Q9NS61 (KCIP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Kv channel-interacting protein 2
Short name=KChIP2

Alternative name(s):
A-type potassium channel modulatory protein 2
Cardiac voltage-gated potassium channel modulatory subunit
Potassium channel-interacting protein 2

Gene names

Name:	KCNIP2
Synonyms:	KCHIP2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	270 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 KCND3 trafficking to the cell surface By similarity. Ref.1 Ref.3 Ref.4 Ref.14 Ref.15 Ref.17
Subunit structure	Component of heteromultimeric potassium channels. The KCND2-KCNIP2 channel complex contains four KCND2 and four KCNIP2 subunits. Interacts with KCND2. Isoform 1 and isoform 3 interact with KCND3 isoform 1. Probably part of a complex consisting of KCNIP1, KCNIP2 isoform 3 and KCND2. At least isoform 2 and isoform 3 can self-associate to form homodimers and homotetramers. Isoform 3 interacts with KCNIP1 in a calcium-dependent manner. Ref.1 Ref.4 Ref.14 Ref.16 Ref.18
Subcellular location	Isoform 1: Cell membrane; Lipid-anchor By similarity. Isoform 2: Cell membrane; Lipid-anchor By similarity. Isoform 6: Cell membrane; Lipid-anchor By similarity.
Tissue specificity	Expressed in brain. Colocalizes with KCND2 in excitatory neurons including cortical and hippocampal CA1 pyramidal cells. Isoform 3 is expressed in heart and in umbilical vein endothelial cells. Not expressed in fetal heart. Ref.2 Ref.3 Ref.18
Post-translational modification	Palmitoylated. Palmitoylation enhances association with the plasma membrane By similarity.
Sequence similarities	Belongs to the recoverin family. Contains 4 EF-hand domains.

Ontologies

Keywords
Biological process	Ion transport Potassium transport Transport
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	Calcium Potassium
Molecular function	Ionic channel Potassium channel Voltage-gated channel
PTM	Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	clustering of voltage-gated potassium channels Inferred from direct assay Ref.4. Source: UniProtKB detection of calcium ion Traceable author statement. Source: ProtInc muscle contraction Non-traceable author statement Ref.4. Source: UniProtKB regulation of heart contraction Traceable author statement Ref.4. Source: UniProtKB signal transduction Traceable author statement. Source: ProtInc synaptic transmission Non-traceable author statement Ref.4. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay Ref.4. Source: UniProtKB voltage-gated potassium channel complex Non-traceable author statement Ref.4. Source: UniProtKB
Molecular function	A-type (transient outward) potassium channel activity Traceable author statement Ref.4. Source: UniProtKB ER retention sequence binding Non-traceable author statement Ref.4. Source: UniProtKB calcium ion binding Traceable author statement Ref.4. Source: UniProtKB identical protein binding Inferred from physical interaction Ref.16. Source: IntAct protein N-terminus binding Inferred from physical interaction Ref.4. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
KCND2	Q9NZV8	3	EBI-1053010,EBI-1646745
KCNIP1	Q9NZI2	4	EBI-1053010,EBI-2120635

Alternative products

This entry describes 9 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NS61-1)

Also known as: KChIP2a; KChIP2b; KCHIP2.4; KCHIP2L;

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: Q9NS61-2)

Also known as: 3; KChIP2.1; KChIP2b;

The sequence of this isoform differs from the canonical sequence as follows:
     57-75: TLAAPASLRPHRPRLLDPD → N

Isoform 3 (identifier: Q9NS61-3)

Also known as: 2; KChIP2.2; KChIP2c; KCHIP2S;

The sequence of this isoform differs from the canonical sequence as follows:
     25-74: Missing.

Isoform 4 (identifier: Q9NS61-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-73: MRGQGRKESL...LRPHRPRLLD → MNRCPRRCRSPLGQAARSLYQLVTGSLS

Isoform 5 (identifier: Q9NS61-5)

The sequence of this isoform differs from the canonical sequence as follows:
     25-74: Missing.
     160-163: Missing.

