Acin1
entrez
56215
canonical
uniprot
Q9JIX8
canonical
ensembl
ENSMUSG00000022185
resolver
ensp
ENSMUSP00000022793
resolver
ensp
ENSMUSP00000107109
resolver
ensp
ENSMUSP00000114546
resolver
ensp
ENSMUSP00000116664
resolver
ensp
ENSMUSP00000118069
resolver
ensp
ENSMUSP00000119080
resolver
ensp
ENSMUSP00000122003
resolver
enst
ENSMUST00000141453
resolver
enst
ENSMUST00000150371
resolver
genesymbol
Acin1
resolver
genesymbol_syn
Acinus
resolver
genesymbol_syn
mKIAA0670
resolver
uniprot
B8JJ87
resolver
uniprot
B8JJ91
resolver
uniprot
F7CEB8
resolver
uniprot
Q52KR6
resolver
uniprot
Q7TSL7
resolver
uniprot
Q80TU6
resolver
uniprot
Q9CSN7
resolver
uniprot
Q9CSR9
resolver
uniprot
Q9CSX7
resolver
uniprot
Q9R046
resolver
uniprot
Q9R047
resolver
uniprot_entry
ACINU_MOUSE
resolver
uniprot_entry
B8JJ91_MOUSE
resolver
uniprot_entry
F7CEB8_MOUSE
resolver
uniprot_entry
Q52KR6_MOUSE
resolver
uniprot_entry
Q7TSL7_MOUSE
resolver
uniprot_entry
Q80TU6_MOUSE
resolver
uniprot_sec
B8JJ87
resolver
uniprot_sec
Q9CSN7
resolver
uniprot_sec
Q9CSR9
resolver
uniprot_sec
Q9CSX7
resolver
uniprot_sec
Q9R046
resolver
uniprot_sec
Q9R047
resolver
amino_acid_sequence
MWGRKRPNSSGETRGILSGNRGVDYGSGRGQSGPFEGRWRKLPKMPEAVGTDPSTSRKMAELEEVTLDGKPLQALRVTDLKAALEQRGLAKSGQKSALVKRLKGALMLENLQKHSTPHAAFQPNSQIGEEMSQNSFIKQYLEKQQELLRQRLEREAREAAELEEASAESEDEMTHPEGVASLLPPDFQSSLNRPELELSTHSPRKSSSFSEEKGESDDEKPRKGERRSSRVRQAKSKLPEYSQTAEEEEDQETPSRNLRVRADRNLKIEEEEEEEEEEEDDDDEEEEEVDEAQKSREAEAPTLKQFEDEEGEERTRAKPEKVVDEKPLNIRSQEKGELEKGGRVTRSQEEARRSHLARQQQEKETQIVSLPQEENEVKSSQSLEEKSQSPSPPPLPEDLEKAPVVLQPEQIVSEEETPPPLLTKEASSPPTHIQLQEEMEPVEGPAPPVLIQLSPPNTDAGAREPLASPHPAQLLRSLSPLSGTTDTKAESPAGRVSDESVLPLAQKSSLPECSTQKGVESEREKSAPLPLTVEEFAPAKGITEEPMKKQSLEQKEGRRASHALFPEHSGKQSADSSSSRSSSPSSSSSPSRSPSPDSVASRPQSSPGSKQRDGAQARVHANPHERPKMGSRSTSESRSRSRSRSRSASSSSRKSLSPGVSRDSNTSYTETKDPSCGQEAAAPSGPQLQVLEPKEKAPTFSASVRGRHLSHPEPEQQHVIQRLQPEQGSPKKCEAEEAEPPAATQPQTSETQISHLLESERTHHTVEEKEEVTMDTSENRPENEVPEPPLPVADQVSNDERPEGGAEEEEKKESSMPKSFKRKISVVSATKGVQAGNSDTEGGQPGRKRRWGASTAATQKKPSISITTESLKSLIPDIKPLAGQEAVVDLHADDSRISEDETERNGDDGTHDKGLKICRTVTQVVPAEGQENGQREEEEEKEPEAELPAPPQVSVEVALPPPVEHEVKKVTLGDTLTRRSISQQKSGVSITIDDPVRTAQVPSPPRGKISNIVHISNLVRPFTLGQLKELLGRTGTLVEEAFWIDKIKSHCFVTYSTVEEAVATRTALHGVKWPQSNPKFLCADYAEQDELDYHRGLLVDRPSETKAEEQGAPRPLHPPPPPPVQPPPHPRAEQREQERAVREQWAEREREMERRERTRSEREWDRDKVREGPRSRSRSRDRRRKERAKSKEKKSEKKEKAQEEPPAKLLDDLFRKTKAAPCIYWLPLTESQIVQKEAEQAERAKEREKRRKEREEEEQKEREKEAERERNRQLEREKRREHSRERERDRERERDRGDRERERERDRDRGRERDRRDTKRHSRSRSRSTPVRDRGGRR
uniprot
proteins
function
FUNCTION: Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets; ACIN1 confers RNA-binding to the complex. The ASAP complex can inhibit RNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function. Induces apoptotic chromatin condensation after activation by CASP3. Regulates cyclin A1, but not cyclin A2, expression in leukemia cells (By similarity). {ECO:0000250}.
uniprot
proteins
mass_dalton
150719
uniprot
proteins
post_translational_modification
PTM: Undergoes proteolytic cleavage; the processed form is active, contrary to the uncleaved form. {ECO:0000250}.; PTM: Phosphorylation on Ser-1179 by SRPK2 up-regulates its stimulatory effect on cyclin A1. {ECO:0000250}.
uniprot
proteins
pubmed
10490026
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
18559500
uniprot
proteins
pubmed
18630941
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
sequence_length
1338
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus speckle {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Note=Phosphorylation on Ser-1179 by SRPK2 redistributes it from the nuclear speckles to the nucleoplasm. {ECO:0000250}.
uniprot
proteins