Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UKV3 (ACINU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Apoptotic chromatin condensation inducer in the nucleus

Short name=Acinus
Gene names
Name:ACIN1
Synonyms:ACINUS, KIAA0670
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1341 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.8 Ref.13 Ref.27 Ref.28

Subunit structure

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. Ref.8 Ref.9 Ref.13 Ref.20 Ref.23 Ref.28

Subcellular location

Nucleus. Nucleus speckle. Nucleusnucleoplasm. Note: Phosphorylation on Ser-1180 by SRPK2 redistributes it from the nuclear speckles to the nucleoplasm. Ref.9 Ref.13 Ref.23

Tissue specificity

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

Post-translational modification

Phosphorylation on Ser-1180 by SRPK2 up-regulates its stimulatory effect on cyclin A1.

Undergoes proteolytic cleavage; the processed form is active, contrary to the uncleaved form.

Sequence similarities

Contains 1 SAP domain.

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 (Ref.28).

Ontologies

Keywords
   Biological processApoptosis
mRNA processing
mRNA splicing
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandRNA-binding
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Non-traceable author statement Ref.1. Source: GOC

RNA splicing

Inferred from electronic annotation. Source: UniProtKB-KW

apoptotic chromosome condensation

Inferred from direct assay Ref.1. Source: UniProtKB

apoptotic process

Traceable author statement. Source: Reactome

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

erythrocyte differentiation

Inferred from expression pattern PubMed 11208865. Source: UniProtKB

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of mRNA splicing, via spliceosome

Inferred from direct assay Ref.8. Source: UniProtKB

positive regulation of apoptotic process

Inferred from direct assay Ref.8. Source: UniProtKB

positive regulation of monocyte differentiation

Inferred from expression pattern PubMed 12393560. Source: UniProtKB

   Cellular_componentASAP complex

Inferred from direct assay Ref.8. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

nuclear speck

Inferred from direct assay Ref.23. Source: UniProtKB

nucleus

Inferred from direct assay Ref.1. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionATPase activity

Non-traceable author statement Ref.1. Source: UniProtKB

enzyme binding

Non-traceable author statement Ref.1. Source: UniProtKB

nucleic acid binding

Non-traceable author statement Ref.1. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.20. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UKV3-1)

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.
Isoform 2 (identifier: Q9UKV3-2)

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
Isoform 3 (identifier: Q9UKV3-3)

Also known as: S;

The sequence of this isoform differs from the canonical sequence as follows:
     1-758: Missing.
     759-766: SERIHHTV → MLSESKEG
Isoform 4 (identifier: Q9UKV3-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13411341Apoptotic chromatin condensation inducer in the nucleus
PRO_0000064436

Regions

Domain72 – 10635SAP
Region1210 – 123728Sufficient for interaction with RNPS1 and SAP18 and formation of th ASAP complex By similarity
Compositional bias142 – 442301Glu-rich
Compositional bias573 – 676104Ser-rich
Compositional bias1114 – 113118Pro-rich
Compositional bias1132 – 1341210Arg/Asp/Glu/Lys-rich

Sites

Site1093 – 10942Cleavage; by caspase-3

Amino acid modifications

Modified residue1661Phosphoserine Ref.17
Modified residue1691Phosphoserine Ref.17
Modified residue2081Phosphoserine Ref.26
Modified residue2101Phosphoserine Ref.26
Modified residue2161Phosphoserine Ref.10 Ref.15 Ref.17 Ref.18 Ref.24 Ref.26
Modified residue2401Phosphoserine Ref.11 Ref.17 Ref.24 Ref.26
Modified residue2431Phosphoserine Ref.11 Ref.17 Ref.24 Ref.26
Modified residue2541Phosphothreonine Ref.11 Ref.17 Ref.21 Ref.24
Modified residue2691Phosphothreonine Ref.21
Modified residue2951Phosphoserine Ref.17
Modified residue3261Phosphothreonine Ref.26
Modified residue3281Phosphoserine Ref.10 Ref.26
Modified residue3651Phosphoserine Ref.17 Ref.24 Ref.26
Modified residue3841Phosphoserine Ref.17 Ref.26
Modified residue3861Phosphoserine Ref.17 Ref.26
Modified residue3881Phosphoserine Ref.17
Modified residue3931Phosphothreonine Ref.17 Ref.26
Modified residue4001Phosphoserine Ref.21
Modified residue4101Phosphoserine Ref.17 Ref.21 Ref.24 Ref.26
Modified residue4141Phosphothreonine Ref.17 Ref.21 Ref.24
Modified residue4341Phosphoserine Ref.14
Modified residue4531Phosphoserine Ref.14 Ref.17
Modified residue4781Phosphoserine Ref.21
Modified residue4901Phosphoserine Ref.10 Ref.17 Ref.21 Ref.24 Ref.26
Modified residue5121Phosphotyrosine Ref.17
Modified residue5611Phosphoserine Ref.17 Ref.24
Modified residue6541N6,N6,N6-trimethyllysine; by EHMT2; alternate Ref.16
Modified residue6541N6,N6-dimethyllysine; by EHMT2; alternate Ref.16
Modified residue6551Phosphoserine Ref.17 Ref.24 Ref.26
Modified residue6571Phosphoserine Ref.17 Ref.24 Ref.26
Modified residue6821Phosphothreonine Ref.17
Modified residue7101Phosphoserine Ref.10 Ref.15 Ref.17 Ref.24 Ref.26
Modified residue7141Phosphoserine Ref.24 Ref.26
Modified residue7171N6-acetyllysine Ref.22
Modified residue7201Phosphothreonine Ref.17
Modified residue7291Phosphoserine Ref.24 Ref.26
Modified residue8251Phosphoserine Ref.26
Modified residue8381Phosphoserine Ref.17 Ref.21 Ref.24 Ref.26
Modified residue8611N6-acetyllysine By similarity
Modified residue8951Phosphoserine Ref.14
Modified residue8981Phosphoserine Ref.14
Modified residue9871Phosphoserine Ref.26
Modified residue9901Phosphoserine Ref.21
Modified residue10041Phosphoserine Ref.10 Ref.15 Ref.17 Ref.24 Ref.26
Modified residue11801Phosphoserine; by SRPK2 and PKB/AKT1 Ref.13
Cross-link5Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.12

Natural variations

Alternative sequence1 – 758758Missing in isoform 3.
VSP_004026
Alternative sequence1 – 727727Missing in isoform 2.
VSP_004025
Alternative sequence728 – 76639GSPKK…IHHTV → MSPADRCRSANTIEPATTSS LALFLLLQRDQSSRTRGLP in isoform 2.
VSP_004028
Alternative sequence759 – 7668SERIHHTV → MLSESKEG in isoform 3.
VSP_004029
Alternative sequence8291Missing in isoform 4.
VSP_042204
Alternative sequence873 – 88412Missing in isoform 4.
VSP_042205
Natural variant2571R → K.
Corresponds to variant rs11555803 [ dbSNP | Ensembl ].
VAR_050632
Natural variant3111I → M.
Corresponds to variant rs3811182 [ dbSNP | Ensembl ].
VAR_022031
Natural variant4471A → P. Ref.1 Ref.2 Ref.4 Ref.5 Ref.6 Ref.14 Ref.17
Corresponds to variant rs941719 [ dbSNP | Ensembl ].
VAR_061547
Natural variant4671S → P.
Corresponds to variant rs1885097 [ dbSNP | Ensembl ].
VAR_022032
Natural variant4781S → F.
Corresponds to variant rs3751501 [ dbSNP | Ensembl ].
VAR_022033
Natural variant11601R → Q in a colorectal cancer sample; somatic mutation. Ref.30
VAR_035777

Experimental info

Mutagenesis10931D → A: Abolishes cleavage by CASP3 and chromatin condensation activity. Ref.1
Sequence conflict1391Q → H in BAA31645. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (L) [UniParc].

