UniProtKB - Q9Y2W7 (CSEN_HUMAN)
UniProt
Q9Y2W7 - CSEN_HUMAN
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Protein
Calsenilin
Gene
KCNIP3
Organism
Homo sapiens (Human)
Sequence features
Status
Functioni
Calcium-dependent transcriptional repressor that binds to the DRE element of genes including PDYN and FOS. Affinity for DNA is reduced upon binding to calcium and enhanced by binding to magnesium. Seems to be involved in nociception (By similarity).By similarity
Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly inactivating A-type potassium channels, such as KCND2/Kv4.2 and KCND3/Kv4.3. Modulates channel expression at the cell membrane, gating characteristics, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner.5 Publications
May play a role in the regulation of PSEN2 proteolytic processing and apoptosis. Together with PSEN2 involved in modulation of beta-amyloid formation.3 Publications
Regions
Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Calcium bindingi | 175 – 186 | 12 | 1PROSITE-ProRule annotation | Add BLAST | ||
Calcium bindingi | 223 – 234 | 12 | 2PROSITE-ProRule annotation | Add BLAST |
GO - Molecular functioni
- calcium ion binding Source: ProtInc
- DNA binding Source: ProtInc
- potassium channel activity Source: UniProtKB-KW
- potassium channel regulator activity Source: UniProtKB
- RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: Ensembl
- transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: Ensembl
- transcription corepressor activity Source: ProtInc
- voltage-gated ion channel activity Source: UniProtKB-KW
GO - Biological processi
- apoptotic process Source: UniProtKB-KW
- behavioral response to pain Source: Ensembl
- protein localization to plasma membrane Source: UniProtKB
- regulation of neuron apoptotic process Source: Ensembl
- regulation of potassium ion transmembrane transport Source: UniProtKB
- regulation of transcription from RNA polymerase II promoter Source: ProtInc
- sensory perception of pain Source: Ensembl
- signal transduction Source: ProtInc
- transcription, DNA-templated Source: UniProtKB-KW
Keywords - Molecular functioni
Ion channel, Potassium channel, Repressor, Voltage-gated channelKeywords - Biological processi
Apoptosis, Ion transport, Potassium transport, Transcription, Transcription regulation, TransportKeywords - Ligandi
Calcium, Metal-binding, PotassiumNames & Taxonomyi
Protein namesi | Recommended name: CalsenilinAlternative name(s): A-type potassium channel modulatory protein 3 DRE-antagonist modulator Short name: DREAM Kv channel-interacting protein 3 Short name: KChIP3 |
Gene namesi | Name:KCNIP3 Synonyms:CSEN, DREAM, KCHIP3 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi | UP000005640: Chromosome 2 Componenti |
Organism-specific databases
HGNCi | HGNC:15523. KCNIP3. |
Subcellular locationi
- Cytoplasm 1 Publication
- Cell membrane 2 Publications; Lipid-anchor By similarity
- Endoplasmic reticulum 1 Publication
- Golgi apparatus
- Nucleus
Note: Also membrane-bound, associated with the plasma membrane (PubMed:15485870). In the presence of PSEN2 associated with the endoplasmic reticulum and Golgi. The sumoylated form is present only in the nucleus.By similarity1 Publication
GO - Cellular componenti
- cytosol Source: UniProtKB
- endoplasmic reticulum Source: UniProtKB-SubCell
