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Protein

Apoptotic chromatin condensation inducer in the nucleus

Gene

ACIN1

Organism
Homo sapiens (Human)
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.5 Publications

GO - Molecular functioni

  • ATPase activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • nucleic acid binding Source: UniProtKB
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • apoptotic chromosome condensation Source: UniProtKB
  • cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  • erythrocyte differentiation Source: UniProtKB
  • mRNA processing Source: UniProtKB-KW
  • negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of monocyte differentiation Source: UniProtKB
  • RNA splicing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Apoptosis, mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-111465. Apoptotic cleavage of cellular proteins.
SIGNORiQ9UKV3.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:17066. ACIN1.

Subcellular locationi

GO - Cellular componenti

  • ASAP complex Source: UniProtKB
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • nuclear speck Source: UniProtKB
  • nucleolus Source: Ensembl
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi1093D → A: Abolishes cleavage by CASP3 and chromatin condensation activity. 1 Publication1

Organism-specific databases

DisGeNETi22985.
OpenTargetsiENSG00000100813.
PharmGKBiPA134912489.

Polymorphism and mutation databases

BioMutaiACIN1.
DMDMi308153407.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000644361 – 1341Apoptotic chromatin condensation inducer in the nucleusAdd BLAST1341

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei132PhosphoserineCombined sources1
Modified residuei166PhosphoserineCombined sources1
Modified residuei169PhosphoserineCombined sources1
Modified residuei208PhosphoserineCombined sources1
Modified residuei210PhosphoserineCombined sources1
Modified residuei216PhosphoserineCombined sources1
Modified residuei240PhosphoserineCombined sources1
Modified residuei243PhosphoserineCombined sources1
Modified residuei254PhosphothreonineCombined sources1
Cross-linki268Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei269PhosphothreonineCombined sources1
Modified residuei295PhosphoserineCombined sources1
Cross-linki305Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki315Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei326PhosphothreonineCombined sources1
Modified residuei328PhosphoserineCombined sources1
Modified residuei365PhosphoserineCombined sources1
Modified residuei384PhosphoserineCombined sources1
Modified residuei386PhosphoserineCombined sources1
Modified residuei388PhosphoserineCombined sources1
Modified residuei393PhosphothreonineCombined sources1
Modified residuei400PhosphoserineCombined sources1
Modified residuei410PhosphoserineCombined sources1
Modified residuei414PhosphothreonineCombined sources1
Modified residuei420PhosphothreonineCombined sources1
Modified residuei434PhosphoserineCombined sources1
Modified residuei453PhosphoserineCombined sources1
Modified residuei478PhosphoserineCombined sources1
Modified residuei490PhosphoserineCombined sources1
Modified residuei512PhosphotyrosineCombined sources1
Modified residuei522PhosphoserineCombined sources1
Cross-linki532Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei561PhosphoserineCombined sources1
Modified residuei654N6,N6,N6-trimethyllysine; by EHMT2; alternate1 Publication1
Modified residuei654N6,N6-dimethyllysine; by EHMT2; alternate1 Publication1
Modified residuei655PhosphoserineCombined sources1
Modified residuei657PhosphoserineCombined sources1
Modified residuei682PhosphothreonineCombined sources1
Modified residuei710PhosphoserineCombined sources1
Modified residuei714PhosphoserineCombined sources1
Modified residuei717N6-acetyllysineCombined sources1
Modified residuei720PhosphothreonineCombined sources1
Modified residuei729PhosphoserineCombined sources1
Modified residuei825PhosphoserineCombined sources1
Modified residuei838PhosphoserineCombined sources1
Modified residuei861N6-acetyllysineBy similarity1
Modified residuei895PhosphoserineCombined sources1
Modified residuei898PhosphoserineCombined sources1
Modified residuei976PhosphothreonineCombined sources1
Modified residuei987PhosphoserineCombined sources1
Modified residuei990PhosphoserineCombined sources1
Modified residuei1004PhosphoserineCombined sources1
Modified residuei1180Phosphoserine; by SRPK2 and PKB/AKT11 Publication1
Isoform 4 (identifier: Q9UKV3-5)
Modified residuei825PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylation on Ser-1180 by SRPK2 up-regulates its stimulatory effect on cyclin A1.1 Publication
Undergoes proteolytic cleavage; the processed form is active, contrary to the uncleaved form.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1093 – 1094Cleavage; by caspase-32

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9UKV3.
PaxDbiQ9UKV3.
PeptideAtlasiQ9UKV3.
PRIDEiQ9UKV3.

PTM databases

iPTMnetiQ9UKV3.
PhosphoSitePlusiQ9UKV3.
SwissPalmiQ9UKV3.

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

BgeeiENSG00000100813.
CleanExiHS_ACIN1.
ExpressionAtlasiQ9UKV3. baseline and differential.
GenevisibleiQ9UKV3. HS.

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

GO - Molecular functioni

  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116634. 112 interactors.
DIPiDIP-32963N.
IntActiQ9UKV3. 27 interactors.
MINTiMINT-5006704.
STRINGi9606.ENSP00000262710.

Structurei

3D structure databases

ProteinModelPortaliQ9UKV3.
SMRiQ9UKV3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini72 – 106SAPPROSITE-ProRule annotationAdd BLAST35

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1210 – 1237Sufficient for interaction with RNPS1 and SAP18 and formation of th ASAP complexBy similarityAdd BLAST28

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi142 – 442Glu-richAdd BLAST301
Compositional biasi573 – 676Ser-richAdd BLAST104
Compositional biasi1114 – 1131Pro-richAdd BLAST18
Compositional biasi1132 – 1341Arg/Asp/Glu/Lys-richAdd BLAST210

Sequence similaritiesi

Contains 1 SAP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2416. Eukaryota.
ENOG4111HR1. LUCA.
GeneTreeiENSGT00710000106790.
HOGENOMiHOG000088615.
HOVERGENiHBG050449.
InParanoidiQ9UKV3.
KOiK12875.
OMAiPENDVPE.
OrthoDBiEOG091G0MO8.
PhylomeDBiQ9UKV3.
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: 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

        10         20         30         40         50
MWRRKHPRTS GGTRGVLSGN RGVEYGSGRG HLGTFEGRWR 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 DEMIHPEGVA SLLPPDFQSS LERPELELSR
210 220 230 240 250
HSPRKSSSIS EEKGDSDDEK PRKGERRSSR VRQARAAKLS EGSQPAEEEE
260 270 280 290 300
DQETPSRNLR VRADRNLKTE EEEEEEEEEE EDDEEEEGDD EGQKSREAPI
310 320 330 340 350
LKEFKEEGEE IPRVKPEEMM DERPKTRSQE QEVLERGGRF TRSQEEARKS
360 370 380 390 400
HLARQQQEKE MKTTSPLEEE EREIKSSQGL KEKSKSPSPP RLTEDRKKAS
410 420 430 440 450
LVALPEQTAS EEETPPPLLT KEASSPPPHP QLHSEEEIEP MEGPAPAVLI
460 470 480 490 500
QLSPPNTDAD TRELLVSQHT VQLVGGLSPL SSPSDTKAES PAEKVPEESV
510 520 530 540 550
LPLVQKSTLA DYSAQKDLEP ESDRSAQPLP LKIEELALAK GITEECLKQP
560 570 580 590 600
SLEQKEGRRA SHTLLPSHRL KQSADSSSSR SSSSSSSSSR SRSRSPDSSG
610 620 630 640 650
SRSHSPLRSK QRDVAQARTH ANPRGRPKMG SRSTSESRSR SRSRSRSASS
660 670 680 690 700
NSRKSLSPGV SRDSSTSYTE TKDPSSGQEV ATPPVPQLQV CEPKERTSTS
710 720 730 740 750
SSSVQARRLS QPESAEKHVT QRLQPERGSP KKCEAEEAEP PAATQPQTSE
760 770 780 790 800
TQTSHLPESE RIHHTVEEKE EVTMDTSENR PENDVPEPPM PIADQVSNDD
810 820 830 840 850
RPEGSVEDEE KKESSLPKSF KRKISVVSAT KGVPAGNSDT EGGQPGRKRR
860 870 880 890 900
WGASTATTQK KPSISITTES LKSLIPDIKP LAGQEAVVDL HADDSRISED
910 920 930 940 950
ETERNGDDGT HDKGLKICRT VTQVVPAEGQ ENGQREEEEE EKEPEAEPPV
960 970 980 990 1000
PPQVSVEVAL PPPAEHEVKK VTLGDTLTRR SISQQKSGVS ITIDDPVRTA
1010 1020 1030 1040 1050
QVPSPPRGKI SNIVHISNLV RPFTLGQLKE LLGRTGTLVE EAFWIDKIKS
1060 1070 1080 1090 1100
HCFVTYSTVE EAVATRTALH GVKWPQSNPK FLCADYAEQD ELDYHRGLLV
1110 1120 1130 1140 1150
DRPSETKTEE QGIPRPLHPP PPPPVQPPQH PRAEQREQER AVREQWAERE
1160 1170 1180 1190 1200
REMERRERTR SEREWDRDKV REGPRSRSRS RDRRRKERAK SKEKKSEKKE
1210 1220 1230 1240 1250
KAQEEPPAKL LDDLFRKTKA APCIYWLPLT DSQIVQKEAE RAERAKEREK
1260 1270 1280 1290 1300
RRKEQEEEEQ KEREKEAERE RNRQLEREKR REHSRERDRE RERERERDRG
1310 1320 1330 1340
DRDRDRERDR ERGRERDRRD TKRHSRSRSR STPVRDRGGR R
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)DescriptionActionsGraphical viewLength
Sequence conflicti139Q → H in BAA31645 (Ref. 2) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_050632257R → K.Corresponds to variant rs11555803dbSNPEnsembl.1
Natural variantiVAR_022031311I → M.Corresponds to variant rs3811182dbSNPEnsembl.1
Natural variantiVAR_061547447A → P.Combined sources5 PublicationsCorresponds to variant rs941719dbSNPEnsembl.1
Natural variantiVAR_022032467S → P.Corresponds to variant rs1885097dbSNPEnsembl.1
Natural variantiVAR_022033478S → F.Corresponds to variant rs3751501dbSNPEnsembl.1
Natural variantiVAR_0357771160R → Q in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs754494408dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0040261 – 758Missing in isoform 3. 2 PublicationsAdd BLAST758
Alternative sequenceiVSP_0040251 – 727Missing in isoform 2. 1 PublicationAdd BLAST727
Alternative sequenceiVSP_004028728 – 766GSPKK…IHHTV → MSPADRCRSANTIEPATTSS LALFLLLQRDQSSRTRGLP in isoform 2. 1 PublicationAdd BLAST39
Alternative sequenceiVSP_004029759 – 766SERIHHTV → MLSESKEG in isoform 3. 2 Publications8
Alternative sequenceiVSP_042204829Missing in isoform 4. 1 Publication1
Alternative sequenceiVSP_042205873 – 884Missing in isoform 4. 1 PublicationAdd BLAST12

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.5. human. [Q9UKV3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ9UKV3.
SMRiQ9UKV3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116634. 112 interactors.
DIPiDIP-32963N.
IntActiQ9UKV3. 27 interactors.
MINTiMINT-5006704.
STRINGi9606.ENSP00000262710.

Protein family/group databases

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

PTM databases

iPTMnetiQ9UKV3.
PhosphoSitePlusiQ9UKV3.
SwissPalmiQ9UKV3.

Polymorphism and mutation databases

BioMutaiACIN1.
DMDMi308153407.

Proteomic databases

EPDiQ9UKV3.
PaxDbiQ9UKV3.
PeptideAtlasiQ9UKV3.
PRIDEiQ9UKV3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.5. human. [Q9UKV3-1]

Organism-specific databases

CTDi22985.
DisGeNETi22985.
GeneCardsiACIN1.
HGNCiHGNC:17066. ACIN1.
HPAiHPA000657.
MIMi604562. gene.
neXtProtiNX_Q9UKV3.
OpenTargetsiENSG00000100813.
PharmGKBiPA134912489.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2416. Eukaryota.
ENOG4111HR1. LUCA.
GeneTreeiENSGT00710000106790.
HOGENOMiHOG000088615.
HOVERGENiHBG050449.
InParanoidiQ9UKV3.
KOiK12875.
OMAiPENDVPE.
OrthoDBiEOG091G0MO8.
PhylomeDBiQ9UKV3.
TreeFamiTF320727.

Enzyme and pathway databases

ReactomeiR-HSA-111465. Apoptotic cleavage of cellular proteins.
SIGNORiQ9UKV3.

Miscellaneous databases

ChiTaRSiACIN1. human.
GeneWikiiACIN1.
GenomeRNAii22985.
PMAP-CutDBQ9UKV3.
PROiQ9UKV3.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100813.
CleanExiHS_ACIN1.
ExpressionAtlasiQ9UKV3. baseline and differential.
GenevisibleiQ9UKV3. HS.

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...

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: November 2, 2016
This is version 163 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

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.