Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q13393

- PLD1_HUMAN

UniProt

Q13393 - PLD1_HUMAN

Protein

Phospholipase D1

Gene

PLD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic By similarity.By similarity

    Catalytic activityi

    A phosphatidylcholine + H2O = choline + a phosphatidate.

    Enzyme regulationi

    Stimulated by phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate, activated by the phosphokinase C-alpha, by the ADP-ribosylation factor-1 (ARF-1), and to a lesser extent by GTP-binding proteins: RHO A, RAC-1 and CDC42. Inhibited by oleate.

    GO - Molecular functioni

    1. N-acylphosphatidylethanolamine-specific phospholipase D activity Source: UniProtKB-EC
    2. phosphatidylinositol binding Source: InterPro
    3. phospholipase D activity Source: ProtInc
    4. protein binding Source: IntAct

    GO - Biological processi

    1. chemotaxis Source: ProtInc
    2. defense response to Gram-positive bacterium Source: Ensembl
    3. glycerophospholipid biosynthetic process Source: Reactome
    4. lipid catabolic process Source: UniProtKB-KW
    5. phosphatidic acid biosynthetic process Source: Reactome
    6. phosphatidylglycerol biosynthetic process Source: Reactome
    7. phospholipid metabolic process Source: Reactome
    8. Ras protein signal transduction Source: ProtInc
    9. small GTPase mediated signal transduction Source: ProtInc
    10. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid degradation, Lipid metabolism

    Enzyme and pathway databases

    BRENDAi3.1.4.4. 2681.
    ReactomeiREACT_120906. Synthesis of PA.
    REACT_121280. Synthesis of PG.
    REACT_160158. Role of phospholipids in phagocytosis.
    SignaLinkiQ13393.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phospholipase D1 (EC:3.1.4.4)
    Short name:
    PLD 1
    Short name:
    hPLD1
    Alternative name(s):
    Choline phosphatase 1
    Phosphatidylcholine-hydrolyzing phospholipase D1
    Gene namesi
    Name:PLD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:9067. PLD1.

    Subcellular locationi

    Cytoplasmperinuclear region By similarity. Endoplasmic reticulum membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Golgi apparatus membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity. Late endosome membrane By similarity; Lipid-anchor By similarity; Cytoplasmic side By similarity

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome
    2. endosome Source: MGI
    3. Golgi apparatus Source: MGI
    4. Golgi membrane Source: UniProtKB-SubCell
    5. late endosome membrane Source: UniProtKB-SubCell
    6. lysosomal membrane Source: UniProtKB
    7. membrane Source: UniProtKB
    8. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA164742228.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10741074Phospholipase D1PRO_0000218802Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi240 – 2401S-palmitoyl cysteineBy similarity
    Lipidationi241 – 2411S-palmitoyl cysteineBy similarity
    Modified residuei629 – 6291Phosphoserine1 Publication

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiQ13393.
    PaxDbiQ13393.
    PRIDEiQ13393.

    PTM databases

    PhosphoSiteiQ13393.

    Expressioni

    Tissue specificityi

    Expressed abundantly in the pancreas and heart and at high levels in brain, placenta, spleen, uterus and small intestine.1 Publication

    Gene expression databases

    ArrayExpressiQ13393.
    BgeeiQ13393.
    CleanExiHS_PLD1.
    GenevestigatoriQ13393.

    Organism-specific databases

    HPAiCAB004527.
    HPA042396.

    Interactioni

    Subunit structurei

    Interacts with PIP5K1B.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CFL1P235284EBI-2827556,EBI-352733

    Protein-protein interaction databases

    BioGridi111353. 17 interactions.
    DIPiDIP-40821N.
    IntActiQ13393. 4 interactions.
    MINTiMINT-141519.
    STRINGi9606.ENSP00000342793.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13393.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini81 – 212132PXPROSITE-ProRule annotationAdd
    BLAST
    Domaini219 – 328110PHAdd
    BLAST
    Domaini459 – 48628PLD phosphodiesterase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini891 – 91828PLD phosphodiesterase 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni463 – 928466CatalyticAdd
    BLAST