Isoform 6 (identifier: Q9NS61-6)

Also known as: KCHIP4.2;

The sequence of this isoform differs from the canonical sequence as follows:
     57-57: T → IGRVFRFLGDSSLPSA

Isoform 7 (identifier: Q9NS61-7)

The sequence of this isoform differs from the canonical sequence as follows:
     25-74: Missing.
     116-116: N → NPGALSFQ

Isoform 8 (identifier: Q9NS61-8)

Also known as: KCHIP2.6;

The sequence of this isoform differs from the canonical sequence as follows:
     1-93: Missing.
     94-162: EQLQEQTKFT...DTNHDGSVSF → MWLSWTAWTM...SRFTPSSFLK

Isoform 9 (identifier: Q9NS61-9)

Also known as: KCHIP2.5;

The sequence of this isoform differs from the canonical sequence as follows:
     25-74: Missing.
     163-198: Missing.
     256-270: DENIMRSMQLFDNVI → VQLPALYITLTWTQA

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 270	270	Kv channel-interacting protein 2		PRO_0000073821
Regions
	Domain	81 – 137	57	EF-hand 1; degenerate
	Domain	140 – 175	36	EF-hand 2
	Domain	176 – 211	36	EF-hand 3
	Domain	224 – 259	36	EF-hand 4
	Calcium binding	189 – 200	12	1 By similarity
	Calcium binding	237 – 248	12	2 By similarity
	Region	257 – 270	14	Interaction with KCND2 By similarity
Amino acid modifications
	Modified residue	103	1	Phosphothreonine Ref.19
	Modified residue	111	1	Phosphotyrosine Ref.19
	Lipidation	45	1	S-palmitoyl cysteine By similarity
	Lipidation	46	1	S-palmitoyl cysteine By similarity
Natural variations
	Alternative sequence	1 – 93	93	Missing in isoform 8.		VSP_015049
	Alternative sequence	1 – 73	73	MRGQG…PRLLD → MNRCPRRCRSPLGQAARSLY QLVTGSLS in isoform 4.		VSP_015050
	Alternative sequence	25 – 74	50	Missing in isoform 3, isoform 5, isoform 7 and isoform 9.		VSP_015051
	Alternative sequence	57 – 75	19	TLAAP…LLDPD → N in isoform 2.		VSP_015052
	Alternative sequence	57	1	T → IGRVFRFLGDSSLPSA in isoform 6.		VSP_015053
	Alternative sequence	94 – 162	69	EQLQE…GSVSF → MWLSWTAWTMNLNCPPCVTG LRVWSSCRSKPNSRARSCRS CTGASRTNVPAELSMRRTSS RFTPSSFLK in isoform 8.		VSP_015054
	Alternative sequence	116	1	N → NPGALSFQ in isoform 7.		VSP_015055
	Alternative sequence	160 – 163	4	Missing in isoform 5.		VSP_015056
	Alternative sequence	163 – 198	36	Missing in isoform 9.		VSP_015057
	Alternative sequence	256 – 270	15	DENIM…FDNVI → VQLPALYITLTWTQA in isoform 9.		VSP_015058
Experimental info
	Sequence conflict	50	1	A → V in BAA96740. Ref.2
	Sequence conflict	71	1	L → P in BAA96740. Ref.2
	Sequence conflict	75	1	D → V in BAA96741. Ref.2
	Sequence conflict	76	1	S → R in BAB55052. Ref.10
	Sequence conflict	78	1	D → E in BAA96740. Ref.2
	Sequence conflict	83	1	L → S in CAB66656. Ref.8
	Sequence conflict	224	1	A → P in BAA96740. Ref.2
	Sequence conflict	224	1	A → P in BAA96741. Ref.2
	Sequence conflict	239	1	N → S in AAP57633. Ref.9
