Q15942 · ZYX_HUMAN
- ProteinZyxin
- GeneZYX
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids572 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Adhesion plaque protein. Binds alpha-actinin and the CRP protein. Important for targeting TES and ENA/VASP family members to focal adhesions and for the formation of actin-rich structures. May be a component of a signal transduction pathway that mediates adhesion-stimulated changes in gene expression (By similarity).
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 | actin cytoskeleton | |
Cellular Component | adherens junction | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | focal adhesion | |
Cellular Component | nucleus | |
Cellular Component | phagocytic vesicle | |
Cellular Component | plasma membrane | |
Cellular Component | stress fiber | |
Molecular Function | metal ion binding | |
Molecular Function | RNA binding | |
Biological Process | cell-cell signaling | |
Biological Process | cell-matrix adhesion | |
Biological Process | cellular response to type II interferon | |
Biological Process | integrin-mediated signaling pathway | |
Biological Process | stress fiber assembly | |
Biological Process | transforming growth factor beta receptor signaling pathway |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameZyxin
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ15942
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Associates with the actin cytoskeleton near the adhesion plaques. Enters the nucleus in the presence of HESX1.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 71 | Reduced interaction with ENAH and VASP. | ||||
Sequence: F → A | ||||||
Mutagenesis | 93 | Reduced interaction with ENAH and VASP. | ||||
Sequence: F → A | ||||||
Mutagenesis | 104 | Greatly reduced interaction with ENAH and VASP; when associated with A-71 or with A-71 and A-93. | ||||
Sequence: F → A | ||||||
Mutagenesis | 114 | No targeting to focal adhesions and reduced actin-rich structures; when associated with A-71; A-93 and A-104. | ||||
Sequence: F → A | ||||||
Natural variant | VAR_034081 | 223 | in dbSNP:rs11978404 | |||
Sequence: H → L |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,314 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000075913 | 2-572 | UniProt | Zyxin | |||
Sequence: AAPRPSPAISVSVSAPAFYAPQKKFGPVVAPKPKVNPFRPGDSEPPPAPGAQRAQMGRVGEIPPPPPEDFPLPPPPLAGDGDDAEGALGGAFPPPPPPIEESFPPAPLEEEIFPSPPPPPEEEGGPEAPIPPPPQPREKVSSIDLEIDSLSSLLDDMTKNDPFKARVSSGYVPPPVATPFSSKSSTKPAAGGTAPLPPWKSPSSSQPLPQVPAPAQSQTQFHVQPQPQPKPQVQLHVQSQTQPVSLANTQPRGPPASSPAPAPKFSPVTPKFTPVASKFSPGAPGGSGSQPNQKLGHPEALSAGTGSPQPPSFTYAQQREKPRVQEKQHPVPPPAQNQNQVRSPGAPGPLTLKEVEELEQLTQQLMQDMEHPQRQNVAVNELCGRCHQPLARAQPAVRALGQLFHIACFTCHQCAQQLQGQQFYSLEGAPYCEGCYTDTLEKCNTCGEPITDRMLRATGKAYHPHCFTCVVCARPLEGTSFIVDQANRPHCVPDYHKQYAPRCSVCSEPIMPEPGRDETVRVVALDKNFHMKCYKCEDCGKPLSIEADDNGCFPLDGHVLCRKCHTARAQT | |||||||
Modified residue (large scale data) | 7 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 13 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 15 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 20 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 116 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 142 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 142 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 143 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 143 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 150 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 152 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 169 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 169 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 170 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 170 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 172 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 179 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 179 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 202 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 250 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 253 | UniProt | Asymmetric dimethylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 258 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 259 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 259 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 265 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 267 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 267 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 270 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 270 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 272 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 274 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 274 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 278 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 279 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 281 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 281 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 288 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 288 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 290 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 303 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 306 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 308 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 308 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 313 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 316 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 344 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 344 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 481 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 505 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Interaction
Subunit
Interacts with HPV type 6 protein E6. Does not interact significantly with E6 proteins from HPV types 11, 16, or 18. Interacts, via the Pro-rich regions, with the EVH1 domains of ENAH, EVL and VASP. Interacts with the first LIM domain of TES. Interacts with NEBL (isoform 2).
Interacts with SYNPO2
Interacts with SYNPO2
(Microbial infection) Interacts with human papillomavirus type 6/HPV6 protein E6. Does not interact significantly with E6 proteins from HPV types 11, 16, or 18.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q15942 | B2R9Y1 | 3 | EBI-444225, EBI-10175746 | |
BINARY | Q15942 | CASS4 Q9NQ75-2 | 4 | EBI-444225, EBI-12270182 | |
BINARY | Q15942 | ENAH Q8N8S7 | 2 | EBI-444225, EBI-2834410 | |
BINARY | Q15942 | EVL Q9UI08-2 | 5 | EBI-444225, EBI-6448852 | |
BINARY | Q15942 | IMP3 Q9NV31 | 8 | EBI-444225, EBI-747481 | |
BINARY | Q15942 | LAP3 P28838 | 3 | EBI-444225, EBI-2339312 | |
BINARY | Q15942 | LATS1 O95835 | 10 | EBI-444225, EBI-444209 | |
BINARY | Q15942 | LIN7A O14910 | 3 | EBI-444225, EBI-2513988 | |
BINARY | Q15942 | NME5 A0A0S2Z4M0 | 4 | EBI-444225, EBI-16430544 | |
BINARY | Q15942 | OPRM1 P35372 | 2 | EBI-444225, EBI-2624570 | |
BINARY | Q15942 | PDLIM5 Q96HC4 | 3 | EBI-444225, EBI-751267 | |
BINARY | Q15942 | PHF21A Q96BD5 | 6 | EBI-444225, EBI-745085 | |
BINARY | Q15942 | QRICH1 Q2TAL8 | 3 | EBI-444225, EBI-2798044 | |
BINARY | Q15942 | RTN4IP1 Q8WWV3 | 5 | EBI-444225, EBI-743502 | |
BINARY | Q15942 | TUFT1 Q9NNX1 | 3 | EBI-444225, EBI-2557363 | |
BINARY | Q15942 | VASP P50552 | 5 | EBI-444225, EBI-748201 | |
BINARY | Q15942 | ZNF512B Q96KM6 | 3 | EBI-444225, EBI-1049952 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 23-351 | Disordered | ||||
Sequence: QKKFGPVVAPKPKVNPFRPGDSEPPPAPGAQRAQMGRVGEIPPPPPEDFPLPPPPLAGDGDDAEGALGGAFPPPPPPIEESFPPAPLEEEIFPSPPPPPEEEGGPEAPIPPPPQPREKVSSIDLEIDSLSSLLDDMTKNDPFKARVSSGYVPPPVATPFSSKSSTKPAAGGTAPLPPWKSPSSSQPLPQVPAPAQSQTQFHVQPQPQPKPQVQLHVQSQTQPVSLANTQPRGPPASSPAPAPKFSPVTPKFTPVASKFSPGAPGGSGSQPNQKLGHPEALSAGTGSPQPPSFTYAQQREKPRVQEKQHPVPPPAQNQNQVRSPGAPGPL | ||||||
Compositional bias | 61-79 | Pro residues | ||||
Sequence: GEIPPPPPEDFPLPPPPLA | ||||||
Compositional bias | 91-139 | Pro residues | ||||
Sequence: GAFPPPPPPIEESFPPAPLEEEIFPSPPPPPEEEGGPEAPIPPPPQPRE | ||||||
Compositional bias | 211-254 | Polar residues | ||||
Sequence: QVPAPAQSQTQFHVQPQPQPKPQVQLHVQSQTQPVSLANTQPRG | ||||||
Compositional bias | 255-269 | Pro residues | ||||
Sequence: PPASSPAPAPKFSPV | ||||||
Compositional bias | 306-320 | Polar residues | ||||
Sequence: TGSPQPPSFTYAQQR | ||||||
Compositional bias | 332-346 | Polar residues | ||||
Sequence: VPPPAQNQNQVRSPG | ||||||
Domain | 384-443 | LIM zinc-binding 1 | ||||
Sequence: CGRCHQPLARAQPAVRALGQLFHIACFTCHQCAQQLQGQQFYSLEGAPYCEGCYTDTLEK | ||||||
Domain | 444-503 | LIM zinc-binding 2 | ||||
Sequence: CNTCGEPITDRMLRATGKAYHPHCFTCVVCARPLEGTSFIVDQANRPHCVPDYHKQYAPR | ||||||
Domain | 504-570 | LIM zinc-binding 3 | ||||
Sequence: CSVCSEPIMPEPGRDETVRVVALDKNFHMKCYKCEDCGKPLSIEADDNGCFPLDGHVLCRKCHTARA |
Sequence similarities
Belongs to the zyxin/ajuba family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q15942-1
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
- Length572
- Mass (Da)61,277
- Last updated1997-11-01 v1
- Checksum2833B1EFA260B762
Q15942-2
- Name2
- Differences from canonical
- 1-157: Missing
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_057288 | 1-157 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 61-79 | Pro residues | ||||
Sequence: GEIPPPPPEDFPLPPPPLA | ||||||
Compositional bias | 91-139 | Pro residues | ||||
Sequence: GAFPPPPPPIEESFPPAPLEEEIFPSPPPPPEEEGGPEAPIPPPPQPRE | ||||||
Compositional bias | 211-254 | Polar residues | ||||
Sequence: QVPAPAQSQTQFHVQPQPQPKPQVQLHVQSQTQPVSLANTQPRG | ||||||
Compositional bias | 255-269 | Pro residues | ||||
Sequence: PPASSPAPAPKFSPV | ||||||
Compositional bias | 306-320 | Polar residues | ||||
Sequence: TGSPQPPSFTYAQQR | ||||||
Compositional bias | 332-346 | Polar residues | ||||
Sequence: VPPPAQNQNQVRSPG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X94991 EMBL· GenBank· DDBJ | CAA64447.1 EMBL· GenBank· DDBJ | mRNA | ||
X95735 EMBL· GenBank· DDBJ | CAA65050.1 EMBL· GenBank· DDBJ | mRNA | ||
AK299005 EMBL· GenBank· DDBJ | BAG61089.1 EMBL· GenBank· DDBJ | mRNA | ||
AK316227 EMBL· GenBank· DDBJ | BAH14598.1 EMBL· GenBank· DDBJ | mRNA | ||
CR457431 EMBL· GenBank· DDBJ | CAG33712.1 EMBL· GenBank· DDBJ | mRNA | ||
AC092214 EMBL· GenBank· DDBJ | AAS07459.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH236959 EMBL· GenBank· DDBJ | EAL23788.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471198 EMBL· GenBank· DDBJ | EAW51848.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC008743 EMBL· GenBank· DDBJ | AAH08743.1 EMBL· GenBank· DDBJ | mRNA | ||
BC009360 EMBL· GenBank· DDBJ | AAH09360.1 EMBL· GenBank· DDBJ | mRNA | ||
BC010031 EMBL· GenBank· DDBJ | AAH10031.1 EMBL· GenBank· DDBJ | mRNA |