STRINGSTRING
A0A077YVI8 A0A077YVI8 A0A077YW08 A0A077YW08 A0A077YWX6 A0A077YWX6 A0A077YX89 A0A077YX89 A0A077YX91 A0A077YX91 A0A077YXY5 A0A077YXY5 A0A077YY60 A0A077YY60 A0A077YZL4 A0A077YZL4 A0A077YZZ7 A0A077YZZ7 A0A077Z196 A0A077Z196 A0A077Z273 A0A077Z273 A0A077Z3E2 A0A077Z3E2 A0A077Z468 A0A077Z468 A0A077Z593 A0A077Z593 A0A077Z7Z4 A0A077Z7Z4 A0A077Z845 A0A077Z845 A0A077Z8D6 A0A077Z8D6 A0A077Z991 A0A077Z991 A0A077Z9T4 A0A077Z9T4 A0A077Z9T7 A0A077Z9T7 A0A077ZAE8 A0A077ZAE8 A0A077ZB19 A0A077ZB19 A0A077ZBH6 A0A077ZBH6 A0A077ZC40 A0A077ZC40 A0A077ZCC2 A0A077ZCC2 A0A077ZE74 A0A077ZE74 A0A077ZEV7 A0A077ZEV7 A0A077ZFF7 A0A077ZFF7 A0A077ZI18 A0A077ZI18 A0A077ZJ45 A0A077ZJ45 A0A077ZJK8 A0A077ZJK8 A0A077ZJN3 A0A077ZJN3 A0A077ZL72 A0A077ZL72 A0A077ZLF5 A0A077ZLF5 A0A077ZLQ8 A0A077ZLQ8 A0A077ZPU1 A0A077ZPU1 A0A077ZR49 A0A077ZR49
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
A0A077YVI8Src substrate cortactin repeat in hs cortactin. (455 aa)
A0A077YW08Dynactin subunit 4. (272 aa)
A0A077YWX6F-actin-capping protein subunit alpha; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. (276 aa)
A0A077YX89ACBP and GOLD 2 domain containing protein. (399 aa)
A0A077YX91Tctex-1 domain containing protein. (130 aa)
A0A077YXY5Dynein light chain. (117 aa)
A0A077YY60Dynein light chain. (103 aa)
A0A077YZL4Dynein light chain. (115 aa)
A0A077YZZ7Platelet activating factor acetylhydrolase IB. (218 aa)
A0A077Z196Dynein light chain. (90 aa)
A0A077Z273Actin-related protein 10; Belongs to the actin family. (275 aa)
A0A077Z3E2PDZ domain-containing protein. (678 aa)
A0A077Z468Dynein light chain. (96 aa)
A0A077Z593Protein bicaudal D. (795 aa)
A0A077Z7Z4Dynactin subunit 6. (127 aa)
A0A077Z845Neurocalcin. (191 aa)
A0A077Z8D6Phosphatidylinositol 4 kinase beta; Belongs to the PI3/PI4-kinase family. (813 aa)
A0A077Z991Dynein heavy domain containing protein. (635 aa)
A0A077Z9T4Dynein light domain containing protein. (314 aa)
A0A077Z9T7Dynein heavy chain. (4052 aa)
A0A077ZAE8Lissencephaly-1 homolog; Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes. Belongs to the WD repeat LIS1/nudF family. (409 aa)
A0A077ZB19Dynein light intermediate chain; Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes. (446 aa)
A0A077ZBH6F-actin-capping protein subunit beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. (279 aa)
A0A077ZC40Dynein heavy chain. (4167 aa)
A0A077ZCC2Dynein intermediate chain. (649 aa)
A0A077ZE74Dynactin subunit 5. (158 aa)
A0A077ZEV7Uncharacterized protein. (525 aa)
A0A077ZFF7Beta centractin alpha centractin. (370 aa)
A0A077ZI18DEAD and CAP GLY and Dynactin domain containing p rotein. (1474 aa)
A0A077ZJ45Ras protein Rab 11B. (182 aa)
A0A077ZJK8Dynein light chain LC6, flagellar outer arm. (502 aa)
A0A077ZJN3Dynein light chain. (88 aa)
A0A077ZL72Major sperm protein; Central component in molecular interactions underlying sperm crawling. Forms an extensive filament system that extends from sperm villipoda, along the leading edge of the pseudopod. (222 aa)
A0A077ZLF5Uncharacterized protein. (183 aa)
A0A077ZLQ8Major sperm protein; Central component in molecular interactions underlying sperm crawling. Forms an extensive filament system that extends from sperm villipoda, along the leading edge of the pseudopod. (238 aa)
A0A077ZPU1Uncharacterized protein. (223 aa)
A0A077ZR49Uncharacterized protein. (161 aa)
Your Current Organism:
Trichuris trichiura
NCBI taxonomy Id: 36087
Other names: T. trichiura, human whipworm
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