- Golgi apparatus Source: UniProtKB-SubCell
- nucleus Source: UniProtKB-SubCell
- voltage-gated potassium channel complex Source: UniProtKB
Keywords - Cellular componenti
Cell membrane, Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Mutagenesisi | 61 – 61 | 1 | D → A: Abolishes cleavage by caspase-3. 1 Publication | |||
Mutagenesisi | 64 – 64 | 1 | D → A: Abolishes cleavage by caspase-3. 1 Publication |
Organism-specific databases
PharmGKBi | PA26934. |
Polymorphism and mutation databases
BioMutai | KCNIP3. |
DMDMi | 13431428. |
PTM / Processingi
Molecule processing
Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Chaini | 1 – 256 | 256 | Calsenilin | PRO_0000073814 | Add BLAST |
Amino acid modifications
Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Modified residuei | 14 – 14 | 1 | PhosphoserineBy similarity | |||
Cross-linki | 26 – 26 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) | ||||
Lipidationi | 45 – 45 | 1 | S-palmitoyl cysteineBy similarity | |||
Lipidationi | 46 – 46 | 1 | S-palmitoyl cysteineBy similarity | |||
Modified residuei | 60 – 60 | 1 | PhosphoserineBy similarity | |||
Modified residuei | 63 – 63 | 1 | Phosphoserine; by CK11 Publication | |||
Cross-linki | 90 – 90 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) |
Post-translational modificationi
Palmitoylated. Palmitoylation enhances association with the plasma membrane (By similarity).By similarity
Proteolytically cleaved by caspase-3.1 Publication
Phosphorylation at Ser-63 inhibits cleavage by CASP3.2 Publications
Keywords - PTMi
Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | Q9Y2W7. |
PRIDEi | Q9Y2W7. |
PTM databases
PhosphoSitei | Q9Y2W7. |
Miscellaneous databases
PMAP-CutDB | Q3YAC3. |
Expressioni
Tissue specificityi
Highly expressed in brain. Widely expressed at lower levels. Expression levels are elevated in brain cortex regions affected by Alzheimer disease.1 Publication
Gene expression databases
Bgeei | Q9Y2W7. |
CleanExi | HS_KCNIP3. |
ExpressionAtlasi | Q9Y2W7. baseline and differential. |
Genevisiblei | Q9Y2W7. HS. |
Organism-specific databases
HPAi | CAB006907. |
Interactioni
Subunit structurei
Binds to DNA as a homomultimer. Dimerization is induced by binding to calcium (PubMed:17962406). Interacts with the C-terminus of PSEN1 and PSEN2 and with PSEN2 CTF subunit. Associates with KCN1. Component of heteromultimeric potassium channels. Identified in potassium channel complexes containing KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (By similarity). Interacts with KCND2 and KCND3.By similarity4 Publications
Binary interactionsi
With | Entry | #Exp. | IntAct | Notes |
---|---|---|---|---|
CD177 | Q8N6Q3 | 4 | EBI-751501,EBI-747170 | |
IGF1R | P08069 | 3 | EBI-751501,EBI-475981 | |
IL6ST | Q17RA0 | 3 | EBI-751501,EBI-10238517 | |
MAVS | Q7Z434 | 3 | EBI-751501,EBI-995373 |
Protein-protein interaction databases
BioGridi | 119042. 20 interactions. |
IntActi | Q9Y2W7. 4 interactions. |
MINTi | MINT-1453732. |
STRINGi | 9606.ENSP00000295225. |
Structurei
Secondary structure
1
256
Legend: HelixTurnBeta strand
Show more detailsFeature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Helixi | 164 – 174 | 11 | Combined sources | |||
Beta strandi | 179 – 182 | 4 | Combined sources | |||
Helixi | 184 – 193 | 10 | Combined sources | |||