    Sequence similaritiesi

    Belongs to the phospholipase D family.Curated
    Contains 1 PH domain.Curated
    Contains 2 PLD phosphodiesterase domains.PROSITE-ProRule annotation
    Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG1502.
    HOGENOMiHOG000246972.
    HOVERGENiHBG006650.
    InParanoidiQ13393.
    KOiK01115.
    OMAiEYSIISQ.
    OrthoDBiEOG7N63KT.
    PhylomeDBiQ13393.
    TreeFamiTF300589.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    3.30.1520.10. 1 hit.
    InterProiIPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR001683. Phox.
    IPR025202. PLD-like_dom.
    IPR001736. PLipase_D/transphosphatidylase.
    IPR016555. PLipase_D_euk.
    IPR015679. PLipase_D_fam.
    [Graphical view]
    PANTHERiPTHR18896. PTHR18896. 1 hit.
    PfamiPF00169. PH. 1 hit.
    PF00614. PLDc. 1 hit.
    PF13091. PLDc_2. 1 hit.
    PF00787. PX. 1 hit.
    [Graphical view]
    PIRSFiPIRSF009376. Phospholipase_D_euk. 1 hit.
    SMARTiSM00233. PH. 1 hit.
    SM00155. PLDc. 2 hits.
    SM00312. PX. 1 hit.
    [Graphical view]
    SUPFAMiSSF64268. SSF64268. 1 hit.
    PROSITEiPS50035. PLD. 2 hits.
    PS50195. PX. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform PLD1A (identifier: Q13393-1) [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

    MSLKNEPRVN TSALQKIAAD MSNIIENLDT RELHFEGEEV DYDVSPSDPK     50
    IQEVYIPFSA IYNTQGFKEP NIQTYLSGCP IKAQVLEVER FTSTTRVPSI 100
    NLYTIELTHG EFKWQVKRKF KHFQEFHREL LKYKAFIRIP IPTRRHTFRR 150
    QNVREEPREM PSLPRSSENM IREEQFLGRR KQLEDYLTKI LKMPMYRNYH 200
    ATTEFLDISQ LSFIHDLGPK GIEGMIMKRS GGHRIPGLNC CGQGRACYRW 250
    SKRWLIVKDS FLLYMKPDSG AIAFVLLVDK EFKIKVGKKE TETKYGIRID 300
    NLSRTLILKC NSYRHARWWG GAIEEFIQKH GTNFLKDHRF GSYAAIQENA 350
    LAKWYVNAKG YFEDVANAME EANEEIFITD WWLSPEIFLK RPVVEGNRWR 400
    LDCILKRKAQ QGVRIFIMLY KEVELALGIN SEYTKRTLMR LHPNIKVMRH 450
    PDHVSSTVYL WAHHEKLVII DQSVAFVGGI DLAYGRWDDN EHRLTDVGSV 500
    KRVTSGPSLG SLPPAAMESM ESLRLKDKNE PVQNLPIQKS IDDVDSKLKG 550
    IGKPRKFSKF SLYKQLHRHH LHDADSISSI DSTSSYFNHY RSHHNLIHGL 600
    KPHFKLFHPS SESEQGLTRP HADTGSIRSL QTGVGELHGE TRFWHGKDYC 650
    NFVFKDWVQL DKPFADFIDR YSTPRMPWHD IASAVHGKAA RDVARHFIQR 700
    WNFTKIMKSK YRSLSYPFLL PKSQTTAHEL RYQVPGSVHA NVQLLRSAAD 750
    WSAGIKYHEE SIHAAYVHVI ENSRHYIYIE NQFFISCADD KVVFNKIGDA 800
    IAQRILKAHR ENQKYRVYVV IPLLPGFEGD ISTGGGNALQ AIMHFNYRTM 850
    CRGENSILGQ LKAELGNQWI NYISFCGLRT HAELEGNLVT ELIYVHSKLL 900
    IADDNTVIIG SANINDRSML GKRDSEMAVI VQDTETVPSV MDGKEYQAGR 950
    FARGLRLQCF RVVLGYLDDP SEDIQDPVSD KFFKEVWVST AARNATIYDK 1000
    VFRCLPNDEV HNLIQLRDFI NKPVLAKEDP IRAEEELKKI RGFLVQFPFY 1050
    FLSEESLLPS VGTKEAIVPM EVWT 1074
    Length:1,074
    Mass (Da):124,184
    Last modified:November 1, 1997 - v1
    Checksum:i734F285790A0BF7A
    GO
    Isoform PLD1B (identifier: Q13393-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         585-623: SYFNHYRSHHNLIHGLKPHFKLFHPSSESEQGLTRPHAD → N

    Show »
    Length:1,036
    Mass (Da):119,693
    Checksum:i7AFA088570479777
    GO
    Isoform PLD1C (identifier: Q13393-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         514-597: PAAMESMESL...NHYRSHHNLI → IPGPSVVYRQ...SSSAGTSQKL
         598-1074: Missing.

    Show »
    Length:597
    Mass (Da):68,898
    Checksum:iBA03FFD5DD72AED7
    GO
    Isoform PLD1D (identifier: Q13393-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         962-971: VVLGYLDDPS → SKMTPGVEDP
         972-1074: Missing.

    Show »
    Length:971
    Mass (Da):112,184
    Checksum:i0B7F963953A48ECC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti832 – 8321S → P in CAB76564. (PubMed:9761774)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti49 – 491P → A.
    Corresponds to variant rs9819927 [ dbSNP | Ensembl ].
    VAR_034387
    Natural varianti622 – 6221A → S.
    Corresponds to variant rs2290480 [ dbSNP | Ensembl ].
    VAR_022056
    Natural varianti820 – 8201V → M.
    Corresponds to variant rs2287579 [ dbSNP | Ensembl ].
    VAR_022057
    Natural varianti1024 – 10241V → I.
    Corresponds to variant rs9827333 [ dbSNP | Ensembl ].
    VAR_051703

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei514 – 59784PAAME…HHNLI → IPGPSVVYRQVWESCMGKPD SGMERTTAISSSKTGFNLIN LLLISLTGTPRPGCPGMTLP LQSTGRRLVMWHVTSSSAGT SQKL in isoform PLD1C. 1 PublicationVSP_005018Add
    BLAST
    Alternative sequencei585 – 62339SYFNH…RPHAD → N in isoform PLD1B. 2 PublicationsVSP_005020Add
    BLAST
    Alternative sequencei598 – 1074477Missing in isoform PLD1C. 1 PublicationVSP_005019Add
    BLAST
    Alternative sequencei962 – 97110VVLGYLDDPS → SKMTPGVEDP in isoform PLD1D. 1 PublicationVSP_005021
    Alternative sequencei972 – 1074103Missing in isoform PLD1D. 1 PublicationVSP_005022Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38545 mRNA. Translation: AAB49031.1.
    BC068976 mRNA. Translation: AAH68976.1.
    AJ276230 mRNA. Translation: CAB76564.1.
    CCDSiCCDS3216.1. [Q13393-1]
    CCDS46957.1. [Q13393-2]
    RefSeqiNP_002653.1. NM_002662.4. [Q13393-1]
    XP_005247590.1. XM_005247533.1. [Q13393-1]
    XP_005247591.1. XM_005247534.1. [Q13393-2]
    UniGeneiHs.382865.

    Genome annotation databases

    EnsembliENST00000351298; ENSP00000342793; ENSG00000075651. [Q13393-1]
    ENST00000356327; ENSP00000348681; ENSG00000075651. [Q13393-2]
    GeneIDi5337.
    KEGGihsa:5337.
    UCSCiuc003fhs.3. human. [Q13393-1]
    uc003fht.3. human. [Q13393-2]

    Polymorphism databases

    DMDMi2499703.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Phospholipase D entry

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U38545 mRNA. Translation: AAB49031.1 .
    BC068976 mRNA. Translation: AAH68976.1 .
    AJ276230 mRNA. Translation: CAB76564.1 .
    CCDSi CCDS3216.1. [Q13393-1 ]
    CCDS46957.1. [Q13393-2 ]
    RefSeqi NP_002653.1. NM_002662.4. [Q13393-1 ]
    XP_005247590.1. XM_005247533.1. [Q13393-1 ]
    XP_005247591.1. XM_005247534.1. [Q13393-2 ]
    UniGenei Hs.382865.

    3D structure databases

    ProteinModelPortali Q13393.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111353. 17 interactions.
    DIPi DIP-40821N.
    IntActi Q13393. 4 interactions.
    MINTi MINT-141519.
    STRINGi 9606.ENSP00000342793.

    Chemistry

    BindingDBi Q13393.
    ChEMBLi CHEMBL2536.
    DrugBanki DB00122. Choline.

    PTM databases

    PhosphoSitei Q13393.

    Polymorphism databases

    DMDMi 2499703.

    Proteomic databases

    MaxQBi Q13393.
    PaxDbi Q13393.
    PRIDEi Q13393.

