Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Phosphatidylserine synthase 1

Gene

PTDSS1

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. 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

    Pathway:iphosphatidylserine 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: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 Componenti: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:9587. PTDSS1.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 3535CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei36 – 5621HelicalSequence AnalysisAdd
    BLAST
    Topological domaini57 – 7216LumenalSequence AnalysisAdd
    BLAST
    Transmembranei73 – 9321HelicalSequence AnalysisAdd
    BLAST
    Topological domaini94 – 1029CytoplasmicSequence Analysis
    Transmembranei103 – 12321HelicalSequence AnalysisAdd
    BLAST
    Topological domaini124 – 18663LumenalSequence AnalysisAdd
    BLAST
    Transmembranei187 – 20721HelicalSequence AnalysisAdd
    BLAST
    Topological domaini208 – 2169CytoplasmicSequence Analysis
    Transmembranei217 – 23721HelicalSequence AnalysisAdd
    BLAST
    Topological domaini238 – 28649LumenalSequence AnalysisAdd
    BLAST
    Transmembranei287 – 30721HelicalSequence AnalysisAdd
    BLAST
    Topological domaini308 – 31912CytoplasmicSequence AnalysisAdd
    BLAST
    Transmembranei320 – 34223HelicalSequence AnalysisAdd
    BLAST
    Topological domaini343 – 35513LumenalSequence AnalysisAdd
    BLAST
    Transmembranei356 – 37621HelicalSequence AnalysisAdd
    BLAST
    Topological domaini377 – 3837CytoplasmicSequence Analysis
    Transmembranei384 – 40421HelicalSequence AnalysisAdd
    BLAST
    Topological domaini405 – 47369LumenalSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    • endoplasmic reticulum membrane Source: UniProtKB
    • integral component of membrane Source: UniProtKB-KW
    • membrane Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Lenz-Majewski hyperostotic dwarfism (LMHD)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA 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.

    See also OMIM:151050
    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.

    Chemistry

    DrugBankiDB00144. Phosphatidylserine.

    Polymorphism and mutation databases

    BioMutaiPTDSS1.
    DMDMi1346881.

    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

    BgeeiP48651.
    CleanExiHS_PTDSS1.
    ExpressionAtlasiP48651. baseline and differential.
    GenevisibleiP48651. HS.

    Organism-specific databases

    HPAiHPA016852.

    Interactioni

    Protein-protein interaction databases

    BioGridi115135. 3 interactions.
    IntActiP48651. 1 interaction.
    STRINGi9606.ENSP00000430548.

    Structurei

    3D structure databases

    ProteinModelPortaliP48651.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG264399.
    GeneTreeiENSGT00530000063576.
    HOGENOMiHOG000069882.
    HOVERGENiHBG053765.
    InParanoidiP48651.
    KOiK08729.
    OMAiHALSWCR.
    OrthoDBiEOG7CRTQC.
    PhylomeDBiP48651.
    TreeFamiTF300012.

    Family and domain databases

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

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    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

            10         20         30         40         50
    MASCVGSRTL SKDDVNYKMH FRMINEQQVE DITIDFFYRP HTITLLSFTI
    60 70 80 90 100
    VSLMYFAFTR DDSVPEDNIW RGILSVIFFF LIISVLAFPN GPFTRPHPAL
    110 120 130 140 150
    WRMVFGLSVL YFLFLVFLLF LNFEQVKSLM YWLDPNLRYA TREADVMEYA
    160 170 180 190 200
    VNCHVITWER IISHFDIFAF GHFWGWAMKA LLIRSYGLCW TISITWELTE
    210 220 230 240 250
    LFFMHLLPNF AECWWDQVIL DILLCNGGGI WLGMVVCRFL EMRTYHWASF
    260 270 280 290 300
    KDIHTTTGKI KRAVLQFTPA SWTYVRWFDP KSSFQRVAGV YLFMIIWQLT
    310 320 330 340 350
    ELNTFFLKHI FVFQASHPLS WGRILFIGGI TAPTVRQYYA YLTDTQCKRV
    360 370 380 390 400
    GTQCWVFGVI GFLEAIVCIK FGQDLFSKTQ ILYVVLWLLC VAFTTFLCLY
    410 420 430 440 450
    GMIWYAEHYG HREKTYSECE DGTYSPEISW HHRKGTKGSE DSPPKHAGNN
    460 470
    ESHSSRRRNR HSKSKVTNGV GKK
    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
    Isoform 3 (identifier: P48651-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-203: Missing.
         449-473: NNESHSSRRRNRHSKSKVTNGVGKK → EGTWGSLFEI...VAARCVEGKR

