GUC2C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GUC2C_HUMAN
• UniProt AC: P25092
• Protein Name: Heat-stable enterotoxin receptor
• Gene Name: GUCY2C
• Organism: Homo sapiens (Human).
• Sequence Length: 1073
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein . Endoplasmic reticulum membrane ; Single-pass type I membrane protein . The 145 kDa plasma membrane form of GC-C contains sialic acid and galactose residues, while a differencially glycosylated 130
• Protein Description: Receptor for the E.coli heat-stable enterotoxin (E.coli enterotoxin markedly stimulates the accumulation of cGMP in mammalian cells expressing GC-C). Also activated by the endogenous peptides guanylin and uroguanylin..
• Protein Sequence: MKTLLLDLALWSLLFQPGWLSFSSQVSQNCHNGSYEISVLMMGNSAFAEPLKNLEDAVNEGLEIVRGRLQNAGLNVTVNATFMYSDGLIHNSGDCRSSTCEGLDLLRKISNAQRMGCVLIGPSCTYSTFQMYLDTELSYPMISAGSFGLSCDYKETLTRLMSPARKLMYFLVNFWKTNDLPFKTYSWSTSYVYKNGTETEDCFWYLNALEASVSYFSHELGFKVVLRQDKEFQDILMDHNRKSNVIIMCGGPEFLYKLKGDRAVAEDIVIILVDLFNDQYFEDNVTAPDYMKNVLVLTLSPGNSLLNSSFSRNLSPTKRDFALAYLNGILLFGHMLKIFLENGENITTPKFAHAFRNLTFEGYDGPVTLDDWGDVDSTMVLLYTSVDTKKYKVLLTYDTHVNKTYPVDMSPTFTWKNSKLPNDITGRGPQILMIAVFTLTGAVVLLLLVALLMLRKYRKDYELRQKKWSHIPPENIFPLETNETNHVSLKIDDDKRRDTIQRLRQCKYDKKRVILKDLKHNDGNFTEKQKIELNKLLQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLREVLNDTISYPDGTFMDWEFKISVLYDIAKGMSYLHSSKTEVHGRLKSTNCVVDSRMVVKITDFGCNSILPPKKDLWTAPEHLRQANISQKGDVYSYGIIAQEIILRKETFYTLSCRDRNEKIFRVENSNGMKPFRPDLFLETAEEKELEVYLLVKNCWEEDPEKRPDFKKIETTLAKIFGLFHDQKNESYMDTLIRRLQLYSRNLEHLVEERTQLYKAERDRADRLNFMLLPRLVVKSLKEKGFVEPELYEEVTIYFSDIVGFTTICKYSTPMEVVDMLNDIYKSFDHIVDHHDVYKVETIGDAYMVASGLPKRNGNRHAIDIAKMALEILSFMGTFELEHLPGLPIWIRIGVHSGPCAAGVVGIKMPRYCLFGDTVNTASRMESTGLPLRIHVSGSTIAILKRTECQFLYEVRGETYLKGRGNETTYWLTGMKDQKFNLPTPPTVENQQRLQAEFSDMIANSLQKRQAAGIRSQKPRRVASYKKGTLEYLQLNTTDKESTYF

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
32	N-linked_Glycosylation	QVSQNCHNGSYEISV CHHCCCCCCCEEEEE	43.22	23269669
75	N-linked_Glycosylation	RLQNAGLNVTVNATF HHHHCCCCEEEEEEE	26.88	23269669
79	N-linked_Glycosylation	AGLNVTVNATFMYSD CCCCEEEEEEEEECC	24.73	23269669
162	Phosphorylation	ETLTRLMSPARKLMY HHHHHHHCHHHHHHH	21.72	24719451
177	Phosphorylation	FLVNFWKTNDLPFKT HHHHHHHHCCCCCCE	25.26	26074081
189	Phosphorylation	FKTYSWSTSYVYKNG CCEEEEEEEEEEECC	20.16	-
193	Phosphorylation	SWSTSYVYKNGTETE EEEEEEEEECCCCCE	7.18	-
195	N-linked_Glycosylation	STSYVYKNGTETEDC EEEEEEECCCCCEEH	44.95	23269669
197	Phosphorylation	SYVYKNGTETEDCFW EEEEECCCCCEEHHH	49.48	28387310
199	Phosphorylation	VYKNGTETEDCFWYL EEECCCCCEEHHHHH	36.64	28387310
212	Phosphorylation	YLNALEASVSYFSHE HHHHHHHHHHHHHHH	11.39	28387310
256	Phosphorylation	CGGPEFLYKLKGDRA ECCHHHHHHHHCCHH	21.42	19835603
284	N-linked_Glycosylation	NDQYFEDNVTAPDYM CCHHCCCCCCCCCHH	26.33	23269669
307	N-linked_Glycosylation	SPGNSLLNSSFSRNL CCCCHHHCCCCCCCC	40.68	23269669
315	Phosphorylation	SSFSRNLSPTKRDFA CCCCCCCCCCHHHHH	33.79	24719451
345	N-linked_Glycosylation	IFLENGENITTPKFA HHHHCCCCCCCHHHH	38.00	23269669
392	Acetylation	SVDTKKYKVLLTYDT ECCCCCEEEEEEEEC	34.97	19413330
396	Phosphorylation	KKYKVLLTYDTHVNK CCEEEEEEEECCCCC	18.39	28509920
397	Phosphorylation	KYKVLLTYDTHVNKT CEEEEEEEECCCCCE	20.86	28509920
399	Phosphorylation	KVLLTYDTHVNKTYP EEEEEEECCCCCEEC	19.81	28509920
402	N-linked_Glycosylation	LTYDTHVNKTYPVDM EEEECCCCCEECCCC	24.29	23269669
404	Phosphorylation	YDTHVNKTYPVDMSP EECCCCCEECCCCCC	28.05	-
414	Phosphorylation	VDMSPTFTWKNSKLP CCCCCCCCCCCCCCC	37.70	-
440	Phosphorylation	MIAVFTLTGAVVLLL HHHHHHHHHHHHHHH	21.75	-
457	Phosphorylation	ALLMLRKYRKDYELR HHHHHHHHHCHHHHH	19.23	26657352
461	Phosphorylation	LRKYRKDYELRQKKW HHHHHCHHHHHHCCC	21.65	26657352
507	Ubiquitination	IQRLRQCKYDKKRVI HHHHHHCCCCCCEEE	48.41	-
516	Acetylation	DKKRVILKDLKHNDG CCCEEEEECCCCCCC	50.30	12437677
563	Phosphorylation	MIFGVIEYCERGSLR EEEHHHHHHHHCCHH	6.62	-
617	Phosphorylation	EVHGRLKSTNCVVDS EECCEECCCCEEEEC	29.46	23879269
618	Phosphorylation	VHGRLKSTNCVVDSR ECCEECCCCEEEECC	30.93	23879269
664	Phosphorylation	ISQKGDVYSYGIIAQ CCCCCCCCHHEEEEE	10.83	-
665	Phosphorylation	SQKGDVYSYGIIAQE CCCCCCCHHEEEEEE	19.41	-
681	Phosphorylation	ILRKETFYTLSCRDR HHCCCCEEEEEECCC	17.75	-
771	Phosphorylation	LIRRLQLYSRNLEHL HHHHHHHHHCCHHHH	7.82	-
772	Phosphorylation	IRRLQLYSRNLEHLV HHHHHHHHCCHHHHH	24.24	24719451
808	Phosphorylation	LPRLVVKSLKEKGFV HHHHHHHHHHHCCCC	32.82	24719451
875	Phosphorylation	VETIGDAYMVASGLP EEEECHHHHHHCCCC	9.25	22985185
940	Phosphorylation	VGIKMPRYCLFGDTV CEECCCCEEEECCCC	6.40	-
965	Phosphorylation	LPLRIHVSGSTIAIL CCEEEEECCCEEEEE	16.92	30576142
968	Phosphorylation	RIHVSGSTIAILKRT EEEECCCEEEEEECC	20.25	30576142
1001	Phosphorylation	NETTYWLTGMKDQKF CCCEEEEECCCCCCC	22.53	-
1027	Phosphorylation	QRLQAEFSDMIANSL HHHHHHHHHHHHHHH	20.13	26270265
1033	Phosphorylation	FSDMIANSLQKRQAA HHHHHHHHHHHHHHC	24.13	26270265
1052	Phosphorylation	QKPRRVASYKKGTLE CCCCEEEECCCCCEE	34.33	23312004
1053	Phosphorylation	KPRRVASYKKGTLEY CCCEEEECCCCCEEE	13.64	23312004
1054	Methylation	PRRVASYKKGTLEYL CCEEEECCCCCEEEE	42.08	-

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

Oops, there are no upstream regulatory protein records of GUC2C_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
75	N	Glycosylation	Glycosylation at Asn-75 and/or Asn-79 is required for interaction with VIP36 while glycosylation at Asn-345 and Asn-402 modulates ligand-mediated GC-C activation.	23269669
79	N	Glycosylation	Glycosylation at Asn-75 and/or Asn-79 is required for interaction with VIP36 while glycosylation at Asn-345 and Asn-402 modulates ligand-mediated GC-C activation.	23269669
345	N	Glycosylation	Glycosylation at Asn-75 and/or Asn-79 is required for interaction with VIP36 while glycosylation at Asn-345 and Asn-402 modulates ligand-mediated GC-C activation.	23269669
402	N	Glycosylation	Glycosylation at Asn-75 and/or Asn-79 is required for interaction with VIP36 while glycosylation at Asn-345 and Asn-402 modulates ligand-mediated GC-C activation.	23269669

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of GUC2C_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NHRF4_HUMAN	PDZD3	physical	11950846

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 614616: Diarrhea 6 (DIAR6)
• 614665: Meconium ileus (MECIL)
• Kegg Drug
• D06612: Linaclotide acetate (USAN)
• D09355: Linaclotide (USAN); Linzess (TN)
• D09948: Plecanatide (USAN/INN)
• DrugBank
• DB08890: Linaclotide