    Protocols and materials databases

    DNASUi 5337.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000351298 ; ENSP00000342793 ; ENSG00000075651 . [Q13393-1 ]
    ENST00000356327 ; ENSP00000348681 ; ENSG00000075651 . [Q13393-2 ]
    GeneIDi 5337.
    KEGGi hsa:5337.
    UCSCi uc003fhs.3. human. [Q13393-1 ]
    uc003fht.3. human. [Q13393-2 ]

    Organism-specific databases

    CTDi 5337.
    GeneCardsi GC03M171318.
    HGNCi HGNC:9067. PLD1.
    HPAi CAB004527.
    HPA042396.
    MIMi 602382. gene.
    neXtProti NX_Q13393.
    PharmGKBi PA164742228.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1502.
    HOGENOMi HOG000246972.
    HOVERGENi HBG006650.
    InParanoidi Q13393.
    KOi K01115.
    OMAi EYSIISQ.
    OrthoDBi EOG7N63KT.
    PhylomeDBi Q13393.
    TreeFami TF300589.

    Enzyme and pathway databases

    BRENDAi 3.1.4.4. 2681.
    Reactomei REACT_120906. Synthesis of PA.
    REACT_121280. Synthesis of PG.
    REACT_160158. Role of phospholipids in phagocytosis.
    SignaLinki Q13393.

    Miscellaneous databases

    ChiTaRSi PLD1. human.
    GeneWikii Phospholipase_D1.
    GenomeRNAii 5337.
    NextBioi 20672.
    PROi Q13393.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13393.
    Bgeei Q13393.
    CleanExi HS_PLD1.
    Genevestigatori Q13393.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    3.30.1520.10. 1 hit.
    InterProi IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR001683. Phox.
    IPR025202. PLD-like_dom.
    IPR001736. PLipase_D/transphosphatidylase.
    IPR016555. PLipase_D_euk.
    IPR015679. PLipase_D_fam.
    [Graphical view ]
    PANTHERi PTHR18896. PTHR18896. 1 hit.
    Pfami PF00169. PH. 1 hit.
    PF00614. PLDc. 1 hit.
    PF13091. PLDc_2. 1 hit.
    PF00787. PX. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF009376. Phospholipase_D_euk. 1 hit.
    SMARTi SM00233. PH. 1 hit.
    SM00155. PLDc. 2 hits.
    SM00312. PX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF64268. SSF64268. 1 hit.
    PROSITEi PS50035. PLD. 2 hits.
    PS50195. PX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family."
      Hammond S.M., Altshuller Y.M., Sung T.-C., Rudge S.A., Rose K., Engebrecht J., Morris A.J., Frohman M.A.
      J. Biol. Chem. 270:29640-29643(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PLD1A).
    2. "Characterization of two alternately spliced forms of phospholipase D1. Activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-binding proteins and protein kinase C-alpha."
      Hammond S.M., Jenco J.M., Nakashima S., Cadwallader K., Gu Q.-M., Cook S., Nozawa Y., Prestwich G.D., Frohman M.A., Morris A.J.
      J. Biol. Chem. 272:3860-3868(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PLD1A AND PLD1B).
    3. "Characterization of human PLD2 and the analysis of PLD isoform splice variants."
      Steed P.M., Clark K.L., Boyar W.C., Lasala D.J.
      FASEB J. 12:1309-1317(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS PLD1A; PLD1B AND PLD1C).
      Tissue: Brain, Cervix carcinoma, Chondrocyte and Skeletal muscle.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PLD1A).
      Tissue: Testis.
    5. "A novel human phospholipase D1 splice variant displays conserved regulation in vitro but altered localisation in vivo."
      Hughes W.E., Parker P.J.
      Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 739-1074 (ISOFORM PLD1D).
    6. "Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2."
      Lopez I., Arnold R.S., Lambeth J.D.
      J. Biol. Chem. 273:12846-12852(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    7. "Interaction of the type Ialpha PIPkinase with phospholipase D: a role for the local generation of phosphatidylinositol 4, 5-bisphosphate in the regulation of PLD2 activity."
      Divecha N., Roefs M., Halstead J.R., D'Andrea S., Fernandez-Borga M., Oomen L., Saqib K.M., Wakelam M.J.O., D'Santos C.
      EMBO J. 19:5440-5449(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIP5K1B.
    8. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-629, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiPLD1_HUMAN
    AccessioniPrimary (citable) accession number: Q13393
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 146 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3