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Q9NRQ2

- PLS4_HUMAN

UniProt

Q9NRQ2 - PLS4_HUMAN

Protein

Phospholipid scramblase 4

Gene

PLSCR4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (04 Nov 2008)
      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.

    Cofactori

    Calcium or magnesium.1 Publication

    GO - Molecular functioni

    1. calcium ion binding Source: UniProtKB
    2. CD4 receptor binding Source: UniProtKB
    3. enzyme binding Source: UniProtKB
    4. phospholipid scramblase activity Source: UniProtKB
    5. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to lipopolysaccharide Source: Ensembl
    2. phospholipid scrambling Source: UniProtKB

    Keywords - Ligandi

    Calcium

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phospholipid scramblase 4
    Short name:
    PL scramblase 4
    Alternative name(s):
    Ca(2+)-dependent phospholipid scramblase 4
    Cell growth-inhibiting gene 43 protein
    TRA1
    Gene namesi
    Name:PLSCR4
    ORF Names:GIG43
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:16497. PLSCR4.

    Subcellular locationi

    Membrane By similarity; Single-pass type II membrane protein By similarity

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi290 – 2901D → A: 50% decrease in scramblase activity in presence of Ca2+, and 40% decrease in scramblase activity in presence of Mg2+. 1 Publication

    Organism-specific databases

    PharmGKBiPA33422.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 329329Phospholipid scramblase 4PRO_0000100792Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei83 – 831Phosphotyrosine; by ABLBy similarity
    Modified residuei88 – 881Phosphotyrosine; by ABLBy similarity
    Lipidationi250 – 2501S-palmitoyl cysteineCurated
    Lipidationi255 – 2551S-palmitoyl cysteineCurated

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NRQ2.
    PaxDbiQ9NRQ2.
    PRIDEiQ9NRQ2.

    PTM databases

    PhosphoSiteiQ9NRQ2.

    Expressioni

    Tissue specificityi

    Expressed in heart, brain, placenta, lung, liver, kidney, pancreas, spleen, thymus, prostate, testis, uterus, small intestine and colon. Not detected in peripheral blood lymphocytes.

    Gene expression databases

    ArrayExpressiQ9NRQ2.
    BgeeiQ9NRQ2.
    CleanExiHS_PLSCR4.
    GenevestigatoriQ9NRQ2.

    Organism-specific databases

    HPAiHPA002276.

    Interactioni

    Subunit structurei

    Interacts with PDCD6.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Hoxa1P090224EBI-769257,EBI-3957603From a different organism.

    Protein-protein interaction databases

    BioGridi121357. 7 interactions.
    IntActiQ9NRQ2. 16 interactions.
    MINTiMINT-1443866.
    STRINGi9606.ENSP00000347038.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3Q5UX-ray2.50B271-283[»]
    ProteinModelPortaliQ9NRQ2.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 303303CytoplasmicBy similarityAdd
    BLAST
    Topological domaini321 – 3299ExtracellularBy similarity

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei304 – 32017HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 9898Proline-rich domain (PRD)By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi18 – 258SH3-binding 1Sequence Analysis
    Motifi30 – 334WW-bindingSequence Analysis
    Motifi41 – 499SH3-binding 2Sequence Analysis
    Motifi98 – 1069SH3-binding 3Sequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi195 – 2028Cys-rich

    Domaini

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

    Sequence similaritiesi

    Belongs to the phospholipid scramblase family.Curated

    Keywords - Domaini

    Repeat, SH3-binding, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG317744.
    HOGENOMiHOG000237356.
    HOVERGENiHBG019157.
    InParanoidiQ9NRQ2.
    OMAiNRYDIKN.
    OrthoDBiEOG77T14X.
    PhylomeDBiQ9NRQ2.
    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: Q9NRQ2-1) [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

