfism.
    PharmGKBi PA33939.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG264399.
    HOVERGENi HBG053765.
    InParanoidi P48651.
    KOi K08729.
    OMAi SGNNESH.
    OrthoDBi EOG7CRTQC.
    PhylomeDBi P48651.
    TreeFami TF300012.

    Enzyme and pathway databases

    UniPathwayi UPA00948 .
    BioCyci MetaCyc:HS08129-MONOMER.
    Reactomei REACT_120823. Synthesis of PS.

    Miscellaneous databases

    GenomeRNAii 9791.
    NextBioi 36870.
    PROi P48651.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P48651.
    Bgeei P48651.
    CleanExi HS_PTDSS1.
    Genevestigatori P48651.

    Family and domain databases

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

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1."
      Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y., Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.
      DNA Res. 1:27-35(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    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] (ISOFORMS 1 AND 2).
      Tissue: Brain, Lymph and Muscle.
    4. "Control of phosphatidylserine biosynthesis through phosphatidylserine-mediated inhibition of phosphatidylserine synthase I in Chinese hamster ovary cells."
      Kuge O., Hasegawa K., Saito K., Nishijima M.
      Proc. Natl. Acad. Sci. U.S.A. 95:4199-4203(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    5. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-425, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, 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-442 AND SER-454, 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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: VARIANTS LMHD PRO-265; SER-269 AND ARG-353, CHARACTERIZATION OF VARIANTS LMHD PRO-265; SER-269 AND ARG-353.

    Entry informationi

    Entry nameiPTSS1_HUMAN
    AccessioniPrimary (citable) accession number: P48651
    Secondary accession number(s): E5RFC5, Q9BUQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 112 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 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3