dbPTM

CLIC1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CLIC1_HUMAN
UniProt AC	O00299
Protein Name	Chloride intracellular channel protein 1
Gene Name	CLIC1
Organism	Homo sapiens (Human).
Sequence Length	241
Subcellular Localization	Nucleus. Nucleus membrane Single-pass membrane protein . Cytoplasm. Cell membrane Single-pass membrane protein . Mostly in the nucleus including in the nuclear membrane. Small amount in the cytoplasm and the plasma membrane. Exists both as solubl
Protein 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..
Protein Sequence	MAEEQPQVELFVKAGSDGAKIGNCPFSQRLFMVLWLKGVTFNVTTVDTKRRTETVQKLCPGGQLPFLLYGTEVHTDTNKIEEFLEAVLCPPRYPKLAALNPESNTAGLDIFAKFSAYIKNSNPALNDNLEKGLLKALKVLDNYLTSPLPEEVDETSAEDEGVSQRKFLDGNELTLADCNLLPKLHIVQVVCKKYRGFTIPEAFRGVHRYLSNAYAREEFASTCPDDEEIELAYEQVAKALK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEEQPQVE ------CCCCCCCEE	29.09	22223895
13	Acetylation	PQVELFVKAGSDGAK CCEEEEEEECCCCCE	39.43	19608861
20	Acetylation	KAGSDGAKIGNCPFS EECCCCCEECCCCHH	57.59	26051181
20	Ubiquitination	KAGSDGAKIGNCPFS EECCCCCEECCCCHH	57.59	21906983
24	S-glutathionyl cysteine	DGAKIGNCPFSQRLF CCCEECCCCHHHHHH	2.80	-
24	S-nitrosylation	DGAKIGNCPFSQRLF CCCEECCCCHHHHHH	2.80	24105792
24	Glutathionylation	DGAKIGNCPFSQRLF CCCEECCCCHHHHHH	2.80	16286078
24	S-palmitoylation	DGAKIGNCPFSQRLF CCCEECCCCHHHHHH	2.80	29575903
44	Phosphorylation	KGVTFNVTTVDTKRR HCCEEEEEECCCCCC	23.39	23186163
45	Phosphorylation	GVTFNVTTVDTKRRT CCEEEEEECCCCCCC	16.47	23186163
48	Phosphorylation	FNVTTVDTKRRTETV EEEEECCCCCCCHHH	23.32	22199227
49	Acetylation	NVTTVDTKRRTETVQ EEEECCCCCCCHHHH	35.10	23954790
49	Ubiquitination	NVTTVDTKRRTETVQ EEEECCCCCCCHHHH	35.10	21890473
49	Malonylation	NVTTVDTKRRTETVQ EEEECCCCCCCHHHH	35.10	26320211
52	Phosphorylation	TVDTKRRTETVQKLC ECCCCCCCHHHHHHC	39.79	20068231
57	Ubiquitination	RRTETVQKLCPGGQL CCCHHHHHHCCCCCC	47.96	21906983
59	S-nitrosylation	TETVQKLCPGGQLPF CHHHHHHCCCCCCCE	3.66	24105792
95	Ubiquitination	LCPPRYPKLAALNPE HCCCCCCCHHHCCCC	41.65	-
95	Acetylation	LCPPRYPKLAALNPE HCCCCCCCHHHCCCC	41.65	25953088
103	Phosphorylation	LAALNPESNTAGLDI HHHCCCCCCCCCHHH	40.51	22817900
105	Phosphorylation	ALNPESNTAGLDIFA HCCCCCCCCCHHHHH	31.23	21601212
113	Ubiquitination	AGLDIFAKFSAYIKN CCHHHHHHHHHHHHC	29.15	21906983
115	Phosphorylation	LDIFAKFSAYIKNSN HHHHHHHHHHHHCCC	21.32	28258704
117	Phosphorylation	IFAKFSAYIKNSNPA HHHHHHHHHHCCCHH	15.95	28258704
119	Acetylation	AKFSAYIKNSNPALN HHHHHHHHCCCHHHC	41.46	19608861
119	Ubiquitination	AKFSAYIKNSNPALN HHHHHHHHCCCHHHC	41.46	21890473
119	Malonylation	AKFSAYIKNSNPALN HHHHHHHHCCCHHHC	41.46	26320211
121	Phosphorylation	FSAYIKNSNPALNDN HHHHHHCCCHHHCCC	38.91	25159151
131	Acetylation	ALNDNLEKGLLKALK HHCCCHHHHHHHHHH	59.01	19608861
131	Ubiquitination	ALNDNLEKGLLKALK HHCCCHHHHHHHHHH	59.01	21890473
131	Malonylation	ALNDNLEKGLLKALK HHCCCHHHHHHHHHH	59.01	26320211
135	Malonylation	NLEKGLLKALKVLDN CHHHHHHHHHHHHHH	57.63	26320211
135	Acetylation	NLEKGLLKALKVLDN CHHHHHHHHHHHHHH	57.63	23749302
135	Ubiquitination	NLEKGLLKALKVLDN CHHHHHHHHHHHHHH	57.63	21890473
