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O15162 (PLS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phospholipid scramblase 1

Short name=PL scramblase 1
Alternative name(s):
Ca(2+)-dependent phospholipid scramblase 1
Erythrocyte phospholipid scramblase
MmTRA1b
Gene names
Name:PLSCR1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length318 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.14 Ref.17

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. Ref.8 Ref.14 Ref.17

Cofactor

Calcium.

Subunit structure

Interacts with ABL.

Subcellular location

Cell membrane; Single-pass type II membrane protein. Membrane; Lipid-anchor; Cytoplasmic side. Nucleus Ref.13 Ref.15 Ref.17.

Tissue specificity

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.

Induction

By phosphorylation by PKC. Induced by IFNB1/IFN-beta in response to a viral infection. Ref.14

Domain

The N-terminal proline-rich domain (PRD) is required for phospholipid scramblase activity. Ref.17

Sequence similarities

Belongs to the phospholipid scramblase family.

Ontologies

Keywords
   Biological processAntiviral defense
   Cellular componentCell membrane
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
SH3-binding
Transmembrane
Transmembrane helix
   LigandCalcium
DNA-binding
   PTMLipoprotein
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processacute-phase response

Inferred from sequence or structural similarity. Source: UniProtKB

apoptotic process

Inferred from direct assay Ref.9. Source: UniProtKB

defense response to virus

Inferred from mutant phenotype Ref.14. Source: UniProtKB

negative regulation of viral genome replication

Inferred from mutant phenotype Ref.14. Source: UniProtKB

phosphatidylserine biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

phospholipid scrambling

Inferred from direct assay Ref.9PubMed 18629440Ref.1. Source: UniProtKB

platelet activation

Non-traceable author statement Ref.1. Source: UniProtKB

positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity

Inferred from direct assay PubMed 17567603. Source: UniProtKB

positive regulation of gene expression

Inferred from mutant phenotype Ref.14. Source: UniProtKB

positive regulation of innate immune response

Inferred from mutant phenotype Ref.14. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.15. Source: UniProtKB

regulation of Fc receptor mediated stimulatory signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of mast cell activation

Inferred from sequence or structural similarity. Source: UniProtKB

response to interferon-beta

Inferred from mutant phenotype Ref.14. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 12586838. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 17712045. Source: UniProtKB

extracellular matrix

Inferred from direct assay PubMed 20870722. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 23376485. Source: UniProt

integral component of plasma membrane

Inferred from direct assay PubMed 12586838Ref.1. Source: UniProtKB

membrane raft

Inferred from direct assay PubMed 12009895. Source: UniProtKB

nucleolus

Inferred from direct assay PubMed 17567603. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 20870722. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 17712045PubMed 19333378PubMed 20870722. Source: UniProtKB

   Molecular_functionCD4 receptor binding

Inferred from physical interaction PubMed 19333378. Source: UniProtKB

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay Ref.15. Source: UniProtKB

SH3 domain binding

Inferred from direct assay Ref.10. Source: UniProtKB

calcium ion binding

Inferred from direct assay PubMed 18629440. Source: UniProtKB

enzyme binding

Inferred from physical interaction PubMed 12586838PubMed 17567603PubMed 17712045. Source: UniProtKB

epidermal growth factor receptor binding

Inferred from physical interaction PubMed 12009895. Source: UniProtKB

phospholipid scramblase activity

Inferred from direct assay Ref.9PubMed 18629440Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 19333378PubMed 20870722. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O15162-1)

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.
Isoform 2 (identifier: O15162-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-23: MDKQNSQMNASHPETNLPVGYPP → MLLTRKQTCQLGILLSIHRQHSK
     24-104: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 318318Phospholipid scramblase 1
PRO_0000100784

Regions

Topological domain1 – 288288Cytoplasmic
Transmembrane289 – 30517Helical; Potential
Topological domain306 – 31813Extracellular
Region1 – 8484Proline-rich domain (PRD)
Motif18 – 269SH3-binding 1 Potential
Motif22 – 254WW-binding 1 Potential
Motif33 – 364WW-binding 2 Potential
Motif42 – 509SH3-binding 2 Potential
Motif84 – 929SH3-binding 3 Potential
Motif257 – 26610Nuclear localization signal Ref.18
Compositional bias181 – 1899Cys-rich

Amino acid modifications

Modified residue691Phosphotyrosine; by ABL Ref.10
Modified residue741Phosphotyrosine; by ABL Ref.10
Modified residue1611Phosphothreonine; by PKC Ref.9
Lipidation1841S-palmitoyl cysteine Probable
Lipidation1851S-palmitoyl cysteine Probable
Lipidation1861S-palmitoyl cysteine Potential
Lipidation1881S-palmitoyl cysteine Probable
Lipidation1891S-palmitoyl cysteine Probable

Natural variations

Alternative sequence1 – 2323MDKQN…VGYPP → MLLTRKQTCQLGILLSIHRQ HSK in isoform 2.
VSP_055237
Alternative sequence24 – 10481Missing in isoform 2.
VSP_055238
Natural variant2621H → Y.
Corresponds to variant rs343320 [ dbSNP | Ensembl ].
VAR_034388

Experimental info

Mutagenesis691Y → F: Decrease in phosphorylation.
Mutagenesis741Y → F: Decrease in phosphorylation.
Mutagenesis1611T → A: No induction by PKC.
Mutagenesis184 – 1896CCCPCC → AAAPAA: No palmitoylation; constitutively localizes in the nucleus. Ref.13 Ref.18
Mutagenesis2731D → A: Reduces the Ca(2+)-dependent phospholipid scrambling.
Mutagenesis2751D → A: Complete inactivation of the Ca(2+)-dependent phospholipid scrambling.
Mutagenesis2771F → A: Reduces the Ca(2+)-dependent phospholipid scrambling.
Mutagenesis2791I → A: Reduces the Ca(2+)-dependent phospholipid scrambling.
Mutagenesis2811F → A: Complete inactivation of the Ca(2+)-dependent phospholipid scrambling.
Mutagenesis2841D → A: Reduces the Ca(2+)-dependent phospholipid scrambling.

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 9860744DEC40616E

FASTA31835,049
        10         20         30         40         50         60 
MDKQNSQMNA SHPETNLPVG YPPQYPPTAF QGPPGYSGYP GPQVSYPPPP AGHSGPGPAG 

        70         80         90        100        110        120 
FPVPNQPVYN QPVYNQPVGA AGVPWMPAPQ PPLNCPPGLE YLSQIDQILI HQQIELLEVL 

       130        140        150        160        170        180 
TGFETNNKYE IKNSFGQRVY FAAEDTDCCT RNCCGPSRPF TLRIIDNMGQ EVITLERPLR 

       190        200        210        220        230        240 
CSSCCCPCCL QEIEIQAPPG VPIGYVIQTW HPCLPKFTIQ NEKREDVLKI SGPCVVCSCC 

       250        260        270        280        290        300 
GDVDFEIKSL DEQCVVGKIS KHWTGILREA FTDADNFGIQ FPLDLDVKMK AVMIGACFLI 

       310 
DFMFFESTGS QEQKSGVW 

« Hide

Isoform 2 [UniParc].

Checksum: 61B33BDD238A5519
Show »

FASTA23726,825

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Phospholipid scramblase 1 potentiates the antiviral activity of interferon."
Dong B., Zhou Q., Zhao J., Zhou A., Harty R.N., Bose S., Banerjee A., Slee R., Guenther J., Williams B.R.G., Wiedmer T., Sims P.J., Silverman R.H.
J. Virol. 78:8983-8993(2004) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Wikipedia

Scramblase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3135.1.
PIRJE0284.
RefSeqNP_066928.1. NM_021105.2.
UniGeneHs.130759.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y2AX-ray2.20P257-266[»]
ProteinModelPortalO15162.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111373. 85 interactions.
IntActO15162. 105 interactions.
MINTMINT-201602.
STRING9606.ENSP00000345494.

Protein family/group databases

TCDB9.A.36.1.1. the ca(2+)-dependent phospholipid scramblase (scramblase) family.

PTM databases

PhosphoSiteO15162.

Proteomic databases

MaxQBO15162.
PaxDbO15162.
PRIDEO15162.

Protocols and materials databases

DNASU5359.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000342435; ENSP00000345494; ENSG00000188313.
ENST00000448787; ENSP00000411675; ENSG00000188313.
GeneID5359.
KEGGhsa:5359.
UCSCuc003evx.4. human.

Organism-specific databases

CTD5359.
GeneCardsGC03M146232.
HGNCHGNC:9092. PLSCR1.
MIM604170. gene.
neXtProtNX_O15162.
PharmGKBPA33419.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG119855.
HOGENOMHOG000237356.
HOVERGENHBG019157.
InParanoidO15162.
OMAFFESTGS.
OrthoDBEOG77T14X.
PhylomeDBO15162.
TreeFamTF314939.

Enzyme and pathway databases

SignaLinkO15162.

Gene expression databases

ArrayExpressO15162.
BgeeO15162.
CleanExHS_PLSCR1.
GenevestigatorO15162.

Family and domain databases

InterProIPR005552. Scramblase.
[Graphical view]
PANTHERPTHR23248. PTHR23248. 1 hit.
PfamPF03803. Scramblase. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPLSCR1. human.
EvolutionaryTraceO15162.
GeneWikiPLSCR1.
GenomeRNAi5359.
NextBio20774.
PROO15162.
SOURCESearch...

Entry information

Entry namePLS1_HUMAN
AccessionPrimary (citable) accession number: O15162
Secondary accession number(s): B2R8H8, B4DTE8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM