dbPTM

CNTN2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CNTN2_HUMAN
UniProt AC	Q02246
Protein Name	Contactin-2
Gene Name	CNTN2
Organism	Homo sapiens (Human).
Sequence Length	1040
Subcellular Localization	Cell membrane Lipid-anchor, GPI-anchor. Attached to the neuronal membrane by a GPI-anchor and is also released from neurons.
Protein Description	In conjunction with another transmembrane protein, CNTNAP2, contributes to the organization of axonal domains at nodes of Ranvier by maintaining voltage-gated potassium channels at the juxtaparanodal region. May be involved in cell adhesion..
Protein Sequence	MGTATRRKPHLLLVAAVALVSSSAWSSALGSQTTFGPVFEDQPLSVLFPEESTEEQVLLACRARASPPATYRWKMNGTEMKLEPGSRHQLVGGNLVIMNPTKAQDAGVYQCLASNPVGTVVSREAILRFGFLQEFSKEERDPVKAHEGWGVMLPCNPPAHYPGLSYRWLLNEFPNFIPTDGRHFVSQTTGNLYIARTNASDLGNYSCLATSHMDFSTKSVFSKFAQLNLAAEDTRLFAPSIKARFPAETYALVGQQVTLECFAFGNPVPRIKWRKVDGSLSPQWTTAEPTLQIPSVSFEDEGTYECEAENSKGRDTVQGRIIVQAQPEWLKVISDTEADIGSNLRWGCAAAGKPRPTVRWLRNGEPLASQNRVEVLAGDLRFSKLSLEDSGMYQCVAENKHGTIYASAELAVQALAPDFRLNPVRRLIPAARGGEILIPCQPRAAPKAVVLWSKGTEILVNSSRVTVTPDGTLIIRNISRSDEGKYTCFAENFMGKANSTGILSVRDATKITLAPSSADINLGDNLTLQCHASHDPTMDLTFTWTLDDFPIDFDKPGGHYRRTNVKETIGDLTILNAQLRHGGKYTCMAQTVVDSASKEATVLVRGPPGPPGGVVVRDIGDTTIQLSWSRGFDNHSPIAKYTLQARTPPAGKWKQVRTNPANIEGNAETAQVLGLTPWMDYEFRVIASNILGTGEPSGPSSKIRTREAAPSVAPSGLSGGGGAPGELIVNWTPMSREYQNGDGFGYLLSFRRQGSTHWQTARVPGADAQYFVYSNESVRPYTPFEVKIRSYNRRGDGPESLTALVYSAEEEPRVAPTKVWAKGVSSSEMNVTWEPVQQDMNGILLGYEIRYWKAGDKEAAADRVRTAGLDTSARVSGLHPNTKYHVTVRAYNRAGTGPASPSANATTMKPPPRRPPGNISWTFSSSSLSIKWDPVVPFRNESAVTGYKMLYQNDLHLTPTLHLTGKNWIEIPVPEDIGHALVQIRTTGPGGDGIPAEVHIVRNGGTSMMVENMAVRPAPHPGTVISHSVAMLILIGSLEL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
70	Phosphorylation	ARASPPATYRWKMNG HHCCCCCEEEEEECC	21.28	24719451
71	Phosphorylation	RASPPATYRWKMNGT HCCCCCEEEEEECCC	19.31	24719451
76	N-linked_Glycosylation	ATYRWKMNGTEMKLE CEEEEEECCCEEECC	50.97	UniProtKB CARBOHYD
86	Phosphorylation	EMKLEPGSRHQLVGG EEECCCCCCCEEECC	36.99	24719451
186	Phosphorylation	TDGRHFVSQTTGNLY CCCCCEEECCCCCEE	22.36	-
197	Phosphorylation	GNLYIARTNASDLGN CCEEEEECCHHHCCC	26.56	30576142
198	N-linked_Glycosylation	NLYIARTNASDLGNY CEEEEECCHHHCCCC	31.71	UniProtKB CARBOHYD
200	Phosphorylation	YIARTNASDLGNYSC EEEECCHHHCCCCCC	35.12	29759185
204	N-linked_Glycosylation	TNASDLGNYSCLATS CCHHHCCCCCCEEEC	32.61	UniProtKB CARBOHYD
205	Phosphorylation	NASDLGNYSCLATSH CHHHCCCCCCEEECC	10.04	-
210	Phosphorylation	GNYSCLATSHMDFST CCCCCEEECCCCCCC	13.25	-
216	Phosphorylation	ATSHMDFSTKSVFSK EECCCCCCCHHHHHH	30.57	30576142
334	Phosphorylation	PEWLKVISDTEADIG CCCEEEECCCCCCCC	41.28	20873877
336	Phosphorylation	WLKVISDTEADIGSN CEEEECCCCCCCCCC	26.70	20873877
342	Phosphorylation	DTEADIGSNLRWGCA CCCCCCCCCCCCCCC	32.78	20873877
386	Phosphorylation	DLRFSKLSLEDSGMY CEEECCCCHHHCCCE	33.19	29507054
461	N-linked_Glycosylation	KGTEILVNSSRVTVT CCCEEEECCCCEEEC	30.72	UniProtKB CARBOHYD
462	Phosphorylation	GTEILVNSSRVTVTP CCEEEECCCCEEECC	16.43	22468782
472	Phosphorylation	VTVTPDGTLIIRNIS EEECCCCCEEEECCC	23.36	24114839
477	N-linked_Glycosylation	DGTLIIRNISRSDEG CCCEEEECCCCCCCC	26.61	UniProtKB CARBOHYD
479	Phosphorylation	TLIIRNISRSDEGKY CEEEECCCCCCCCCE	29.31	22468782
481	Phosphorylation	IIRNISRSDEGKYTC EEECCCCCCCCCEEE	32.97	22468782
498	N-linked_Glycosylation	ENFMGKANSTGILSV ECCCCCCCCCEEEEE	43.52	UniProtKB CARBOHYD
500	Phosphorylation	FMGKANSTGILSVRD CCCCCCCCEEEEEEC	28.22	22210691
525	N-linked_Glycosylation	ADINLGDNLTLQCHA CCCCCCCCEEEEEEC	32.88	UniProtKB CARBOHYD
647	Phosphorylation	KYTLQARTPPAGKWK EEEEEECCCCCCCCE	36.32	22496350
669	Phosphorylation	NIEGNAETAQVLGLT CCCCCHHHHHHCCCC	21.71	26074081
676	Phosphorylation	TAQVLGLTPWMDYEF HHHHCCCCCCCCCEE	17.07	26074081
681	Phosphorylation	GLTPWMDYEFRVIAS CCCCCCCCEEEEEEE	10.81	26074081
688	Phosphorylation	YEFRVIASNILGTGE CEEEEEEECCCCCCC	17.18	26074081
693	Phosphorylation	IASNILGTGEPSGPS EEECCCCCCCCCCCC	34.62	26074081
718	Phosphorylation	SVAPSGLSGGGGAPG CCCCCCCCCCCCCCC	38.63	22210691
735	Phosphorylation	IVNWTPMSREYQNGD EEECCCCCCCCCCCC	24.14	22210691
738	Phosphorylation	WTPMSREYQNGDGFG CCCCCCCCCCCCCCE	13.23	22210691
749	Phosphorylation	DGFGYLLSFRRQGST CCCEEEEEEEECCCC	17.70	24719451
830	N-linked_Glycosylation	GVSSSEMNVTWEPVQ CCCCCCCCCEEEEEE	24.82	UniProtKB CARBOHYD
887	Phosphorylation	PNTKYHVTVRAYNRA CCCEEEEEEEEECCC	7.32	-
891	Phosphorylation	YHVTVRAYNRAGTGP EEEEEEEECCCCCCC	8.46	-
904	N-linked_Glycosylation	GPASPSANATTMKPP CCCCCCCCCCCCCCC	42.00	16335952
918	N-linked_Glycosylation	PPRRPPGNISWTFSS CCCCCCCCEEEEEEC	30.78	UniProtKB CARBOHYD
927	Phosphorylation	SWTFSSSSLSIKWDP EEEEECCCEEEEECC	28.25	24719451
929	Phosphorylation	TFSSSSLSIKWDPVV EEECCCEEEEECCCC	24.87	24719451
940	N-linked_Glycosylation	DPVVPFRNESAVTGY CCCCCCCCCHHCCCE	48.21	UniProtKB CARBOHYD
951	Phosphorylation	VTGYKMLYQNDLHLT CCCEEEEECCCCCCC	11.19	29759185
958	Phosphorylation	YQNDLHLTPTLHLTG ECCCCCCCCEEEECC	11.95	29759185
960	Phosphorylation	NDLHLTPTLHLTGKN CCCCCCCEEEECCCC	22.90	29759185
964	Phosphorylation	LTPTLHLTGKNWIEI CCCEEEECCCCCEEE	35.05	29759185
986	Phosphorylation	HALVQIRTTGPGGDG EEEEEEEECCCCCCC	37.42	17322306
987	Phosphorylation	ALVQIRTTGPGGDGI EEEEEEECCCCCCCC	31.37	17322306
1012	GPI-anchor	GTSMMVENMAVRPAP CCEEEEEEEEECCCC	16.59	-

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
Oops, there are no upstream regulatory protein records of CNTN2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CNTN2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of CNTN2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CNTP2_HUMAN	CNTNAP2	physical	12975355
NRCAM_HUMAN	NRCAM	physical	12139915
L1CAM_HUMAN	L1CAM	physical	12139915
CNTN1_HUMAN	CNTN1	physical	12139915
NCAN_HUMAN	NCAN	physical	8663515

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615400	Epilepsy, familial adult myoclonic, 5 (FAME5)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CNTN2_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"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-904, AND MASSSPECTROMETRY.	16335952 [Abstract]