Q9UKV3 (ACINU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Apoptotic chromatin condensation inducer in the nucleus
Short name=Acinus

Gene names

Name:	ACIN1
Synonyms:	ACINUS, KIAA0670

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1341 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of a splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of a few core proteins and several more peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Induces apoptotic chromatin condensation after activation by CASP3. Regulates cyclin A1, but not cyclin A2, expression in leukemia cells. Ref.1 Ref.18
Subunit structure	Found in a mRNA splicing-dependent exon junction complex (EJC), at least composed of ACIN1, CASC3, EIF4A3, MAGOH, PNN, RBM8A, RNPS1, SAP18 and THOC4. Forms heterodimers with RNPS1. Found in a heterotrimeric complex with ACIN1, RNPS1 and SAP18. Interacts with API5. Interacts with SRPK2 in a phosphorylation-dependent manner. Ref.8 Ref.18 Ref.25
Subcellular location	Nucleus. Nucleus speckle. Nucleus › nucleoplasm. Note: Phosphorylation on Ser-1180 by SRPK2 redistributes it from the nuclear speckles to the nucleoplasm. Ref.8 Ref.18
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 upregulates 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.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
PTM	Acetylation Isopeptide bond Methylation Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	apoptotic chromosome condensation Inferred from direct assay Ref.1. Source: UniProtKB erythrocyte differentiation Inferred from expression pattern. Source: UniProtKB positive regulation of monocyte differentiation Inferred from expression pattern. Source: UniProtKB
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	ATPase 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PCBD1	P61457	2	EBI-396258,EBI-740475

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1341	1341	Apoptotic chromatin condensation inducer in the nucleus		PRO_0000064436
Regions
	Domain	72 – 106	35	SAP
	Compositional bias	142 – 442	301	Glu-rich
	Compositional bias	573 – 676	104	Ser-rich
	Compositional bias	1114 – 1131	18	Pro-rich
	Compositional bias	1132 – 1341	210	Arg/Asp/Glu/Lys-rich
Sites
	Site	1093 – 1094	2	Cleavage; by caspase-3
Amino acid modifications
	Modified residue	166	1	Phosphoserine Ref.22
	Modified residue	169	1	Phosphoserine Ref.22
	Modified residue	208	1	Phosphoserine Ref.14
	Modified residue	216	1	Phosphoserine Ref.11 Ref.14 Ref.22 Ref.23
	Modified residue	228	1	Phosphoserine Ref.14
	Modified residue	229	1	Phosphoserine Ref.14
	Modified residue	240	1	Phosphoserine Ref.9 Ref.11 Ref.22 Ref.26
	Modified residue	243	1	Phosphoserine Ref.9 Ref.11 Ref.22 Ref.26
	Modified residue	254	1	Phosphothreonine Ref.12 Ref.14 Ref.16 Ref.22 Ref.24 Ref.26
	Modified residue	256	1	Phosphoserine Ref.14
	Modified residue	269	1	Phosphothreonine Ref.22 Ref.26
	Modified residue	295	1	Phosphoserine Ref.22
	Modified residue	328	1	Phosphoserine Ref.11 Ref.22 Ref.26
	Modified residue	365	1	Phosphoserine Ref.9 Ref.11 Ref.16 Ref.22 Ref.26
	Modified residue	384	1	Phosphoserine Ref.11 Ref.14 Ref.22
	Modified residue	386	1	Phosphoserine Ref.9 Ref.10 Ref.11 Ref.14 Ref.22
	Modified residue	388	1	Phosphoserine Ref.9 Ref.10 Ref.14 Ref.22
	Modified residue	393	1	Phosphothreonine Ref.11 Ref.22
	Modified residue	400	1	Phosphoserine Ref.26
	Modified residue	408	1	Phosphothreonine Ref.11 Ref.24 Ref.26
	Modified residue	410	1	Phosphoserine Ref.11 Ref.22 Ref.24 Ref.26
	Modified residue	414	1	Phosphothreonine Ref.9 Ref.22 Ref.24 Ref.26
	Modified residue	424	1	Phosphoserine Ref.19
	Modified residue	425	1	Phosphoserine Ref.14 Ref.19 Ref.22
	Modified residue	434	1	Phosphoserine Ref.19 Ref.22
	Modified residue	453	1	Phosphoserine Ref.19 Ref.22
	Modified residue	478	1	Phosphoserine Ref.26
	Modified residue	490	1	Phosphoserine Ref.11 Ref.22 Ref.26
	Modified residue	512	1	Phosphotyrosine Ref.22
	Modified residue	561	1	Phosphoserine Ref.14 Ref.22
	Modified residue	654	1	N6,N6,N6-trimethyllysine; by EHMT2; alternate Ref.21
	Modified residue	654	1	N6,N6-dimethyllysine; by EHMT2; alternate Ref.21
	Modified residue	655	1	Phosphoserine Ref.11 Ref.22 Ref.24
	Modified residue	657	1	Phosphoserine Ref.9 Ref.11 Ref.16 Ref.17 Ref.22 Ref.24
	Modified residue	661	1	Phosphoserine Ref.9 Ref.16
	Modified residue	664	1	Phosphoserine Ref.24
	Modified residue	675	1	Phosphoserine Ref.24
	Modified residue	676	1	Phosphoserine Ref.9 Ref.24
	Modified residue	682	1	Phosphothreonine Ref.9 Ref.12 Ref.22 Ref.24
	Modified residue	710	1	Phosphoserine Ref.10 Ref.11 Ref.13 Ref.14 Ref.20 Ref.22
	Modified residue	714	1	Phosphoserine Ref.13 Ref.22
	Modified residue	717	1	N6-acetyllysine Ref.27
	Modified residue	720	1	Phosphothreonine Ref.22
	Modified residue	729	1	Phosphoserine Ref.11 Ref.13 Ref.14
	Modified residue	814	1	Phosphoserine Ref.14
	Modified residue	815	1	Phosphoserine Ref.14
	Modified residue	825	1	Phosphoserine Ref.24
	Modified residue	830	1	Phosphothreonine Ref.14
	Modified residue	838	1	Phosphoserine Ref.14 Ref.22 Ref.24 Ref.26
	Modified residue	840	1	Phosphothreonine Ref.24
	Modified residue	895	1	Phosphoserine Ref.19
	Modified residue	898	1	Phosphoserine Ref.19
	Modified residue	976	1	Phosphothreonine Ref.14
	Modified residue	978	1	Phosphothreonine Ref.14
	Modified residue	981	1	Phosphoserine Ref.14
	Modified residue	983	1	Phosphoserine Ref.14
	Modified residue	987	1	Phosphoserine Ref.26
	Modified residue	990	1	Phosphoserine Ref.26
	Modified residue	1004	1	Phosphoserine Ref.9 Ref.11 Ref.12 Ref.13 Ref.19 Ref.22 Ref.24 Ref.26
	Modified residue	1176	1	Phosphoserine Ref.11 Ref.14
	Modified residue	1178	1	Phosphoserine Ref.11 Ref.14
	Modified residue	1180	1	Phosphoserine; by SRPK2 and PKB/AKT1 Ref.14 Ref.18
	Modified residue	1284	1	Phosphoserine Ref.11
	Modified residue	1329	1	Phosphoserine By similarity
	Modified residue	1331	1	Phosphoserine By similarity
	Modified residue	1332	1	Phosphothreonine By similarity
	Cross-link	5		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.15
Natural variations
	Alternative sequence	1 – 758	758	Missing in isoform 3.		VSP_004026
	Alternative sequence	1 – 727	727	Missing in isoform 2.		VSP_004025
	Alternative sequence	728 – 766	39	GSPKK…IHHTV → MSPADRCRSANTIEPATTSS LALFLLLQRDQSSRTRGLP in isoform 2.		VSP_004028
	Alternative sequence	759 – 766	8	SERIHHTV → MLSESKEG in isoform 3.		VSP_004029
	Alternative sequence	829	1	Missing in isoform 4.		VSP_042204
	Alternative sequence	873 – 884	12	Missing in isoform 4.		VSP_042205
	Natural variant	257	1	R → K. Corresponds to variant rs11555803 [ dbSNP | Ensembl ].		VAR_050632
	Natural variant	311	1	I → M. Corresponds to variant rs3811182 [ dbSNP | Ensembl ].		VAR_022031
	Natural variant	447	1	A → P. Ref.1 Ref.2 Ref.4 Ref.6 Corresponds to variant rs941719 [ dbSNP | Ensembl ].		VAR_061547
	Natural variant	467	1	S → P. Corresponds to variant rs1885097 [ dbSNP | Ensembl ].		VAR_022032
	Natural variant	478	1	S → F. Corresponds to variant rs3751501 [ dbSNP | Ensembl ].		VAR_022033
	Natural variant	1160	1	R → Q in a colorectal cancer sample; somatic mutation. Ref.29		VAR_035777
Experimental info
	Mutagenesis	1093	1	D → A: Abolishes cleavage by CASP3 and chromatin condensation activity. Ref.1
	Sequence conflict	139	1	Q → H in BAA31645. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (L) [UniParc]. Last modified October 5, 2010. Version 2. Checksum: DCCBF310A4680691	FASTA	1,341	151,862
	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