    Note: No experimental confirmation available.
    Show »
    Length:301
    Mass (Da):34,579
    Checksum:i12C03D0EEAF2DB9F
    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 – 203203Missing in isoform 3. 1 PublicationVSP_057421Add
    BLAST
    Alternative sequencei1 – 146146Missing in isoform 2. 1 PublicationVSP_055980Add
    BLAST
    Alternative sequencei449 – 47325NNESH…GVGKK → EGTWGSLFEIVSLVSHRPGR VRQIIAWGAFANVGSLLTSA LDMRSPVAARCVEGKR in isoform 3. 1 PublicationVSP_057422Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D14694 mRNA. Translation: BAA03520.1.
    AK293513 mRNA. Translation: BAG56996.1.
    AP003465 Genomic DNA. No translation available.
    KC877275 Genomic DNA. No translation available.
    BC004192 mRNA. Translation: AAH04192.1.
    BC002376 mRNA. Translation: AAH02376.2.
    BC004390 mRNA. Translation: AAH04390.1.
    CCDSiCCDS6271.1. [P48651-1]
    RefSeqiNP_001277154.1. NM_001290225.1. [P48651-2]
    NP_055569.1. NM_014754.2. [P48651-1]
    UniGeneiHs.292579.

    Genome annotation databases

    EnsembliENST00000517309; ENSP00000430548; ENSG00000156471.
    ENST00000522072; ENSP00000430928; ENSG00000156471. [P48651-3]
    GeneIDi9791.
    KEGGihsa:9791.
    UCSCiuc003yht.1. human. [P48651-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D14694 mRNA. Translation: BAA03520.1.
    AK293513 mRNA. Translation: BAG56996.1.
    AP003465 Genomic DNA. No translation available.
    KC877275 Genomic DNA. No translation available.
    BC004192 mRNA. Translation: AAH04192.1.
    BC002376 mRNA. Translation: AAH02376.2.
    BC004390 mRNA. Translation: AAH04390.1.
    CCDSiCCDS6271.1. [P48651-1]
    RefSeqiNP_001277154.1. NM_001290225.1. [P48651-2]
    NP_055569.1. NM_014754.2. [P48651-1]
    UniGeneiHs.292579.

    3D structure databases

    ProteinModelPortaliP48651.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi115135. 3 interactions.
    IntActiP48651. 1 interaction.
    STRINGi9606.ENSP00000430548.

    Chemistry

    DrugBankiDB00144. Phosphatidylserine.

    PTM databases

    PhosphoSiteiP48651.

    Polymorphism and mutation databases

    BioMutaiPTDSS1.
    DMDMi1346881.

    Proteomic databases

    MaxQBiP48651.
    PaxDbiP48651.
    PeptideAtlasiP48651.
    PRIDEiP48651.

    Protocols and materials databases

    DNASUi9791.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000517309; ENSP00000430548; ENSG00000156471.
    ENST00000522072; ENSP00000430928; ENSG00000156471. [P48651-3]
    GeneIDi9791.
    KEGGihsa:9791.
    UCSCiuc003yht.1. human. [P48651-1]

    Organism-specific databases

    CTDi9791.
    GeneCardsiGC08P097273.
    HGNCiHGNC:9587. PTDSS1.
    HPAiHPA016852.
    MIMi151050. phenotype.
    612792. gene.
    neXtProtiNX_P48651.
    Orphaneti2658. Lenz-Majewski hyperostotic dwarfism.
    PharmGKBiPA33939.
    HUGEiSearch...
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG264399.
    GeneTreeiENSGT00530000063576.
    HOGENOMiHOG000069882.
    HOVERGENiHBG053765.
    InParanoidiP48651.
    KOiK08729.
    OMAiHALSWCR.
    OrthoDBiEOG7CRTQC.
    PhylomeDBiP48651.
    TreeFamiTF300012.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSiPTDSS1. human.
    GenomeRNAii9791.
    NextBioi35471145.
    PROiP48651.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP48651.
    CleanExiHS_PTDSS1.
    ExpressionAtlasiP48651. baseline and differential.
    GenevisibleiP48651. 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. "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. "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.
      , 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Cerebellum.
    3. "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].
    4. "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.
    5. "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.
    6. "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.
    7. "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.
    8. "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.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-425, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "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.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-442, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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.
    13. "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].
    14. 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): B4DE85, E5RFC5, Q9BUQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: July 22, 2015
    This is version 121 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

    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.