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Q9NZI2 (KCIP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Kv channel-interacting protein 1

Short name=KChIP1
Alternative name(s):
A-type potassium channel modulatory protein 1
Potassium channel-interacting protein 1
Vesicle APC-binding protein
Gene names
Name:KCNIP1
Synonyms:KCHIP1, VABP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length227 AA.
Sequence statusComplete.
Protein existenceEvidence 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 KCND1/Kv4.1 and KCND2/Kv4.2 currents. Seems to be involved in KCND2 trafficking to the cell surface. Ref.1 Ref.10 Ref.11

Subunit structure

Component of heteromultimeric potassium channels. Interacts with KCND3 and the N-terminal domain of KCND2. Probably part of a complex consisting of KCNIP1, KCNIP2 isoform 3 and KCND2. Self-associates to form homodimers and homotetramers. Interacts with KCNIP2 isoform 3 in a calcium-dependent manner. Interacts with Naja atra venom CTX3. Ref.1 Ref.12 Ref.13 Ref.14 Ref.15

Subcellular location

Cell membrane; Peripheral membrane protein By similarity.

Tissue specificity

Isoform 1 and isoform 2 are expressed in brain and kidney. Isoform 1 is also expressed in liver, pancreas, skeletal muscle, small intestine and testis. Isoform 2 is also expressed in lung, pancreas, leukocytes, prostate and thymus. Ref.9

Sequence similarities

Belongs to the recoverin family.

Contains 4 EF-hand domains.

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NZI2-1)

Also known as: KCHIP1b;

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: Q9NZI2-2)

Also known as: KCHIP1a;

The sequence of this isoform differs from the canonical sequence as follows:
     21-31: Missing.
     93-130: Missing.
Isoform 3 (identifier: Q9NZI2-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.
Isoform 4 (identifier: Q9NZI2-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: MGAVMGTFSSLQTKQRRPSKDIAWWYYQYQR → MSGCSKRCKLGFVKFAQTIFKLITGTLSK
Isoform 5 (identifier: Q9NZI2-5)

The sequence of this isoform differs from the canonical sequence as follows:
     21-31: Missing.
     96-96: G → GALPCLEGSPCVEFLPPSPALLFCLV

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 227227Kv channel-interacting protein 1
PRO_0000073818

Regions

Domain38 – 9457EF-hand 1; degenerate
Domain97 – 13236EF-hand 2
Domain133 – 16836EF-hand 3
Domain181 – 21636EF-hand 4
Calcium binding146 – 157121 Ref.15
Calcium binding194 – 205122 Ref.15
Region214 – 22714Interaction with KCND2 By similarity

Natural variations

Alternative sequence1 – 3939Missing in isoform 3.
VSP_015043
Alternative sequence1 – 3131MGAVM…YQYQR → MSGCSKRCKLGFVKFAQTIF KLITGTLSK in isoform 4.
VSP_041511
Alternative sequence21 – 3111Missing in isoform 2 and isoform 5.
VSP_015044
Alternative sequence93 – 13038Missing in isoform 2.
VSP_047686
Alternative sequence961G → GALPCLEGSPCVEFLPPSPA LLFCLV in isoform 5.
VSP_047687

Experimental info

Sequence conflict1161S → P in BAH13550. Ref.5

Secondary structure

................................... 227
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (KCHIP1b) [UniParc].

Last modified August 16, 2005. Version 2.
Checksum: D39DD5F8EA13B0FD

FASTA22726,817
        10         20         30         40         50         60 
MGAVMGTFSS LQTKQRRPSK DIAWWYYQYQ RDKIEDELEM TMVCHRPEGL EQLEAQTNFT 

        70         80         90        100        110        120 
KRELQVLYRG FKNECPSGVV NEDTFKQIYA QFFPHGDAST YAHYLFNAFD TTQTGSVKFE 

       130        140        150        160        170        180 
DFVTALSILL RGTVHEKLRW TFNLYDINKD GYINKEEMMD IVKAIYDMMG KYTYPVLKED 

       190        200        210        220 
TPRQHVDVFF QKMDKNKDGI VTLDEFLESC QEDDNIMRSL QLFQNVM 

« Hide

Isoform 2 (KCHIP1a) [UniParc].