	Isoform 2 (S') [UniParc]. Checksum: 2E994FB0FA922F4C	FASTA	614	70,948
	10 20 30 40 50 60 MSPADRCRSA NTIEPATTSS LALFLLLQRD QSSRTRGLPE EKEEVTMDTS ENRPENDVPE 70 80 90 100 110 120 PPMPIADQVS NDDRPEGSVE DEEKKESSLP KSFKRKISVV SATKGVPAGN SDTEGGQPGR 130 140 150 160 170 180 KRRWGASTAT TQKKPSISIT TESLKSLIPD IKPLAGQEAV VDLHADDSRI SEDETERNGD 190 200 210 220 230 240 DGTHDKGLKI CRTVTQVVPA EGQENGQREE EEEEKEPEAE PPVPPQVSVE VALPPPAEHE 250 260 270 280 290 300 VKKVTLGDTL TRRSISQQKS GVSITIDDPV RTAQVPSPPR GKISNIVHIS NLVRPFTLGQ 310 320 330 340 350 360 LKELLGRTGT LVEEAFWIDK IKSHCFVTYS TVEEAVATRT ALHGVKWPQS NPKFLCADYA 370 380 390 400 410 420 EQDELDYHRG LLVDRPSETK TEEQGIPRPL HPPPPPPVQP PQHPRAEQRE QERAVREQWA 430 440 450 460 470 480 EREREMERRE RTRSEREWDR DKVREGPRSR SRSRDRRRKE RAKSKEKKSE KKEKAQEEPP 490 500 510 520 530 540 AKLLDDLFRK TKAAPCIYWL PLTDSQIVQK EAERAERAKE REKRRKEQEE EEQKEREKEA 550 560 570 580 590 600 ERERNRQLER EKRREHSRER DRERERERER DRGDRDRDRE RDRERGRERD RRDTKRHSRS 610 RSRSTPVRDR GGRR
	Isoform 3 (S) [UniParc]. Checksum: F227265F2F6BBF68	FASTA	583	67,566
	10 20 30 40 50 60 MLSESKEGEE KEEVTMDTSE NRPENDVPEP PMPIADQVSN DDRPEGSVED EEKKESSLPK 70 80 90 100 110 120 SFKRKISVVS ATKGVPAGNS DTEGGQPGRK RRWGASTATT QKKPSISITT ESLKSLIPDI 130 140 150 160 170 180 KPLAGQEAVV DLHADDSRIS EDETERNGDD GTHDKGLKIC RTVTQVVPAE GQENGQREEE 190 200 210 220 230 240 EEEKEPEAEP PVPPQVSVEV ALPPPAEHEV KKVTLGDTLT RRSISQQKSG VSITIDDPVR 250 260 270 280 290 300 TAQVPSPPRG KISNIVHISN LVRPFTLGQL KELLGRTGTL VEEAFWIDKI KSHCFVTYST 310 320 330 340 350 360 VEEAVATRTA LHGVKWPQSN PKFLCADYAE QDELDYHRGL LVDRPSETKT EEQGIPRPLH 370 380 390 400 410 420 PPPPPPVQPP QHPRAEQREQ ERAVREQWAE REREMERRER TRSEREWDRD KVREGPRSRS 430 440 450 460 470 480 RSRDRRRKER AKSKEKKSEK KEKAQEEPPA KLLDDLFRKT KAAPCIYWLP LTDSQIVQKE 490 500 510 520 530 540 AERAERAKER EKRRKEQEEE EQKEREKEAE RERNRQLERE KRREHSRERD RERERERERD 550 560 570 580 RGDRDRDRER DRERGRERDR RDTKRHSRSR SRSTPVRDRG GRR
	Isoform 4 [UniParc]. Checksum: 47A3C106859D46DB	FASTA	1,328	150,557
	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 KRKISVVSTK GVPAGNSDTE 850 860 870 880 890 900 GGQPGRKRRW GASTATTQKK PSISITTESL KEAVVDLHAD DSRISEDETE RNGDDGTHDK 910 920 930 940 950 960 GLKICRTVTQ VVPAEGQENG QREEEEEEKE PEAEPPVPPQ VSVEVALPPP AEHEVKKVTL 970 980 990 1000 1010 1020 GDTLTRRSIS QQKSGVSITI DDPVRTAQVP SPPRGKISNI VHISNLVRPF TLGQLKELLG 1030 1040 1050 1060 1070 1080 RTGTLVEEAF WIDKIKSHCF VTYSTVEEAV ATRTALHGVK WPQSNPKFLC ADYAEQDELD 1090 1100 1110 1120 1130 1140 YHRGLLVDRP SETKTEEQGI PRPLHPPPPP PVQPPQHPRA EQREQERAVR EQWAEREREM 1150 1160 1170 1180 1190 1200 ERRERTRSER EWDRDKVREG PRSRSRSRDR RRKERAKSKE KKSEKKEKAQ EEPPAKLLDD 1210 1220 1230 1240 1250 1260 LFRKTKAAPC IYWLPLTDSQ IVQKEAERAE RAKEREKRRK EQEEEEQKER EKEAERERNR 1270 1280 1290 1300 1310 1320 QLEREKRREH SRERDRERER ERERDRGDRD RDRERDRERG RERDRRDTKR HSRSRSRSTP VRDRGGRR

