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O00592

- PODXL_HUMAN

UniProt

O00592 - PODXL_HUMAN

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Protein

Podocalyxin

Gene

PODXL

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

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 - 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 461439ExtracellularSequence AnalysisAdd
BLAST
Transmembranei462 – 48221HelicalSequence AnalysisAdd
BLAST
Topological domaini483 – 55876CytoplasmicSequence AnalysisAdd
BLAST

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: UniProtKB
  6. filopodium Source: UniProtKB
  7. integral component of plasma membrane Source: ProtInc
  8. lamellipodium Source: UniProtKB
  9. microvillus membrane Source: UniProtKB
  10. plasma membrane Source: UniProtKB
  11. ruffle Source: UniProtKB
  12. slit diaphragm Source: UniProtKB
Complete GO annotation...

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

BgeeiO00592.
CleanExiHS_PODXL.
ExpressionAtlasiO00592. baseline and differential.
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. 9 interactions.
DIPiDIP-58638N.
IntActiO00592. 1 interaction.
MINTiMINT-5000334.
STRINGi9606.ENSP00000367817.

Structurei

3D structure databases

ProteinModelPortaliO00592.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00730000111314.
HOVERGENiHBG053629.
InParanoidiO00592.
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

        10         20         30         40         50
MRCALALSAL LLLLSTPPLL PSSPSPSPSP SQNATQTTTD SSNKTAPTPA
60 70 80 90 100
SSVTIMATDT AQQSTVPTSK ANEILASVKA TTLGVSSDSP GTTTLAQQVS
110 120 130 140 150
GPVNTTVARG GGSGNPTTTI ESPKSTKSAD TTTVATSTAT AKPNTTSSQN
160 170 180 190 200
GAEDTTNSGG KSSHSVTTDL TSTKAEHLTT PHPTSPLSPR QPTSTHPVAT
210 220 230 240 250
PTSSGHDHLM KISSSSSTVA IPGYTFTSPG MTTTLLETVF HHVSQAGLEL
260 270 280 290 300
LTSGDLPTLA SQSAGITASS VISQRTQQTS SQMPASSTAP SSQETVQPTS
310 320 330 340 350
PATALRTPTL PETMSSSPTA ASTTHRYPKT PSPTVAHESN WAKCEDLETQ
360 370 380 390 400
TQSEKQLVLN LTGNTLCAGG ASDEKLISLI CRAVKATFNP AQDKCGIRLA
410 420 430 440 450
SVPGSQTVVV KEITIHTKLP AKDVYERLKD KWDELKEAGV SDMKLGDQGP
460 470 480 490 500
PEEAEDRFSM PLIITIVCMA SFLLLVAALY GCCHQRLSQR KDQQRLTEEL
510 520 530 540 550
QTVENGYHDN PTLEVMETSS EMQEKKVVSL NGELGDSWIV PLDNLTKDDL

DEEEDTHL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 9 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.
GeneTreei ENSGT00730000111314.
HOVERGENi HBG053629.
InParanoidi O00592.
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

Bgeei O00592.
CleanExi HS_PODXL.
ExpressionAtlasi O00592. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 108 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