Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9Y2W7

- CSEN_HUMAN

UniProt

Q9Y2W7 - CSEN_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Calsenilin

Gene

KCNIP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. Probably modulates channels density, inactivation kinetics and rate of recovery from inactivation in a calcium-dependent and isoform-specific manner. In vitro, modulates KCND2/Kv4.2 and KCND3/Kv4.3 currents. Involved in KCND2 and probably KCND3 trafficking to the cell surface.
May play a role in the regulation of PSEN2 proteolytic processing and apoptosis. Together with PSEN2 involved in modulation of beta-amyloid formation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi175 – 186121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi223 – 234122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: ProtInc
  2. DNA binding Source: ProtInc
  3. potassium channel activity Source: UniProtKB-KW
  4. potassium channel regulator activity Source: Ensembl
  5. sequence-specific DNA binding Source: Ensembl
  6. transcription corepressor activity Source: ProtInc
  7. voltage-gated ion channel activity Source: UniProtKB-KW

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. behavioral response to pain Source: Ensembl
  3. intracellular protein transport Source: Ensembl
  4. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  5. regulation of neuron apoptotic process Source: Ensembl
  6. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  7. sensory perception of pain Source: Ensembl
  8. signal transduction Source: ProtInc
  9. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel, Repressor, Voltage-gated channel

Keywords - Biological processi

Apoptosis, Ion transport, Potassium transport, Transcription, Transcription regulation, Transport

Keywords - Ligandi

Calcium, Metal-binding, Potassium

Names & Taxonomyi

Protein namesi
Recommended name:
Calsenilin
Alternative 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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:15523. KCNIP3.

Subcellular locationi

Cytoplasm. Cell membrane By similarity; Lipid-anchor By similarity. Endoplasmic reticulum. Golgi apparatus. Nucleus
Note: Also membrane-bound, associated with the plasma membrane (By similarity). In the presence of PSEN2 associated with the endoplasmic reticulum and Golgi. The sumoylated form is present only in the nucleus.By similarity

GO - Cellular componenti

  1. axon terminus Source: Ensembl
  2. cytosol Source: Ensembl
  3. dendrite Source: Ensembl
  4. endoplasmic reticulum Source: UniProtKB-KW
  5. Golgi apparatus Source: UniProtKB-KW
  6. nucleus Source: UniProtKB-KW
  7. plasma membrane Source: UniProtKB-KW
  8. protein-DNA complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Golgi apparatus, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi61 – 611D → A: Abolishes cleavage by caspase-3. 1 Publication
Mutagenesisi64 – 641D → A: Abolishes cleavage by caspase-3. 1 Publication

Organism-specific databases

PharmGKBiPA26934.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 256256CalsenilinPRO_0000073814Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki26 – 26Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)
Lipidationi45 – 451S-palmitoyl cysteineBy similarity
Lipidationi46 – 461S-palmitoyl cysteineBy similarity
Modified residuei63 – 631Phosphoserine; by CK11 Publication
Cross-linki90 – 90Glycyl 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 conjugation

Proteomic databases

PaxDbiQ9Y2W7.
PRIDEiQ9Y2W7.

PTM databases

PhosphoSiteiQ9Y2W7.

Miscellaneous databases

PMAP-CutDBQ3YAC3.

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

BgeeiQ9Y2W7.
CleanExiHS_KCNIP3.
GenevestigatoriQ9Y2W7.

Organism-specific databases

HPAiCAB006907.

Interactioni

Subunit structurei

Binds to DNA as a homomultimer. Dimerization is induced by binding to calcium. Component of heteromultimeric potassium channels. Interacts with KCND2 and KCND3 (By similarity). Interacts with the C-terminus of PSEN1 and PSEN2 and with PSEN2 CTF subunit. Associates with KCN1.By similarity2 Publications

Protein-protein interaction databases

BioGridi119042. 17 interactions.
IntActiQ9Y2W7. 1 interaction.
MINTiMINT-1453732.
STRINGi9606.ENSP00000295225.

Structurei

Secondary structure

1
256
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi164 – 17411Combined sources
Beta strandi179 – 1824Combined sources
Helixi184 – 19310Combined sources
Beta strandi211 – 2133Combined sources
Helixi214 – 2229Combined sources
Beta strandi227 – 2315Combined sources
Helixi232 – 2398Combined sources
Helixi243 – 25412Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E6WNMR-A161-256[»]
ProteinModelPortaliQ9Y2W7.
SMRiQ9Y2W7. Positions 76-256.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y2W7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini67 – 12357EF-hand 1; degeneratePROSITE-ProRule annotationAdd
BLAST
Domaini126 – 16136EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini162 – 19736EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini210 – 24536EF-hand 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni243 – 25614Interaction with KCND2By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the recoverin family.Curated
Contains 4 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5126.
GeneTreeiENSGT00760000118820.
HOGENOMiHOG000233019.
HOVERGENiHBG108179.
InParanoidiQ9Y2W7.
OMAiMGIQGME.
OrthoDBiEOG7GJ6F3.
PhylomeDBiQ9Y2W7.
TreeFamiTF318560.

Family and domain databases

Gene3Di1.10.238.10. 3 hits.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR028846. Recoverin.
[Graphical view]
PANTHERiPTHR23055. PTHR23055. 1 hit.
PfamiPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 3 hits.
[Graphical view]
PROSITEiPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

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.

« Hide

        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
Length:256
Mass (Da):29,231
Last modified:November 1, 1999 - v1
Checksum:i635C3EDF8B91E1C5
GO
Isoform 2 (identifier: Q9Y2W7-2) [UniParc]FASTAAdd to Basket

Also known as: KChIP3.2, KChIP4.2

The sequence of this isoform differs from the canonical sequence as follows:
     103-124: Missing.

Note: No experimental confirmation available.

Show »
Length:234
Mass (Da):26,687
Checksum:i4AC9058CBBD08169
GO
Isoform 3 (identifier: Q9Y2W7-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.
     27-60: KEGIKWQRPRLSRQALMRCCLVKWILSSTAPQGS → MGIQGMELCAMAVVVLLFIAVLKQFGILEPISME

Show »
Length:230
Mass (Da):26,335
Checksum:iE6CEC7D4A37E5705
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti182 – 1821I → V in CAB56836. (PubMed:10078534)Curated
Sequence conflicti182 – 1821I → V in CAB56835. (PubMed:10078534)Curated
Sequence conflicti207 – 2071R → Q in CAB56836. (PubMed:10078534)Curated
Sequence conflicti207 – 2071R → Q in CAB56835. (PubMed:10078534)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti119 – 1191A → V.
Corresponds to variant rs35658670 [ dbSNP | Ensembl ].
VAR_048663
Natural varianti170 – 1701A → S in a breast cancer sample; somatic mutation. 1 Publication
VAR_035463
Natural varianti179 – 1791D → Y in a breast cancer sample; somatic mutation. 1 Publication
VAR_035464

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2626Missing in isoform 3. 1 PublicationVSP_040982Add
BLAST
Alternative sequencei27 – 6034KEGIK…APQGS → MGIQGMELCAMAVVVLLFIA VLKQFGILEPISME in isoform 3. 1 PublicationVSP_040983Add
BLAST
Alternative sequencei103 – 12422Missing in isoform 2. 1 PublicationVSP_015040Add
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.
CCDSiCCDS2013.1. [Q9Y2W7-1]
CCDS33245.1. [Q9Y2W7-3]
RefSeqiNP_001030086.1. NM_001034914.1. [Q9Y2W7-3]
NP_038462.1. NM_013434.4. [Q9Y2W7-1]
UniGeneiHs.437376.

Genome annotation databases

EnsembliENST00000295225; ENSP00000295225; ENSG00000115041. [Q9Y2W7-1]
ENST00000468529; ENSP00000417499; ENSG00000115041. [Q9Y2W7-3]
GeneIDi30818.
KEGGihsa:30818.
UCSCiuc002sup.3. human. [Q9Y2W7-1]
uc002suq.3. human. [Q9Y2W7-3]

Polymorphism databases

DMDMi13431428.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-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
Entry Method Resolution (Å) Chain Positions PDBsum
2E6W NMR - A 161-256 [» ]
ProteinModelPortali Q9Y2W7.
SMRi Q9Y2W7. Positions 76-256.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119042. 17 interactions.
IntActi Q9Y2W7. 1 interaction.
MINTi MINT-1453732.
STRINGi 9606.ENSP00000295225.

PTM databases

PhosphoSitei Q9Y2W7.

Polymorphism databases

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 GC02P095963.
HGNCi HGNC:15523. KCNIP3.
HPAi CAB006907.
MIMi 604662. gene.
neXtProti NX_Q9Y2W7.
PharmGKBi PA26934.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5126.
GeneTreei ENSGT00760000118820.
HOGENOMi HOG000233019.
HOVERGENi HBG108179.
InParanoidi Q9Y2W7.
OMAi MGIQGME.
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.
Genevestigatori Q9Y2W7.

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

« Hide 'large scale' publications
  1. "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.
  2. "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.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN POTASSIUM TRANSPORT.
  4. "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.
  5. Isbrandt D., Pongs O.
    Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  6. "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 databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "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.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Brain.
  8. "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.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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.
  11. "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.
  12. Cited for: FUNCTION IN APOPTOSIS.
  13. "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.
  14. "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.
  15. "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.
  16. "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.
  17. Cited for: SUMOYLATION AT LYS-26 AND LYS-90, SUBCELLULAR LOCATION.
  18. "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.
  19. Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-170 AND TYR-179.

Entry informationi

Entry nameiCSEN_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2W7
Secondary accession number(s): H7BY46
, Q3YAC3, Q3YAC4, Q53TJ5, Q96T40, Q9UJ84, Q9UJ85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1999
Last modified: November 26, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3