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Q9Y2W7 (CSEN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:KCNIP3
Synonyms:CSEN, DREAM, KCHIP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length256 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.3 Ref.12 Ref.13 Ref.14

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. Ref.1 Ref.2 Ref.3 Ref.12 Ref.13 Ref.14

May play a role in the regulation of PSEN2 proteolytic processing and apoptosis. Together with PSEN2 involved in modulation of beta-amyloid formation. Ref.1 Ref.2 Ref.3 Ref.12 Ref.13 Ref.14

Subunit structure

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. Ref.11 Ref.18

Subcellular location

Cytoplasm. Cell membrane; 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. Ref.11 Ref.17

Tissue specificity

Highly expressed in brain. Widely expressed at lower levels. Expression levels are elevated in brain cortex regions affected by Alzheimer disease. Ref.16

Post-translational modification

Palmitoylated. Palmitoylation enhances association with the plasma membrane By similarity.

Proteolytically cleaved by caspase-3. Ref.11

Phosphorylation at Ser-63 inhibits cleavage by CASP3.

Sequence similarities

Belongs to the recoverin family.

Contains 4 EF-hand domains.

Ontologies

Keywords
   Biological processApoptosis
Ion transport
Potassium transport
Transcription
Transcription regulation
Transport
   Cellular componentCell membrane
Cytoplasm
Endoplasmic reticulum
Golgi apparatus
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandCalcium
Metal-binding
Potassium
   Molecular functionIon channel
Potassium channel
Repressor
Voltage-gated channel
   PTMIsopeptide bond
Lipoprotein
Palmitate
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

behavioral response to pain

Inferred from electronic annotation. Source: Ensembl

intracellular protein transport

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.2. Source: ProtInc

sensory perception of pain

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement PubMed 10900016. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

axon terminus

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: Ensembl

dendrite

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein-DNA complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionDNA binding

Traceable author statement Ref.2. Source: ProtInc

calcium ion binding

Traceable author statement PubMed 10900016. Source: ProtInc

potassium channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

potassium channel regulator activity

Inferred from electronic annotation. Source: Ensembl

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

transcription corepressor activity

Traceable author statement Ref.2. Source: ProtInc

voltage-gated ion channel activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y2W7-1)

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.
Isoform 2 (identifier: Q9Y2W7-2)

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.
Isoform 3 (identifier: Q9Y2W7-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 256256Calsenilin
PRO_0000073814

Regions

Domain67 – 12357EF-hand 1; degenerate
Domain126 – 16136EF-hand 2
Domain162 – 19736EF-hand 3
Domain210 – 24536EF-hand 4
Calcium binding175 – 186121 By similarity
Calcium binding223 – 234122 By similarity
Region243 – 25614Interaction with KCND2 By similarity

Amino acid modifications

Modified residue631Phosphoserine; by CK1 Ref.15
Lipidation451S-palmitoyl cysteine By similarity
Lipidation461S-palmitoyl cysteine By similarity
Cross-link26Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) Ref.17
Cross-link90Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) Ref.17

Natural variations

Alternative sequence1 – 2626Missing in isoform 3.
VSP_040982
Alternative sequence27 – 6034KEGIK…APQGS → MGIQGMELCAMAVVVLLFIA VLKQFGILEPISME in isoform 3.
VSP_040983
Alternative sequence103 – 12422Missing in isoform 2.
VSP_015040
Natural variant1191A → V.
Corresponds to variant rs35658670 [ dbSNP | Ensembl ].
VAR_048663
Natural variant1701A → S in a breast cancer sample; somatic mutation. Ref.19
VAR_035463
Natural variant1791D → Y in a breast cancer sample; somatic mutation. Ref.19
VAR_035464

Experimental info

Mutagenesis611D → A: Abolishes cleavage by caspase-3. Ref.11
Mutagenesis641D → A: Abolishes cleavage by caspase-3. Ref.11
Sequence conflict1821I → V in CAB56836. Ref.2
Sequence conflict1821I → V in CAB56835. Ref.2
Sequence conflict2071R → Q in CAB56836. Ref.2
Sequence conflict2071R → Q in CAB56835. Ref.2

Secondary structure

............... 256
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (KChIP3.1) [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 635C3EDF8B91E1C5

FASTA25629,231
        10         20         30         40         50         60 
MQPAKEVTKA SDGSLLGDLG HTPLSKKEGI KWQRPRLSRQ ALMRCCLVKW ILSSTAPQGS 

        70         80         90        100        110        120 
DSSDSELELS TVRHQPEGLD QLQAQTKFTK KELQSLYRGF KNECPTGLVD EDTFKLIYAQ 

       130        140        150        160        170        180 
FFPQGDATTY AHFLFNAFDA DGNGAIHFED FVVGLSILLR GTVHEKLKWA FNLYDINKDG 

       190        200        210        220        230        240 
YITKEEMLAI MKSIYDMMGR HTYPILREDA PAEHVERFFE KMDRNQDGVV TIEEFLEACQ 

       250 
KDENIMSSMQ LFENVI 

« Hide

Isoform 2 (KChIP3.2) (KChIP4.2) [UniParc].

Checksum: 4AC9058CBBD08169
Show »

FASTA23426,687
Isoform 3 [UniParc].

Checksum: E6CEC7D4A37E5705
Show »

FASTA23026,335

References

« Hide 'large scale' references
[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]"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.
[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. expand/collapse author list , 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. expand/collapse author list , 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]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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"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.
[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]"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.
[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]"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. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-170 AND TYR-179.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001030086.1. NM_001034914.1.
NP_038462.1. NM_013434.4.
UniGeneHs.437376.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E6WNMR-A161-256[»]
ProteinModelPortalQ9Y2W7.
SMRQ9Y2W7. Positions 76-256.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119042. 16 interactions.
IntActQ9Y2W7. 1 interaction.
MINTMINT-1453732.
STRING9606.ENSP00000295225.

PTM databases

PhosphoSiteQ9Y2W7.

Polymorphism databases

DMDM13431428.

Proteomic databases

PaxDbQ9Y2W7.
PRIDEQ9Y2W7.

Protocols and materials databases

DNASU30818.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295225; ENSP00000295225; ENSG00000115041. [Q9Y2W7-1]
ENST00000468529; ENSP00000417499; ENSG00000115041. [Q9Y2W7-3]
GeneID30818.
KEGGhsa:30818.
UCSCuc002sup.3. human. [Q9Y2W7-1]
uc002suq.3. human. [Q9Y2W7-3]

Organism-specific databases

CTD30818.
GeneCardsGC02P095963.
HGNCHGNC:15523. KCNIP3.
HPACAB006907.
MIM604662. gene.
neXtProtNX_Q9Y2W7.
PharmGKBPA26934.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5126.
HOGENOMHOG000233019.
HOVERGENHBG108179.
InParanoidQ9Y2W7.
OMAMGIQGME.
OrthoDBEOG7GJ6F3.
PhylomeDBQ9Y2W7.
TreeFamTF318560.

Gene expression databases

BgeeQ9Y2W7.
CleanExHS_KCNIP3.
GenevestigatorQ9Y2W7.

Family and domain databases

Gene3D1.10.238.10. 3 hits.
InterProIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001125. Recoverin_like.
[Graphical view]
PfamPF13499. EF-hand_7. 1 hit.
[Graphical view]
PRINTSPR00450. RECOVERIN.
SMARTSM00054. EFh. 3 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9Y2W7.
GeneWikiCalsenilin.
GenomeRNAi30818.
NextBio35528162.
PMAP-CutDBQ3YAC3.
PROQ9Y2W7.
SOURCESearch...

Entry information

Entry nameCSEN_HUMAN
AccessionPrimary (citable) accession number: Q9Y2W7
Secondary accession number(s): H7BY46 expand/collapse secondary AC list , Q3YAC3, Q3YAC4, Q53TJ5, Q96T40, Q9UJ84, Q9UJ85
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1999
Last modified: March 19, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM