O00592 · PODXL_HUMAN
- ProteinPodocalyxin
- GenePODXL
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids558 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | apical plasma membrane | |
Cellular Component | centriolar satellite | |
Cellular Component | cytoplasm | |
Cellular Component | extracellular exosome | |
Cellular Component | extracellular space | |
Cellular Component | filopodium | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | lamellipodium | |
Cellular Component | membrane raft | |
Cellular Component | microvillus membrane | |
Cellular Component | nucleolus | |
Cellular Component | plasma membrane | |
Cellular Component | ruffle | |
Cellular Component | slit diaphragm | |
Biological Process | cell adhesion | |
Biological Process | cell migration | |
Biological Process | epithelial tube formation | |
Biological Process | negative regulation of cell adhesion | |
Biological Process | negative regulation of cell-cell adhesion | |
Biological Process | podocyte development | |
Biological Process | positive regulation of cell migration | |
Biological Process | positive regulation of cell-cell adhesion mediated by integrin | |
Biological Process | regulation of microvillus assembly |
Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePodocalyxin
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO00592
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
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).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 23-461 | Extracellular | ||||
Sequence: SPSPSPSPSQNATQTTTDSSNKTAPTPASSVTIMATDTAQQSTVPTSKANEILASVKATTLGVSSDSPGTTTLAQQVSGPVNTTVARGGGSGNPTTTIESPKSTKSADTTTVATSTATAKPNTTSSQNGAEDTTNSGGKSSHSVTTDLTSTKAEHLTTPHPTSPLSPRQPTSTHPVATPTSSGHDHLMKISSSSSTVAIPGYTFTSPGMTTTLLETVFHHVSQAGLELLTSGDLPTLASQSAGITASSVISQRTQQTSSQMPASSTAPSSQETVQPTSPATALRTPTLPETMSSSPTAASTTHRYPKTPSPTVAHESNWAKCEDLETQTQSEKQLVLNLTGNTLCAGGASDEKLISLICRAVKATFNPAQDKCGIRLASVPGSQTVVVKEITIHTKLPAKDVYERLKDKWDELKEAGVSDMKLGDQGPPEEAEDRFSMP | ||||||
Transmembrane | 462-482 | Helical | ||||
Sequence: LIITIVCMASFLLLVAALYGC | ||||||
Topological domain | 483-558 | Cytoplasmic | ||||
Sequence: CHQRLSQRKDQQRLTEELQTVENGYHDNPTLEVMETSSEMQEKKVVSLNGELGDSWIVPLDNLTKDDLDEEEDTHL |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_012236 | 60 | ||||
Sequence: T → R | ||||||
Natural variant | VAR_055237 | 112 | in dbSNP:rs3735035 | |||
Sequence: G → S | ||||||
Natural variant | VAR_062136 | 126 | in dbSNP:rs55698400 | |||
Sequence: T → P | ||||||
Natural variant | VAR_012237 | 194 | in dbSNP:rs12670788 | |||
Sequence: S → L | ||||||
Natural variant | VAR_060090 | 298 | in dbSNP:rs35893129 | |||
Sequence: P → A | ||||||
Natural variant | VAR_055238 | 358 | in dbSNP:rs3212298 | |||
Sequence: V → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 659 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-22 | UniProt | |||||
Sequence: MRCALALSALLLLLSTPPLLPS | |||||||
Chain | PRO_0000024754 | 23-558 | UniProt | Podocalyxin | |||
Sequence: SPSPSPSPSQNATQTTTDSSNKTAPTPASSVTIMATDTAQQSTVPTSKANEILASVKATTLGVSSDSPGTTTLAQQVSGPVNTTVARGGGSGNPTTTIESPKSTKSADTTTVATSTATAKPNTTSSQNGAEDTTNSGGKSSHSVTTDLTSTKAEHLTTPHPTSPLSPRQPTSTHPVATPTSSGHDHLMKISSSSSTVAIPGYTFTSPGMTTTLLETVFHHVSQAGLELLTSGDLPTLASQSAGITASSVISQRTQQTSSQMPASSTAPSSQETVQPTSPATALRTPTLPETMSSSPTAASTTHRYPKTPSPTVAHESNWAKCEDLETQTQSEKQLVLNLTGNTLCAGGASDEKLISLICRAVKATFNPAQDKCGIRLASVPGSQTVVVKEITIHTKLPAKDVYERLKDKWDELKEAGVSDMKLGDQGPPEEAEDRFSMPLIITIVCMASFLLLVAALYGCCHQRLSQRKDQQRLTEELQTVENGYHDNPTLEVMETSSEMQEKKVVSLNGELGDSWIVPLDNLTKDDLDEEEDTHL | |||||||
