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Protein

Phospholipid scramblase 1

Gene

PLSCR1

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

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

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. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: UniProtKB
  8. 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
Complete GO annotation...

Keywords - Biological processi

Antiviral defense

Keywords - Ligandi

Calcium, DNA-binding

Enzyme and pathway databases

BRENDAi3.6.99.B1. 2681.
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 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:9092. PLSCR1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 288288CytoplasmicAdd
BLAST
Transmembranei289 – 30517HelicalSequence AnalysisAdd
BLAST
Topological domaini306 – 31813ExtracellularAdd
BLAST

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extracellular matrix Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  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
Complete GO annotation...

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. 2 Publications
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.

Polymorphism and mutation databases

BioMutaiPLSCR1.

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

BgeeiO15162.
CleanExiHS_PLSCR1.
ExpressionAtlasiO15162. baseline and differential.
GenevestigatoriO15162.

Interactioni

Subunit structurei

Interacts with ABL.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9WMX28EBI-740019,EBI-710918From a different organism.
BCL6BA8KA133EBI-740019,EBI-10174813
CATSPER1Q8NEC53EBI-740019,EBI-744545
CHRDQ9H2X03EBI-740019,EBI-947551
CPSF6Q166302EBI-740019,EBI-358410
CTSZQ9UBR23EBI-740019,EBI-8636823
DAZAP2Q150384EBI-740019,EBI-724310
DEF6Q9H4E73EBI-740019,EBI-745369
DMRT3Q9NQL93EBI-740019,EBI-9679045
DOCK2Q926083EBI-740019,EBI-448771
ESR2Q927313EBI-740019,EBI-78505
EWSR1Q018444EBI-740019,EBI-739737
FRS3O435593EBI-740019,EBI-725515
GDPD5Q9HBR33EBI-740019,EBI-10310206
GLRX3O760034EBI-740019,EBI-374781
Hoxa1P090223EBI-740019,EBI-3957603From a different organism.
ILF3Q9NXX04EBI-740019,EBI-743980
KRTAP10-11P604123EBI-740019,EBI-10217483
KRTAP10-9P604113EBI-740019,EBI-10172052
KRTAP4-11Q9BYQ63EBI-740019,EBI-10302392
KRTAP4-2Q9BYR53EBI-740019,EBI-10172511
KRTAP5-6Q6L8G93EBI-740019,EBI-10250562
KRTAP9-2Q9BYQ43EBI-740019,EBI-1044640
LCE2DQ5TA823EBI-740019,EBI-10246750
LCE4AQ5TA783EBI-740019,EBI-10246358
LGALS9CQ6DKI23EBI-740019,EBI-9088829
NEU4Q8WWR82EBI-740019,EBI-746964
OCLNQ166252EBI-740019,EBI-2903088
P2RY6Q150773EBI-740019,EBI-10235794
PKD2Q135633EBI-740019,EBI-7813714
PRR13Q9NZ813EBI-740019,EBI-740924
RGS3P497963EBI-740019,EBI-2107809
SCNM1Q9BWG63EBI-740019,EBI-748391
SMARCC1Q929223EBI-740019,EBI-355653
SPATA8Q6RVD63EBI-740019,EBI-8635958
STK16O757163EBI-740019,EBI-749295
TFGQ927342EBI-740019,EBI-357061
TRIM42Q8IWZ53EBI-740019,EBI-5235829
VPS37CA5D8V63EBI-740019,EBI-2559305
ZNF417Q8TAU33EBI-740019,EBI-740727
ZNF587Q96SQ53EBI-740019,EBI-6427977

Protein-protein interaction databases

BioGridi111373. 130 interactions.
IntActiO15162. 137 interactions.
MINTiMINT-201602.
STRINGi9606.ENSP00000345494.

Structurei

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO15162.

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.
GeneTreeiENSGT00390000002884.
HOGENOMiHOG000237356.
HOVERGENiHBG019157.
InParanoidiO15162.
OMAiCVVGKIS.
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. AlignAdd to basket

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

        10         20         30         40         50
MDKQNSQMNA SHPETNLPVG YPPQYPPTAF QGPPGYSGYP GPQVSYPPPP
60 70 80 90 100
AGHSGPGPAG FPVPNQPVYN QPVYNQPVGA AGVPWMPAPQ PPLNCPPGLE
110 120 130 140 150
YLSQIDQILI HQQIELLEVL TGFETNNKYE IKNSFGQRVY FAAEDTDCCT
160 170 180 190 200
RNCCGPSRPF TLRIIDNMGQ EVITLERPLR CSSCCCPCCL QEIEIQAPPG
210 220 230 240 250
VPIGYVIQTW HPCLPKFTIQ NEKREDVLKI SGPCVVCSCC GDVDFEIKSL
260 270 280 290 300
DEQCVVGKIS KHWTGILREA FTDADNFGIQ FPLDLDVKMK AVMIGACFLI
310
DFMFFESTGS QEQKSGVW
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:
EMBLi
GenBanki
DDBJi
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. [O15162-1]
XP_005247595.1. XM_005247538.2. [O15162-2]
UniGeneiHs.130759.

Genome annotation databases

EnsembliENST00000342435; ENSP00000345494; ENSG00000188313. [O15162-1]
ENST00000448787; ENSP00000411675; ENSG00000188313. [O15162-2]
GeneIDi5359.
KEGGihsa:5359.
UCSCiuc003evx.4. human. [O15162-1]
uc011bnn.2. human.

Polymorphism and mutation databases

BioMutaiPLSCR1.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Scramblase entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [O15162-1]
XP_005247595.1. XM_005247538.2. [O15162-2]
UniGeneiHs.130759.

3D structure databases

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

Protein-protein interaction databases

BioGridi111373. 130 interactions.
IntActiO15162. 137 interactions.
MINTiMINT-201602.
STRINGi9606.ENSP00000345494.

Protein family/group databases

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

PTM databases

PhosphoSiteiO15162.

Polymorphism and mutation databases

BioMutaiPLSCR1.

Proteomic databases

MaxQBiO15162.
PaxDbiO15162.
PRIDEiO15162.

Protocols and materials databases

DNASUi5359.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000342435; ENSP00000345494; ENSG00000188313. [O15162-1]
ENST00000448787; ENSP00000411675; ENSG00000188313. [O15162-2]
GeneIDi5359.
KEGGihsa:5359.
UCSCiuc003evx.4. human. [O15162-1]
uc011bnn.2. human.

Organism-specific databases

CTDi5359.
GeneCardsiGC03M146232.
HGNCiHGNC:9092. PLSCR1.
MIMi604170. gene.
neXtProtiNX_O15162.
PharmGKBiPA33419.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG119855.
GeneTreeiENSGT00390000002884.
HOGENOMiHOG000237356.
HOVERGENiHBG019157.
InParanoidiO15162.
OMAiCVVGKIS.
OrthoDBiEOG77T14X.
PhylomeDBiO15162.
TreeFamiTF314939.

Enzyme and pathway databases

BRENDAi3.6.99.B1. 2681.
SignaLinkiO15162.

Miscellaneous databases

ChiTaRSiPLSCR1. human.
EvolutionaryTraceiO15162.
GeneWikiiPLSCR1.
GenomeRNAii5359.
NextBioi20774.
PROiO15162.
SOURCEiSearch...

Gene expression databases

BgeeiO15162.
CleanExiHS_PLSCR1.
ExpressionAtlasiO15162. baseline and differential.
GenevestigatoriO15162.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "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: April 29, 2015
This is version 149 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

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.