Statements in which the resource exists as a subject.
PredicateObject
rdf:type
biopax3:comment
FUNCTION: Plays a critical role in both constitutive and enhancer- dependent splicing by mediating protein-protein interactions and protein-RNA interactions required for accurate 3'-splice site selection. Recruits U2 snRNP to the branch point. Directly mediates interactions between U2AF2 and proteins bound to the enhancers and thus may function as a bridge between U2AF2 and the enhancer complex to recruit it to the adjacent intron (By similarity). SUBUNIT: Identified in the spliceosome C complex. Heterodimer with U2AF2. Interacts with ZRANB2 (By similarity). Interacts (via RS domain) with PHF5A (via N-terminus). SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. TISSUE SPECIFICITY: Expressed in primary spermatocytes and elongating spermatids (at protein level). DOMAIN: The C-terminal SR-rich domain is required for interactions with SR proteins and the splicing regulators TRA and TRA2, and the N-terminal domain is required for formation of the U2AF1/U2AF2 heterodimer (By similarity). PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By similarity). SIMILARITY: Belongs to the splicing factor SR family. SIMILARITY: Contains 2 C3H1-type zinc fingers. SIMILARITY: Contains 1 RRM (RNA recognition motif) domain. GENE SYNONYMS:U2af1. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License., SEQUENCE 239 AA; 27815 MW; DFF944210581244D CRC64;
biopax3:xref
biopax3:displayName
U2AF1_MOUSE
biopax3:name
U2 auxiliary factor 35 kDa subunit, U2 snRNP auxiliary factor small subunit, U2af1
biopax3:entityFeature
biopax3:organism
biopax3:sequence
MAEYLASIFGTEKDKVNCSFYFKIGACRHGDRCSRLHNKPTFSQTIALLNIYRNPQNSSQSADGLRCAVSDVEMQEHYDEFFEEVFTEMEEKYGEVEEMNVCDNLGDHLVGNVYVKFRREEDAEKAVIDLNNRWFNGQPIHAELSPVTDFREACCRQYEMGECTRGGFCNFMHLKPISRELRRELYGRRRKKHRSRSRSRERRSRSRDRGRGGGGGGGGGGGRERDRRRSRDRERSGRF
biopax3:standardName
Splicing factor U2AF 35 kDa subunit