Protein enabled homolog (Protein name
), ENAH_HUMAN from NCBI database.
top
|
General Annotation
|
Antigen Annotation
|
3D
|
Predicted Eptitope
|
Vaild Sequence
|
Related Databases
|
Feedback
Gene name:
ENAH(MENA);
Protein name:
Protein enabled homolog;
Alternative:
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Homotetramer (By similarity). Interacts with APBB1IP, APBB1, PFN1 and ROBO4. Isoforms, containing the polyproline-rich regions with PPLP motifs, bind the WW domain of APBB1IP. Isoforms, containing the PPSY motif, bind, in vitro, to the WW2 and WW3 domains of NEDD4 and to the WW1 domain of YAP1. Binds the SH3 domain of BAIAP2-alpha but only after the autoinhibitory region of BAIAP2-alpha has been blocked by interaction with CDC42. Interacts, via the EVH1/WH1 domain, with the Pro-rich domains from VCL, ZYX and Listeria monocytogenes actA and with TES (via LIM domains). The TES LIM domain and the Pro-rich domains from VCL or ZYX compete for the same binding site. Interaction with ZYX is important for targeting ENAH to focal adhesions and enhances production of actin-rich structures at the apical surface of cells. Interacts, through the Pro-rich region, with the C-terminal SH3 domain of DNMPB. Binds GPHN (By similarity). Interacts with FAT1 (via EVH1 domains) (By similarity). Heterotrimer with TES and ACTL7A.
Function:
Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation. Required for the actin-based mobility of Listeria monocytogenes.
Subcellular Location:
Cytoplasm
Cytoplasm
cytoskeleton
Cell projection
lamellipodium
Cell projection
filopodium
Cell junction
synapse
Cell junction
focal adhesion
Targeted to the leading edge of lamellipodia and filopodia by MRL family members. Colocalizes at filopodial tips with a number of other proteins including vinculin and zyxlin. Colocalizes with N-WASP at the leading edge. Colocalizes with GPHN and PFN at synapses.
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);TISSUE SPECIFICITY
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1);NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-591 (ISOFORM 2)
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-591 (ISOFORM 2)
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 393-591 (ISOFORM 2)
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: PROTEIN SEQUENCE OF 23-47; 70-81; 123-145; 403-427; 484-499 AND 573-587;FUNCTION;INTERACTION WITH BAIAP2
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: INTERACTION WITH VCL; ZYX AND L.MONOCYTOGENES ACTA
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-506 AND SER-508;PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-502 (ISOFORM 2);PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-465 (ISOFORM 3);IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-506 AND SER-508;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512 (ISOFORM 2);PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475 (ISOFORM 3);IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 347-356 IN COMPLEX WITH APBB1
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-113 IN COMPLEX WITH TES;INTERACTION WITH ZYX;FUNCTION;SUBCELLULAR LOCATION
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 1-116 IN COMPLEX WITH TES AND ACTL7A
Vaild Sequence:
