CNTN1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CNTN1_HUMAN
• UniProt AC: Q12860
• Protein Name: Contactin-1
• Gene Name: CNTN1
• Organism: Homo sapiens (Human).
• Sequence Length: 1018
• Subcellular Localization: Isoform 1: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side.; Isoform 2: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side.
• Protein Description: Contactins mediate cell surface interactions during nervous system development. Involved in the formation of paranodal axo-glial junctions in myelinated peripheral nerves and in the signaling between axons and myelinating glial cells via its association with CNTNAP1. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus. Interaction with TNR induces a repulsion of neurons and an inhibition of neurite outgrowth (By similarity)..
• Protein Sequence: MKMWLLVSHLVIISITTCLAEFTWYRRYGHGVSEEDKGFGPIFEEQPINTIYPEESLEGKVSLNCRARASPFPVYKWRMNNGDVDLTSDRYSMVGGNLVINNPDKQKDAGIYYCLASNNYGMVRSTEATLSFGYLDPFPPEERPEVRVKEGKGMVLLCDPPYHFPDDLSYRWLLNEFPVFITMDKRRFVSQTNGNLYIANVEASDKGNYSCFVSSPSITKSVFSKFIPLIPIPERTTKPYPADIVVQFKDVYALMGQNVTLECFALGNPVPDIRWRKVLEPMPSTAEISTSGAVLKIFNIQLEDEGIYECEAENIRGKDKHQARIYVQAFPEWVEHINDTEVDIGSDLYWPCVATGKPIPTIRWLKNGYAYHKGELRLYDVTFENAGMYQCIAENTYGAIYANAELKILALAPTFEMNPMKKKILAAKGGRVIIECKPKAAPKPKFSWSKGTEWLVNSSRILIWEDGSLEINNITRNDGGIYTCFAENNRGKANSTGTLVITDPTRIILAPINADITVGENATMQCAASFDPALDLTFVWSFNGYVIDFNKENIHYQRNFMLDSNGELLIRNAQLKHAGRYTCTAQTIVDNSSASADLVVRGPPGPPGGLRIEDIRATSVALTWSRGSDNHSPISKYTIQTKTILSDDWKDAKTDPPIIEGNMEAARAVDLIPWMEYEFRVVATNTLGRGEPSIPSNRIKTDGAAPNVAPSDVGGGGGRNRELTITWAPLSREYHYGNNFGYIVAFKPFDGEEWKKVTVTNPDTGRYVHKDETMSPSTAFQVKVKAFNNKGDGPYSLVAVINSAQDAPSEAPTEVGVKVLSSSEISVHWEHVLEKIVESYQIRYWAAHDKEEAANRVQVTSQEYSARLENLLPDTQYFIEVGACNSAGCGPPSDMIEAFTKKAPPSQPPRIISSVRSGSRYIITWDHVVALSNESTVTGYKVLYRPDGQHDGKLYSTHKHSIEVPIPRDGEYVVEVRAHSDGGDGVVSQVKISGAPTLSPSLLGLLLPAFGILVYLEF

