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O15162

- PLS1_HUMAN

UniProt

O15162 - PLS1_HUMAN

Protein

Phospholipid scramblase 1

Gene

PLSCR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system.
    May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes. May contribute to cytokine-regulated cell proliferation and differentiation.

    Cofactori

    Calcium.

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. CD4 receptor binding Source: UniProtKB
    3. DNA binding Source: UniProtKB-KW
    4. enzyme binding Source: UniProtKB
    5. epidermal growth factor receptor binding Source: UniProtKB
    6. phospholipid scramblase activity Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: UniProtKB
    9. SH3 domain binding Source: UniProtKB

    GO - Biological processi

    1. acute-phase response Source: UniProtKB
    2. apoptotic process Source: UniProtKB
    3. defense response to virus Source: UniProtKB
    4. negative regulation of viral genome replication Source: UniProtKB
    5. phosphatidylserine biosynthetic process Source: UniProtKB
    6. phospholipid scrambling Source: UniProtKB
    7. platelet activation Source: UniProtKB
    8. positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity Source: UniProtKB
    9. positive regulation of gene expression Source: UniProtKB
    10. positive regulation of innate immune response Source: UniProtKB
    11. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    12. regulation of Fc receptor mediated stimulatory signaling pathway Source: UniProtKB
    13. regulation of mast cell activation Source: UniProtKB
    14. response to interferon-beta Source: UniProtKB

    Keywords - Biological processi

    Antiviral defense

    Keywords - Ligandi

    Calcium, DNA-binding

    Enzyme and pathway databases

    SignaLinkiO15162.

    Protein family/group databases

    TCDBi9.A.36.1.1. the ca(2+)-dependent phospholipid scramblase (scramblase) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phospholipid scramblase 1
    Short name:
    PL scramblase 1
    Alternative name(s):
    Ca(2+)-dependent phospholipid scramblase 1
    Erythrocyte phospholipid scramblase
    MmTRA1b
    Gene namesi
    Name:PLSCR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:9092. PLSCR1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. extracellular matrix Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. Golgi apparatus Source: UniProtKB
    5. integral component of plasma membrane Source: UniProtKB
    6. membrane Source: UniProtKB
    7. membrane raft Source: UniProtKB
    8. nucleolus Source: UniProtKB
    9. nucleus Source: UniProtKB
    10. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi69 – 691Y → F: Decrease in phosphorylation.
    Mutagenesisi74 – 741Y → F: Decrease in phosphorylation.
    Mutagenesisi161 – 1611T → A: No induction by PKC.
    Mutagenesisi184 – 1896CCCPCC → AAAPAA: No palmitoylation; constitutively localizes in the nucleus.
    Mutagenesisi273 – 2731D → A: Reduces the Ca(2+)-dependent phospholipid scrambling.
    Mutagenesisi275 – 2751D → A: Complete inactivation of the Ca(2+)-dependent phospholipid scrambling.
    Mutagenesisi277 – 2771F → A: Reduces the Ca(2+)-dependent phospholipid scrambling.
    Mutagenesisi279 – 2791I → A: Reduces the Ca(2+)-dependent phospholipid scrambling.
    Mutagenesisi281 – 2811F → A: Complete inactivation of the Ca(2+)-dependent phospholipid scrambling.
    Mutagenesisi284 – 2841D → A: Reduces the Ca(2+)-dependent phospholipid scrambling.

    Organism-specific databases

    PharmGKBiPA33419.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 318318Phospholipid scramblase 1PRO_0000100784Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei69 – 691Phosphotyrosine; by ABL1 Publication
    Modified residuei74 – 741Phosphotyrosine; by ABL1 Publication
    Modified residuei161 – 1611Phosphothreonine; by PKC1 Publication
    Lipidationi184 – 1841S-palmitoyl cysteineCurated
    Lipidationi185 – 1851S-palmitoyl cysteineCurated
    Lipidationi186 – 1861S-palmitoyl cysteineSequence Analysis
    Lipidationi188 – 1881S-palmitoyl cysteineCurated
    Lipidationi189 – 1891S-palmitoyl cysteineCurated

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiO15162.
    PaxDbiO15162.
    PRIDEiO15162.

    PTM databases

    PhosphoSiteiO15162.