Glycosylation | 33 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 43 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 104 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 122 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 144 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 185 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 188 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 360 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 497 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 502 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 507 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 512 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 518 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 518 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 519 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 520 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 529 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 529 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 537 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 537 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 556 | UniProt | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with EZR
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O00592 | IQGAP1 P46940 | 4 | EBI-6897823, EBI-297509 | |
BINARY | O00592 | NHERF2 Q15599 | 2 | EBI-6897823, EBI-1149760 | |
BINARY | O00592-2 | SGTB Q96EQ0 | 3 | EBI-12407415, EBI-744081 | |
BINARY | O00592-2 | UBQLN2 Q9UHD9 | 5 | EBI-12407415, EBI-947187 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 20-50 | Disordered | ||||
Sequence: LPSSPSPSPSPSQNATQTTTDSSNKTAPTPA | ||||||
Compositional bias | 29-50 | Polar residues | ||||
Sequence: SPSQNATQTTTDSSNKTAPTPA | ||||||
Compositional bias | 83-184 | Polar residues | ||||
Sequence: LGVSSDSPGTTTLAQQVSGPVNTTVARGGGSGNPTTTIESPKSTKSADTTTVATSTATAKPNTTSSQNGAEDTTNSGGKSSHSVTTDLTSTKAEHLTTPHPT | ||||||
Region | 83-210 | Disordered | ||||
Sequence: LGVSSDSPGTTTLAQQVSGPVNTTVARGGGSGNPTTTIESPKSTKSADTTTVATSTATAKPNTTSSQNGAEDTTNSGGKSSHSVTTDLTSTKAEHLTTPHPTSPLSPRQPTSTHPVATPTSSGHDHLM | ||||||
Compositional bias | 191-210 | Polar residues | ||||
Sequence: QPTSTHPVATPTSSGHDHLM | ||||||
Compositional bias | 270-337 | Polar residues | ||||
Sequence: SVISQRTQQTSSQMPASSTAPSSQETVQPTSPATALRTPTLPETMSSSPTAASTTHRYPKTPSPTVAH | ||||||
Region | 270-338 | Disordered | ||||
Sequence: SVISQRTQQTSSQMPASSTAPSSQETVQPTSPATALRTPTLPETMSSSPTAASTTHRYPKTPSPTVAHE |
Domain
The large highly anionic extracellular domain allows to maintain open filtration pathways between neighboring podocyte foot processes
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
O00592-1
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.
- Name1
- Length558
- Mass (Da)58,635
- Last updated2009-05-05 v2
- Checksum8B1CF30D14D51691
O00592-2
- Name2
- Differences from canonical
- 236-268: LETVFHHVSQAGLELLTSGDLPTLASQSAGITA → P
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
G3V0E6 | G3V0E6_HUMAN | PODXL | 324 |
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 29-50 | Polar residues | ||||
Sequence: SPSQNATQTTTDSSNKTAPTPA | ||||||
Sequence conflict | 31 | in Ref. 1; AAB61574 | ||||
Sequence: S → SPS | ||||||
Compositional bias | 83-184 | Polar residues | ||||
Sequence: LGVSSDSPGTTTLAQQVSGPVNTTVARGGGSGNPTTTIESPKSTKSADTTTVATSTATAKPNTTSSQNGAEDTTNSGGKSSHSVTTDLTSTKAEHLTTPHPT | ||||||
Compositional bias | 191-210 | Polar residues | ||||
Sequence: QPTSTHPVATPTSSGHDHLM | ||||||
Alternative sequence | VSP_037220 | 236-268 | in isoform 2 | |||
Sequence: LETVFHHVSQAGLELLTSGDLPTLASQSAGITA → P | ||||||
Compositional bias | 270-337 | Polar residues | ||||
Sequence: SVISQRTQQTSSQMPASSTAPSSQETVQPTSPATALRTPTLPETMSSSPTAASTTHRYPKTPSPTVAH | ||||||
Sequence conflict | 404 | in Ref. 8; AA sequence | ||||
Sequence: G → Q |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U97519 EMBL· GenBank· DDBJ | AAB61574.1 EMBL· GenBank· DDBJ | mRNA | ||
AK223573 EMBL· GenBank· DDBJ | BAD97293.1 EMBL· GenBank· DDBJ | mRNA | ||
AC008264 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH236950 EMBL· GenBank· DDBJ | EAL24080.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471070 EMBL· GenBank· DDBJ | EAW83786.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC093730 EMBL· GenBank· DDBJ | AAH93730.1 EMBL· GenBank· DDBJ | mRNA | ||
BC112035 EMBL· GenBank· DDBJ | AAI12036.1 EMBL· GenBank· DDBJ | mRNA | ||
BP234810 EMBL· GenBank· DDBJ | - | mRNA | No translation available. |