Contents

Search


actin-binding protein anillin (ANLN)

Function: - required for cytokinesis - essential for structural integrity of cleavage furrow & for completion of cleavage furrow ingression - interacts with F-actin - interacts with CD2AP - may interact with RHOA - interacts with FZR1/CDH1 during mitotic exit - phosphorylated during mitosis - ubiquitinated, requires FZR1/CDH1 Structure: contains 1 PH domain Compartment: - nucleus - mainly found in nucleus during interphase - colocalizes with cortical F-actin upon nuclear envelope breakdown in mitosis & subsequently concentrates in the area of the prospective contractile ring in anaphase; pattern persists until telophase, when the protein becomes concentrated in the midbody Alternative splicing: named isoforms=2 Expression: - ubiquitously expressed - expressed in brain > placenta, testis > intestine, ovary, skeletal muscle, thymus > heart, kidney, liver, lung, pancreas, prostate, spleen - expressed in fetal brain, heart, kidney, liver, lung, skeletal muscle, spleen & thymus - in dividing cells expression increases during S & G2 phases, peaks at mitosis & subsequently drops as cells enter G1 phase Pathology: - overexpressed in many tumor types including breast cancer, colorectal cancer, endometrial cancer, hepatocelluar carcinoma, kidney cancer, lung cancer, ovarian cancer, pancreatic cancer

General

cytoskeletal protein phosphoprotein

Properties

SIZE: MW = 124 kD entity length = 1124 aa COMPARTMENT: cell nucleus MOTIF: nuclear localization {1-230} MOTIF: CD2AP interaction {1-155} ubiquitination {1-45} Ser phosphorylation site {S99} Thr phosphorylation site {T194} F-actin interaction {231-676} MOTIF: Thr phosphorylation site {T320} Ser phosphorylation site {S323} Thr phosphorylation site {T401} Ser phosphorylation site {S449} Ser phosphorylation site {S485} Thr phosphorylation site {T515} coiled coil {569-604} Ser phosphorylation site {S637} cleavage furrow {730-1124} MOTIF: PH domain {983-1107}

Database Correlations

UniProt Q9NQW6 Pfam PF00169

References

UniProt :accession Q9NQW6