CNTP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CNTP1_MOUSE
• UniProt AC: O54991
• Protein Name: Contactin-associated protein 1
• Gene Name: Cntnap1
• Organism: Mus musculus (Mouse).
• Sequence Length: 1385
• Subcellular Localization: Membrane ; Single-pass type I membrane protein . Cell junction, paranodal septate junction .
• Protein Description: Required, with CNTNAP2, for radial and longitudinal organization of myelinated axons. [PubMed: 25378149 Plays a role in the formation of functional distinct domains critical for saltatory conduction of nerve impulses in myelinated nerve fibers. Demarcates the paranodal region of the axo-glial junction. In association with contactin involved in the signaling between axons and myelinating glial cells]
• Protein Sequence: MMSLRLFSILLATVVSGAWGWGYYGCNEELVGPLYARSLGASSYYGLFTTARFARLHGISGWSPRIGDPNPWLQIDLMKKHRIRAVATQGAFNSWDWVTRYMLLYGDRVDSWTPFYQKGHNATFFGNVNDSAVVRHDLHYHFTARYIRIVPLAWNPRGKIGLRLGIYGCPYTSSILYFDGDDAISYRFQRGASQSLWDVFAFSFKTEEKDGLLLHTEGSQGDYVTLELQGAHLLLHMSLGSSPIQPRPGHTTVSLGGVLNDLSWHYVRVDRYGRDANFTLDGYAHHFVLNGDFERLNLENEIFIGGLVGAARKNLAYRHNFRGCIENVIYNRINIAEMAVMRHSRITFEGNVAFRCLDPVPHPINFGGPHNFVQVPGFPRRGRLAVSFRFRTWDLTGLLLFSHLGDGLGHVELMLSEGQVNVSIAQTGRKKLQFAAGYRLNDGFWHEVNFVAQENHAVISIDDVEGAEVRVSYPLLIRTGTSYFFGGCPKPASRWGCHSNQTAFHGCMELLKVDGQLVNLTLVEFRKLGYFAEVLFDTCGITDRCSPNMCEHDGRCYQSWDDFICYCELTGYKGVTCHEPLYKESCEAYRLSGKYSGNYTIDPDGSGPLKPFVVYCDIRENRAWTVVRHDRLWTTRVTGSSMDRPFLGAIQYWNASWEEVSALANASQHCEQWIEFSCYNSRLLNTAGGYPYSFWIGRNEEQHFYWGGSQPGIQRCACGLDQSCVDPALHCNCDADQPQWRTDKGLLTFVDHLPVTQVVVGDTNRSNSEAQFFLRPLRCYGDRNSWNTISFHTGAALRFPPIRANHSLDVSFYFRTSAPSGVFLENMGGPFCRWRRPYVRVELNTSRDVVFAFDIGNGDENLTVHSDDFEFNDDEWHLVRAEINVKQARLRVDHRPWVLRPMPLQTYIWLVYDQPLYVGSAELKRRPFVGCLRAMRLNGVTLNLEGRANASEGTFPNCTGHCTHPRFPCFHGGRCVERYSYYTCDCDLTAFDGPYCNHDIGGFFETGTWMRYNLQSALRSAAREFSHMLSRPVPGYEPGYVPGYDTPGYVPGYHGPGYRLPEYPRPGRPVPGYRGPVYNVTGEEVSFSFSTNSAPAVLLYVSSFVRDYMAVLIKEDGTLQLRYQLGTSPYVYQLTTRPVTDGQPHSVNITRVYRNLFIQVDYFPLTEQKFSLLVDSQLDSPKALYLGRVMETGVIDPEIQRYNTPGFSGCLSGVRFNNVAPLKTHFRTPRPMTAELAEAMRVQGELSESNCGAMPRLVSEVPPELDPWYLPPDFPYYHDDGWIAILLGFLVAFLLLGLVGMLVLFYLQNHRYKGSYHTNEPKATHDSHPGGKAPLPPSGPAQAPAPTPAPTQLPTPAPAPAPAPASGPGPRDQNLPQILEESRSE

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
42	Phosphorylation	YARSLGASSYYGLFT HHHHCCCCCHHHHHH	19.64	21183079
49	Phosphorylation	SSYYGLFTTARFARL CCHHHHHHHHHHHHH	25.29	21183079
50	Phosphorylation	SYYGLFTTARFARLH CHHHHHHHHHHHHHH	14.43	22817900
60	Phosphorylation	FARLHGISGWSPRIG HHHHHCCCCCCCCCC	38.51	26160508
121	N-linked_Glycosylation	PFYQKGHNATFFGNV CCEECCCCEEEECCC	49.71	-
129	N-linked_Glycosylation	ATFFGNVNDSAVVRH EEEECCCCCCCEEEC	41.33	-
277	N-linked_Glycosylation	DRYGRDANFTLDGYA ECCCCCCCEEECCCE	34.42	-
421	N-linked_Glycosylation	MLSEGQVNVSIAQTG EEECCCEEEEEEHHC	17.58	-
500	N-linked_Glycosylation	SRWGCHSNQTAFHGC HHCCCCCCCHHHCHH	21.40	-
519	N-linked_Glycosylation	KVDGQLVNLTLVEFR EECCEEEEEEEEEHH	35.58	-
598	N-linked_Glycosylation	LSGKYSGNYTIDPDG CCCCCCCCEEECCCC	25.49	-
654	N-linked_Glycosylation	LGAIQYWNASWEEVS HHHHHHHCCCHHHHH	21.11	-
665	N-linked_Glycosylation	EEVSALANASQHCEQ HHHHHHHHHHHHHHH	40.76	-
764	N-linked_Glycosylation	QVVVGDTNRSNSEAQ EEEECCCCCCCCCEE	50.55	-
805	N-linked_Glycosylation	RFPPIRANHSLDVSF CCCCCCCCCCEEEEE	18.55	-
816	Phosphorylation	DVSFYFRTSAPSGVF EEEEEEECCCCCCCE	21.24	22817900
817	Phosphorylation	VSFYFRTSAPSGVFL EEEEEECCCCCCCEE	33.65	22817900
820	Phosphorylation	YFRTSAPSGVFLENM EEECCCCCCCEEECC	47.51	22817900
844	N-linked_Glycosylation	PYVRVELNTSRDVVF CEEEEEECCCCCEEE	23.62	-
861	N-linked_Glycosylation	DIGNGDENLTVHSDD ECCCCCCCEEEEECC	45.83	-
949	N-linked_Glycosylation	LNLEGRANASEGTFP EEEECCCCCCCCCCC	42.51	-
957	N-linked_Glycosylation	ASEGTFPNCTGHCTH CCCCCCCCCCCCCCC	31.62	-
1079	N-linked_Glycosylation	GYRGPVYNVTGEEVS CCCCCEEECCCCEEE	25.71	-
1148	N-linked_Glycosylation	DGQPHSVNITRVYRN CCCCCCEEEEEEEEC	32.69	-
1171	Phosphorylation	PLTEQKFSLLVDSQL ECCCHHEEEHHHCCC	28.03	22817900
1210	S-nitrosylation	NTPGFSGCLSGVRFN CCCCCCCCCCCCEEC	2.37	24895380
1236	Ubiquitination	PRPMTAELAEAMRVQ CCCCHHHHHHHHHHH	4.91	27667366
1312	Phosphorylation	FYLQNHRYKGSYHTN HHHHCCCCCCCEECC	16.49	20139300
1313	Ubiquitination	YLQNHRYKGSYHTNE HHHCCCCCCCEECCC	41.14	27667366
1315	Phosphorylation	QNHRYKGSYHTNEPK HCCCCCCCEECCCCC	15.02	20139300
1332	Ubiquitination	HDSHPGGKAPLPPSG CCCCCCCCCCCCCCC	53.39	22790023
1366	Phosphorylation	APAPAPASGPGPRDQ CCCCCCCCCCCCCCC	44.45	29899451
1382	Phosphorylation	LPQILEESRSE---- HHHHHHHHHCC----	31.56	25521595
1384	Phosphorylation	QILEESRSE------ HHHHHHHCC------	57.86	25521595

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

Oops, there are no upstream regulatory protein records of CNTP1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CNTP1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CNTP1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of CNTP1_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1384, AND MASSSPECTROMETRY.
PubMed: 17114649