Beta strandi | 211 – 213 | 3 | Combined sources | |||
Helixi | 214 – 222 | 9 | Combined sources | |||
Beta strandi | 227 – 231 | 5 | Combined sources | |||
Helixi | 232 – 239 | 8 | Combined sources | |||
Helixi | 243 – 254 | 12 | Combined sources |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated |
| ||||||||||||
ProteinModelPortali | Q9Y2W7. | ||||||||||||
SMRi | Q9Y2W7. Positions 76-256. | ||||||||||||
ModBasei | Search... | ||||||||||||
MobiDBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q9Y2W7. |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Domaini | 67 – 123 | 57 | EF-hand 1; degeneratePROSITE-ProRule annotation | Add BLAST | ||
Domaini | 126 – 161 | 36 | EF-hand 2PROSITE-ProRule annotation | Add BLAST | ||
Domaini | 162 – 197 | 36 | EF-hand 3PROSITE-ProRule annotation | Add BLAST | ||
Domaini | 210 – 245 | 36 | EF-hand 4PROSITE-ProRule annotation | Add BLAST |
Region
Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Regioni | 243 – 256 | 14 | Interaction with KCND2By similarity | Add BLAST |
Sequence similaritiesi
Belongs to the recoverin family.Curated
Contains 4 EF-hand domains.PROSITE-ProRule annotation
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG0044. Eukaryota. COG5126. LUCA. |
GeneTreei | ENSGT00760000118820. |
HOGENOMi | HOG000233019. |
HOVERGENi | HBG108179. |
InParanoidi | Q9Y2W7. |
OMAi | FGILEPM. |
OrthoDBi | EOG7GJ6F3. |
PhylomeDBi | Q9Y2W7. |
TreeFami | TF318560. |
Family and domain databases
Gene3Di | 1.10.238.10. 3 hits. |
InterProi | IPR011992. EF-hand-dom_pair. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. IPR028846. Recoverin. [Graphical view] |
PANTHERi | PTHR23055. PTHR23055. 1 hit. |
Pfami | PF13499. EF-hand_7. 1 hit. [Graphical view] |
SMARTi | SM00054. EFh. 3 hits. [Graphical view] |
PROSITEi | PS00018. EF_HAND_1. 2 hits. PS50222. EF_HAND_2. 3 hits. [Graphical view] |
s (3)i Sequence
Sequence statusi: Complete.
This entry describes 3 produced by isoformsialternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q9Y2W7-1) [UniParc]FASTAAdd to basket
Also known as: KChIP3.1
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.
10 20 30 40 50
MQPAKEVTKA SDGSLLGDLG HTPLSKKEGI KWQRPRLSRQ ALMRCCLVKW
60 70 80 90 100
ILSSTAPQGS DSSDSELELS TVRHQPEGLD QLQAQTKFTK KELQSLYRGF
110 120 130 140 150
KNECPTGLVD EDTFKLIYAQ FFPQGDATTY AHFLFNAFDA DGNGAIHFED
160 170 180 190 200
FVVGLSILLR GTVHEKLKWA FNLYDINKDG YITKEEMLAI MKSIYDMMGR
210 220 230 240 250
HTYPILREDA PAEHVERFFE KMDRNQDGVV TIEEFLEACQ KDENIMSSMQ
LFENVI
Experimental Info
Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Sequence conflicti | 182 – 182 | 1 | I → V in CAB56836 (PubMed:10078534).Curated | |||
Sequence conflicti | 182 – 182 | 1 | I → V in CAB56835 (PubMed:10078534).Curated | |||
Sequence conflicti | 207 – 207 | 1 | R → Q in CAB56836 (PubMed:10078534).Curated | |||
Sequence conflicti | 207 – 207 | 1 | R → Q in CAB56835 (PubMed:10078534).Curated |
Natural variant
Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Natural varianti | 119 – 119 | 1 | A → V. Corresponds to variant rs35658670 [ dbSNP | Ensembl ]. | VAR_048663 | ||
Natural varianti | 170 – 170 | 1 | A → S in a breast cancer sample; somatic mutation. 1 Publication | VAR_035463 | ||
Natural varianti | 179 – 179 | 1 | D → Y in a breast cancer sample; somatic mutation. 1 Publication | VAR_035464 |
