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Protein

Apoptotic chromatin condensation inducer in the nucleus

Gene

Acin1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Apoptosis, mRNA processing, mRNA splicing

Enzyme and pathway databases

ReactomeiR-MMU-111465. Apoptotic cleavage of cellular proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Apoptotic chromatin condensation inducer in the nucleus
Short name:
Acinus
Gene namesi
Name:Acin1
Synonyms:Acinus
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1891824. Acin1.

Subcellular locationi

  • Nucleus By similarity
  • Nucleus speckle By similarity
  • Nucleusnucleoplasm By similarity

  • Note: Phosphorylation on Ser-1179 by SRPK2 redistributes it from the nuclear speckles to the nucleoplasm.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13381338Apoptotic chromatin condensation inducer in the nucleusPRO_0000064437Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki5 – 5Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei166 – 1661PhosphoserineBy similarity
Modified residuei169 – 1691PhosphoserineBy similarity
Modified residuei208 – 2081PhosphoserineBy similarity
Modified residuei210 – 2101PhosphoserineBy similarity
Modified residuei216 – 2161PhosphoserineCombined sources
Modified residuei242 – 2421PhosphoserineBy similarity
Modified residuei253 – 2531PhosphothreonineBy similarity
Modified residuei295 – 2951PhosphoserineCombined sources
Cross-linki318 – 318Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei332 – 3321PhosphoserineBy similarity
Modified residuei369 – 3691PhosphoserineBy similarity
Modified residuei387 – 3871PhosphoserineCombined sources
Modified residuei389 – 3891PhosphoserineCombined sources
Modified residuei391 – 3911PhosphoserineCombined sources
Modified residuei413 – 4131PhosphoserineCombined sources
Modified residuei417 – 4171PhosphothreonineCombined sources
Modified residuei454 – 4541PhosphoserineCombined sources
Modified residuei477 – 4771PhosphoserineCombined sources
Modified residuei479 – 4791PhosphoserineCombined sources
Modified residuei491 – 4911PhosphoserineCombined sources
Modified residuei497 – 4971PhosphoserineCombined sources
Modified residuei561 – 5611PhosphoserineBy similarity
Modified residuei654 – 6541N6,N6,N6-trimethyllysine; by EHMT2; alternateBy similarity
Modified residuei654 – 6541N6,N6-dimethyllysine; by EHMT2; alternateBy similarity
Modified residuei655 – 6551PhosphoserineBy similarity
Modified residuei657 – 6571PhosphoserineBy similarity
Modified residuei710 – 7101PhosphoserineCombined sources
Modified residuei729 – 7291PhosphoserineBy similarity
Modified residuei825 – 8251PhosphoserineBy similarity
Modified residuei838 – 8381PhosphoserineCombined sources
Modified residuei861 – 8611N6-acetyllysineCombined sources
Modified residuei895 – 8951PhosphoserineBy similarity
Modified residuei898 – 8981PhosphoserineCombined sources
Modified residuei986 – 9861PhosphoserineCombined sources
Modified residuei989 – 9891PhosphoserineBy similarity
Modified residuei1003 – 10031PhosphoserineCombined sources
Modified residuei1179 – 11791Phosphoserine; by SRPK2 and PKB/AKT1By similarity

Post-translational modificationi

Undergoes proteolytic cleavage; the processed form is active, contrary to the uncleaved form.By similarity
Phosphorylation on Ser-1179 by SRPK2 up-regulates its stimulatory effect on cyclin A1.By similarity

Sites

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

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9JIX8.
MaxQBiQ9JIX8.
PaxDbiQ9JIX8.
PRIDEiQ9JIX8.

PTM databases

iPTMnetiQ9JIX8.
PhosphoSiteiQ9JIX8.

Expressioni

Gene expression databases

BgeeiQ9JIX8.
CleanExiMM_ACIN1.
ExpressionAtlasiQ9JIX8. baseline and differential.
GenevisibleiQ9JIX8. MM.

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi207849. 2 interactions.
IntActiQ9JIX8. 3 interactions.
MINTiMINT-1867001.
STRINGi10090.ENSMUSP00000022793.

Structurei

3D structure databases

ProteinModelPortaliQ9JIX8.
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
Regioni1209 – 123628Sufficient for interaction with RNPS1 and SAP18 and formation of th ASAP complexBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi142 – 443302Glu-richAdd
BLAST
Compositional biasi569 – 66799Ser-richAdd
BLAST
Compositional biasi1113 – 113018Pro-richAdd
BLAST
Compositional biasi1131 – 1338208Arg/Asp/Glu/Lys-richAdd
BLAST

Sequence similaritiesi

Contains 1 SAP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2416. Eukaryota.
ENOG4111HR1. LUCA.
GeneTreeiENSGT00710000106790.
HOVERGENiHBG050449.
InParanoidiQ9JIX8.
KOiK12875.
OMAiLESERTH.
OrthoDBiEOG76MK8M.
TreeFamiTF320727.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR032552. RSB_motif.
IPR003034. SAP_dom.
[Graphical view]
PfamiPF16294. RSB_motif. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTiSM00513. SAP. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50800. SAP. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9JIX8-1) [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

        10         20         30         40         50
MWGRKRPNSS GETRGILSGN RGVDYGSGRG QSGPFEGRWR KLPKMPEAVG
60 70 80 90 100
TDPSTSRKMA ELEEVTLDGK PLQALRVTDL KAALEQRGLA KSGQKSALVK
110 120 130 140 150
RLKGALMLEN LQKHSTPHAA FQPNSQIGEE MSQNSFIKQY LEKQQELLRQ
160 170 180 190 200
RLEREAREAA ELEEASAESE DEMTHPEGVA SLLPPDFQSS LNRPELELST
210 220 230 240 250
HSPRKSSSFS EEKGESDDEK PRKGERRSSR VRQAKSKLPE YSQTAEEEED
260 270 280 290 300
QETPSRNLRV RADRNLKIEE EEEEEEEEED DDDEEEEEVD EAQKSREAEA
310 320 330 340 350
PTLKQFEDEE GEERTRAKPE KVVDEKPLNI RSQEKGELEK GGRVTRSQEE
360 370 380 390 400
ARRSHLARQQ QEKETQIVSL PQEENEVKSS QSLEEKSQSP SPPPLPEDLE
410 420 430 440 450
KAPVVLQPEQ IVSEEETPPP LLTKEASSPP THIQLQEEME PVEGPAPPVL
460 470 480 490 500
IQLSPPNTDA GAREPLASPH PAQLLRSLSP LSGTTDTKAE SPAGRVSDES
510 520 530 540 550
VLPLAQKSSL PECSTQKGVE SEREKSAPLP LTVEEFAPAK GITEEPMKKQ
560 570 580 590 600
SLEQKEGRRA SHALFPEHSG KQSADSSSSR SSSPSSSSSP SRSPSPDSVA
610 620 630 640 650
SRPQSSPGSK QRDGAQARVH ANPHERPKMG SRSTSESRSR SRSRSRSASS
660 670 680 690 700
SSRKSLSPGV SRDSNTSYTE TKDPSCGQEA AAPSGPQLQV LEPKEKAPTF
710 720 730 740 750
SASVRGRHLS HPEPEQQHVI QRLQPEQGSP KKCEAEEAEP PAATQPQTSE
760 770 780 790 800
TQISHLLESE RTHHTVEEKE EVTMDTSENR PENEVPEPPL PVADQVSNDE
810 820 830 840 850
RPEGGAEEEE KKESSMPKSF KRKISVVSAT KGVQAGNSDT EGGQPGRKRR
860 870 880 890 900
WGASTAATQK KPSISITTES LKSLIPDIKP LAGQEAVVDL HADDSRISED
910 920 930 940 950
ETERNGDDGT HDKGLKICRT VTQVVPAEGQ ENGQREEEEE KEPEAELPAP
960 970 980 990 1000
PQVSVEVALP PPVEHEVKKV TLGDTLTRRS ISQQKSGVSI TIDDPVRTAQ
1010 1020 1030 1040 1050
VPSPPRGKIS NIVHISNLVR PFTLGQLKEL LGRTGTLVEE AFWIDKIKSH
1060 1070 1080 1090 1100
CFVTYSTVEE AVATRTALHG VKWPQSNPKF LCADYAEQDE LDYHRGLLVD
1110 1120 1130 1140 1150
RPSETKAEEQ GAPRPLHPPP PPPVQPPPHP RAEQREQERA VREQWAERER
1160 1170 1180 1190 1200
EMERRERTRS EREWDRDKVR EGPRSRSRSR DRRRKERAKS KEKKSEKKEK
1210 1220 1230 1240 1250
AQEEPPAKLL DDLFRKTKAA PCIYWLPLTE SQIVQKEAEQ AERAKEREKR
1260 1270 1280 1290 1300
RKEREEEEQK EREKEAERER NRQLEREKRR EHSRERERDR ERERDRGDRE
1310 1320 1330
RERERDRDRG RERDRRDTKR HSRSRSRSTP VRDRGGRR
Length:1,338
Mass (Da):150,719
Last modified:July 27, 2011 - v3
Checksum:i683E56058723C9D8
GO
Isoform 2 (identifier: Q9JIX8-2) [UniParc]FASTAAdd to basket

Also known as: S

The sequence of this isoform differs from the canonical sequence as follows:
     1-757: Missing.
     758-766: ESERTHHTV → MMFSDSRAG

Show »
Length:581
Mass (Da):67,185
Checksum:i38C74E0629009255
GO
Isoform 3 (identifier: Q9JIX8-3) [UniParc]FASTAAdd to basket

Also known as: S'

The sequence of this isoform differs from the canonical sequence as follows:
     1-773: Missing.

Show »
Length:565
Mass (Da):65,357
Checksum:iA68FF1692E30B303
GO
Isoform 4 (identifier: Q9JIX8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     164-204: EASAESEDEMTHPEGVASLLPPDFQSSLNRPELELSTHSPR → G

Show »
Length:1,298
Mass (Da):146,302
Checksum:iFFEC0D9BF7838055
GO

Sequence cautioni

The sequence AAF89661.1 differs from that shown. Reason: Frameshift at positions 110 and 112. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti244 – 2441T → A in AAF89661 (Ref. 2) Curated
Sequence conflicti515 – 5151T → A in AAF89661 (Ref. 2) Curated
Sequence conflicti536 – 5361F → L in AAF89661 (Ref. 2) Curated
Sequence conflicti557 – 5571G → D in AAF89661 (Ref. 2) Curated
Sequence conflicti568 – 5681H → Y in AAF89661 (Ref. 2) Curated
Sequence conflicti599 – 5991V → A in AAF89661 (Ref. 2) Curated
Sequence conflicti729 – 7291S → I in AAF89661 (Ref. 2) Curated
Sequence conflicti757 – 7571L → P in AAF89661 (Ref. 2) Curated
Sequence conflicti773 – 7731T → A in AAD56723 (PubMed:10490026).Curated
Sequence conflicti829 – 8291Missing in BAB28030 (PubMed:16141072).Curated
Sequence conflicti896 – 8961R → Q in AAD56723 (PubMed:10490026).Curated
Sequence conflicti896 – 8961R → Q in AAD56727 (PubMed:10490026).Curated
Sequence conflicti896 – 8961R → Q in AAF89661 (Ref. 2) Curated
Sequence conflicti1035 – 10351G → R in BAB28030 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 773773Missing in isoform 3. 1 PublicationVSP_004031Add
BLAST
Alternative sequencei1 – 757757Missing in isoform 2. 2 PublicationsVSP_004030Add
BLAST
Alternative sequencei164 – 20441EASAE…THSPR → G in isoform 4. 1 PublicationVSP_004032Add
BLAST
Alternative sequencei758 – 7669ESERTHHTV → MMFSDSRAG in isoform 2. 2 PublicationsVSP_004033

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF124725 mRNA. Translation: AAD56723.1.
AF124729 mRNA. Translation: AAD56727.1.
AF168782 mRNA. Translation: AAF89661.1. Frameshift.
CT009512 Genomic DNA. Translation: CAX15406.1.
AK011698 mRNA. No translation available.
AK012099 mRNA. Translation: BAB28030.1.
AK012337 mRNA. Translation: BAB28171.3.
AK050467 mRNA. Translation: BAC34272.1.
CCDSiCCDS27097.1. [Q9JIX8-1]
CCDS49492.1. [Q9JIX8-2]
CCDS56957.1. [Q9JIX8-3]
RefSeqiNP_001078942.2. NM_001085473.2.
NP_001229534.1. NM_001242605.1. [Q9JIX8-3]
NP_062513.3. NM_019567.3.
NP_075679.2. NM_023190.3. [Q9JIX8-1]
XP_006519361.1. XM_006519298.2. [Q9JIX8-4]
XP_006519367.1. XM_006519304.2. [Q9JIX8-3]
UniGeneiMm.297078.

Genome annotation databases

EnsembliENSMUST00000022793; ENSMUSP00000022793; ENSMUSG00000022185. [Q9JIX8-1]
ENSMUST00000111484; ENSMUSP00000107109; ENSMUSG00000022185. [Q9JIX8-4]
ENSMUST00000126166; ENSMUSP00000114546; ENSMUSG00000022185. [Q9JIX8-3]
ENSMUST00000148754; ENSMUSP00000122003; ENSMUSG00000022185. [Q9JIX8-2]
ENSMUST00000167015; ENSMUSP00000125776; ENSMUSG00000022185. [Q9JIX8-2]
GeneIDi56215.
KEGGimmu:56215.
UCSCiuc007twr.2. mouse. [Q9JIX8-3]
uc007twv.2. mouse. [Q9JIX8-1]
uc007twx.2. mouse. [Q9JIX8-4]
uc011zld.1. mouse. [Q9JIX8-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF124725 mRNA. Translation: AAD56723.1.
AF124729 mRNA. Translation: AAD56727.1.
AF168782 mRNA. Translation: AAF89661.1. Frameshift.
CT009512 Genomic DNA. Translation: CAX15406.1.
AK011698 mRNA. No translation available.
AK012099 mRNA. Translation: BAB28030.1.
AK012337 mRNA. Translation: BAB28171.3.
AK050467 mRNA. Translation: BAC34272.1.
CCDSiCCDS27097.1. [Q9JIX8-1]
CCDS49492.1. [Q9JIX8-2]
CCDS56957.1. [Q9JIX8-3]
RefSeqiNP_001078942.2. NM_001085473.2.
NP_001229534.1. NM_001242605.1. [Q9JIX8-3]
NP_062513.3. NM_019567.3.
NP_075679.2. NM_023190.3. [Q9JIX8-1]
XP_006519361.1. XM_006519298.2. [Q9JIX8-4]
XP_006519367.1. XM_006519304.2. [Q9JIX8-3]
UniGeneiMm.297078.

3D structure databases

ProteinModelPortaliQ9JIX8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207849. 2 interactions.
IntActiQ9JIX8. 3 interactions.
MINTiMINT-1867001.
STRINGi10090.ENSMUSP00000022793.

PTM databases

iPTMnetiQ9JIX8.
PhosphoSiteiQ9JIX8.

Proteomic databases

EPDiQ9JIX8.
MaxQBiQ9JIX8.
PaxDbiQ9JIX8.
PRIDEiQ9JIX8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000022793; ENSMUSP00000022793; ENSMUSG00000022185. [Q9JIX8-1]
ENSMUST00000111484; ENSMUSP00000107109; ENSMUSG00000022185. [Q9JIX8-4]
ENSMUST00000126166; ENSMUSP00000114546; ENSMUSG00000022185. [Q9JIX8-3]
ENSMUST00000148754; ENSMUSP00000122003; ENSMUSG00000022185. [Q9JIX8-2]
ENSMUST00000167015; ENSMUSP00000125776; ENSMUSG00000022185. [Q9JIX8-2]
GeneIDi56215.
KEGGimmu:56215.
UCSCiuc007twr.2. mouse. [Q9JIX8-3]
uc007twv.2. mouse. [Q9JIX8-1]
uc007twx.2. mouse. [Q9JIX8-4]
uc011zld.1. mouse. [Q9JIX8-2]

Organism-specific databases

CTDi22985.
MGIiMGI:1891824. Acin1.

Phylogenomic databases

eggNOGiKOG2416. Eukaryota.
ENOG4111HR1. LUCA.
GeneTreeiENSGT00710000106790.
HOVERGENiHBG050449.
InParanoidiQ9JIX8.
KOiK12875.
OMAiLESERTH.
OrthoDBiEOG76MK8M.
TreeFamiTF320727.

Enzyme and pathway databases

ReactomeiR-MMU-111465. Apoptotic cleavage of cellular proteins.

Miscellaneous databases

ChiTaRSiAcin1. mouse.
NextBioi312066.
PROiQ9JIX8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JIX8.
CleanExiMM_ACIN1.
ExpressionAtlasiQ9JIX8. baseline and differential.
GenevisibleiQ9JIX8. MM.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR032552. RSB_motif.
IPR003034. SAP_dom.
[Graphical view]
PfamiPF16294. RSB_motif. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTiSM00513. SAP. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50800. SAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 2 AND 3).
  2. "Molecular cloning of murine acinusL, a gene for apoptotic chromatin condensation."
    Mamoru A., Setsuko S., Yoshihide T.
    Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-284 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1190 (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-806 (ISOFORM 4).
    Strain: C57BL/6J.
    Tissue: Embryo and Pancreatic islet.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-391; SER-479; SER-491 AND SER-710, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "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: INTERACTION WITH SRPK2.
  7. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
    Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
    J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1003, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND SER-710, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479; SER-491 AND SER-1003, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-387; SER-389; SER-391; SER-413; THR-417; SER-454; SER-477; SER-479; SER-491; SER-497; SER-710; SER-838; SER-898; SER-986 AND SER-1003, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  11. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-861, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiACINU_MOUSE
AccessioniPrimary (citable) accession number: Q9JIX8
Secondary accession number(s): B8JJ87
, Q9CSN7, Q9CSR9, Q9CSX7, Q9R046, Q9R047
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 28, 2003
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.