References

	« Hide 'large scale' referencesShow '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: 10490026] [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: 12508121] [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. , 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: 15489334] [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: 9734811] [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: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 798-813. Tissue: Uterus.
[8]	"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: 16314458] [Abstract] Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, HETERODIMERIZATION, IDENTIFICATION IN A HETEROTRIMERIC COMPLEX, SUBCELLULAR LOCATION, MASS SPECTROMETRY.
[9]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-243; SER-365; SER-386; SER-388; THR-414; SER-657; SER-661; SER-676; THR-682 AND SER-1004, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Global phosphoproteome of HT-29 human colon adenocarcinoma cells." Kim J.-E., Tannenbaum S.R., White F.M. J. Proteome Res. 4:1339-1346(2005) [PubMed: 16083285] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-388 AND SER-710, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma.
[11]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-240; SER-243; SER-328; SER-365; SER-384; SER-386; THR-393; THR-408; SER-410; SER-490; SER-655; SER-657; SER-710; SER-729; SER-1004; SER-1176; SER-1178 AND SER-1284, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254; THR-682 AND SER-1004, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710; SER-714; SER-729 AND SER-1004, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208; SER-216; SER-228; SER-229; THR-254; SER-256; SER-384; SER-386; SER-388; SER-425; SER-561; SER-710; SER-729; SER-814; SER-815; THR-830; SER-838; THR-976; THR-978; SER-981; SER-983; SER-1176; SER-1178 AND SER-1180, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"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: 17370265] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-5, MASS SPECTROMETRY. Tissue: Mammary cancer.
[16]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254; SER-365; SER-657 AND SER-661, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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: 18559500] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-1180 BY SRPK2, INTERACTION WITH SRPK2, SUBCELLULAR LOCATION.
[19]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-424; SER-425; SER-434; SER-453; SER-895; SER-898 AND SER-1004, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-710, MASS SPECTROMETRY. Tissue: T-cell.
[21]	"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: 18438403] [Abstract] Cited for: METHYLATION AT LYS-654, MASS SPECTROMETRY.
[22]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166; SER-169; SER-216; SER-240; SER-243; THR-254; THR-269; SER-295; SER-328; SER-365; SER-384; SER-386; SER-388; THR-393; SER-410; THR-414; SER-425; SER-434; SER-453; SER-490; TYR-512; SER-561; SER-655; SER-657; THR-682; SER-710; SER-714; THR-720; SER-838 AND SER-1004, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, MASS SPECTROMETRY. Tissue: Liver.
[24]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-254; THR-408; SER-410; THR-414; SER-655; SER-657; SER-664; SER-675; SER-676; THR-682; SER-825; SER-838; THR-840 AND SER-1004, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[25]	"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: 19387494] [Abstract] Cited for: INTERACTION WITH API5.
[26]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-243; THR-254; THR-269; SER-328; SER-365; SER-400; THR-408; SER-410; THR-414; SER-478; SER-490; SER-838; SER-987; SER-990 AND SER-1004, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[27]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-717, MASS SPECTROMETRY.
[28]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]	"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. , 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: 16959974] [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.
IPI	IPI00007334. IPI00215975. IPI00297991. IPI00946415.
RefSeq	NP_001158286.1. NM_001164814.1. NP_001158287.1. NM_001164815.1. NP_001158288.1. NM_001164816.1. NP_001158289.1. NM_001164817.1. NP_055792.1. NM_014977.3.
UniGene	Hs.124490.
3D structure databases
ProteinModelPortal	Q9UKV3.
SMR	Q9UKV3. Positions 72-104.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UKV3. 7 interactions.
MINT	MINT-5006704.
STRING	Q9UKV3.
Protein family/group databases
TCDB	3.A.18.1.1. nuclear mRNA exporter (mRNA-E) family.
PTM databases
PhosphoSite	Q9UKV3.
Polymorphism databases
DMDM	308153407.
Proteomic databases
PRIDE	Q9UKV3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262710; ENSP00000262710; ENSG00000100813.
GeneID	22985.
KEGG	hsa:22985.
UCSC	uc001wip.2. human. uc001wir.2. human. uc001wit.2. human.
Organism-specific databases
CTD	22985.
GeneCards	GC14M023527.
H-InvDB	HIX0011531.
HGNC	HGNC:17066. ACIN1.
HPA	HPA000657.
MIM	604562. gene.
neXtProt	NX_Q9UKV3.
PharmGKB	PA134912489.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG17620.
GeneTree	ENSGT00570000079212.
HOGENOM	HBG125341.
HOVERGEN	HBG050449.
InParanoid	Q9UKV3.
OMA	RADRNLK.
OrthoDB	EOG45QHCG.
PhylomeDB	Q9UKV3.
Enzyme and pathway databases
Reactome	REACT_578. Apoptosis.
Gene expression databases
ArrayExpress	Q9UKV3.
Bgee	Q9UKV3.
CleanEx	HS_ACIN1.
Genevestigator	Q9UKV3.
GermOnline	ENSG00000100813. Homo sapiens.
Family and domain databases
InterPro	IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. IPR003034. SAP_DNA-bd. [Graphical view]
Gene3D	G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.
KO	K12875.
Pfam	PF02037. SAP. 1 hit. [Graphical view]
SMART	SM00360. RRM. 1 hit. SM00513. SAP. 1 hit. [Graphical view]
PROSITE	PS50800. SAP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	43823.
PMAP-CutDB	Q9UKV3.
SOURCE	Search...

Entry information

Entry name

ACINU_HUMAN

Accession

Primary (citable) accession number: Q9UKV3
Secondary accession number(s): B2RTT4 , D3DS45, O75158, Q9UG91, Q9UKV1, Q9UKV2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 28, 2003
Last sequence update:	October 5, 2010
Last modified:	January 25, 2012
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.