    MSGVVPTAPE QPAGEMENQT KPPDPRPDAP PEYNSHFLPG PPGTAVPPPT    50
    GYPGGLPMGY YSPQQPSTFP LYQPVGGIHP VRYQPGKYPM PNQSVPITWM 100
    PGPTPMANCP PGLEYLVQLD NIHVLQHFEP LEMMTCFETN NRYDIKNNSD 150
    QMVYIVTEDT DDFTRNAYRT LRPFVLRVTD CMGREIMTMQ RPFRCTCCCF 200
    CCPSARQELE VQCPPGVTIG FVAEHWNLCR AVYSIQNEKK ENVMRVRGPC 250
    STYGCGSDSV FEVKSLDGIS NIGSIIRKWN GLLSAMADAD HFDIHFPLDL 300
    DVKMKAMIFG ACFLIDFMYF ERSPPQRSR 329
    Length:329
    Mass (Da):37,005
    Last modified:November 4, 2008 - v2
    Checksum:i12BE86728D54F794
    GO
    Isoform 2 (identifier: Q9NRQ2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-15: Missing.
         119-208: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:224
    Mass (Da):24,797
    Checksum:i55E36F0305DAB876
    GO

    Sequence cautioni

    The sequence AAP97186.1 differs from that shown. Reason: Frameshift at positions 152, 155, 163 and 325.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti56 – 572LP → FL in AAP97186. 1 PublicationCurated
    Sequence conflicti74 – 741P → S in AAT52217. 1 PublicationCurated
    Sequence conflicti149 – 1491S → L in AAP97186. 1 PublicationCurated
    Sequence conflicti163 – 1631F → V in AAP97186. 1 PublicationCurated
    Sequence conflicti175 – 1751V → G in AAP97186. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti34 – 341N → S.2 Publications
    Corresponds to variant rs3762685 [ dbSNP | Ensembl ].
    VAR_011315
    Natural varianti155 – 1551I → V.2 Publications
    Corresponds to variant rs1061409 [ dbSNP | Ensembl ].
    VAR_011316

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 1515Missing in isoform 2. 1 PublicationVSP_042931Add
    BLAST
    Alternative sequencei119 – 20890Missing in isoform 2. 1 PublicationVSP_042932Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF199023 mRNA. Translation: AAF89960.1.
    AY550971 mRNA. Translation: AAT52217.1.
    AK128442 mRNA. Translation: BAC87442.1.
    AK290214 mRNA. Translation: BAF82903.1.
    AL833760 mRNA. Translation: CAH56232.1.
    AC092982 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78935.1.
    BC028354 mRNA. Translation: AAH28354.1.
    AF087887 mRNA. Translation: AAP97186.1. Sequence problems.
    CCDSiCCDS3133.1. [Q9NRQ2-1]
    CCDS54651.1. [Q9NRQ2-2]
    RefSeqiNP_001121776.1. NM_001128304.1. [Q9NRQ2-1]
    NP_001121777.1. NM_001128305.1. [Q9NRQ2-1]
    NP_001121778.1. NM_001128306.1.
    NP_001170775.1. NM_001177304.1. [Q9NRQ2-2]
    NP_065086.2. NM_020353.2. [Q9NRQ2-1]
    XP_005247711.1. XM_005247654.1. [Q9NRQ2-1]
    XP_005247712.1. XM_005247655.1. [Q9NRQ2-1]
    UniGeneiHs.477869.

    Genome annotation databases

    EnsembliENST00000354952; ENSP00000347038; ENSG00000114698. [Q9NRQ2-1]
    ENST00000433593; ENSP00000415605; ENSG00000114698. [Q9NRQ2-2]
    ENST00000446574; ENSP00000399315; ENSG00000114698. [Q9NRQ2-1]
    ENST00000493382; ENSP00000419040; ENSG00000114698. [Q9NRQ2-1]
    GeneIDi57088.
    KEGGihsa:57088.
    UCSCiuc003evt.4. human. [Q9NRQ2-1]
    uc003evu.4. human. [Q9NRQ2-2]