Last modified October 5, 2010. Version 2.
Checksum: DCCBF310A4680691

FASTA1,341151,862
        10         20         30         40         50         60 
MWRRKHPRTS GGTRGVLSGN RGVEYGSGRG HLGTFEGRWR KLPKMPEAVG TDPSTSRKMA 

        70         80         90        100        110        120 
ELEEVTLDGK PLQALRVTDL KAALEQRGLA KSGQKSALVK RLKGALMLEN LQKHSTPHAA 

       130        140        150        160        170        180 
FQPNSQIGEE MSQNSFIKQY LEKQQELLRQ RLEREAREAA ELEEASAESE DEMIHPEGVA 

       190        200        210        220        230        240 
SLLPPDFQSS LERPELELSR HSPRKSSSIS EEKGDSDDEK PRKGERRSSR VRQARAAKLS 

       250        260        270        280        290        300 
EGSQPAEEEE DQETPSRNLR VRADRNLKTE EEEEEEEEEE EDDEEEEGDD EGQKSREAPI 

       310        320        330        340        350        360 
LKEFKEEGEE IPRVKPEEMM DERPKTRSQE QEVLERGGRF TRSQEEARKS HLARQQQEKE 

       370        380        390        400        410        420 
MKTTSPLEEE EREIKSSQGL KEKSKSPSPP RLTEDRKKAS LVALPEQTAS EEETPPPLLT 

       430        440        450        460        470        480 
KEASSPPPHP QLHSEEEIEP MEGPAPAVLI QLSPPNTDAD TRELLVSQHT VQLVGGLSPL 

       490        500        510        520        530        540 
SSPSDTKAES PAEKVPEESV LPLVQKSTLA DYSAQKDLEP ESDRSAQPLP LKIEELALAK 

       550        560        570        580        590        600 
GITEECLKQP SLEQKEGRRA SHTLLPSHRL KQSADSSSSR SSSSSSSSSR SRSRSPDSSG 

       610        620        630        640        650        660 
SRSHSPLRSK QRDVAQARTH ANPRGRPKMG SRSTSESRSR SRSRSRSASS NSRKSLSPGV 

       670        680        690        700        710        720 
SRDSSTSYTE TKDPSSGQEV ATPPVPQLQV CEPKERTSTS SSSVQARRLS QPESAEKHVT 

       730        740        750        760        770        780 
QRLQPERGSP KKCEAEEAEP PAATQPQTSE TQTSHLPESE RIHHTVEEKE EVTMDTSENR 

       790        800        810        820        830        840 
PENDVPEPPM PIADQVSNDD RPEGSVEDEE KKESSLPKSF KRKISVVSAT KGVPAGNSDT 

       850        860        870        880        890        900 
EGGQPGRKRR WGASTATTQK KPSISITTES LKSLIPDIKP LAGQEAVVDL HADDSRISED 

       910        920        930        940        950        960 
ETERNGDDGT HDKGLKICRT VTQVVPAEGQ ENGQREEEEE EKEPEAEPPV PPQVSVEVAL 

       970        980        990       1000       1010       1020 
PPPAEHEVKK VTLGDTLTRR SISQQKSGVS ITIDDPVRTA QVPSPPRGKI SNIVHISNLV 

      1030       1040       1050       1060       1070       1080 
RPFTLGQLKE LLGRTGTLVE EAFWIDKIKS HCFVTYSTVE EAVATRTALH GVKWPQSNPK 

      1090       1100       1110       1120       1130       1140 
FLCADYAEQD ELDYHRGLLV DRPSETKTEE QGIPRPLHPP PPPPVQPPQH PRAEQREQER 

      1150       1160       1170       1180       1190       1200 
AVREQWAERE REMERRERTR SEREWDRDKV REGPRSRSRS RDRRRKERAK SKEKKSEKKE 

      1210       1220       1230       1240       1250       1260 
KAQEEPPAKL LDDLFRKTKA APCIYWLPLT DSQIVQKEAE RAERAKEREK RRKEQEEEEQ 

      1270       1280       1290       1300       1310       1320 
KEREKEAERE RNRQLEREKR REHSRERDRE RERERERDRG DRDRDRERDR ERGRERDRRD 

      1330       1340 
TKRHSRSRSR STPVRDRGGR R 

« Hide

Isoform 2 (S') [UniParc].