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
8 (in isoform 2)	Phosphorylation	-	15.86	27067055
8	Phosphorylation	MKMWLLVSHLVIISI CCHHHHHHHHHHHHH	15.86	24043423
14 (in isoform 2)	Phosphorylation	-	11.62	27067055
14	Phosphorylation	VSHLVIISITTCLAE HHHHHHHHHHHHHHH	11.62	24043423
16 (in isoform 2)	Phosphorylation	-	12.50	27067055
16	Phosphorylation	HLVIISITTCLAEFT HHHHHHHHHHHHHHH	12.50	24043423
17 (in isoform 2)	Phosphorylation	-	12.12	27067055
17	Phosphorylation	LVIISITTCLAEFTW HHHHHHHHHHHHHHH	12.12	24043423
22 (in isoform 2)	Phosphorylation	-	4.90	27067055
23	Phosphorylation	TTCLAEFTWYRRYGH HHHHHHHHHHHHHCC	17.06	24043423
25	Phosphorylation	CLAEFTWYRRYGHGV HHHHHHHHHHHCCCC	5.11	24043423
87	Phosphorylation	NNGDVDLTSDRYSMV CCCCCCCCCCCEEEE	24.90	-
208	N-linked_Glycosylation	VEASDKGNYSCFVSS EEECCCCCCEEEECC	31.14	UniProtKB CARBOHYD
258	N-linked_Glycosylation	VYALMGQNVTLECFA HHHHCCCCEEEEEEE	24.02	UniProtKB CARBOHYD
296	Ubiquitination	STSGAVLKIFNIQLE ECCCCEEEEECEEEC	38.36	-
338	N-linked_Glycosylation	PEWVEHINDTEVDIG HHHHHHCCCCCCCCC	52.65	UniProtKB CARBOHYD
414	Phosphorylation	KILALAPTFEMNPMK EEEEECCCCCCCHHH	26.98	23401153
428	2-Hydroxyisobutyrylation	KKKILAAKGGRVIIE HHHHHEECCCEEEEE	57.18	-
457	N-linked_Glycosylation	KGTEWLVNSSRILIW CCCEEEECCCCEEEE	31.90	UniProtKB CARBOHYD
458	Phosphorylation	GTEWLVNSSRILIWE CCEEEECCCCEEEEC	17.32	27732954
459	Phosphorylation	TEWLVNSSRILIWED CEEEECCCCEEEECC	20.38	27732954
473	N-linked_Glycosylation	DGSLEINNITRNDGG CCCEEEECEEECCCC	42.54	UniProtKB CARBOHYD
494	N-linked_Glycosylation	ENNRGKANSTGTLVI ECCCCCCCCCEEEEE	43.52	16335952
495	O-linked_Glycosylation	NNRGKANSTGTLVIT CCCCCCCCCEEEEEC	32.83	28657654
521	N-linked_Glycosylation	ADITVGENATMQCAA CCEECCCCCHHCEEH	34.48	UniProtKB CARBOHYD
591	N-linked_Glycosylation	TAQTIVDNSSASADL EEEEEECCCCCCCCE	27.28	UniProtKB CARBOHYD
638	Phosphorylation	HSPISKYTIQTKTIL CCCCCEEEEEEEECC	15.45	-
650	2-Hydroxyisobutyrylation	TILSDDWKDAKTDPP ECCCCCHHCCCCCCC	55.60	-
742	Phosphorylation	HYGNNFGYIVAFKPF ECCCCCEEEEEECCC	6.51	-
767	Phosphorylation	TNPDTGRYVHKDETM ECCCCCCEEECCCCC	14.30	-
850	2-Hydroxyisobutyrylation	RYWAAHDKEEAANRV HHHEECCHHHHHHCE	47.81	-
860	Phosphorylation	AANRVQVTSQEYSAR HHHCEEECCHHHHHH	13.96	28450419
861	Phosphorylation	ANRVQVTSQEYSARL HHCEEECCHHHHHHH	23.35	28450419
913	Phosphorylation	SQPPRIISSVRSGSR CCCCCEEEEECCCCC	22.02	23312004
914	Phosphorylation	QPPRIISSVRSGSRY CCCCEEEEECCCCCE	15.90	23312004
933	N-linked_Glycosylation	DHVVALSNESTVTGY CEEEECCCCCEECEE	48.35	UniProtKB CARBOHYD
972	Phosphorylation	PIPRDGEYVVEVRAH ECCCCCCEEEEEEEE	18.48	18452278
988	Phosphorylation	DGGDGVVSQVKISGA CCCCCEEEEEEECCC	27.18	26699800
993	GPI-anchor	VVSQVKISGAPTLSP EEEEEEECCCCCCCH	24.16	-

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

Oops, there are no upstream regulatory protein records of CNTN1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CNTN1_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 CNTN1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PTPRB_HUMAN	PTPRB	physical	9049255

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 612540: Myopathy, congenital, Compton-North (MYPCN)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-494, AND MASSSPECTROMETRY.
PubMed: 16335952