Checksum: 8D1E9F2FEB2D5502
Show »

FASTA17821,036
Isoform 3 [UniParc].

Checksum: 5712C89FF2FA0176
Show »

FASTA18822,079
Isoform 4 [UniParc].

Checksum: 15705CD8C4385B7B
Show »

FASTA22526,227
Isoform 5 [UniParc].

Checksum: 856A1EC2DEE17668
Show »

FASTA24127,842

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH KCND2.
[2]"Molecular cloning of human VABP gene."
Xia K., Fang H.Y., Zhong X.Y., Xia J.H., Zhang Z.H.
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Brain.
[3]"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; 2; 4 AND 5), ALTERNATIVE SPLICING.
[4]"Study on mutations in KCNIP1 gene."
Zheng L., Jun X.X., Yue F.F., Min L.Y., Ming S.Y., Jun Y.F.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[5]"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 4).
Tissue: Testis.
[6]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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 2).
Tissue: Brain.
[9]"Differential modulation of Kv4 kinetics by KCHIP1 splice variants."
Van Hoorick D., Raes A., Keysers W., Mayeur E., Snyders D.J.
Mol. Cell. Neurosci. 24:357-366(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1), TISSUE SPECIFICITY (ISOFORMS 1 AND 2).
[10]"Different effects of the Ca(2+)-binding protein, KChIP1, on two Kv4 subfamily members, Kv4.1 and Kv4.2."
Nakamura T.Y., Nandi S., Pountney D.J., Artman M., Rudy B., Coetzee W.A.
FEBS Lett. 499:205-209(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"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.
[12]"Evidence showing an intermolecular interaction between KChIP proteins and Taiwan cobra cardiotoxins."
Lin Y.-L., Lin S.-R., Wu T.T., Chang L.-S.
Biochem. Biophys. Res. Commun. 319:720-724(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNAKE CTX3.
[13]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCNIP2 AND KCDN2, HOMOOLIGOMERIZATION.
[14]"Two N-terminal domains of Kv4 K(+) channels regulate binding to and modulation by KChIP1."
Scannevin R.H., Wang K., Jow F., Megules J., Kopsco D.C., Edris W., Carroll K.C., Lu Q., Xu W., Xu Z., Katz A.H., Olland S., Lin L., Taylor M., Stahl M., Malakian K., Somers W., Mosyak L. expand/collapse author list , Bowlby M.R., Chanda P., Rhodes K.J.
Neuron 41:587-598(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) (ISOFORM 2), INTERACTION WITH KCDN2 AND KCDN3.
[15]"Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer."
Pioletti M., Findeisen F., Hura G.L., Minor D.L. Jr.
Nat. Struct. Mol. Biol. 13:987-995(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS) OF 48-227 IN COMPLEX WITH KCND3, SUBUNIT, CALCIUM-BINDING.
[16]"Structural basis for modulation of Kv4 K+ channels by auxiliary KChIP subunits."
Wang H., Yan Y., Liu Q., Huang Y., Shen Y., Chen L., Chen Y., Yang Q., Hao Q., Wang K., Chai J.
Nat. Neurosci. 10:32-39(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 49-227 IN COMPLEX WITH KCND3.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF199597 mRNA. Translation: AAF33682.1.
AY170821 mRNA. Translation: AAN77491.1.
DQ148476 mRNA. Translation: AAZ77793.1.
DQ148477 mRNA. Translation: AAZ77794.1.
DQ148478 mRNA. Translation: AAZ77795.1.
DQ148479 mRNA. Translation: AAZ77796.1.
AY780424 mRNA. Translation: AAV51968.1.
AK301775 mRNA. Translation: BAH13550.1.
AC008619 Genomic DNA. No translation available.
AC008719 Genomic DNA. No translation available.
AC027306 Genomic DNA. No translation available.
AC027312 Genomic DNA. No translation available.
AC034199 Genomic DNA. No translation available.
AC113432 Genomic DNA. No translation available.
AC134820 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61470.1.
BC050375 mRNA. Translation: AAH50375.1.
CCDSCCDS34285.1. [Q9NZI2-4]
CCDS34286.1. [Q9NZI2-1]
CCDS64312.1. [Q9NZI2-5]
CCDS64313.1. [Q9NZI2-3]
RefSeqNP_001030009.1. NM_001034837.2. [Q9NZI2-1]
NP_001030010.1. NM_001034838.2. [Q9NZI2-4]
NP_001265268.1. NM_001278339.1. [Q9NZI2-5]
NP_001265269.1. NM_001278340.1. [Q9NZI2-3]
NP_055407.1. NM_014592.3.
UniGeneHs.484111.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1S1EX-ray2.30A1-227[»]
2I2RX-ray3.35E/F/G/H/M/N/O/P48-227[»]
2NZ0X-ray3.20A/C49-227[»]
ProteinModelPortalQ9NZI2.
SMRQ9NZI2. Positions 49-227.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119044. 3 interactions.
DIPDIP-29246N.
IntActQ9NZI2. 2 interactions.
STRING9606.ENSP00000395323.

Polymorphism databases

DMDM73621122.

Proteomic databases

MaxQBQ9NZI2.
PaxDbQ9NZI2.
PRIDEQ9NZI2.

Protocols and materials databases

DNASU30820.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328939; ENSP00000329686; ENSG00000182132.
ENST00000377360; ENSP00000366577; ENSG00000182132. [Q9NZI2-4]
ENST00000390656; ENSP00000375071; ENSG00000182132.
ENST00000411494; ENSP00000395323; ENSG00000182132. [Q9NZI2-1]
ENST00000434108; ENSP00000414886; ENSG00000182132. [Q9NZI2-5]
ENST00000520740; ENSP00000431102; ENSG00000182132. [Q9NZI2-3]
GeneID30820.
KEGGhsa:30820.
UCSCuc003mas.3. human. [Q9NZI2-1]
uc003mat.3. human. [Q9NZI2-2]

Organism-specific databases

CTD30820.
GeneCardsGC05P169780.
HGNCHGNC:15521. KCNIP1.
HPAHPA022864.
MIM604660. gene.
neXtProtNX_Q9NZI2.
PharmGKBPA30041.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5126.
HOGENOMHOG000233019.
HOVERGENHBG108179.
InParanoidQ9NZI2.
OMAKQHVDAF.
OrthoDBEOG7GJ6F3.
PhylomeDBQ9NZI2.
TreeFamTF318560.

Gene expression databases

ArrayExpressQ9NZI2.
BgeeQ9NZI2.
CleanExHS_KCNIP1.
GenevestigatorQ9NZI2.

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.
IPR028846. Recoverin.
[Graphical view]
PANTHERPTHR23055. PTHR23055. 1 hit.
PfamPF13499. EF-hand_7. 1 hit.
[Graphical view]
SMARTSM00054. EFh. 3 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKCNIP1. human.
EvolutionaryTraceQ9NZI2.
GeneWikiKCNIP1.
GenomeRNAi30820.
NextBio52920.
PROQ9NZI2.
SOURCESearch...

Entry information

Entry nameKCIP1_HUMAN
AccessionPrimary (citable) accession number: Q9NZI2
Secondary accession number(s): B7Z7B4 expand/collapse secondary AC list , Q3YAD0, Q3YAD1, Q3YAD2, Q3YAD3, Q5U822
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: July 9, 2014
This is version 120 of the entry and version 2 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 chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM