ACIN1
entrez
22985
canonical
uniprot
Q9UKV3
canonical
ensembl
ENSG00000100813
resolver
ensp
ENSP00000262710
resolver
ensp
ENSP00000345541
resolver
ensp
ENSP00000350073
resolver
ensp
ENSP00000380502
resolver
ensp
ENSP00000405677
resolver
ensp
ENSP00000451328
resolver
ensp
ENSP00000474349
resolver
ensp
ENSP00000567611
resolver
ensp
ENSP00000567612
resolver
ensp
ENSP00000567613
resolver
ensp
ENSP00000567614
resolver
ensp
ENSP00000567616
resolver
ensp
ENSP00000744438
resolver
enst
ENST00000457657
resolver
enst
ENST00000605057
resolver
genesymbol
ACIN1
resolver
genesymbol_syn
ACINUS
resolver
genesymbol_syn
KIAA0670
resolver
hgnc
HGNC:17066
resolver
uniprot
B2RTT4
resolver
uniprot
B4DQZ7
resolver
uniprot
D3DS45
resolver
uniprot
E7EQT4
resolver
uniprot
O75158
resolver
uniprot
Q9UG91
resolver
uniprot
Q9UKV1
resolver
uniprot
Q9UKV2
resolver
uniprot
S4R3H4
resolver
uniprot_entry
ACINU_HUMAN
resolver
uniprot_entry
B4DQZ7_HUMAN
resolver
uniprot_entry
E7EQT4_HUMAN
resolver
uniprot_entry
S4R3H4_HUMAN
resolver
uniprot_sec
B2RTT4
resolver
uniprot_sec
D3DS45
resolver
uniprot_sec
O75158
resolver
uniprot_sec
Q9UG91
resolver
uniprot_sec
Q9UKV1
resolver
uniprot_sec
Q9UKV2
resolver
amino_acid_sequence
MWRRKHPRTSGGTRGVLSGNRGVEYGSGRGHLGTFEGRWRKLPKMPEAVGTDPSTSRKMAELEEVTLDGKPLQALRVTDLKAALEQRGLAKSGQKSALVKRLKGALMLENLQKHSTPHAAFQPNSQIGEEMSQNSFIKQYLEKQQELLRQRLEREAREAAELEEASAESEDEMIHPEGVASLLPPDFQSSLERPELELSRHSPRKSSSISEEKGDSDDEKPRKGERRSSRVRQARAAKLSEGSQPAEEEEDQETPSRNLRVRADRNLKTEEEEEEEEEEEEDDEEEEGDDEGQKSREAPILKEFKEEGEEIPRVKPEEMMDERPKTRSQEQEVLERGGRFTRSQEEARKSHLARQQQEKEMKTTSPLEEEEREIKSSQGLKEKSKSPSPPRLTEDRKKASLVALPEQTASEEETPPPLLTKEASSPPPHPQLHSEEEIEPMEGPAPAVLIQLSPPNTDADTRELLVSQHTVQLVGGLSPLSSPSDTKAESPAEKVPEESVLPLVQKSTLADYSAQKDLEPESDRSAQPLPLKIEELALAKGITEECLKQPSLEQKEGRRASHTLLPSHRLKQSADSSSSRSSSSSSSSSRSRSRSPDSSGSRSHSPLRSKQRDVAQARTHANPRGRPKMGSRSTSESRSRSRSRSRSASSNSRKSLSPGVSRDSSTSYTETKDPSSGQEVATPPVPQLQVCEPKERTSTSSSSVQARRLSQPESAEKHVTQRLQPERGSPKKCEAEEAEPPAATQPQTSETQTSHLPESERIHHTVEEKEEVTMDTSENRPENDVPEPPMPIADQVSNDDRPEGSVEDEEKKESSLPKSFKRKISVVSATKGVPAGNSDTEGGQPGRKRRWGASTATTQKKPSISITTESLKSLIPDIKPLAGQEAVVDLHADDSRISEDETERNGDDGTHDKGLKICRTVTQVVPAEGQENGQREEEEEEKEPEAEPPVPPQVSVEVALPPPAEHEVKKVTLGDTLTRRSISQQKSGVSITIDDPVRTAQVPSPPRGKISNIVHISNLVRPFTLGQLKELLGRTGTLVEEAFWIDKIKSHCFVTYSTVEEAVATRTALHGVKWPQSNPKFLCADYAEQDELDYHRGLLVDRPSETKTEEQGIPRPLHPPPPPPVQPPQHPRAEQREQERAVREQWAEREREMERRERTRSEREWDRDKVREGPRSRSRSRDRRRKERAKSKEKKSEKKEKAQEEPPAKLLDDLFRKTKAAPCIYWLPLTDSQIVQKEAERAERAKEREKRRKEQEEEEQKEREKEAERERNRQLEREKRREHSRERDRERERERERDRGDRDRDRERDRERGRERDRRDTKRHSRSRSRSTPVRDRGGRR
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. {ECO:0000269|PubMed:10490026, ECO:0000269|PubMed:12665594, ECO:0000269|PubMed:18559500, ECO:0000269|PubMed:22203037, ECO:0000269|PubMed:22388736}.
uniprot
proteins
mass_dalton
151862
uniprot
proteins
mutagenesis
MUTAGEN 1093; /note="D->A: Abolishes cleavage by CASP3 and chromatin condensation activity."; /evidence="ECO:0000269|PubMed:10490026
uniprot
proteins
post_translational_modification
PTM: Phosphorylation on Ser-1180 by SRPK2 up-regulates its stimulatory effect on cyclin A1. {ECO:0000269|PubMed:18559500}.; PTM: Undergoes proteolytic cleavage; the processed form is active, contrary to the uncleaved form.
uniprot
proteins
pubmed
10490026
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
12665594
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16314458
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18438403
uniprot
proteins
pubmed
18559500
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19367720
uniprot
proteins
pubmed
19387494
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20966198
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22203037
uniprot
proteins
pubmed
22388736
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25772364
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
9734811
uniprot
proteins
sequence_length
1341
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus. Nucleus speckle. Nucleus, nucleoplasm. Note=Phosphorylation on Ser-1180 by SRPK2 redistributes it from the nuclear speckles to the nucleoplasm.
uniprot
proteins