    Expressioni

    Tissue specificityi

    Expressed in platelets, erythrocyte membranes, lymphocytes, spleen, thymus, prostate, testis, uterus, intestine, colon, heart, placenta, lung, liver, kidney and pancreas. Not detected in brain and skeletal muscle.

    Inductioni

    By phosphorylation by PKC. Induced by IFNB1/IFN-beta in response to a viral infection.1 Publication

    Gene expression databases

    ArrayExpressiO15162.
    BgeeiO15162.
    CleanExiHS_PLSCR1.
    GenevestigatoriO15162.

    Interactioni

    Subunit structurei

    Interacts with ABL.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q9WMX28EBI-740019,EBI-710918From a different organism.
    CPSF6Q166302EBI-740019,EBI-358410
    Hoxa1P090223EBI-740019,EBI-3957603From a different organism.
    NEU4Q8WWR82EBI-740019,EBI-746964
    OCLNQ166252EBI-740019,EBI-2903088
    TFGQ927342EBI-740019,EBI-357061

    Protein-protein interaction databases

    BioGridi111373. 85 interactions.
    IntActiO15162. 105 interactions.
    MINTiMINT-201602.
    STRINGi9606.ENSP00000345494.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Y2AX-ray2.20P257-266[»]
    ProteinModelPortaliO15162.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO15162.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 288288CytoplasmicAdd
    BLAST
    Topological domaini306 – 31813ExtracellularAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei289 – 30517HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 8484Proline-rich domain (PRD)Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi18 – 269SH3-binding 1Sequence Analysis
    Motifi22 – 254WW-binding 1Sequence Analysis
    Motifi33 – 364WW-binding 2Sequence Analysis
    Motifi42 – 509SH3-binding 2Sequence Analysis
    Motifi84 – 929SH3-binding 3Sequence Analysis
    Motifi257 – 26610Nuclear localization signal1 Publication

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi181 – 1899Cys-rich

    Domaini

    The N-terminal proline-rich domain (PRD) is required for phospholipid scramblase activity.

    Sequence similaritiesi

    Belongs to the phospholipid scramblase family.Curated

    Keywords - Domaini

    Repeat, SH3-binding, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG119855.
    HOGENOMiHOG000237356.
    HOVERGENiHBG019157.
    InParanoidiO15162.
    OMAiFFESTGS.
    OrthoDBiEOG77T14X.
    PhylomeDBiO15162.
    TreeFamiTF314939.

    Family and domain databases

    InterProiIPR005552. Scramblase.
    [Graphical view]
    PANTHERiPTHR23248. PTHR23248. 1 hit.
    PfamiPF03803. Scramblase. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O15162-1) [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

    MDKQNSQMNA SHPETNLPVG YPPQYPPTAF QGPPGYSGYP GPQVSYPPPP    50
    AGHSGPGPAG FPVPNQPVYN QPVYNQPVGA AGVPWMPAPQ PPLNCPPGLE 100
    YLSQIDQILI HQQIELLEVL TGFETNNKYE IKNSFGQRVY FAAEDTDCCT 150
    RNCCGPSRPF TLRIIDNMGQ EVITLERPLR CSSCCCPCCL QEIEIQAPPG 200
    VPIGYVIQTW HPCLPKFTIQ NEKREDVLKI SGPCVVCSCC GDVDFEIKSL 250
    DEQCVVGKIS KHWTGILREA FTDADNFGIQ FPLDLDVKMK AVMIGACFLI 300
    DFMFFESTGS QEQKSGVW 318
    Length:318
    Mass (Da):35,049
    Last modified:January 1, 1998 - v1
    Checksum:i9860744DEC40616E
    GO
    Isoform 2 (identifier: O15162-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-23: MDKQNSQMNASHPETNLPVGYPP → MLLTRKQTCQLGILLSIHRQHSK
         24-104: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:237
    Mass (Da):26,825
    Checksum:i61B33BDD238A5519
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti262 – 2621H → Y.
    Corresponds to variant rs343320 [ dbSNP | Ensembl ].
    VAR_034388

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2323MDKQN…VGYPP → MLLTRKQTCQLGILLSIHRQ HSK in isoform 2. 1 PublicationVSP_055237Add
    BLAST
    Alternative sequencei24 – 10481Missing in isoform 2. 1 PublicationVSP_055238Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF098642 mRNA. Translation: AAC99413.1.
    AB006746 mRNA. Translation: BAA32568.1.
    AF224492 Genomic DNA. Translation: AAF80593.1.
    AK300181 mRNA. Translation: BAG61960.1.
    AC069528 Genomic DNA. No translation available.
    AC116544 Genomic DNA. No translation available.
    AK313377 mRNA. Translation: BAG36175.1.
    CH471052 Genomic DNA. Translation: EAW78926.1.
    BC021100 mRNA. Translation: AAH21100.1.
    BC032718 mRNA. Translation: AAH32718.1.
    CCDSiCCDS3135.1. [O15162-1]
    PIRiJE0284.
    RefSeqiNP_066928.1. NM_021105.2.
    XP_005247595.1. XM_005247538.1.
    UniGeneiHs.130759.

    Genome annotation databases

    EnsembliENST00000342435; ENSP00000345494; ENSG00000188313. [O15162-1]
    ENST00000448787; ENSP00000411675; ENSG00000188313. [O15162-2]
    GeneIDi5359.
    KEGGihsa:5359.
    UCSCiuc003evx.4. human. [O15162-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Scramblase entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF098642 mRNA. Translation: AAC99413.1 .
    AB006746 mRNA. Translation: BAA32568.1 .
    AF224492 Genomic DNA. Translation: AAF80593.1 .
    AK300181 mRNA. Translation: BAG61960.1 .
    AC069528 Genomic DNA. No translation available.
    AC116544 Genomic DNA. No translation available.
    AK313377 mRNA. Translation: BAG36175.1 .
    CH471052 Genomic DNA. Translation: EAW78926.1 .
    BC021100 mRNA. Translation: AAH21100.1 .
    BC032718 mRNA. Translation: AAH32718.1 .
    CCDSi CCDS3135.1. [O15162-1 ]
    PIRi JE0284.
    RefSeqi NP_066928.1. NM_021105.2.
    XP_005247595.1. XM_005247538.1.
    UniGenei Hs.130759.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Y2A X-ray 2.20 P 257-266 [» ]
    ProteinModelPortali O15162.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111373. 85 interactions.
    IntActi O15162. 105 interactions.
    MINTi MINT-201602.
    STRINGi 9606.ENSP00000345494.

    Protein family/group databases

    TCDBi 9.A.36.1.1. the ca(2+)-dependent phospholipid scramblase (scramblase) family.

    PTM databases

    PhosphoSitei O15162.

    Proteomic databases

    MaxQBi O15162.
    PaxDbi O15162.
    PRIDEi O15162.

    Protocols and materials databases

    DNASUi 5359.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000342435 ; ENSP00000345494 ; ENSG00000188313 . [O15162-1 ]
    ENST00000448787 ; ENSP00000411675 ; ENSG00000188313 . [O15162-2 ]
    GeneIDi 5359.
    KEGGi hsa:5359.
    UCSCi uc003evx.4. human. [O15162-1 ]

    Organism-specific databases

    CTDi 5359.
    GeneCardsi GC03M146232.
    HGNCi HGNC:9092. PLSCR1.
    MIMi 604170. gene.
    neXtProti NX_O15162.
    PharmGKBi PA33419.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG119855.
    HOGENOMi HOG000237356.
    HOVERGENi HBG019157.
    InParanoidi O15162.
    OMAi FFESTGS.
    OrthoDBi EOG77T14X.
    PhylomeDBi O15162.
    TreeFami TF314939.

    Enzyme and pathway databases

    SignaLinki O15162.

    Miscellaneous databases

    ChiTaRSi PLSCR1. human.
    EvolutionaryTracei O15162.
    GeneWikii PLSCR1.
    GenomeRNAii 5359.
    NextBioi 20774.
    PROi O15162.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15162.
    Bgeei O15162.
    CleanExi HS_PLSCR1.
    Genevestigatori O15162.

    Family and domain databases

    InterProi IPR005552. Scramblase.
    [Graphical view ]
    PANTHERi PTHR23248. PTHR23248. 1 hit.
    Pfami PF03803. Scramblase. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of human plasma membrane phospholipid scramblase. A protein mediating transbilayer movement of plasma membrane phospholipids."
      Zhou Q., Zhao J., Stout J.G., Luhm R.A., Wiedmer T., Sims P.J.
      J. Biol. Chem. 272:18240-18244(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 87-118.
      Tissue: Erythrocyte.
    2. "Identity of human normal counterpart (MmTRA1b) of mouse leukemogenesis-associated gene (MmTRA1a) product as plasma membrane phospholipid scramblase and chromosome mapping of the human MmTRA1b/phospholipid scramblase gene."
      Kasukabe T., Kobayashi H., Kaneko Y., Okabe-Kado J., Honma Y.
      Biochem. Biophys. Res. Commun. 249:449-455(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Monocytic leukemia.
    3. "Identification of three new members of the phospholipid scramblase gene family."
      Wiedmer T., Zhou Q., Kwoh D.Y., Sims P.J.
      Biochim. Biophys. Acta 1467:244-253(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "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] (ISOFORMS 1 AND 2).
      Tissue: Kidney and Placenta.
    5. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Colon and Uterus.
    8. "Isolation of an erythrocyte membrane protein that mediates Ca2+-dependent transbilayer movement of phospholipid."
      Basse F., Stout J.G., Sims P.J., Wiedmer T.
      J. Biol. Chem. 271:17205-17210(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, FUNCTION.
      Tissue: Erythrocyte.
    9. "Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase Cdelta."
      Frasch S.C., Henson P.M., Kailey J.M., Richter D.A., Janes M.S., Fadok V.A., Bratton D.L.
      J. Biol. Chem. 275:23065-23073(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-161, MUTAGENESIS.
    10. "c-Abl tyrosine kinase binds and phosphorylates phospholipid scramblase 1."
      Sun J., Zhao J., Schwartz M.A., Wang J.Y., Wiedmer T., Sims P.J.
      J. Biol. Chem. 276:28984-28990(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-69 AND TYR-74, MUTAGENESIS.
    11. "Palmitoylation of phospholipid scramblase is required for normal function in promoting Ca2+-activated transbilayer movement of membrane phospholipids."
      Zhao J., Zhou Q., Wiedmer T., Sims P.J.
      Biochemistry 37:6361-6366(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION.
    12. "Identity of a conserved motif in phospholipid scramblase that is required for Ca2+-accelerated transbilayer movement of membrane phospholipids."
      Zhou Q., Sims P.J., Wiedmer T.
      Biochemistry 37:2356-2360(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS.
    13. "Palmitoylation of phospholipid scramblase 1 controls its distribution between nucleus and plasma membrane."
      Wiedmer T., Zhao J., Nanjundan M., Sims P.J.
      Biochemistry 42:1227-1233(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PALMITOYLATION, MUTAGENESIS OF 184-CYS--CYS-189.
    14. Cited for: FUNCTION, INDUCTION.
    15. "Phospholipid scramblase 1 binds to the promoter region of the inositol 1,4,5-triphosphate receptor type 1 gene to enhance its expression."
      Zhou Q., Ben-Efraim I., Bigcas J.L., Junqueira D., Wiedmer T., Sims P.J.
      J. Biol. Chem. 280:35062-35068(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, DNA-BINDING.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "N-terminal proline-rich domain is required for scrambling activity of human phospholipid scramblases."
      Rayala S., Francis V.G., Sivagnanam U., Gummadi S.N.
      J. Biol. Chem. 289:13206-13218(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PROLINE-RICH DOMAIN, SUBCELLULAR LOCATION.
    18. "Phospholipid scramblase 1 contains a nonclassical nuclear localization signal with unique binding site in importin alpha."
      Chen M.H., Ben-Efraim I., Mitrousis G., Walker-Kopp N., Sims P.J., Cingolani G.
      J. Biol. Chem. 280:10599-10606(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 257-266 IN COMPLEX WITH MOUSE KPNA2, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF 184-CYS--CYS-189.

    Entry informationi

    Entry nameiPLS1_HUMAN
    AccessioniPrimary (citable) accession number: O15162
    Secondary accession number(s): B2R8H8, B4DTE8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 142 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3