CPLM-000053

Genbank Nucleotide ID

Chloride intracellular channel protein 1

Protein Synonyms/Alias

Chloride channel ABP; Nuclear chloride ion channel 27; NCC27; Regulatory nuclear chloride ion channel protein; hRNCC

Homo sapiens (Human)

Position	Peptide	Type	References
13	PQVELFVKAGSDGAK	acetylation	[1, 2]
20	KAGSDGAKIGNCPFS	ubiquitination	[3, 4]
49	NVTTVDTKRRTETVQ	acetylation	[5, 6]
49	NVTTVDTKRRTETVQ	ubiquitination	[3, 7]
57	RRTETVQKLCPGGQL	ubiquitination	[7]
113	AGLDIFAKFSAYIKN	ubiquitination	[3]
119	AKFSAYIKNSNPALN	acetylation	[1, 2, 5, 6]
119	AKFSAYIKNSNPALN	ubiquitination	[2, 3, 4, 7, 8, 9, 10, 11, 12]
131	ALNDNLEKGLLKALK	acetylation	[1, 2, 5, 6]
131	ALNDNLEKGLLKALK	ubiquitination	[2, 3, 4, 7, 11, 12]
135	NLEKGLLKALKVLDN	acetylation	[1, 2, 5]
135	NLEKGLLKALKVLDN	ubiquitination	[2, 3, 4, 7, 11]
138	KGLLKALKVLDNYLT	ubiquitination	[3, 4, 7, 12]
166	DEGVSQRKFLDGNEL	ubiquitination	[4, 7, 11]
183	ADCNLLPKLHIVQVV	acetylation	[2, 6]
183	ADCNLLPKLHIVQVV	ubiquitination	[2, 4, 9]
192	HIVQVVCKKYRGFTI	ubiquitination	[4]
193	IVQVVCKKYRGFTIP	ubiquitination	[4]

[1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[5] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
[6] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[7] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[8] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
[9] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[10] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[11] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[12] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]

Functional Description

Can insert into membranes and form chloride ion channels. Channel activity depends on the pH. Membrane insertion seems to be redox-regulated and may occur only under oxydizing conditions. Involved in regulation of the cell cycle.

DOMAIN 93 233 GST C-terminal.
REGION 2 90 Required for insertion into the membrane.
BINDING 64 64 Glutathione; via carbonyl oxygen.
BINDING 77 77 Glutathione.
MOD_RES 2 2 N-acetylalanine.
MOD_RES 13 13 N6-acetyllysine.
MOD_RES 24 24 S-glutathionyl cysteine.
MOD_RES 119 119 N6-acetyllysine.
MOD_RES 131 131 N6-acetyllysine.
MOD_RES 135 135 N6-acetyllysine.
MOD_RES 233 233 Phosphotyrosine (By similarity).
DISULFID 24 59

3D-structure; Acetylation; Cell membrane; Chloride; Chloride channel; Complete proteome; Cytoplasm; Direct protein sequencing; Disulfide bond; Glutathionylation; Ion channel; Ion transport; Membrane; Nucleus; Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005903; C:brush border; TAS:UniProtKB.
GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
GO:0005739; C:mitochondrion; IEA:Compara.
GO:0005635; C:nuclear envelope; IDA:MGI.
GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO:0005254; F:chloride channel activity; IDA:MGI.
GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro.
GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Compara.
GO:0051881; P:regulation of mitochondrial membrane potential; IEA:Compara.
GO:0007165; P:signal transduction; TAS:UniProtKB.

IPR010987; Glutathione-S-Trfase_C-like.
IPR017933; Glutathione_S_Trfase/Cl_chnl_C.
IPR002946; Int_Cl_channel.
IPR012336; Thioredoxin-like_fold.

PR01263; INTCLCHANNEL.