Alternative sequence
Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | Actions |
---|---|---|---|---|---|---|
Alternative sequencei | 1 – 26 | 26 | Missing in isoform 3. 1 Publication | VSP_040982 | Add BLAST | |
Alternative sequencei | 27 – 60 | 34 | KEGIK…APQGS → MGIQGMELCAMAVVVLLFIA VLKQFGILEPISME in isoform 3. 1 Publication | VSP_040983 | Add BLAST | |
Alternative sequencei | 103 – 124 | 22 | Missing in isoform 2. 1 Publication | VSP_015040 | Add BLAST |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF120102 mRNA. Translation: AAD20350.1. AJ131730 mRNA. Translation: CAB56836.1. AJ131730 mRNA. Translation: CAB56835.1. AF199599 mRNA. Translation: AAF33684.1. DQ148485 mRNA. Translation: AAZ77802.1. DQ148486 mRNA. Translation: AAZ77803.1. AF367022 mRNA. Translation: AAK53711.1. BT020075 mRNA. Translation: AAV38878.1. AK315437 mRNA. Translation: BAG37825.1. AC009238 Genomic DNA. Translation: AAY14752.1. CH471219 Genomic DNA. Translation: EAX10724.1. BC012850 mRNA. Translation: AAH12850.1. |
CCDSi | CCDS2013.1. [Q9Y2W7-1] CCDS33245.1. [Q9Y2W7-3] |
RefSeqi | NP_001030086.1. NM_001034914.1. [Q9Y2W7-3] NP_038462.1. NM_013434.4. [Q9Y2W7-1] |
UniGenei | Hs.437376. |
Genome annotation databases
Ensembli | ENST00000295225; ENSP00000295225; ENSG00000115041. [Q9Y2W7-1] ENST00000468529; ENSP00000417499; ENSG00000115041. [Q9Y2W7-3] |
GeneIDi | 30818. |
KEGGi | hsa:30818. |
UCSCi | uc002sup.3. human. [Q9Y2W7-1] uc002suq.3. human. [Q9Y2W7-3] |
Keywords - Coding sequence diversityi
Alternative splicing, PolymorphismCross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF120102 mRNA. Translation: AAD20350.1. AJ131730 mRNA. Translation: CAB56836.1. AJ131730 mRNA. Translation: CAB56835.1. AF199599 mRNA. Translation: AAF33684.1. DQ148485 mRNA. Translation: AAZ77802.1. DQ148486 mRNA. Translation: AAZ77803.1. AF367022 mRNA. Translation: AAK53711.1. BT020075 mRNA. Translation: AAV38878.1. AK315437 mRNA. Translation: BAG37825.1. AC009238 Genomic DNA. Translation: AAY14752.1. CH471219 Genomic DNA. Translation: EAX10724.1. BC012850 mRNA. Translation: AAH12850.1. |
CCDSi | CCDS2013.1. [Q9Y2W7-1] CCDS33245.1. [Q9Y2W7-3] |
RefSeqi | NP_001030086.1. NM_001034914.1. [Q9Y2W7-3] NP_038462.1. NM_013434.4. [Q9Y2W7-1] |
UniGenei | Hs.437376. |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated |
| ||||||||||||
ProteinModelPortali | Q9Y2W7. | ||||||||||||
SMRi | Q9Y2W7. Positions 76-256. | ||||||||||||
ModBasei | Search... | ||||||||||||
MobiDBi | Search... |
Protein-protein interaction databases
BioGridi | 119042. 20 interactions. |
IntActi | Q9Y2W7. 4 interactions. |
MINTi | MINT-1453732. |
STRINGi | 9606.ENSP00000295225. |
PTM databases
PhosphoSitei | Q9Y2W7. |
Polymorphism and mutation databases
BioMutai | KCNIP3. |
DMDMi | 13431428. |
Proteomic databases
PaxDbi | Q9Y2W7. |
PRIDEi | Q9Y2W7. |
Protocols and materials databases
DNASUi | 30818. |
Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembli | ENST00000295225; ENSP00000295225; ENSG00000115041. [Q9Y2W7-1] ENST00000468529; ENSP00000417499; ENSG00000115041. [Q9Y2W7-3] |
GeneIDi | 30818. |
KEGGi | hsa:30818. |
UCSCi | uc002sup.3. human. [Q9Y2W7-1] uc002suq.3. human. [Q9Y2W7-3] |
Organism-specific databases
CTDi | 30818. |
GeneCardsi | KCNIP3. |
HGNCi | HGNC:15523. KCNIP3. |
HPAi | CAB006907. |
MIMi | 604662. gene. |
neXtProti | NX_Q9Y2W7. |
PharmGKBi | PA26934. |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0044. Eukaryota. COG5126. LUCA. |
GeneTreei | ENSGT00760000118820. |
HOGENOMi | HOG000233019. |
HOVERGENi | HBG108179. |
InParanoidi | Q9Y2W7. |
OMAi | FGILEPM. |
OrthoDBi | EOG7GJ6F3. |
PhylomeDBi | Q9Y2W7. |
TreeFami | TF318560. |
Miscellaneous databases
ChiTaRSi | KCNIP3. human. |
EvolutionaryTracei | Q9Y2W7. |
GeneWikii | Calsenilin. |
GenomeRNAii | 30818. |
NextBioi | 35528162. |
PMAP-CutDB | Q3YAC3. |
PROi | Q9Y2W7. |
SOURCEi | Search... |
Gene expression databases
Bgeei | Q9Y2W7. |
CleanExi | HS_KCNIP3. |
ExpressionAtlasi | Q9Y2W7. baseline and differential. |
Genevisiblei | Q9Y2W7. HS. |
Family and domain databases
Gene3Di | 1.10.238.10. 3 hits. |
InterProi | IPR011992. EF-hand-dom_pair. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. IPR028846. Recoverin. [Graphical view] |
PANTHERi | PTHR23055. PTHR23055. 1 hit. |
Pfami | PF13499. EF-hand_7. 1 hit. [Graphical view] |
SMARTi | SM00054. EFh. 3 hits. [Graphical view] |
PROSITEi | PS00018. EF_HAND_1. 2 hits. PS50222. EF_HAND_2. 3 hits. [Graphical view] |
ProtoNeti | Search... |
Publicationsi
- "Calsenilin: a calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment."
Buxbaum J.D., Choi E.K., Luo Y., Lilliehook C., Crowley A.C., Merriam D.E., Wasco W.
Nat. Med. 4:1177-1181(1998) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN PRESENILIN REGULATION. - "DREAM is a Ca2+-regulated transcriptional repressor."
Carrion A.M., Link W.A., Ledo F., Mellstrom B., Naranjo J.R.
Nature 398:80-84(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN TRANSCRIPTION REGULATION.Tissue: Caudate nucleus. - "Modulation of A-type potassium channels by a family of calcium sensors."
An W.F., Bowlby M.R., Betty M., Cao J., Ling H.-P., Mendoza G., Hinson J.W., Mattsson K.I., Strassle B.W., Trimmer J.S., Rhodes K.J.
Nature 403:553-556(2000) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN POTASSIUM TRANSPORT. - "Structure, alternative splicing, and expression of the human and mouse KCNIP gene family."
Pruunsild P., Timmusk T.
Genomics 86:581-593(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), ALTERNATIVE SPLICING. - Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
- "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). - "Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).Tissue: Brain. - "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. - Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. - "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).Tissue: Brain. - "Calsenilin is a substrate for caspase-3 that preferentially interacts with the familial Alzheimer's disease-associated C-terminal fragment of presenilin 2."
Choi E.K., Zaidi N.F., Miller J.S., Crowley A.C., Merriam D.E., Lilliehook C., Buxbaum J.D., Wasco W.
J. Biol. Chem. 276:19197-19204(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PSEN2, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF ASP-61 AND ASP-64. - "Pro-apoptotic function of calsenilin/DREAM/KChIP3."
Jo D.G., Kim M.J., Choi Y.H., Kim I.K., Song Y.H., Woo H.N., Chung C.W., Jung Y.K.
FASEB J. 15:589-591(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN APOPTOSIS. - "Calsenilin enhances apoptosis by altering endoplasmic reticulum calcium signaling."
Lilliehook C., Chan S., Choi E.K., Zaidi N.F., Wasco W., Mattson M.P., Buxbaum J.D.
Mol. Cell. Neurosci. 19:552-559(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN APOPTOSIS. - "A fundamental role for KChIPs in determining the molecular properties and trafficking of Kv4.2 potassium channels."
Shibata R., Misonou H., Campomanes C.R., Anderson A.E., Schrader L.A., Doliveira L.C., Carroll K.I., Sweatt J.D., Rhodes K.J., Trimmer J.S.
J. Biol. Chem. 278:36445-36454(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN POTASSIUM TRANSPORT. - "Phosphorylation of calsenilin at Ser63 regulates its cleavage by caspase-3."
Choi E.K., Miller J.S., Zaidi N.F., Salih E., Buxbaum J.D., Wasco W.
Mol. Cell. Neurosci. 23:495-506(2003) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION AT SER-63. - "KChIP3 rescues the functional expression of Shal channel tetramerization mutants."
Kunjilwar K., Strang C., DeRubeis D., Pfaffinger P.J.
J. Biol. Chem. 279:54542-54551(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH KCND2, FUNCTION IN POTASSIUM TRANSPORT, SUBUNIT, SUBCELLULAR LOCATION. - "Induction of pro-apoptotic calsenilin/DREAM/KChIP3 in Alzheimer's disease and cultured neurons after amyloid-beta exposure."
Jo D.G., Lee J.Y., Hong Y.M., Song S., Mook-Jung I., Koh J.Y., Jung Y.K.
J. Neurochem. 88:604-611(2004) [PubMed] [Europe PMC] [Abstract]Cited for: TISSUE SPECIFICITY. - "Multiprotein assembly of Kv4.2, KChIP3 and DPP10 produces ternary channel complexes with ISA-like properties."
Jerng H.H., Kunjilwar K., Pfaffinger P.J.
J. Physiol. (Lond.) 568:767-788(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN POTASSIUM TRANSPORT. - "Multiple Kv channel-interacting proteins contain an N-terminal transmembrane domain that regulates Kv4 channel trafficking and gating."
Jerng H.H., Pfaffinger P.J.
J. Biol. Chem. 283:36046-36059(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN POTASSIUM TRANSPORT, INTERACTION WITH KCND2, SUBCELLULAR LOCATION. - "Sumoylation regulates nuclear localization of repressor DREAM."
Palczewska M., Casafont I., Ghimire K., Rojas A.M., Valencia A., Lafarga M., Mellstrom B., Naranjo J.R.
Biochim. Biophys. Acta 1813:1050-1058(2011) [PubMed] [Europe PMC] [Abstract]Cited for: SUMOYLATION AT LYS-26 AND LYS-90, SUBCELLULAR LOCATION. - "Solution structure and calcium-binding properties of EF-hands 3 and 4 of calsenilin."
Yu L., Sun C., Mendoza R., Wang J., Matayoshi E.D., Hebert E., Pereda-Lopez A., Hajduk P.J., Olejniczak E.T.
Protein Sci. 16:2502-2509(2007) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 161-256, SUBUNIT, CALCIUM-BINDING. - "The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-170 AND TYR-179.
Entry informationi
Entry namei | CSEN_HUMAN | ||||||||
Accessioni | Q9Y2W7Primary (citable) accession number: Q9Y2W7 Secondary accession number(s): H7BY46 Q9UJ85 | ||||||||
Entry historyi |
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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. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- Human chromosome 2Human chromosome 2: entries, gene names and cross-references to MIM
- Human entries with polymorphisms or disease mutationsList of human entries with polymorphisms or disease mutations
- Human polymorphisms and disease mutationsIndex of human polymorphisms and disease mutations
- MIM cross-referencesOnline Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
- PDB cross-referencesIndex of Protein Data Bank (PDB) cross-references
- SIMILARITY commentsIndex of protein domains and families
External Data
Dasty 3Similar 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 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. |