LRC8B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LRC8B_HUMAN
• UniProt AC: Q6P9F7
• Protein Name: Volume-regulated anion channel subunit LRRC8B
• Gene Name: LRRC8B
• Organism: Homo sapiens (Human).
• Sequence Length: 803
• Subcellular Localization: Cell membrane ; Multi-pass membrane protein . Endoplasmic reticulum membrane . In the absence of LRRC8A, resides primarily in a cytoplasmic compartment, probably the endoplasmic reticulum. Requires LRRC8A for expression at the cell membrane.
• Protein Description: Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes. The VRAC channel conducts iodide better than chloride and may also conduct organic osmolytes like taurine. Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition..
• Protein Sequence: MITLTELKCLADAQSSYHILKPWWDVFWYYITLIMLLVAVLAGALQLTQSRVLCCLPCKVEFDNHCAVPWDILKASMNTSSNPGTPLPLPLRIQNDLHRQQYSYIDAVCYEKQLHWFAKFFPYLVLLHTLIFAACSNFWLHYPSTSSRLEHFVAILHKCFDSPWTTRALSETVAEQSVRPLKLSKSKILLSSSGCSADIDSGKQSLPYPQPGLESAGIESPTSSVLDKKEGEQAKAIFEKVKRFRMHVEQKDIIYRVYLKQIIVKVILFVLIITYVPYFLTHITLEIDCSVDVQAFTGYKRYQCVYSLAEIFKVLASFYVILVILYGLTSSYSLWWMLRSSLKQYSFEALREKSNYSDIPDVKNDFAFILHLADQYDPLYSKRFSIFLSEVSENKLKQINLNNEWTVEKLKSKLVKNAQDKIELHLFMLNGLPDNVFELTEMEVLSLELIPEVKLPSAVSQLVNLKELRVYHSSLVVDHPALAFLEENLKILRLKFTEMGKIPRWVFHLKNLKELYLSGCVLPEQLSTMQLEGFQDLKNLRTLYLKSSLSRIPQVVTDLLPSLQKLSLDNEGSKLVVLNNLKKMVNLKSLELISCDLERIPHSIFSLNNLHELDLRENNLKTVEEIISFQHLQNLSCLKLWHNNIAYIPAQIGALSNLEQLSLDHNNIENLPLQLFLCTKLHYLDLSYNHLTFIPEEIQYLSNLQYFAVTNNNIEMLPDGLFQCKKLQCLLLGKNSLMNLSPHVGELSNLTHLELIGNYLETLPPELEGCQSLKRNCLIVEENLLNTLPLPVTERLQTCLDKC

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MITLTELKCL -----CCCHHHHHHH	26.74	30622161
5	Phosphorylation	---MITLTELKCLAD ---CCCHHHHHHHHH	30.53	30622161
15	Phosphorylation	KCLADAQSSYHILKP HHHHHHHHHHHCCHH	34.29	30622161
16	Phosphorylation	CLADAQSSYHILKPW HHHHHHHHHHCCHHH	14.51	30622161
17	Phosphorylation	LADAQSSYHILKPWW HHHHHHHHHCCHHHH	9.72	30622161
78	N-linked_Glycosylation	DILKASMNTSSNPGT HHHHHHCCCCCCCCC	34.02	UniProtKB CARBOHYD
85	O-linked_Glycosylation	NTSSNPGTPLPLPLR CCCCCCCCCCCCCEE	23.94	OGP
170	Phosphorylation	PWTTRALSETVAEQS HHHHHHHHHHHHHHC	30.18	29523821
172	Phosphorylation	TTRALSETVAEQSVR HHHHHHHHHHHHCCC	22.95	29523821
177	Phosphorylation	SETVAEQSVRPLKLS HHHHHHHCCCCCCCC	16.17	29523821
184	Phosphorylation	SVRPLKLSKSKILLS CCCCCCCCCCEEEEC	33.04	29523821
185	Acetylation	VRPLKLSKSKILLSS CCCCCCCCCEEEECC	67.23	28736161
186	Phosphorylation	RPLKLSKSKILLSSS CCCCCCCCEEEECCC	22.89	23312004
191	Phosphorylation	SKSKILLSSSGCSAD CCCEEEECCCCCCCC	21.00	28270605
192	Phosphorylation	KSKILLSSSGCSADI CCEEEECCCCCCCCC	30.62	28270605
193	Phosphorylation	SKILLSSSGCSADID CEEEECCCCCCCCCC	40.21	28270605
196	Phosphorylation	LLSSSGCSADIDSGK EECCCCCCCCCCCCC	32.28	28270605
201	Phosphorylation	GCSADIDSGKQSLPY CCCCCCCCCCCCCCC	48.50	28270605
205	Phosphorylation	DIDSGKQSLPYPQPG CCCCCCCCCCCCCCC	34.49	28270605
208	Phosphorylation	SGKQSLPYPQPGLES CCCCCCCCCCCCHHH	21.57	28270605
215	Phosphorylation	YPQPGLESAGIESPT CCCCCHHHCCCCCCC	36.52	28270605
220	Phosphorylation	LESAGIESPTSSVLD HHHCCCCCCCCCCCC	31.40	28270605
222	Phosphorylation	SAGIESPTSSVLDKK HCCCCCCCCCCCCCC	42.80	28270605
223	Phosphorylation	AGIESPTSSVLDKKE CCCCCCCCCCCCCCC	23.10	28270605
224	Phosphorylation	GIESPTSSVLDKKEG CCCCCCCCCCCCCCH	29.22	28270605
228	Acetylation	PTSSVLDKKEGEQAK CCCCCCCCCCHHHHH	48.87	20167786
229	Acetylation	TSSVLDKKEGEQAKA CCCCCCCCCHHHHHH	71.29	20167786
343	Ubiquitination	WMLRSSLKQYSFEAL HHHHHHHHHHCHHHH	49.49	-
460	Phosphorylation	VKLPSAVSQLVNLKE CCCCHHHHHHCCHHH	19.95	23312004
547	Phosphorylation	LRTLYLKSSLSRIPQ HHHHHHHHHHHCCHH	33.64	22468782
548	Phosphorylation	RTLYLKSSLSRIPQV HHHHHHHHHHCCHHH	28.86	22468782
557	Phosphorylation	SRIPQVVTDLLPSLQ HCCHHHHHHHHHHHH	23.29	22468782

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

Oops, there are no upstream regulatory protein records of LRC8B_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LRC8B_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of LRC8B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LRC8D_HUMAN	LRRC8D	physical	28514442
LRC8C_HUMAN	LRRC8C	physical	28514442
LRC8A_HUMAN	LRRC8A	physical	28514442
LRC8E_HUMAN	LRRC8E	physical	28514442
TSN3_HUMAN	TSPAN3	physical	28514442
AT2A3_HUMAN	ATP2A3	physical	28514442
CTL1_HUMAN	SLC44A1	physical	28514442
ABCB9_HUMAN	ABCB9	physical	28514442
TM164_HUMAN	TMEM164	physical	28514442
ANO6_HUMAN	ANO6	physical	28514442
TM2D3_HUMAN	TM2D3	physical	28514442
PM34_HUMAN	SLC25A17	physical	28514442
ADCK2_HUMAN	ADCK2	physical	28514442
LMBR1_HUMAN	LMBR1	physical	28514442
CHPT1_HUMAN	CHPT1	physical	28514442
T179B_HUMAN	TMEM179B	physical	28514442
GP1BB_HUMAN	GP1BB	physical	28514442
PDE3B_HUMAN	PDE3B	physical	28514442
SGT1_HUMAN	SUGT1	physical	28514442
RHBD3_HUMAN	RHBDD3	physical	28514442

Drug and Disease Associations

• Kegg Disease
• H00085: Agammaglobulinemias, including the following six diseases: X-linked agammaglobulinemia (Bruton's aga
• 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.