138	Acetylation	KGLLKALKVLDNYLT HHHHHHHHHHHHHHC	45.68	25953088
138	Ubiquitination	KGLLKALKVLDNYLT HHHHHHHHHHHHHHC	45.68	21906983
143	Phosphorylation	ALKVLDNYLTSPLPE HHHHHHHHHCCCCCH	15.83	23403867
145	Phosphorylation	KVLDNYLTSPLPEEV HHHHHHHCCCCCHHC	20.24	23403867
146	Phosphorylation	VLDNYLTSPLPEEVD HHHHHHCCCCCHHCC	23.11	28176443
155	Phosphorylation	LPEEVDETSAEDEGV CCHHCCCCCCCCCCC	28.86	25159151
156	Phosphorylation	PEEVDETSAEDEGVS CHHCCCCCCCCCCCC	27.84	28355574
163	Phosphorylation	SAEDEGVSQRKFLDG CCCCCCCCCCCCCCC	34.81	25159151
166	Ubiquitination	DEGVSQRKFLDGNEL CCCCCCCCCCCCCCE	42.51	21890473
166	Acetylation	DEGVSQRKFLDGNEL CCCCCCCCCCCCCCE	42.51	23954790
178	S-nitrosylation	NELTLADCNLLPKLH CCEEHHHCCCCCCCE	3.00	24105792
178	S-palmitoylation	NELTLADCNLLPKLH CCEEHHHCCCCCCCE	3.00	26865113
183	Ubiquitination	ADCNLLPKLHIVQVV HHCCCCCCCEEEEHH	53.30	-
183	Acetylation	ADCNLLPKLHIVQVV HHCCCCCCCEEEEHH	53.30	23749302
191	S-palmitoylation	LHIVQVVCKKYRGFT CEEEEHHHHHHCCCC	3.10	29575903
191	S-nitrosocysteine	LHIVQVVCKKYRGFT CEEEEHHHHHHCCCC	3.10	-
191	S-nitrosylation	LHIVQVVCKKYRGFT CEEEEHHHHHHCCCC	3.10	20140087
192	Ubiquitination	HIVQVVCKKYRGFTI EEEEHHHHHHCCCCC	41.03	-
192	Acetylation	HIVQVVCKKYRGFTI EEEEHHHHHHCCCCC	41.03	25953088
193	Ubiquitination	IVQVVCKKYRGFTIP EEEHHHHHHCCCCCC	34.74	-
195	Methylation	QVVCKKYRGFTIPEA EHHHHHHCCCCCCHH	42.50	-
198	Phosphorylation	CKKYRGFTIPEAFRG HHHHCCCCCCHHHHH	38.15	21712546
204	Methylation	FTIPEAFRGVHRYLS CCCCHHHHHHHHHHH	53.96	-
209	Phosphorylation	AFRGVHRYLSNAYAR HHHHHHHHHHHHHHH	10.29	23186163
211	Phosphorylation	RGVHRYLSNAYAREE HHHHHHHHHHHHHHH	15.52	27499020
214	Phosphorylation	HRYLSNAYAREEFAS HHHHHHHHHHHHHHH	15.50	23312004
221	Phosphorylation	YAREEFASTCPDDEE HHHHHHHHHCCCHHH	35.54	28102081
222	Phosphorylation	AREEFASTCPDDEEI HHHHHHHHCCCHHHH	25.32	20873877
223	S-palmitoylation	REEFASTCPDDEEIE HHHHHHHCCCHHHHH	3.01	29575903
223	Glutathionylation	REEFASTCPDDEEIE HHHHHHHCCCHHHHH	3.01	22555962
233	Phosphorylation	DEEIELAYEQVAKAL HHHHHHHHHHHHHHH	21.37	28796482
238	Ubiquitination	LAYEQVAKALK---- HHHHHHHHHHC----	56.23	-
241	Ubiquitination	EQVAKALK------- HHHHHHHC-------	64.25	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of CLIC1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CLIC1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of CLIC1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LSM1_HUMAN	LSM1	physical	14667819
AKAP9_HUMAN	AKAP9	physical	12163479
CPT1A_HUMAN	CPT1A	physical	21988832
NTF4_HUMAN	NTF4	physical	21988832
RLA1_HUMAN	RPLP1	physical	21988832
THA_HUMAN	THRA	physical	21988832
ZN184_HUMAN	ZNF184	physical	21988832
NEMO_HUMAN	IKBKG	physical	21988832
PRDX4_HUMAN	PRDX4	physical	21988832
NUP62_HUMAN	NUP62	physical	21988832
ZN302_HUMAN	ZNF302	physical	21988832
DDB1_HUMAN	DDB1	physical	26344197
SPS1_HUMAN	SEPHS1	physical	26344197
TPRN_HUMAN	TPRN	physical	28514442
PRSR2_HUMAN	PROSER2	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CLIC1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-119; LYS-131 ANDLYS-135, AND MASS SPECTROMETRY.	19608861 [Abstract]