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Q9UKV3

- ACINU_HUMAN

UniProt

Q9UKV3 - ACINU_HUMAN

Protein

Apoptotic chromatin condensation inducer in the nucleus

Gene

ACIN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    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.5 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei1093 – 10942Cleavage; by caspase-3

    GO - Molecular functioni

    1. ATPase activity Source: UniProtKB
    2. enzyme binding Source: UniProtKB
    3. nucleic acid binding Source: UniProtKB
    4. nucleotide binding Source: InterPro
    5. poly(A) RNA binding Source: UniProtKB
    6. protein binding Source: IntAct

    GO - Biological processi

    1. apoptotic chromosome condensation Source: UniProtKB
    2. apoptotic process Source: Reactome
    3. ATP catabolic process Source: GOC
    4. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    5. erythrocyte differentiation Source: UniProtKB
    6. mRNA processing Source: UniProtKB-KW
    7. negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
    8. positive regulation of apoptotic process Source: UniProtKB
    9. positive regulation of monocyte differentiation Source: UniProtKB
    10. RNA splicing Source: UniProtKB-KW

    Keywords - Biological processi

    Apoptosis, mRNA processing, mRNA splicing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_107. Apoptotic cleavage of cellular proteins.

    Protein family/group databases

    TCDBi3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Apoptotic chromatin condensation inducer in the nucleus
    Short name:
    Acinus
    Gene namesi
    Name:ACIN1
    Synonyms:ACINUS, KIAA0670
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:17066. ACIN1.

    Subcellular locationi

    Nucleus. Nucleus speckle. Nucleusnucleoplasm
    Note: Phosphorylation on Ser-1180 by SRPK2 redistributes it from the nuclear speckles to the nucleoplasm.

    GO - Cellular componenti

    1. ASAP complex Source: UniProtKB
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. nuclear speck Source: UniProtKB
    5. nucleus Source: UniProtKB
    6. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1093 – 10931D → A: Abolishes cleavage by CASP3 and chromatin condensation activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134912489.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13411341Apoptotic chromatin condensation inducer in the nucleusPRO_0000064436Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki5 – 5Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei166 – 1661Phosphoserine1 Publication
    Modified residuei169 – 1691Phosphoserine1 Publication
    Modified residuei208 – 2081Phosphoserine1 Publication
    Modified residuei210 – 2101Phosphoserine1 Publication
    Modified residuei216 – 2161Phosphoserine6 Publications
    Modified residuei240 – 2401Phosphoserine4 Publications
    Modified residuei243 – 2431Phosphoserine4 Publications
    Modified residuei254 – 2541Phosphothreonine4 Publications
    Modified residuei269 – 2691Phosphothreonine1 Publication
    Modified residuei295 – 2951Phosphoserine1 Publication
    Modified residuei326 – 3261Phosphothreonine1 Publication
    Modified residuei328 – 3281Phosphoserine2 Publications
    Modified residuei365 – 3651Phosphoserine3 Publications
    Modified residuei384 – 3841Phosphoserine2 Publications
    Modified residuei386 – 3861Phosphoserine2 Publications
    Modified residuei388 – 3881Phosphoserine1 Publication
    Modified residuei393 – 3931Phosphothreonine2 Publications
    Modified residuei400 – 4001Phosphoserine1 Publication
    Modified residuei410 – 4101Phosphoserine4 Publications
    Modified residuei414 – 4141Phosphothreonine3 Publications
    Modified residuei434 – 4341Phosphoserine1 Publication
    Modified residuei453 – 4531Phosphoserine2 Publications
    Modified residuei478 – 4781Phosphoserine1 Publication
    Modified residuei490 – 4901Phosphoserine5 Publications
    Modified residuei512 – 5121Phosphotyrosine1 Publication
    Modified residuei561 – 5611Phosphoserine2 Publications
    Modified residuei654 – 6541N6,N6,N6-trimethyllysine; by EHMT2; alternate1 Publication
    Modified residuei654 – 6541N6,N6-dimethyllysine; by EHMT2; alternate1 Publication
    Modified residuei655 – 6551Phosphoserine3 Publications
    Modified residuei657 – 6571Phosphoserine3 Publications
    Modified residuei682 – 6821Phosphothreonine1 Publication
    Modified residuei710 – 7101Phosphoserine5 Publications
    Modified residuei714 – 7141Phosphoserine2 Publications
    Modified residuei717 – 7171N6-acetyllysine1 Publication
    Modified residuei720 – 7201Phosphothreonine1 Publication
    Modified residuei729 – 7291Phosphoserine2 Publications
    Modified residuei825 – 8251Phosphoserine1 Publication
    Modified residuei838 – 8381Phosphoserine4 Publications
    Modified residuei861 – 8611N6-acetyllysineBy similarity
    Modified residuei895 – 8951Phosphoserine1 Publication
    Modified residuei898 – 8981Phosphoserine1 Publication
    Modified residuei987 – 9871Phosphoserine1 Publication
    Modified residuei990 – 9901Phosphoserine1 Publication
    Modified residuei1004 – 10041Phosphoserine5 Publications
    Modified residuei1180 – 11801Phosphoserine; by SRPK2 and PKB/AKT11 Publication

    Post-translational modificationi

    Phosphorylation on Ser-1180 by SRPK2 up-regulates its stimulatory effect on cyclin A1.10 Publications
    Undergoes proteolytic cleavage; the processed form is active, contrary to the uncleaved form.

    Keywords - PTMi

    Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UKV3.
    PaxDbiQ9UKV3.
    PRIDEiQ9UKV3.

    PTM databases

    PhosphoSiteiQ9UKV3.

    Miscellaneous databases

    PMAP-CutDBQ9UKV3.

    Expressioni

    Tissue specificityi

    Ubiquitous. The Ser-1180 phosphorylated form (by SRPK2) is highly expressed and phosphorylated in patients with myeloid hematologic malignancies.

    Gene expression databases

    ArrayExpressiQ9UKV3.
    BgeeiQ9UKV3.
    CleanExiHS_ACIN1.
    GenevestigatoriQ9UKV3.

    Organism-specific databases

    HPAiHPA000657.

    Interactioni

    Subunit structurei

    Found in a mRNA splicing-dependent exon junction complex (EJC). Component of the heterotrimeric ASAP (apoptosis- and splicing-associated protein) complexes consisting of RNPS1, SAP18 and different isoforms of ACIN1; the association of SAP18 seems to require a preformed RNPS1:ACIN1 complex. Interacts with API5. Interacts with SRPK2 in a phosphorylation-dependent manner.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    API5Q9BZZ52EBI-6976596,EBI-1048422
    PCBD1P614572EBI-396258,EBI-740475

    Protein-protein interaction databases

    BioGridi116634. 74 interactions.
    DIPiDIP-32963N.
    IntActiQ9UKV3. 21 interactions.
    MINTiMINT-5006704.
    STRINGi9606.ENSP00000262710.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UKV3.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini72 – 10635SAPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1210 – 123728Sufficient for interaction with RNPS1 and SAP18 and formation of th ASAP complexBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi142 – 442301Glu-richAdd
    BLAST
    Compositional biasi573 – 676104Ser-richAdd
    BLAST
    Compositional biasi1114 – 113118Pro-richAdd
    BLAST
    Compositional biasi1132 – 1341210Arg/Asp/Glu/Lys-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 SAP domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG291715.
    HOGENOMiHOG000088615.
    HOVERGENiHBG050449.
    InParanoidiQ9UKV3.
    KOiK12875.
    OMAiADRNLKT.
    PhylomeDBiQ9UKV3.
    TreeFamiTF320727.

    Family and domain databases

    Gene3Di1.10.720.30. 1 hit.
    3.30.70.330. 1 hit.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR003034. SAP_dom.
    [Graphical view]
    PfamiPF02037. SAP. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 1 hit.
    SM00513. SAP. 1 hit.
    [Graphical view]
    PROSITEiPS50800. SAP. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UKV3-1) [UniParc]FASTAAdd to Basket

    Also known as: L

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MWRRKHPRTS GGTRGVLSGN RGVEYGSGRG HLGTFEGRWR KLPKMPEAVG     50
    TDPSTSRKMA ELEEVTLDGK PLQALRVTDL KAALEQRGLA KSGQKSALVK 100
    RLKGALMLEN LQKHSTPHAA FQPNSQIGEE MSQNSFIKQY LEKQQELLRQ 150
    RLEREAREAA ELEEASAESE DEMIHPEGVA SLLPPDFQSS LERPELELSR 200
    HSPRKSSSIS EEKGDSDDEK PRKGERRSSR VRQARAAKLS EGSQPAEEEE 250
    DQETPSRNLR VRADRNLKTE EEEEEEEEEE EDDEEEEGDD EGQKSREAPI 300
    LKEFKEEGEE IPRVKPEEMM DERPKTRSQE QEVLERGGRF TRSQEEARKS 350
    HLARQQQEKE MKTTSPLEEE EREIKSSQGL KEKSKSPSPP RLTEDRKKAS 400
    LVALPEQTAS EEETPPPLLT KEASSPPPHP QLHSEEEIEP MEGPAPAVLI 450
    QLSPPNTDAD TRELLVSQHT VQLVGGLSPL SSPSDTKAES PAEKVPEESV 500
    LPLVQKSTLA DYSAQKDLEP ESDRSAQPLP LKIEELALAK GITEECLKQP 550
    SLEQKEGRRA SHTLLPSHRL KQSADSSSSR SSSSSSSSSR SRSRSPDSSG 600
    SRSHSPLRSK QRDVAQARTH ANPRGRPKMG SRSTSESRSR SRSRSRSASS 650
    NSRKSLSPGV SRDSSTSYTE TKDPSSGQEV ATPPVPQLQV CEPKERTSTS 700
    SSSVQARRLS QPESAEKHVT QRLQPERGSP KKCEAEEAEP PAATQPQTSE 750
    TQTSHLPESE RIHHTVEEKE EVTMDTSENR PENDVPEPPM PIADQVSNDD 800
    RPEGSVEDEE KKESSLPKSF KRKISVVSAT KGVPAGNSDT EGGQPGRKRR 850
    WGASTATTQK KPSISITTES LKSLIPDIKP LAGQEAVVDL HADDSRISED 900
    ETERNGDDGT HDKGLKICRT VTQVVPAEGQ ENGQREEEEE EKEPEAEPPV 950
    PPQVSVEVAL PPPAEHEVKK VTLGDTLTRR SISQQKSGVS ITIDDPVRTA 1000
    QVPSPPRGKI SNIVHISNLV RPFTLGQLKE LLGRTGTLVE EAFWIDKIKS 1050
    HCFVTYSTVE EAVATRTALH GVKWPQSNPK FLCADYAEQD ELDYHRGLLV 1100
    DRPSETKTEE QGIPRPLHPP PPPPVQPPQH PRAEQREQER AVREQWAERE 1150
    REMERRERTR SEREWDRDKV REGPRSRSRS RDRRRKERAK SKEKKSEKKE 1200
    KAQEEPPAKL LDDLFRKTKA APCIYWLPLT DSQIVQKEAE RAERAKEREK 1250
    RRKEQEEEEQ KEREKEAERE RNRQLEREKR REHSRERDRE RERERERDRG 1300
    DRDRDRERDR ERGRERDRRD TKRHSRSRSR STPVRDRGGR R 1341
    Length:1,341
    Mass (Da):151,862
    Last modified:October 5, 2010 - v2
    Checksum:iDCCBF310A4680691
    GO
    Isoform 2 (identifier: Q9UKV3-2) [UniParc]FASTAAdd to Basket

    Also known as: S'

    The sequence of this isoform differs from the canonical sequence as follows:
         1-727: Missing.
         728-766: GSPKKCEAEE...PESERIHHTV → MSPADRCRSA...DQSSRTRGLP

    Show »
    Length:614
    Mass (Da):70,948
    Checksum:i2E994FB0FA922F4C
    GO
    Isoform 3 (identifier: Q9UKV3-3) [UniParc]FASTAAdd to Basket

    Also known as: S

    The sequence of this isoform differs from the canonical sequence as follows:
         1-758: Missing.
         759-766: SERIHHTV → MLSESKEG

    Show »
    Length:583
    Mass (Da):67,566
    Checksum:iF227265F2F6BBF68
    GO
    Isoform 4 (identifier: Q9UKV3-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         829-829: Missing.
         873-884: Missing.

    Show »
    Length:1,328
    Mass (Da):150,557
    Checksum:i47A3C106859D46DB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti139 – 1391Q → H in BAA31645. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti257 – 2571R → K.
    Corresponds to variant rs11555803 [ dbSNP | Ensembl ].
    VAR_050632
    Natural varianti311 – 3111I → M.
    Corresponds to variant rs3811182 [ dbSNP | Ensembl ].
    VAR_022031
    Natural varianti447 – 4471A → P.7 Publications
    Corresponds to variant rs941719 [ dbSNP | Ensembl ].
    VAR_061547
    Natural varianti467 – 4671S → P.
    Corresponds to variant rs1885097 [ dbSNP | Ensembl ].
    VAR_022032
    Natural varianti478 – 4781S → F.
    Corresponds to variant rs3751501 [ dbSNP | Ensembl ].
    VAR_022033
    Natural varianti1160 – 11601R → Q in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035777

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 758758Missing in isoform 3. 2 PublicationsVSP_004026Add
    BLAST
    Alternative sequencei1 – 727727Missing in isoform 2. 1 PublicationVSP_004025Add
    BLAST
    Alternative sequencei728 – 76639GSPKK…IHHTV → MSPADRCRSANTIEPATTSS LALFLLLQRDQSSRTRGLP in isoform 2. 1 PublicationVSP_004028Add
    BLAST
    Alternative sequencei759 – 7668SERIHHTV → MLSESKEG in isoform 3. 2 PublicationsVSP_004029
    Alternative sequencei829 – 8291Missing in isoform 4. 1 PublicationVSP_042204
    Alternative sequencei873 – 88412Missing in isoform 4. 1 PublicationVSP_042205Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF124726 mRNA. Translation: AAD56724.1.
    AF124727 mRNA. Translation: AAD56725.1.
    AF124728 mRNA. Translation: AAD56726.1.
    BX247975 mRNA. Translation: CAD62309.1.
    AL117258 Genomic DNA. No translation available.
    AL132780 Genomic DNA. No translation available.
    CH471078 Genomic DNA. Translation: EAW66187.1.
    CH471078 Genomic DNA. Translation: EAW66188.1.
    BC140805 mRNA. Translation: AAI40806.1.
    AB014570 mRNA. Translation: BAA31645.2.
    AL050382 mRNA. Translation: CAB43681.2.
    CCDSiCCDS53887.1. [Q9UKV3-3]
    CCDS53888.1. [Q9UKV3-2]
    CCDS55905.1. [Q9UKV3-5]
    CCDS9587.1. [Q9UKV3-1]
    RefSeqiNP_001158286.1. NM_001164814.1.
    NP_001158287.1. NM_001164815.1.
    NP_001158288.1. NM_001164816.1. [Q9UKV3-2]
    NP_001158289.1. NM_001164817.1. [Q9UKV3-3]
    NP_055792.1. NM_014977.3.
    XP_005267475.1. XM_005267418.1. [Q9UKV3-3]
    UniGeneiHs.124490.

    Genome annotation databases

    EnsembliENST00000262710; ENSP00000262710; ENSG00000100813. [Q9UKV3-1]
    ENST00000338631; ENSP00000345541; ENSG00000100813. [Q9UKV3-2]
    ENST00000357481; ENSP00000350073; ENSG00000100813. [Q9UKV3-3]
    ENST00000397341; ENSP00000380502; ENSG00000100813. [Q9UKV3-3]
    ENST00000555053; ENSP00000451328; ENSG00000100813. [Q9UKV3-5]
    GeneIDi22985.
    KEGGihsa:22985.
    UCSCiuc001wip.4. human. [Q9UKV3-3]
    uc001wir.4. human. [Q9UKV3-2]
    uc001wis.4. human. [Q9UKV3-1]
    uc010akg.3. human. [Q9UKV3-5]

    Polymorphism databases

    DMDMi308153407.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF124726 mRNA. Translation: AAD56724.1 .
    AF124727 mRNA. Translation: AAD56725.1 .
    AF124728 mRNA. Translation: AAD56726.1 .
    BX247975 mRNA. Translation: CAD62309.1 .
    AL117258 Genomic DNA. No translation available.
    AL132780 Genomic DNA. No translation available.
    CH471078 Genomic DNA. Translation: EAW66187.1 .
    CH471078 Genomic DNA. Translation: EAW66188.1 .
    BC140805 mRNA. Translation: AAI40806.1 .
    AB014570 mRNA. Translation: BAA31645.2 .
    AL050382 mRNA. Translation: CAB43681.2 .
    CCDSi CCDS53887.1. [Q9UKV3-3 ]
    CCDS53888.1. [Q9UKV3-2 ]
    CCDS55905.1. [Q9UKV3-5 ]
    CCDS9587.1. [Q9UKV3-1 ]
    RefSeqi NP_001158286.1. NM_001164814.1.
    NP_001158287.1. NM_001164815.1.
    NP_001158288.1. NM_001164816.1. [Q9UKV3-2 ]
    NP_001158289.1. NM_001164817.1. [Q9UKV3-3 ]
    NP_055792.1. NM_014977.3.
    XP_005267475.1. XM_005267418.1. [Q9UKV3-3 ]
    UniGenei Hs.124490.

    3D structure databases

    ProteinModelPortali Q9UKV3.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116634. 74 interactions.
    DIPi DIP-32963N.
    IntActi Q9UKV3. 21 interactions.
    MINTi MINT-5006704.
    STRINGi 9606.ENSP00000262710.

    Protein family/group databases

    TCDBi 3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

    PTM databases

    PhosphoSitei Q9UKV3.

    Polymorphism databases

    DMDMi 308153407.

    Proteomic databases

    MaxQBi Q9UKV3.
    PaxDbi Q9UKV3.
    PRIDEi Q9UKV3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262710 ; ENSP00000262710 ; ENSG00000100813 . [Q9UKV3-1 ]
    ENST00000338631 ; ENSP00000345541 ; ENSG00000100813 . [Q9UKV3-2 ]
    ENST00000357481 ; ENSP00000350073 ; ENSG00000100813 . [Q9UKV3-3 ]
    ENST00000397341 ; ENSP00000380502 ; ENSG00000100813 . [Q9UKV3-3 ]
    ENST00000555053 ; ENSP00000451328 ; ENSG00000100813 . [Q9UKV3-5 ]
    GeneIDi 22985.
    KEGGi hsa:22985.
    UCSCi uc001wip.4. human. [Q9UKV3-3 ]
    uc001wir.4. human. [Q9UKV3-2 ]
    uc001wis.4. human. [Q9UKV3-1 ]
    uc010akg.3. human. [Q9UKV3-5 ]

    Organism-specific databases

    CTDi 22985.
    GeneCardsi GC14M023527.
    HGNCi HGNC:17066. ACIN1.
    HPAi HPA000657.
    MIMi 604562. gene.
    neXtProti NX_Q9UKV3.
    PharmGKBi PA134912489.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG291715.
    HOGENOMi HOG000088615.
    HOVERGENi HBG050449.
    InParanoidi Q9UKV3.
    KOi K12875.
    OMAi ADRNLKT.
    PhylomeDBi Q9UKV3.
    TreeFami TF320727.

    Enzyme and pathway databases

    Reactomei REACT_107. Apoptotic cleavage of cellular proteins.

    Miscellaneous databases

    ChiTaRSi ACIN1. human.
    GeneWikii ACIN1.
    GenomeRNAii 22985.
    NextBioi 43823.
    PMAP-CutDB Q9UKV3.
    PROi Q9UKV3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UKV3.
    Bgeei Q9UKV3.
    CleanExi HS_ACIN1.
    Genevestigatori Q9UKV3.

    Family and domain databases

    Gene3Di 1.10.720.30. 1 hit.
    3.30.70.330. 1 hit.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR003034. SAP_dom.
    [Graphical view ]
    Pfami PF02037. SAP. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 1 hit.
    SM00513. SAP. 1 hit.
    [Graphical view ]
    PROSITEi PS50800. SAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation."
      Sahara S., Aoto M., Eguchi Y., Imamoto N., Yoneda Y., Tsujimoto Y.
      Nature 401:168-173(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), PARTIAL PROTEIN SEQUENCE, FUNCTION, MUTAGENESIS OF ASP-1093, VARIANT PRO-447.
    2. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), VARIANT PRO-447.
      Tissue: Fetal brain.
    3. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-447.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANT PRO-447.
    6. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-1341 (ISOFORM 1), VARIANT PRO-447.
      Tissue: Brain.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 798-813.
      Tissue: Uterus.
    8. Cited for: IDENTIFICATION IN THE ASAP COMPLEX, FUNCTION OF THE ASAP COMPLEX.
    9. "Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core."
      Tange T.O., Shibuya T., Jurica M.S., Moore M.J.
      RNA 11:1869-1883(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, INTERACTION WITH RNPS1 AND SAP18, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-328; SER-490; SER-710 AND SER-1004, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-243 AND THR-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
      Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
      Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-5.
      Tissue: Mammary cancer.
    13. "Serine/arginine protein-specific kinase 2 promotes leukemia cell proliferation by phosphorylating acinus and regulating cyclin A1."
      Jang S.W., Yang S.J., Ehlen A., Dong S., Khoury H., Chen J., Persson J.L., Ye K.
      Cancer Res. 68:4559-4570(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-1180 BY SRPK2, INTERACTION WITH SRPK2, SUBCELLULAR LOCATION.
    14. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434; SER-453; SER-895 AND SER-898, VARIANT [LARGE SCALE ANALYSIS] PRO-447, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-710 AND SER-1004, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    16. Cited for: METHYLATION AT LYS-654, IDENTIFICATION BY MASS SPECTROMETRY.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166; SER-169; SER-216; SER-240; SER-243; THR-254; SER-295; SER-365; SER-384; SER-386; SER-388; THR-393; SER-410; THR-414; SER-453; SER-490; TYR-512; SER-561; SER-655; SER-657; THR-682; SER-710; THR-720; SER-838 AND SER-1004, VARIANT [LARGE SCALE ANALYSIS] PRO-447, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    19. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "The antiapoptotic protein AAC-11 interacts with and regulates Acinus-mediated DNA fragmentation."
      Rigou P., Piddubnyak V., Faye A., Rain J.-C., Michel L., Calvo F., Poyet J.-L.
      EMBO J. 28:1576-1588(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH API5.
    21. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254; THR-269; SER-400; SER-410; THR-414; SER-478; SER-490; SER-838 AND SER-990, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    22. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-717, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Human SAP18 mediates assembly of a splicing regulatory multiprotein complex via its ubiquitin-like fold."
      Singh K.K., Erkelenz S., Rattay S., Dehof A.K., Hildebrandt A., Schulze-Osthoff K., Schaal H., Schwerk C.
      RNA 16:2442-2454(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SAP18 AND RNPS1.
    24. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-240; SER-243; THR-254; SER-365; SER-410; THR-414; SER-490; SER-561; SER-655; SER-657; SER-710; SER-714; SER-729; SER-838 AND SER-1004, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208; SER-210; SER-216; SER-240; SER-243; THR-326; SER-328; SER-365; SER-384; SER-386; THR-393; SER-410; SER-490; SER-655; SER-657; SER-710; SER-714; SER-729; SER-825; SER-838; SER-987 AND SER-1004, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "Proteins associated with the exon junction complex also control the alternative splicing of apoptotic regulators."
      Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P., Durand M., Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H., Klinck R., Elela S.A., Prinos P., Chabot B.
      Mol. Cell. Biol. 32:954-967(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    28. "The structure of the ASAP core complex reveals the existence of a Pinin-containing PSAP complex."
      Murachelli A.G., Ebert J., Basquin C., Le Hir H., Conti E.
      Nat. Struct. Mol. Biol. 19:378-386(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RNPS1, COMPOSITION OF THE ASAP COMPLEX, FUNCTION OF THE ASAP COMPLEX.
    29. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    30. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-1160.

    Entry informationi

    Entry nameiACINU_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKV3
    Secondary accession number(s): B2RTT4
    , D3DS45, O75158, Q9UG91, Q9UKV1, Q9UKV2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 28, 2003
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 140 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Caution

    Structural and functional studies of the ASAP complex have been conducted with a chimeric complex involving a conserved fragment of Drosophila melanogaster Acinus/hkl.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3