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O00592

- PODXL_HUMAN

UniProt

O00592 - PODXL_HUMAN

Protein

Podocalyxin

Gene

PODXL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (05 May 2009)
      Previous versions | rss
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    Functioni

    Involved in the regulation of both adhesion and cell morphology and cancer progression. Function as an anti-adhesive molecule that maintains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Acts as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner. Induces the formation of apical actin-dependent microvilli. Involved in the formation of a preapical plasma membrane subdomain to set up inital epithelial polarization and the apical lumen formation during renal tubulogenesis. Plays a role in cancer development and aggressiveness by inducing cell migration and invasion through its interaction with the actin-binding protein EZR. Affects EZR-dependent signaling events, leading to increased activities of the MAPK and PI3K pathways in cancer cells.2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. cell migration Source: UniProtKB
    3. epithelial tube formation Source: UniProtKB
    4. glomerular visceral epithelial cell development Source: UniProtKB
    5. leukocyte migration Source: Ensembl
    6. negative regulation of cell adhesion Source: UniProtKB
    7. negative regulation of cell-cell adhesion Source: UniProtKB
    8. positive regulation of cell-cell adhesion mediated by integrin Source: UniProtKB
    9. positive regulation of cell migration Source: UniProtKB
    10. regulation of microvillus assembly Source: UniProtKB

    Keywords - Biological processi

    Cell adhesion

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Podocalyxin
    Alternative name(s):
    GCTM-2 antigen
    Gp200
    Podocalyxin-like protein 1
    Short name:
    PC
    Short name:
    PCLP-1
    Gene namesi
    Name:PODXL
    Synonyms:PCLP, PCLP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:9171. PODXL.

    Subcellular locationi

    Apical cell membrane. Cell projectionlamellipodium. Cell projectionfilopodium. Cell projectionruffle. Cell projectionmicrovillus By similarity. Membrane raft By similarity. Membrane Curated; Single-pass type I membrane protein Curated
    Note: In single attached epithelial cells is restricted to a preapical pole on the free plasma membrane whereas other apical and basolateral proteins are not yet polarized. Colocalizes with SLC9A3R2 at the apical plasma membrane during epithelial polarization. Colocalizes with SLC9A3R1 at the trans-Golgi network (transiently) and at the apical plasma membrane. Its association with the membrane raft is transient. Colocalizes with actin filaments, EZR and SLC9A3R1 in a punctate pattern at the apical cell surface where microvilli form. Colocalizes with EZR and SLC9A3R2 at the apical cell membrane of glomerular epithelium cells By similarity. Forms granular, punctuated pattern, forming patches, preferentially adopting a polar distribution, located on the migrating poles of the cell or forming clusters along the terminal ends of filipodia establishing contact with the endothelial cells. Colocalizes with the submembrane actin of lamellipodia, particularly associated with ruffles. Colocalizes with vinculin at protrusions of cells. Colocalizes with ITGB1. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, RAB11A and RAB8A in apical membrane initiation sites (AMIS) during the generation of apical surface and luminogenesis By similarity.By similarity

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB
    2. cell body Source: Ensembl
    3. cytoplasm Source: UniProtKB
    4. extracellular space Source: UniProt
    5. extracellular vesicular exosome Source: UniProt
    6. filopodium Source: UniProtKB
    7. integral component of plasma membrane Source: ProtInc
    8. lamellipodium Source: UniProtKB
    9. membrane raft Source: UniProtKB-SubCell
    10. microvillus membrane Source: UniProtKB
    11. plasma membrane Source: UniProtKB
    12. ruffle Source: UniProtKB
    13. slit diaphragm Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33493.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 558536PodocalyxinPRO_0000024754Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi33 – 331N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi43 – 431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi144 – 1441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi360 – 3601N-linked (GlcNAc...)Sequence Analysis
    Modified residuei529 – 5291Phosphoserine1 Publication
    Modified residuei537 – 5371Phosphoserine1 Publication
    Modified residuei556 – 5561Phosphothreonine1 Publication

    Post-translational modificationi

    N- and O-linked glycosylated. Sialoglycoprotein By similarity.By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiO00592.
    PaxDbiO00592.
    PRIDEiO00592.

    PTM databases

    PhosphoSiteiO00592.

    Expressioni

    Tissue specificityi

    Glomerular epithelium cell (podocyte).

    Gene expression databases

    ArrayExpressiO00592.
    BgeeiO00592.
    CleanExiHS_PODXL.
    GenevestigatoriO00592.

    Organism-specific databases

    HPAiCAB016169.
    CAB062558.
    HPA002110.
    HPA045507.

    Interactioni

    Subunit structurei

    Monomer; when associated with the membrane raft. Oligomer; when integrated in the apical membrane. Interacts (via the C-terminal PDZ-binding motif DTHL) with SLC9A3R1 (via the PDZ domains); the interaction is not detected in glomerular epithelium cells, take place early in the secretory pathway and is necessary for its apical membrane sorting. Found in a complex with EZR, PODXL and SLC9A3R2. Associates with the actin cytoskeleton through complex formation with EZR and SLC9A3R2. Interacts (via the C-terminal PDZ-binding motif DTHL) with SLC9A3R2 (via the PDZ 1 domain); interaction is detected in glomerular epithelium cells By similarity. Interacts with EZR.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IQGAP1P469404EBI-6897823,EBI-297509

    Protein-protein interaction databases

    BioGridi111416. 4 interactions.
    DIPiDIP-58638N.
    IntActiO00592. 1 interaction.
    MINTiMINT-5000334.
    STRINGi9606.ENSP00000367817.

    Structurei

    3D structure databases

    ProteinModelPortaliO00592.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 461439ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini483 – 55876CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei462 – 48221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi35 – 334300Thr-richAdd
    BLAST

    Domaini

    Both the O-glycan-rich domain of the extracellular domain and the C-terminus PDZ-binding motif (DTHL) in the cytoplasmic tail harbor an apical sorting signal. The cytoplasmic domain is necessary for the apical membrane targeting and renal tubulogenesis. The cytoplasmic C-terminus PDZ-binding motif (DTHL) is essential for interaction with SLC9A3R1 and for targeting SLC9A3R1 to the apical cell membrane. The extracellular domain is necessary for microvillus formation By similarity. The large highly anionic extracellular domain allows to maintain open filtration pathways between neighboring podocyte foot processes.By similarity

    Sequence similaritiesi

    Belongs to the podocalyxin family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG47672.
    HOVERGENiHBG053629.
    KOiK06817.
    OrthoDBiEOG7CVQ0P.
    PhylomeDBiO00592.
    TreeFamiTF333564.

    Family and domain databases

    InterProiIPR013836. CD34/Podocalyxin.
    IPR017403. Podocalyxin-like_p1.
    [Graphical view]
    PfamiPF06365. CD34_antigen. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038143. Podocalyxin-like_p1. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O00592-1) [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

    MRCALALSAL LLLLSTPPLL PSSPSPSPSP SQNATQTTTD SSNKTAPTPA    50
    SSVTIMATDT AQQSTVPTSK ANEILASVKA TTLGVSSDSP GTTTLAQQVS 100
    GPVNTTVARG GGSGNPTTTI ESPKSTKSAD TTTVATSTAT AKPNTTSSQN 150
    GAEDTTNSGG KSSHSVTTDL TSTKAEHLTT PHPTSPLSPR QPTSTHPVAT 200
    PTSSGHDHLM KISSSSSTVA IPGYTFTSPG MTTTLLETVF HHVSQAGLEL 250
    LTSGDLPTLA SQSAGITASS VISQRTQQTS SQMPASSTAP SSQETVQPTS 300
    PATALRTPTL PETMSSSPTA ASTTHRYPKT PSPTVAHESN WAKCEDLETQ 350
    TQSEKQLVLN LTGNTLCAGG ASDEKLISLI CRAVKATFNP AQDKCGIRLA 400
    SVPGSQTVVV KEITIHTKLP AKDVYERLKD KWDELKEAGV SDMKLGDQGP 450
    PEEAEDRFSM PLIITIVCMA SFLLLVAALY GCCHQRLSQR KDQQRLTEEL 500
    QTVENGYHDN PTLEVMETSS EMQEKKVVSL NGELGDSWIV PLDNLTKDDL 550
    DEEEDTHL 558
    Length:558
    Mass (Da):58,635
    Last modified:May 5, 2009 - v2
    Checksum:i8B1CF30D14D51691
    GO
    Isoform 2 (identifier: O00592-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         236-268: LETVFHHVSQAGLELLTSGDLPTLASQSAGITA → P

    Show »
    Length:526
    Mass (Da):55,386
    Checksum:i3F14C259BDB3AC76
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311S → SPS in AAB61574. (PubMed:9188463)Curated
    Sequence conflicti404 – 4041G → Q AA sequence (PubMed:12504081)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti60 – 601T → R.
    VAR_012236
    Natural varianti112 – 1121G → S.
    Corresponds to variant rs3735035 [ dbSNP | Ensembl ].
    VAR_055237
    Natural varianti126 – 1261T → P.
    Corresponds to variant rs55698400 [ dbSNP | Ensembl ].
    VAR_062136
    Natural varianti194 – 1941S → L.1 Publication
    Corresponds to variant rs12670788 [ dbSNP | Ensembl ].
    VAR_012237
    Natural varianti298 – 2981P → A.
    Corresponds to variant rs35893129 [ dbSNP | Ensembl ].
    VAR_060090
    Natural varianti358 – 3581V → I.1 Publication
    Corresponds to variant rs3212298 [ dbSNP | Ensembl ].
    VAR_055238

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei236 – 26833LETVF…AGITA → P in isoform 2. 3 PublicationsVSP_037220Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U97519 mRNA. Translation: AAB61574.1.
    AK223573 mRNA. Translation: BAD97293.1.
    AC008264 Genomic DNA. No translation available.
    CH236950 Genomic DNA. Translation: EAL24080.1.
    CH471070 Genomic DNA. Translation: EAW83786.1.
    BC093730 mRNA. Translation: AAH93730.1.
    BC112035 mRNA. Translation: AAI12036.1.
    BP234810 mRNA. No translation available.
    CCDSiCCDS34755.1. [O00592-1]
    CCDS47714.1. [O00592-2]
    RefSeqiNP_001018121.1. NM_001018111.2. [O00592-1]
    NP_005388.2. NM_005397.3. [O00592-2]
    UniGeneiHs.744213.

    Genome annotation databases

    EnsembliENST00000322985; ENSP00000319782; ENSG00000128567. [O00592-2]
    ENST00000378555; ENSP00000367817; ENSG00000128567. [O00592-1]
    GeneIDi5420.
    KEGGihsa:5420.
    UCSCiuc003vqw.4. human. [O00592-1]
    uc003vqx.4. human. [O00592-2]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U97519 mRNA. Translation: AAB61574.1 .
    AK223573 mRNA. Translation: BAD97293.1 .
    AC008264 Genomic DNA. No translation available.
    CH236950 Genomic DNA. Translation: EAL24080.1 .
    CH471070 Genomic DNA. Translation: EAW83786.1 .
    BC093730 mRNA. Translation: AAH93730.1 .
    BC112035 mRNA. Translation: AAI12036.1 .
    BP234810 mRNA. No translation available.
    CCDSi CCDS34755.1. [O00592-1 ]
    CCDS47714.1. [O00592-2 ]
    RefSeqi NP_001018121.1. NM_001018111.2. [O00592-1 ]
    NP_005388.2. NM_005397.3. [O00592-2 ]
    UniGenei Hs.744213.

    3D structure databases

    ProteinModelPortali O00592.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111416. 4 interactions.
    DIPi DIP-58638N.
    IntActi O00592. 1 interaction.
    MINTi MINT-5000334.
    STRINGi 9606.ENSP00000367817.

    PTM databases

    PhosphoSitei O00592.

    Proteomic databases

    MaxQBi O00592.
    PaxDbi O00592.
    PRIDEi O00592.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322985 ; ENSP00000319782 ; ENSG00000128567 . [O00592-2 ]
    ENST00000378555 ; ENSP00000367817 ; ENSG00000128567 . [O00592-1 ]
    GeneIDi 5420.
    KEGGi hsa:5420.
    UCSCi uc003vqw.4. human. [O00592-1 ]
    uc003vqx.4. human. [O00592-2 ]

    Organism-specific databases

    CTDi 5420.
    GeneCardsi GC07M131185.
    H-InvDB HIX0007089.
    HGNCi HGNC:9171. PODXL.
    HPAi CAB016169.
    CAB062558.
    HPA002110.
    HPA045507.
    MIMi 602632. gene.
    neXtProti NX_O00592.
    PharmGKBi PA33493.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47672.
    HOVERGENi HBG053629.
    KOi K06817.
    OrthoDBi EOG7CVQ0P.
    PhylomeDBi O00592.
    TreeFami TF333564.

    Miscellaneous databases

    ChiTaRSi PODXL. human.
    GeneWikii PODXL.
    GenomeRNAii 5420.
    NextBioi 20969.
    PROi O00592.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00592.
    Bgeei O00592.
    CleanExi HS_PODXL.
    Genevestigatori O00592.

    Family and domain databases

    InterProi IPR013836. CD34/Podocalyxin.
    IPR017403. Podocalyxin-like_p1.
    [Graphical view ]
    Pfami PF06365. CD34_antigen. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038143. Podocalyxin-like_p1. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of human podocalyxin-like protein. Orthologous relationship to rabbit PCLP1 and rat podocalyxin."
      Kershaw D.B., Beck S.G., Wharram B.L., Wiggins J.E., Goyal M., Thomas P.E., Wiggins R.C.
      J. Biol. Chem. 272:15708-15714(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LEU-194.
    2. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT ILE-358.
      Tissue: Heart.
    3. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 2).
      Tissue: Liver.
    7. Suzuki Y., Yamashita R., Shirota M., Sakakibara Y., Chiba J., Nakai K., Sugano S.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-310 (ISOFORM 1).
    8. "Human embryonal carcinoma tumor antigen, Gp200/GCTM-2, is podocalyxin."
      Schopperle W.M., Kershaw D.B., DeWolf W.C.
      Biochem. Biophys. Res. Commun. 300:285-290(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 399-411 AND 445-372.
    9. "Podocalyxin increases the aggressive phenotype of breast and prostate cancer cells in vitro through its interaction with ezrin."
      Sizemore S., Cicek M., Sizemore N., Ng K.P., Casey G.
      Cancer Res. 67:6183-6191(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH EZR, SUBCELLULAR LOCATION.
    10. "Expression of podocalyxin enhances the adherence, migration, and intercellular communication of cells."
      Larrucea S., Butta N., Arias-Salgado E.G., Alonso-Martin S., Ayuso M.S., Parrilla R.
      Exp. Cell Res. 314:2004-2015(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529 AND THR-556, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPODXL_HUMAN
    AccessioniPrimary (citable) accession number: O00592
    Secondary accession number(s): A6NHX8, Q52LZ7, Q53ER6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 13, 2001
    Last sequence update: May 5, 2009
    Last modified: October 1, 2014
    This is version 107 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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