Checksum: 2E994FB0FA922F4C
Show »

FASTA61470,948
Isoform 3 (S) [UniParc].

Checksum: F227265F2F6BBF68
Show »

FASTA58367,566
Isoform 4 [UniParc].

Checksum: 47A3C106859D46DB
Show »

FASTA1,328150,557

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 798-813.
Tissue: Uterus.
[8]"ASAP, a novel protein complex involved in RNA processing and apoptosis."
Schwerk C., Prasad J., Degenhardt K., Erdjument-Bromage H., White E., Tempst P., Kidd V.J., Manley J.L., Lahti J.M., Reinberg D.
Mol. Cell. Biol. 23:2981-2990(2003) [PubMed] [Europe PMC] [Abstract]
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]"Protein lysine methyltransferase G9a acts on non-histone targets."
Rathert P., Dhayalan A., Murakami M., Zhang X., Tamas R., Jurkowska R., Komatsu Y., Shinkai Y., Cheng X., Jeltsch A.
Nat. Chem. Biol. 4:344-346(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-654, IDENTIFICATION BY MASS SPECTROMETRY.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-1160.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS53887.1. [Q9UKV3-3]
CCDS53888.1. [Q9UKV3-2]
CCDS55905.1. [Q9UKV3-5]
CCDS9587.1. [Q9UKV3-1]
RefSeqNP_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]
UniGeneHs.124490.

3D structure databases

ProteinModelPortalQ9UKV3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116634. 73 interactions.
DIPDIP-32963N.
IntActQ9UKV3. 21 interactions.
MINTMINT-5006704.
STRING9606.ENSP00000262710.

Protein family/group databases

TCDB3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

PhosphoSiteQ9UKV3.

Polymorphism databases

DMDM308153407.

Proteomic databases

MaxQBQ9UKV3.
PaxDbQ9UKV3.
PRIDEQ9UKV3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262710; ENSP00000262710; ENSG00000100813. [Q9UKV3-1]
ENST00000338631; ENSP00000345541; ENSG00000100813. [Q9UKV3-2]
ENST00000357481; ENSP00000350073; ENSG00000100813. [Q9UKV3-3]
ENST00000397341; ENSP00000380502; ENSG00000100813. [Q9UKV3-3]
ENST00000555053; ENSP00000451328; ENSG00000100813. [Q9UKV3-5]
GeneID22985.
KEGGhsa:22985.
UCSCuc001wip.4. human. [Q9UKV3-3]
uc001wir.4. human. [Q9UKV3-2]
uc001wis.4. human. [Q9UKV3-1]
uc010akg.3. human. [Q9UKV3-5]

Organism-specific databases

CTD22985.
GeneCardsGC14M023527.
HGNCHGNC:17066. ACIN1.
HPAHPA000657.
MIM604562. gene.
neXtProtNX_Q9UKV3.
PharmGKBPA134912489.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG291715.
HOGENOMHOG000088615.
HOVERGENHBG050449.
InParanoidQ9UKV3.
KOK12875.
OMAADRNLKT.
PhylomeDBQ9UKV3.
TreeFamTF320727.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.

Gene expression databases

ArrayExpressQ9UKV3.
BgeeQ9UKV3.
CleanExHS_ACIN1.
GenevestigatorQ9UKV3.

Family and domain databases

Gene3D1.10.720.30. 1 hit.
3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR003034. SAP_dom.
[Graphical view]
PfamPF02037. SAP. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]
PROSITEPS50800. SAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACIN1. human.
GeneWikiACIN1.
GenomeRNAi22985.
NextBio43823.
PMAP-CutDBQ9UKV3.
PROQ9UKV3.
SOURCESearch...

Entry information

Entry nameACINU_HUMAN
AccessionPrimary (citable) accession number: Q9UKV3
Secondary accession number(s): B2RTT4 expand/collapse secondary AC list , D3DS45, O75158, Q9UG91, Q9UKV1, Q9UKV2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM