UniProtKB - Q9UKV3 (ACINU_HUMAN)
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>sp|Q9UKV3|ACINU_HUMAN Apoptotic chromatin condensation inducer in the nucleus OS=Homo sapiens OX=9606 GN=ACIN1 PE=1 SV=2 MWRRKHPRTSGGTRGVLSGNRGVEYGSGRGHLGTFEGRWRKLPKMPEAVGTDPSTSRKMA ELEEVTLDGKPLQALRVTDLKAALEQRGLAKSGQKSALVKRLKGALMLENLQKHSTPHAA FQPNSQIGEEMSQNSFIKQYLEKQQELLRQRLEREAREAAELEEASAESEDEMIHPEGVA SLLPPDFQSSLERPELELSRHSPRKSSSISEEKGDSDDEKPRKGERRSSRVRQARAAKLS EGSQPAEEEEDQETPSRNLRVRADRNLKTEEEEEEEEEEEEDDEEEEGDDEGQKSREAPI LKEFKEEGEEIPRVKPEEMMDERPKTRSQEQEVLERGGRFTRSQEEARKSHLARQQQEKE MKTTSPLEEEEREIKSSQGLKEKSKSPSPPRLTEDRKKASLVALPEQTASEEETPPPLLT KEASSPPPHPQLHSEEEIEPMEGPAPAVLIQLSPPNTDADTRELLVSQHTVQLVGGLSPL SSPSDTKAESPAEKVPEESVLPLVQKSTLADYSAQKDLEPESDRSAQPLPLKIEELALAK GITEECLKQPSLEQKEGRRASHTLLPSHRLKQSADSSSSRSSSSSSSSSRSRSRSPDSSG SRSHSPLRSKQRDVAQARTHANPRGRPKMGSRSTSESRSRSRSRSRSASSNSRKSLSPGV SRDSSTSYTETKDPSSGQEVATPPVPQLQVCEPKERTSTSSSSVQARRLSQPESAEKHVT QRLQPERGSPKKCEAEEAEPPAATQPQTSETQTSHLPESERIHHTVEEKEEVTMDTSENR PENDVPEPPMPIADQVSNDDRPEGSVEDEEKKESSLPKSFKRKISVVSATKGVPAGNSDT EGGQPGRKRRWGASTATTQKKPSISITTESLKSLIPDIKPLAGQEAVVDLHADDSRISED ETERNGDDGTHDKGLKICRTVTQVVPAEGQENGQREEEEEEKEPEAEPPVPPQVSVEVAL PPPAEHEVKKVTLGDTLTRRSISQQKSGVSITIDDPVRTAQVPSPPRGKISNIVHISNLV RPFTLGQLKELLGRTGTLVEEAFWIDKIKSHCFVTYSTVEEAVATRTALHGVKWPQSNPK FLCADYAEQDELDYHRGLLVDRPSETKTEEQGIPRPLHPPPPPPVQPPQHPRAEQREQER AVREQWAEREREMERRERTRSEREWDRDKVREGPRSRSRSRDRRRKERAKSKEKKSEKKE KAQEEPPAKLLDDLFRKTKAAPCIYWLPLTDSQIVQKEAERAERAKEREKRRKEQEEEEQ KEREKEAERERNRQLEREKRREHSRERDRERERERERDRGDRDRDRERDRERGRERDRRD TKRHSRSRSRSTPVRDRGGRRHelp videoAdd a publicationFeedback
Protein
Apoptotic chromatin condensation inducer in the nucleus
Gene
ACIN1
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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. - Ref.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. - Ref.12"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. - Ref.26"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. - Ref.27"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.
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
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.27"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.
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- ATPase activity Source: UniProtKB
<p>Non-traceable Author Statement</p>
<p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p>
Non-traceable author statementi
- Ref.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.
- enzyme binding Source: UniProtKBNon-traceable author statementi
- Ref.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.
- nucleic acid binding Source: UniProtKBNon-traceable author statementi
- Ref.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.
- RNA binding Source: UniProtKBInferred from high throughput direct assayi
- "Insights into RNA biology from an atlas of mammalian mRNA-binding proteins."
Castello A., Fischer B., Eichelbaum K., Horos R., Beckmann B.M., Strein C., Davey N.E., Humphreys D.T., Preiss T., Steinmetz L.M., Krijgsveld J., Hentze M.W.
Cell 149:1393-1406(2012) [PubMed] [Europe PMC] [Abstract] - "The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts."
Baltz A.G., Munschauer M., Schwanhausser B., Vasile A., Murakawa Y., Schueler M., Youngs N., Penfold-Brown D., Drew K., Milek M., Wyler E., Bonneau R., Selbach M., Dieterich C., Landthaler M.
Mol. Cell 46:674-690(2012) [PubMed] [Europe PMC] [Abstract]
GO - Biological processi
- apoptotic chromosome condensation Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.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.
- erythrocyte differentiation Source: UniProtKB
<p>Inferred from Expression Pattern</p>
<p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p>
Inferred from expression patterni
- "Caspase activation is required for terminal erythroid differentiation."
Zermati Y., Garrido C., Amsellem S., Fishelson S., Bouscary D., Valensi F., Varet B., Solary E., Hermine O.
J. Exp. Med. 193:247-254(2001) [PubMed] [Europe PMC] [Abstract]
- mRNA processing Source: UniProtKB-KW
- negative regulation of mRNA splicing, via spliceosome Source: UniProtKBInferred from direct assayi
- Ref.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.
- positive regulation of apoptotic process Source: UniProtKBInferred from direct assayi
- Ref.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.
- positive regulation of monocyte differentiation Source: UniProtKBInferred from expression patterni
- "Specific involvement of caspases in the differentiation of monocytes into macrophages."
Sordet O., Rebe C., Plenchette S., Zermati Y., Hermine O., Vainchenker W., Garrido C., Solary E., Dubrez-Daloz L.
Blood 100:4446-4453(2002) [PubMed] [Europe PMC] [Abstract]
- RNA splicing Source: UniProtKB-KW
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | RNA-binding |
| Biological process | Apoptosis, mRNA processing, mRNA splicing |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-111465 Apoptotic cleavage of cellular proteins |
SIGNOR Signaling Network Open Resource More...SIGNORi | Q9UKV3 |
Protein family/group databases
Transport Classification Database More...TCDBi | 3.A.18.1.1 the nuclear mrna exporter (mrna-e) family |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Apoptotic chromatin condensation inducer in the nucleusShort name: Acinus |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:ACIN1 Synonyms:ACINUS, KIAA0670 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Human Gene Nomenclature Database More...HGNCi | HGNC:17066 ACIN1 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 604562 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_Q9UKV3 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Nucleus
Note: Phosphorylation on Ser-1180 by SRPK2 redistributes it from the nuclear speckles to the nucleoplasm.
Cytosol
- cytosol Source: HPA
Nucleus
- nuclear speck Source: UniProtKBInferred from direct assayi
- Ref.22"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.
- nucleolus Source: Ensembl
- nucleoplasm Source: HPA
- nucleus Source: UniProtKBInferred from direct assayi
- Ref.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.
- nuclear speck Source: UniProtKBInferred from direct assayi
Plasma Membrane
- plasma membrane Source: HPA
Other locations
- ASAP complex Source: UniProtKBInferred from direct assayi
- Ref.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.
- ASAP complex Source: UniProtKBInferred from direct assayi
Keywords - Cellular componenti
Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 1093 | D → A: Abolishes cleavage by CASP3 and chromatin condensation activity. 1 Publication Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 22985 |
Open Targets More...OpenTargetsi | ENSG00000100813 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA134912489 |
Miscellaneous databases
Pharos NIH Druggable Genome Knowledgebase More...Pharosi | Q9UKV3 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | ACIN1 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 308153407 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000064436 | 1 – 1341 | Apoptotic chromatin condensation inducer in the nucleusAdd BLAST | 1341 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
|---|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 132 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 166 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 169 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 208 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 210 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 216 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 240 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 243 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 254 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 268 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources Manual assertion inferred from combination of experimental and computational evidencei
| |||
| Modified residuei | 269 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 295 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Cross-linki | 305 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidencei
| |||
| Cross-linki | 315 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidencei
| |||
| Modified residuei | 326 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 328 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 365 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Cross-linki | 375 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidencei
| |||
| Modified residuei | 384 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 386 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 388 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 393 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 400 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 410 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 414 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 420 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 434 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 453 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 478 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 490 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 512 | PhosphotyrosineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 522 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Cross-linki | 532 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidencei
| |||
| Modified residuei | 561 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 654 | N6,N6,N6-trimethyllysine; by EHMT2; alternate1 Publication Manual assertion based on experiment ini
| 1 | ||
| Modified residuei | 654 | N6,N6-dimethyllysine; by EHMT2; alternate1 Publication Manual assertion based on experiment ini
| 1 | ||
| Modified residuei | 655 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 657 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 682 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 710 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 714 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 717 | N6-acetyllysineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 720 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 729 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Cross-linki | 732 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidencei
| |||
| Modified residuei | 825 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 838 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 861 | N6-acetyllysine; alternateBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | ||
| Cross-linki | 861 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| |||
| Cross-linki | 879 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidencei
| |||
| Modified residuei | 895 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 898 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Cross-linki | 970 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidencei
| |||
| Modified residuei | 976 | PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 987 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 990 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Modified residuei | 1004 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
| Cross-linki | 1047 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidencei
| |||
| Cross-linki | 1107 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidencei
| |||
| Modified residuei | 1180 | Phosphoserine; by SRPK2 and PKB/AKT11 Publication Manual assertion based on experiment ini
| 1 | ||
| Isoform 4 (identifier: Q9UKV3-5) | |||||
| Modified residuei | 825 | PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidencei
| 1 | ||
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Phosphorylation on Ser-1180 by SRPK2 up-regulates its stimulatory effect on cyclin A1.1 Publication
Manual assertion based on experiment ini
- Ref.12"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.
Undergoes proteolytic cleavage; the processed form is active, contrary to the uncleaved form.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 1093 – 1094 | Cleavage; by caspase-3 | 2 |
Keywords - PTMi
Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
The CPTAC Assay portal More...CPTACi | CPTAC-1342 |
Encyclopedia of Proteome Dynamics More...EPDi | Q9UKV3 |
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | Q9UKV3 |
MassIVE - Mass Spectrometry Interactive Virtual Environment More...MassIVEi | Q9UKV3 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | Q9UKV3 |
PeptideAtlas More...PeptideAtlasi | Q9UKV3 |
PRoteomics IDEntifications database More...PRIDEi | Q9UKV3 |
ProteomicsDB: a multi-organism proteome resource More...ProteomicsDBi | 84889 [Q9UKV3-1] 84890 [Q9UKV3-2] 84891 [Q9UKV3-3] 84892 [Q9UKV3-5] |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | Q9UKV3 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | Q9UKV3 |
SwissPalm database of S-palmitoylation events More...SwissPalmi | Q9UKV3 |
Miscellaneous databases
CutDB - Proteolytic event database More...PMAP-CutDBi | Q9UKV3 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Ubiquitous. The Ser-1180 phosphorylated form (by SRPK2) is highly expressed and phosphorylated in patients with myeloid hematologic malignancies.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000100813 Expressed in 227 organ(s), highest expression level in left lobe of thyroid gland |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | Q9UKV3 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | Q9UKV3 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA000657 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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 PublicationsManual assertion based on experiment ini
- Ref.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. - Ref.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. - Ref.12"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. - Ref.19"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. - Ref.22"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. - Ref.27"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.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| API5 | Q9BZZ5 | 2 | EBI-6976596,EBI-1048422 | |
| PCBD1 | P61457 | 2 | EBI-396258,EBI-740475 | |
| PNN | Q9H307 | 2 | EBI-396258,EBI-681904 | |
| RNPS1 | Q15287-1 | 4 | EBI-5279966,EBI-15972541 |
GO - Molecular functioni
- enzyme binding Source: UniProtKBNon-traceable author statementi
- Ref.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.
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 116634, 137 interactors |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | Q9UKV3 |
Database of interacting proteins More...DIPi | DIP-32963N |
Protein interaction database and analysis system More...IntActi | Q9UKV3, 58 interactors |
Molecular INTeraction database More...MINTi | Q9UKV3 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000262710 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure_section">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 1012 – 1017 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure_section">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 1025 – 1032 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 1040 – 1042 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 1049 – 1058 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 1059 – 1069 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Beta strandi | 1083 – 1087 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 1089 – 1095 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9UKV3 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 72 – 106 | SAPPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 35 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 1210 – 1237 | Sufficient for interaction with RNPS1 and SAP18 and formation of th ASAP complexBy similarityAdd BLAST | 28 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 142 – 442 | Glu-richAdd BLAST | 301 | |
| Compositional biasi | 573 – 676 | Ser-richAdd BLAST | 104 | |
| Compositional biasi | 1114 – 1131 | Pro-richAdd BLAST | 18 | |
| Compositional biasi | 1132 – 1341 | Arg/Asp/Glu/Lys-richAdd BLAST | 210 |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2416 Eukaryota ENOG4111HR1 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00710000106790 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000088615 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9UKV3 |
KEGG Orthology (KO) More...KOi | K12875 |
Identification of Orthologs from Complete Genome Data More...OMAi | PMQLRHP |
Database of Orthologous Groups More...OrthoDBi | 828911at2759 |
Database for complete collections of gene phylogenies More...PhylomeDBi | Q9UKV3 |
TreeFam database of animal gene trees More...TreeFami | TF320727 |
Family and domain databases
Conserved Domains Database More...CDDi | cd12432 RRM_ACINU, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.720.30, 1 hit 3.30.70.330, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR034257 Acinus_RRM IPR012677 Nucleotide-bd_a/b_plait_sf IPR035979 RBD_domain_sf IPR032552 RSB_motif IPR003034 SAP_dom IPR036361 SAP_dom_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF16294 RSB_motif, 1 hit PF02037 SAP, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00513 SAP, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF54928 SSF54928, 1 hit SSF68906 SSF68906, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50800 SAP, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basketThis entry has 4 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All
Isoform 1 (identifier: Q9UKV3-1) [UniParc]FASTAAdd to basketAdded to basket
Also known as: L
This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
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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
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iDCCBF310A4680691
Isoform 2 (identifier: Q9UKV3-2) [UniParc]FASTAAdd to basketAdded 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
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MSPADRCRSA NTIEPATTSS LALFLLLQRD QSSRTRGLPE EKEEVTMDTS
60 70 80 90 100
ENRPENDVPE PPMPIADQVS NDDRPEGSVE DEEKKESSLP KSFKRKISVV
110 120 130 140 150
SATKGVPAGN SDTEGGQPGR KRRWGASTAT TQKKPSISIT TESLKSLIPD
160 170 180 190 200
IKPLAGQEAV VDLHADDSRI SEDETERNGD DGTHDKGLKI CRTVTQVVPA
210 220 230 240 250
EGQENGQREE EEEEKEPEAE PPVPPQVSVE VALPPPAEHE VKKVTLGDTL
260 270 280 290 300
TRRSISQQKS GVSITIDDPV RTAQVPSPPR GKISNIVHIS NLVRPFTLGQ
310 320 330 340 350
LKELLGRTGT LVEEAFWIDK IKSHCFVTYS TVEEAVATRT ALHGVKWPQS
360 370 380 390 400
NPKFLCADYA EQDELDYHRG LLVDRPSETK TEEQGIPRPL HPPPPPPVQP
410 420 430 440 450
PQHPRAEQRE QERAVREQWA EREREMERRE RTRSEREWDR DKVREGPRSR
460 470 480 490 500
SRSRDRRRKE RAKSKEKKSE KKEKAQEEPP AKLLDDLFRK TKAAPCIYWL
510 520 530 540 550
PLTDSQIVQK EAERAERAKE REKRRKEQEE EEQKEREKEA ERERNRQLER
560 570 580 590 600
EKRREHSRER DRERERERER DRGDRDRDRE RDRERGRERD RRDTKRHSRS
610
RSRSTPVRDR GGRR
Isoform 3 (identifier: Q9UKV3-3) [UniParc]FASTAAdd to basketAdded 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
« Hide
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MLSESKEGEE KEEVTMDTSE NRPENDVPEP PMPIADQVSN DDRPEGSVED
60 70 80 90 100
EEKKESSLPK SFKRKISVVS ATKGVPAGNS DTEGGQPGRK RRWGASTATT
110 120 130 140 150
QKKPSISITT ESLKSLIPDI KPLAGQEAVV DLHADDSRIS EDETERNGDD
160 170 180 190 200
GTHDKGLKIC RTVTQVVPAE GQENGQREEE EEEKEPEAEP PVPPQVSVEV
210 220 230 240 250
ALPPPAEHEV KKVTLGDTLT RRSISQQKSG VSITIDDPVR TAQVPSPPRG
260 270 280 290 300
KISNIVHISN LVRPFTLGQL KELLGRTGTL VEEAFWIDKI KSHCFVTYST
310 320 330 340 350
VEEAVATRTA LHGVKWPQSN PKFLCADYAE QDELDYHRGL LVDRPSETKT
360 370 380 390 400
EEQGIPRPLH PPPPPPVQPP QHPRAEQREQ ERAVREQWAE REREMERRER
410 420 430 440 450
TRSEREWDRD KVREGPRSRS RSRDRRRKER AKSKEKKSEK KEKAQEEPPA
460 470 480 490 500
KLLDDLFRKT KAAPCIYWLP LTDSQIVQKE AERAERAKER EKRRKEQEEE
510 520 530 540 550
EQKEREKEAE RERNRQLERE KRREHSRERD RERERERERD RGDRDRDRER
560 570 580
DRERGRERDR RDTKRHSRSR SRSTPVRDRG GRR
Isoform 4 (identifier: Q9UKV3-5) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
829-829: Missing.
873-884: Missing.
« Hide
Show »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 KRKISVVSTK GVPAGNSDTE GGQPGRKRRW
860 870 880 890 900
GASTATTQKK PSISITTESL KEAVVDLHAD DSRISEDETE RNGDDGTHDK
910 920 930 940 950
GLKICRTVTQ VVPAEGQENG QREEEEEEKE PEAEPPVPPQ VSVEVALPPP
960 970 980 990 1000
AEHEVKKVTL GDTLTRRSIS QQKSGVSITI DDPVRTAQVP SPPRGKISNI
1010 1020 1030 1040 1050
VHISNLVRPF TLGQLKELLG RTGTLVEEAF WIDKIKSHCF VTYSTVEEAV
1060 1070 1080 1090 1100
ATRTALHGVK WPQSNPKFLC ADYAEQDELD YHRGLLVDRP SETKTEEQGI
1110 1120 1130 1140 1150
PRPLHPPPPP PVQPPQHPRA EQREQERAVR EQWAEREREM ERRERTRSER
1160 1170 1180 1190 1200
EWDRDKVREG PRSRSRSRDR RRKERAKSKE KKSEKKEKAQ EEPPAKLLDD
1210 1220 1230 1240 1250
LFRKTKAAPC IYWLPLTDSQ IVQKEAERAE RAKEREKRRK EQEEEEQKER
1260 1270 1280 1290 1300
EKEAERERNR QLEREKRREH SRERDRERER ERERDRGDRD RDRERDRERG
1310 1320
RERDRRDTKR HSRSRSRSTP VRDRGGRR
<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi
There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket| Entry | Entry name | Protein names | Gene names | Length | Annotation | ||
|---|---|---|---|---|---|---|---|
| E7EQT4 | E7EQT4_HUMAN | Apoptotic chromatin condensation in... Apoptotic chromatin condensation inducer in the nucleus | ACIN1 | 1,301 | Annotation score: Annotation score:2 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
| S4R3H4 | S4R3H4_HUMAN | Apoptotic chromatin condensation in... Apoptotic chromatin condensation inducer in the nucleus | ACIN1 | 1,283 | Annotation score: Annotation score:2 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
| G3V3B0 | G3V3B0_HUMAN | Apoptotic chromatin condensation in... Apoptotic chromatin condensation inducer in the nucleus | ACIN1 | 582 | Annotation score: Annotation score:2 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
| G3V3T3 | G3V3T3_HUMAN | Apoptotic chromatin condensation in... Apoptotic chromatin condensation inducer in the nucleus | ACIN1 | 194 | Annotation score: Annotation score:1 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
| A0A087WYN3 | A0A087WYN3_HUMAN | Apoptotic chromatin condensation in... Apoptotic chromatin condensation inducer in the nucleus | ACIN1 | 82 | Annotation score: Annotation score:1 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
| A0A087X0D2 | A0A087X0D2_HUMAN | Apoptotic chromatin condensation in... Apoptotic chromatin condensation inducer in the nucleus | ACIN1 | 36 | Annotation score: Annotation score:1 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 139 | Q → H in BAA31645 (Ref. 2) Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_050632 | 257 | R → K. Corresponds to variant dbSNP:rs11555803Ensembl. | 1 | |
| Natural variantiVAR_022031 | 311 | I → M. Corresponds to variant dbSNP:rs3811182Ensembl. | 1 | |
| Natural variantiVAR_061547 | 447 | A → PCombined sources Manual assertion inferred from combination of experimental and computational evidencei
Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_022032 | 467 | S → P. Corresponds to variant dbSNP:rs1885097Ensembl. | 1 | |
| Natural variantiVAR_022033 | 478 | S → F. Corresponds to variant dbSNP:rs3751501Ensembl. | 1 | |
| Natural variantiVAR_035777 | 1160 | R → Q in a colorectal cancer sample; somatic mutation. 1 Publication Manual assertion based on experiment ini
| 1 |
Alternative sequence
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004026 | 1 – 758 | Missing in isoform 3. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
| 758 | |
| Alternative sequenceiVSP_004025 | 1 – 727 | Missing in isoform 2. 1 Publication Manual assertion based on opinion ini
| 727 | |
| Alternative sequenceiVSP_004028 | 728 – 766 | GSPKK…IHHTV → MSPADRCRSANTIEPATTSS LALFLLLQRDQSSRTRGLP in isoform 2. 1 Publication Manual assertion based on opinion ini
| 39 | |
| Alternative sequenceiVSP_004029 | 759 – 766 | SERIHHTV → MLSESKEG in isoform 3. 2 Publications Manual assertion based on opinion ini
| 8 | |
| Alternative sequenceiVSP_042204 | 829 | Missing in isoform 4. 1 Publication Manual assertion based on opinion ini
| 1 | |
| Alternative sequenceiVSP_042205 | 873 – 884 | Missing in isoform 4. 1 Publication Manual assertion based on opinion ini
| 12 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks 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 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS53887.1 [Q9UKV3-3] CCDS53888.1 [Q9UKV3-2] CCDS55905.1 [Q9UKV3-5] CCDS9587.1 [Q9UKV3-1] |
NCBI Reference Sequences More...RefSeqi | NP_001158286.1, NM_001164814.1 NP_001158287.1, NM_001164815.1 NP_001158288.1, NM_001164816.1 [Q9UKV3-2] NP_001158289.1, NM_001164817.1 [Q9UKV3-3] NP_055792.1, NM_014977.3 XP_005267475.1, XM_005267418.1 [Q9UKV3-3] |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000262710; ENSP00000262710; ENSG00000100813 [Q9UKV3-1] ENST00000338631; ENSP00000345541; ENSG00000100813 [Q9UKV3-2] ENST00000357481; ENSP00000350073; ENSG00000100813 [Q9UKV3-3] ENST00000397341; ENSP00000380502; ENSG00000100813 [Q9UKV3-3] ENST00000555053; ENSP00000451328; ENSG00000100813 [Q9UKV3-5] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 22985 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:22985 |
UCSC genome browser More...UCSCi | uc001wip.5 human [Q9UKV3-1] |
Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q9UKV3 | Apoptotic chromatin condensation inducer in the nucleus | 1283 | UniRef100_Q9UKV3 | |||
| Q9UKV3-2 | ACIN1 isoform 4 | 614 | UniRef100_K7BB02 | |||
| Apoptotic chromatin condensation inducer in the nucleus isoform 4 | 614 | |||||
| ACIN1 isoform 12 | 614 | |||||
| Uncharacterized protein | 614 | |||||
| Uncharacterized protein | 614 | |||||
| +4 | ||||||
| Q9UKV3-3 | ACIN1 isoform 11 | 1352 | UniRef100_A0A2J8QK52 | |||
| ACIN1 isoform 10 | 583 | |||||
| Apoptotic chromatin condensation inducer in the nucleus isoform 5 | 583 | |||||
| Uncharacterized protein | 583 | |||||
| Uncharacterized protein | 583 | |||||
| +4 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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 |
| CCDSi | CCDS53887.1 [Q9UKV3-3] CCDS53888.1 [Q9UKV3-2] CCDS55905.1 [Q9UKV3-5] CCDS9587.1 [Q9UKV3-1] |
| RefSeqi | NP_001158286.1, NM_001164814.1 NP_001158287.1, NM_001164815.1 NP_001158288.1, NM_001164816.1 [Q9UKV3-2] NP_001158289.1, NM_001164817.1 [Q9UKV3-3] NP_055792.1, NM_014977.3 XP_005267475.1, XM_005267418.1 [Q9UKV3-3] |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 6G6S | X-ray | 1.65 | A/B | 1008-1100 | [»] | |
| SMRi | Q9UKV3 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| BioGridi | 116634, 137 interactors |
| CORUMi | Q9UKV3 |
| DIPi | DIP-32963N |
| IntActi | Q9UKV3, 58 interactors |
| MINTi | Q9UKV3 |
| STRINGi | 9606.ENSP00000262710 |
Protein family/group databases
| TCDBi | 3.A.18.1.1 the nuclear mrna exporter (mrna-e) family |
PTM databases
| iPTMneti | Q9UKV3 |
| PhosphoSitePlusi | Q9UKV3 |
| SwissPalmi | Q9UKV3 |
Polymorphism and mutation databases
| BioMutai | ACIN1 |
| DMDMi | 308153407 |
Proteomic databases
| CPTACi | CPTAC-1342 |
| EPDi | Q9UKV3 |
| jPOSTi | Q9UKV3 |
| MassIVEi | Q9UKV3 |
| PaxDbi | Q9UKV3 |
| PeptideAtlasi | Q9UKV3 |
| PRIDEi | Q9UKV3 |
| ProteomicsDBi | 84889 [Q9UKV3-1] 84890 [Q9UKV3-2] 84891 [Q9UKV3-3] 84892 [Q9UKV3-5] |
Genome annotation databases
| Ensembli | ENST00000262710; ENSP00000262710; ENSG00000100813 [Q9UKV3-1] ENST00000338631; ENSP00000345541; ENSG00000100813 [Q9UKV3-2] ENST00000357481; ENSP00000350073; ENSG00000100813 [Q9UKV3-3] ENST00000397341; ENSP00000380502; ENSG00000100813 [Q9UKV3-3] ENST00000555053; ENSP00000451328; ENSG00000100813 [Q9UKV3-5] |
| GeneIDi | 22985 |
| KEGGi | hsa:22985 |
| UCSCi | uc001wip.5 human [Q9UKV3-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 22985 |
| DisGeNETi | 22985 |
GeneCards: human genes, protein and diseases More...GeneCardsi | ACIN1 |
| HGNCi | HGNC:17066 ACIN1 |
| HPAi | HPA000657 |
| MIMi | 604562 gene |
| neXtProti | NX_Q9UKV3 |
| OpenTargetsi | ENSG00000100813 |
| PharmGKBi | PA134912489 |
Human Unidentified Gene-Encoded large proteins database More...HUGEi | Search... |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
| eggNOGi | KOG2416 Eukaryota ENOG4111HR1 LUCA |
| GeneTreei | ENSGT00710000106790 |
| HOGENOMi | HOG000088615 |
| InParanoidi | Q9UKV3 |
| KOi | K12875 |
| OMAi | PMQLRHP |
| OrthoDBi | 828911at2759 |
| PhylomeDBi | Q9UKV3 |
| TreeFami | TF320727 |
Enzyme and pathway databases
| Reactomei | R-HSA-111465 Apoptotic cleavage of cellular proteins |
| SIGNORi | Q9UKV3 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | ACIN1 human |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | ACIN1 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 22985 |
| Pharosi | Q9UKV3 |
| PMAP-CutDBi | Q9UKV3 |
Protein Ontology More...PROi | PR:Q9UKV3 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
| Bgeei | ENSG00000100813 Expressed in 227 organ(s), highest expression level in left lobe of thyroid gland |
| ExpressionAtlasi | Q9UKV3 baseline and differential |
| Genevisiblei | Q9UKV3 HS |
Family and domain databases
| CDDi | cd12432 RRM_ACINU, 1 hit |
| Gene3Di | 1.10.720.30, 1 hit 3.30.70.330, 1 hit |
| InterProi | View protein in InterPro IPR034257 Acinus_RRM IPR012677 Nucleotide-bd_a/b_plait_sf IPR035979 RBD_domain_sf IPR032552 RSB_motif IPR003034 SAP_dom IPR036361 SAP_dom_sf |
| Pfami | View protein in Pfam PF16294 RSB_motif, 1 hit PF02037 SAP, 1 hit |
| SMARTi | View protein in SMART SM00513 SAP, 1 hit |
| SUPFAMi | SSF54928 SSF54928, 1 hit SSF68906 SSF68906, 1 hit |
| PROSITEi | View protein in PROSITE PS50800 SAP, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | ACINU_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q9UKV3Primary (citable) accession number: Q9UKV3 Secondary accession number(s): B2RTT4 , D3DS45, O75158, Q9UG91, Q9UKV1, Q9UKV2 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 28, 2003 |
| Last sequence update: | October 5, 2010 | |
| Last modified: | October 16, 2019 | |
| This is version 188 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | 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. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - Human chromosome 14
Human chromosome 14: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