    Polymorphism databases

    DMDMi212276457.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF199023 mRNA. Translation: AAF89960.1 .
    AY550971 mRNA. Translation: AAT52217.1 .
    AK128442 mRNA. Translation: BAC87442.1 .
    AK290214 mRNA. Translation: BAF82903.1 .
    AL833760 mRNA. Translation: CAH56232.1 .
    AC092982 Genomic DNA. No translation available.
    CH471052 Genomic DNA. Translation: EAW78935.1 .
    BC028354 mRNA. Translation: AAH28354.1 .
    AF087887 mRNA. Translation: AAP97186.1 . Sequence problems.
    CCDSi CCDS3133.1. [Q9NRQ2-1 ]
    CCDS54651.1. [Q9NRQ2-2 ]
    RefSeqi NP_001121776.1. NM_001128304.1. [Q9NRQ2-1 ]
    NP_001121777.1. NM_001128305.1. [Q9NRQ2-1 ]
    NP_001121778.1. NM_001128306.1.
    NP_001170775.1. NM_001177304.1. [Q9NRQ2-2 ]
    NP_065086.2. NM_020353.2. [Q9NRQ2-1 ]
    XP_005247711.1. XM_005247654.1. [Q9NRQ2-1 ]
    XP_005247712.1. XM_005247655.1. [Q9NRQ2-1 ]
    UniGenei Hs.477869.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3Q5U X-ray 2.50 B 271-283 [» ]
    ProteinModelPortali Q9NRQ2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121357. 7 interactions.
    IntActi Q9NRQ2. 16 interactions.
    MINTi MINT-1443866.
    STRINGi 9606.ENSP00000347038.

    PTM databases

    PhosphoSitei Q9NRQ2.

    Polymorphism databases

    DMDMi 212276457.

    Proteomic databases

    MaxQBi Q9NRQ2.
    PaxDbi Q9NRQ2.
    PRIDEi Q9NRQ2.

    Protocols and materials databases

    DNASUi 57088.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000354952 ; ENSP00000347038 ; ENSG00000114698 . [Q9NRQ2-1 ]
    ENST00000433593 ; ENSP00000415605 ; ENSG00000114698 . [Q9NRQ2-2 ]
    ENST00000446574 ; ENSP00000399315 ; ENSG00000114698 . [Q9NRQ2-1 ]
    ENST00000493382 ; ENSP00000419040 ; ENSG00000114698 . [Q9NRQ2-1 ]
    GeneIDi 57088.
    KEGGi hsa:57088.
    UCSCi uc003evt.4. human. [Q9NRQ2-1 ]
    uc003evu.4. human. [Q9NRQ2-2 ]

    Organism-specific databases

    CTDi 57088.
    GeneCardsi GC03M145910.
    HGNCi HGNC:16497. PLSCR4.
    HPAi HPA002276.
    MIMi 607612. gene.
    neXtProti NX_Q9NRQ2.
    PharmGKBi PA33422.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG317744.
    HOGENOMi HOG000237356.
    HOVERGENi HBG019157.
    InParanoidi Q9NRQ2.
    OMAi NRYDIKN.
    OrthoDBi EOG77T14X.
    PhylomeDBi Q9NRQ2.
    TreeFami TF314939.

    Miscellaneous databases

    GeneWikii PLSCR4.
    GenomeRNAii 57088.
    NextBioi 62887.
    PROi Q9NRQ2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NRQ2.
    Bgeei Q9NRQ2.
    CleanExi HS_PLSCR4.
    Genevestigatori Q9NRQ2.

    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. "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 [MRNA] (ISOFORM 1), VARIANTS SER-34 AND VAL-155.
      Tissue: Pancreas.
    2. "Identification of a human cell growth inhibiting gene."
      Kim J.W.
      Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS SER-34 AND VAL-155.
    3. "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: Thalamus and Thymus.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Stomach.
    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: Testis.
    8. "Cloning and characterization of a novel human cDNA homology to murine TRA1 mRNA."
      Cui W.C., Yu L., Gao J., Fan Y.X., Xu Y.F., Zhao S.Y.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 46-329 (ISOFORM 1).
    9. "Identification of Alix-type and non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutants."
      Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T., Maki M.
      J. Biol. Chem. 283:9623-9632(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PDCD6.
    10. "Biochemical and functional characterization of human phospholipid scramblase 4 (hPLSCR4)."
      Francis V.G., Gummadi S.N.
      Biol. Chem. 393:1173-1181(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR, MUTAGENESIS OF ASP-290.

    Entry informationi

    Entry nameiPLS4_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRQ2
    Secondary accession number(s): A8K2E9
    , Q2TTR3, Q658L3, Q6ZR73, Q7Z505
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: November 4, 2008
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 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, 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