CFTR_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CFTR_RAT
• UniProt AC: P34158
• Protein Name: Cystic fibrosis transmembrane conductance regulator
• Gene Name: Cftr
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 1476
• Subcellular Localization: Apical cell membrane ; Multi-pass membrane protein . Early endosome membrane ; Multi-pass membrane protein . Cell membrane ; Multi-pass membrane protein . Recycling endosome membrane ; Multi-pass membrane protein . Endoplasmic reticulum membrane ; Multi-p
• Protein Description: Epithelial ion channel that plays an important role in the regulation of epithelial ion and water transport and fluid homeostasis. Mediates the transport of chloride ions across the cell membrane (By similarity). Channel activity is coupled to ATP hydrolysis. The ion channel is also permeable to HCO(3-); selectivity depends on the extracellular chloride concentration. Exerts its function also by modulating the activity of other ion channels and transporters. Contributes to the regulation of the pH and the ion content of the epithelial fluid layer. Modulates the activity of the epithelial sodium channel (ENaC) complex, in part by regulating the cell surface expression of the ENaC complex. May regulate bicarbonate secretion and salvage in epithelial cells by regulating the transporter SLC4A7. Can inhibit the chloride channel activity of ANO1 (By similarity). Plays a role in the chloride and bicarbonate homeostasis during sperm epididymal maturation and capacitation (By similarity)..
• Protein Sequence: MQKSPLEKASFISKLFFSWTTPILRKGYRHHLELSDIYQAPSSDSADHLSEKLEREWDREQASKKKPQLIHALRRCFVWRFVFYGVLLYLGEVTKAVQPVLLGRIIASYDPDNTEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLISLLSNNLNKFDEGLALAHFIWIAPLQVVLLMGLLWDLLQFSAFCGLGLLIVLVIFQAILGKMMVKYRDKRAAKINERLVITSEVIDNIYSVKAYCWESAMEKIIESLREEELKMTRRSAYMRFFTSSAFFFSGFFVVFLSVLPYTVINGIVLRKIFTTISFCIVLRMSVTRQFPTAVQIWYDSLGMIRKIQDFLQTQEYKVLEYNLMFTGLVMENVTAFWEEGFQELLEKVQLNNDDRKTSNGENHLSFSHLCLVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFSSQISWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFESCVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTFDQFTEERRSSILTETLRRFSVDDASTTWNKAKQSFRQTGEFGEKRKNSILSSFSSVKKISIVQKTPLSIEGESDDLQERRLSLVPDSEHGEAALPRSNMITAGPTFPGRRRQSVLDLMTFTPSSVSSSLQRTRASIRKISLAPRISLKEEDIYSRRLSQDSTLNITEEINEEDLKECFFDDMVKIPTVTTWNTYLRYFTLHRGLFAVLIWCVLVFLVEVAASLFVLWLLKNNPVNGGNNGTKIANTSYVVVITSSSFYYIFYIYVGVADTLLALSLFRGLPLVHTLITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQPYIFLATVPGLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQMRIDMIFVLFFIVVTFISILTTGEGEGTTGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRVFKFIDIQTEESICTKIMKELHSEDSPNALVIKNEHVKKCDTWPSGGEMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNLDPNGKWRDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVFQRALSSSEKMKLFHGRHSSKQKPRTQITAVKEETEEEVQETRL

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
517	Phosphorylation	VSYDEYRYKSVVKAC ECCCHHHHHHHHHHH	13.50	-
524	S-palmitoylation	YKSVVKACQLQEDIT HHHHHHHHHCHHHHH	3.25	-
547	Phosphorylation	VLGEGGVTLSGGQRA EEECCCEECCCCHHH	20.62	22673903
549	Phosphorylation	GEGGVTLSGGQRARI ECCCEECCCCHHHHH	31.35	22673903
660	Phosphorylation	FTEERRSSILTETLR HCHHHHHHHHHHHHH	21.58	-
670	Phosphorylation	TETLRRFSVDDASTT HHHHHHCCCCCHHCH	23.87	-
684	Phosphorylation	TWNKAKQSFRQTGEF HHHHHHHHHHHHCCC	22.99	-
698	Phosphorylation	FGEKRKNSILSSFSS CCHHHHHHHHHHHCC	28.13	-
710	Phosphorylation	FSSVKKISIVQKTPL HCCCEEEEEEEECCC	26.11	-
715	Phosphorylation	KISIVQKTPLSIEGE EEEEEEECCCCCCCC	16.63	-
732	Phosphorylation	DLQERRLSLVPDSEH HHHHHHHHCCCCCCC	26.05	-
763	Phosphorylation	FPGRRRQSVLDLMTF CCCCCCCHHHHHHCC	23.88	-
785	Phosphorylation	SLQRTRASIRKISLA HHHHHHHHHHHHHCC	21.45	-
790	Phosphorylation	RASIRKISLAPRISL HHHHHHHHCCCCCCC	22.86	-
808	Phosphorylation	DIYSRRLSQDSTLNI HHHHCCCCCCCCCCC	30.08	22673903
811	Phosphorylation	SRRLSQDSTLNITEE HCCCCCCCCCCCCCC	27.45	22673903
812	Phosphorylation	RRLSQDSTLNITEEI CCCCCCCCCCCCCCC	31.92	22673903
889	N-linked_Glycosylation	NPVNGGNNGTKIANT CCCCCCCCCCEECCE	63.89	-
895	N-linked_Glycosylation	NNGTKIANTSYVVVI CCCCEECCEEEEEEE	32.79	-
1391	S-palmitoylation	LRQAFAGCTVVLCEH HHHHHCCCEEEEECH	2.04	-
1440	Phosphorylation	FQRALSSSEKMKLFH HHHHCCCHHHHHHHC	37.55	-
1451	Phosphorylation	KLFHGRHSSKQKPRT HHHCCCCCCCCCCCC	37.56	22673903
1452	Phosphorylation	LFHGRHSSKQKPRTQ HHCCCCCCCCCCCCE	32.74	22673903

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
670	S	Phosphorylation	Kinase	PKA	-	Uniprot

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of CFTR_RAT !!

Drug and Disease Associations

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