	Sequence conflict	246	1	I → N in CAB66656. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (KChIP2a) (KChIP2b) (KCHIP2.4) (KCHIP2L) [UniParc]. Last modified June 28, 2011. Version 3. Checksum: B75AD02B9E273243	FASTA	270	30,907
	10 20 30 40 50 60 MRGQGRKESL SDSRDLDGSY DQLTGHPPGP TKKALKQRFL KLLPCCGPQA LPSVSETLAA 70 80 90 100 110 120 PASLRPHRPR LLDPDSVDDE FELSTVCHRP EGLEQLQEQT KFTRKELQVL YRGFKNECPS 130 140 150 160 170 180 GIVNEENFKQ IYSQFFPQGD SSTYATFLFN AFDTNHDGSV SFEDFVAGLS VILRGTVDDR 190 200 210 220 230 240 LNWAFNLYDL NKDGCITKEE MLDIMKSIYD MMGKYTYPAL REEAPREHVE SFFQKMDRNK 250 260 270 DGVVTIEEFI ESCQKDENIM RSMQLFDNVI
	Isoform 2 (3) (KChIP2.1) (KChIP2b) [UniParc]. Checksum: 7502F0C69D2B35FE	FASTA	252	28,943
	10 20 30 40 50 60 MRGQGRKESL SDSRDLDGSY DQLTGHPPGP TKKALKQRFL KLLPCCGPQA LPSVSENSVD 70 80 90 100 110 120 DEFELSTVCH RPEGLEQLQE QTKFTRKELQ VLYRGFKNEC PSGIVNEENF KQIYSQFFPQ 130 140 150 160 170 180 GDSSTYATFL FNAFDTNHDG SVSFEDFVAG LSVILRGTVD DRLNWAFNLY DLNKDGCITK 190 200 210 220 230 240 EEMLDIMKSI YDMMGKYTYP ALREEAPREH VESFFQKMDR NKDGVVTIEE FIESCQKDEN 250 IMRSMQLFDN VI
	Isoform 3 (2) (KChIP2.2) (KChIP2c) (KCHIP2S) [UniParc]. Checksum: 52FD8C601356338F	FASTA	220	25,562
	10 20 30 40 50 60 MRGQGRKESL SDSRDLDGSY DQLTDSVDDE FELSTVCHRP EGLEQLQEQT KFTRKELQVL 70 80 90 100 110 120 YRGFKNECPS GIVNEENFKQ IYSQFFPQGD SSTYATFLFN AFDTNHDGSV SFEDFVAGLS 130 140 150 160 170 180 VILRGTVDDR LNWAFNLYDL NKDGCITKEE MLDIMKSIYD MMGKYTYPAL REEAPREHVE 190 200 210 220 SFFQKMDRNK DGVVTIEEFI ESCQKDENIM RSMQLFDNVI
	Isoform 4 [UniParc]. Checksum: 7919AFDD3A5FACF1	FASTA	225	26,066
	10 20 30 40 50 60 MNRCPRRCRS PLGQAARSLY QLVTGSLSPD SVDDEFELST VCHRPEGLEQ LQEQTKFTRK 70 80 90 100 110 120 ELQVLYRGFK NECPSGIVNE ENFKQIYSQF FPQGDSSTYA TFLFNAFDTN HDGSVSFEDF 130 140 150 160 170 180 VAGLSVILRG TVDDRLNWAF NLYDLNKDGC ITKEEMLDIM KSIYDMMGKY TYPALREEAP 190 200 210 220 REHVESFFQK MDRNKDGVVT IEEFIESCQK DENIMRSMQL FDNVI
	Isoform 5 [UniParc]. Checksum: EDDF7A3B16108F08	FASTA	216	25,100
	10 20 30 40 50 60 MRGQGRKESL SDSRDLDGSY DQLTDSVDDE FELSTVCHRP EGLEQLQEQT KFTRKELQVL 70 80 90 100 110 120 YRGFKNECPS GIVNEENFKQ IYSQFFPQGD SSTYATFLFN AFDTNHDGSD FVAGLSVILR 130 140 150 160 170 180 GTVDDRLNWA FNLYDLNKDG CITKEEMLDI MKSIYDMMGK YTYPALREEA PREHVESFFQ 190 200 210 KMDRNKDGVV TIEEFIESCQ KDENIMRSMQ LFDNVI
	Isoform 6 (KCHIP4.2) [UniParc]. Checksum: 38A62414577BCF49	FASTA	285	32,510
	10 20 30 40 50 60 MRGQGRKESL SDSRDLDGSY DQLTGHPPGP TKKALKQRFL KLLPCCGPQA LPSVSEIGRV 70 80 90 100 110 120 FRFLGDSSLP SALAAPASLR PHRPRLLDPD SVDDEFELST VCHRPEGLEQ LQEQTKFTRK 130 140 150 160 170 180 ELQVLYRGFK NECPSGIVNE ENFKQIYSQF FPQGDSSTYA TFLFNAFDTN HDGSVSFEDF 190 200 210 220 230 240 VAGLSVILRG TVDDRLNWAF NLYDLNKDGC ITKEEMLDIM KSIYDMMGKY TYPALREEAP 250 260 270 280 REHVESFFQK MDRNKDGVVT IEEFIESCQK DENIMRSMQL FDNVI
	Isoform 7 [UniParc]. Checksum: 7F1D2B8E7F85D8B9	FASTA	227	26,263
	10 20 30 40 50 60 MRGQGRKESL SDSRDLDGSY DQLTDSVDDE FELSTVCHRP EGLEQLQEQT KFTRKELQVL 70 80 90 100 110 120 YRGFKNPGAL SFQECPSGIV NEENFKQIYS QFFPQGDSST YATFLFNAFD TNHDGSVSFE 130 140 150 160 170 180 DFVAGLSVIL RGTVDDRLNW AFNLYDLNKD GCITKEEMLD IMKSIYDMMG KYTYPALREE 190 200 210 220 APREHVESFF QKMDRNKDGV VTIEEFIESC QKDENIMRSM QLFDNVI
	Isoform 8 (KCHIP2.6) [UniParc]. Checksum: 8CF26C549F293353	FASTA	177	20,482
	10 20 30 40 50 60 MWLSWTAWTM NLNCPPCVTG LRVWSSCRSK PNSRARSCRS CTGASRTNVP AELSMRRTSS 70 80 90 100 110 120 RFTPSSFLKE DFVAGLSVIL RGTVDDRLNW AFNLYDLNKD GCITKEEMLD IMKSIYDMMG 130 140 150 160 170 KYTYPALREE APREHVESFF QKMDRNKDGV VTIEEFIESC QKDENIMRSM QLFDNVI
	Isoform 9 (KCHIP2.5) [UniParc]. Checksum: 4B810CA98F45A052	FASTA	184	21,401
	10 20 30 40 50 60 MRGQGRKESL SDSRDLDGSY DQLTDSVDDE FELSTVCHRP EGLEQLQEQT KFTRKELQVL 70 80 90 100 110 120 YRGFKNECPS GIVNEENFKQ IYSQFFPQGD SSTYATFLFN AFDTNHDGSV SFEEMLDIMK 130 140 150 160 170 180 SIYDMMGKYT YPALREEAPR EHVESFFQKM DRNKDGVVTI EEFIESCQKV QLPALYITLT WTQA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 10676964] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH KCND2.
[2]	"Molecular cloning and expression of the novel splice variants of K(+) channel-interacting protein 2." Ohya S., Morohashi Y., Muraki K., Tomita T., Watanabe M., Iwatsubo T., Imaizumi Y. Biochem. Biophys. Res. Commun. 282:96-102(2001) [PubMed: 11263977] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY. Tissue: Umbilical vein endothelial cell.
[3]	"hKChIP2 is a functional modifier of hKv4.3 potassium channels: cloning and expression of a short hKChIP2 splice variant." Decher N., Uyguner O., Scherer C.R., Karaman B., Yuksel-Apak M., Busch A.E., Steinmeyer K., Wollnik B. Cardiovasc. Res. 52:255-264(2001) [PubMed: 11684073] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY.
[4]	"Conserved Kv4 N-terminal domain critical for effects of Kv channel-interacting protein 2.2 on channel expression and gating." Baehring R., Dannenberg J., Peters H.C., Leicher T., Pongs O., Isbrandt D. J. Biol. Chem. 276:23888-23894(2001) [PubMed: 11287421] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH KCND2.
[5]	"Modulatory elements of voltage gated potassium channels." Juang G.J., Tomaselli G.F. Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 7). Tissue: Heart.
[6]	Isbrandt D., Pongs O. Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6; 8 AND 9).
[7]	"Structure, alternative splicing, and expression of the human and mouse KCNIP gene family." Pruunsild P., Timmusk T. Genomics 86:581-593(2005) [PubMed: 16112838] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING.
[8]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed: 11230166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Kidney.
[9]	Li H., Zhong J., Zhou G., Shen C., Lin L., Yang S. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
[10]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4). Tissue: Brain and Embryo.
[11]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[13]	"Full-length of some muscular transcripts, Telethon (Italy) project B41." Ievolella C., Trevisan S., Pacchioni B., Stanchi F., Frigimelica E., Scannapieco P., Corso V., Biasio B., Lanfranchi G. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 213-270. Tissue: Skeletal muscle.
[14]	"Modulation of Kv4.3 current by accessory subunits." Deschenes I., Tomaselli G.F. FEBS Lett. 528:183-188(2002) [PubMed: 12297301] [Abstract] Cited for: FUNCTION, INTERACTION WITH KCND3.
[15]	"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: 12829703] [Abstract] Cited for: FUNCTION.
[16]	"Protein-protein interactions of KChIP proteins and Kv4.2." Lin Y.-L., Chen C.Y., Cheng C.P., Chang L.S. Biochem. Biophys. Res. Commun. 321:606-610(2004) [PubMed: 15358149] [Abstract] Cited for: INTERACTION WITH KCNIP1 AND KCDN2, HOMOOLIGOMERIZATION.
[17]	"Ito channels are octomeric complexes with four subunits of each Kv4.2 and K+ channel-interacting protein 2." Kim L.A., Furst J., Butler M.H., Xu S., Grigorieff N., Goldstein S.A. J. Biol. Chem. 279:5549-5554(2004) [PubMed: 14623880] [Abstract] Cited for: FUNCTION, COMPOSITION OF THE KCND2-KCNIP2 COMPLEX.
[18]	"KChIPs and Kv4 alpha subunits as integral components of A-type potassium channels in mammalian brain." Rhodes K.J., Carroll K.I., Sung M.A., Doliveira L.C., Monaghan M.M., Burke S.L., Strassle B.W., Buchwalder L., Menegola M., Cao J., An W.F., Trimmer J.S. J. Neurosci. 24:7903-7915(2004) [PubMed: 15356203] [Abstract] Cited for: TISSUE SPECIFICITY, INTERACTION WITH KCND2.
[19]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-103 AND TYR-111, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Three-dimensional structure of I(to); Kv4.2-KChIP2 ion channels by electron microscopy at 21 Angstrom resolution." Kim L.A., Furst J., Gutierrez D., Butler M.H., Xu S., Goldstein S.A., Grigorieff N. Neuron 41:513-519(2004) [PubMed: 14980201] [Abstract] Cited for: ELECTRON MICROSCOPY OF THE KCND2-KCNIP2 COMPLEX.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF199598 mRNA. Translation: AAF33683.1. AB044584 mRNA. Translation: BAA96740.1. AB044585 mRNA. Translation: BAA96741.1. AY026328 mRNA. Translation: AAK07674.1. AY026331, AY026329, AY026330 Genomic DNA. Translation: AAK21972.1. AF347114 mRNA. Translation: AAK70356.1. AF295076 mRNA. Translation: AAG02120.1. AF295530 mRNA. Translation: AAG02121.1. AF367018 mRNA. Translation: AAK53707.1. AF367019 mRNA. Translation: AAK53708.1. AF367020 mRNA. Translation: AAK53709.1. AF367021 mRNA. Translation: AAK53710.1. DQ148480 mRNA. Translation: AAZ77797.1. DQ148481 mRNA. Translation: AAZ77798.1. AL136722 mRNA. Translation: CAB66656.1. AY302141 mRNA. Translation: AAP57633.1. AK027347 mRNA. Translation: BAB55052.1. AK315042 mRNA. Translation: BAG37523.1. AC010789 Genomic DNA. No translation available. BC034685 mRNA. Translation: AAH34685.1. AJ276317 mRNA. Translation: CAB77054.1.
IPI	IPI00005558. IPI00008959. IPI00045897. IPI00045898. IPI00173952. IPI00289162. IPI00298990. IPI00306640. IPI00646538.
RefSeq	NP_055406.2. NM_014591.4. NP_775283.1. NM_173191.2. NP_775284.1. NM_173192.2. NP_775285.1. NM_173193.2. NP_775286.1. NM_173194.2. NP_775287.1. NM_173195.2. NP_775289.1. NM_173197.2.
UniGene	Hs.97044.
3D structure databases
ProteinModelPortal	Q9NS61.
SMR	Q9NS61. Positions 6-84, 90-270.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NS61. 9 interactions.
STRING	Q9NS61.
PTM databases
PhosphoSite	Q9NS61.
Polymorphism databases
DMDM	73621125.
Proteomic databases
PRIDE	Q9NS61.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000356640; ENSP00000349055; ENSG00000120049.
GeneID	30819.
KEGG	hsa:30819.
UCSC	uc001kty.1. human. uc001ktz.1. human. uc001kuc.1. human. uc001kud.1. human. uc001kuf.1. human. uc001kug.1. human. uc009xwv.1. human.
Organism-specific databases
CTD	30819.
GeneCards	GC10M103575.
HGNC	HGNC:15522. KCNIP2.
MIM	604661. gene.
neXtProt	NX_Q9NS61.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00560000076973.
HOVERGEN	HBG108179.
OMA	ILRGTTD.
PhylomeDB	Q9NS61.
Gene expression databases
ArrayExpress	Q9NS61.
Bgee	Q9NS61.
Genevestigator	Q9NS61.
GermOnline	ENSG00000120049. Homo sapiens.
Family and domain databases
InterPro	IPR018248. EF-hand. IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR018249. EF_HAND_2. IPR002048. EF_hand_Ca-bd. IPR001125. Recoverin. [Graphical view]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 1 hit.
Pfam	PF00036. efhand. 1 hit. [Graphical view]
PRINTS	PR00450. RECOVERIN.
SMART	SM00054. EFh. 3 hits. [Graphical view]
PROSITE	PS00018. EF_HAND_1. 3 hits. PS50222. EF_HAND_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other
NextBio	52904.
SOURCE	Search...

Entry information

Entry name

KCIP2_HUMAN

Accession

Primary (citable) accession number: Q9NS61
Secondary accession number(s): A6NJE5 , A8MQ75, Q3YAC8, Q3YAC9, Q7Z6F1, Q96K86, Q96T41, Q96T42, Q96T43, Q96T44, Q9H0N4, Q9HD10, Q9HD11, Q9NS60, Q9NY10, Q9NZI1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	June 28, 2011
Last modified:	January 25, 2012
This is version 93 of the entry and version 3 of the sequence. [Complete history]

Entry status

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.