CNTP2_HUMAN - dbPTM
CNTP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNTP2_HUMAN
UniProt AC Q9UHC6
Protein Name Contactin-associated protein-like 2
Gene Name CNTNAP2
Organism Homo sapiens (Human).
Sequence Length 1331
Subcellular Localization Membrane
Single-pass type I membrane protein . Cell projection, axon . Cell junction, paranodal septate junction . Expressed in the juxtaparadonal region.
Protein Description Required, with CNTNAP1, for radial and longitudinal organization of myelinated axons. Plays a role in the formation of functional distinct domains critical for saltatory conduction of nerve impulses in myelinated nerve fibers. Demarcates the juxtaparanodal region of the axo-glial junction..
Protein Sequence MQAAPRAGCGAALLLWIVSSCLCRAWTAPSTSQKCDEPLVSGLPHVAFSSSSSISGSYSPGYAKINKRGGAGGWSPSDSDHYQWLQVDFGNRKQISAIATQGRYSSSDWVTQYRMLYSDTGRNWKPYHQDGNIWAFPGNINSDGVVRHELQHPIIARYVRIVPLDWNGEGRIGLRIEVYGCSYWADVINFDGHVVLPYRFRNKKMKTLKDVIALNFKTSESEGVILHGEGQQGDYITLELKKAKLVLSLNLGSNQLGPIYGHTSVMTGSLLDDHHWHSVVIERQGRSINLTLDRSMQHFRTNGEFDYLDLDYEITFGGIPFSGKPSSSSRKNFKGCMESINYNGVNITDLARRKKLEPSNVGNLSFSCVEPYTVPVFFNATSYLEVPGRLNQDLFSVSFQFRTWNPNGLLVFSHFADNLGNVEIDLTESKVGVHINITQTKMSQIDISSGSGLNDGQWHEVRFLAKENFAILTIDGDEASAVRTNSPLQVKTGEKYFFGGFLNQMNNSSHSVLQPSFQGCMQLIQVDDQLVNLYEVAQRKPGSFANVSIDMCAIIDRCVPNHCEHGGKCSQTWDSFKCTCDETGYSGATCHNSIYEPSCEAYKHLGQTSNYYWIDPDGSGPLGPLKVYCNMTEDKVWTIVSHDLQMQTPVVGYNPEKYSVTQLVYSASMDQISAITDSAEYCEQYVSYFCKMSRLLNTPDGSPYTWWVGKANEKHYYWGGSGPGIQKCACGIERNCTDPKYYCNCDADYKQWRKDAGFLSYKDHLPVSQVVVGDTDRQGSEAKLSVGPLRCQGDRNYWNAASFPNPSSYLHFSTFQGETSADISFYFKTLTPWGVFLENMGKEDFIKLELKSATEVSFSFDVGNGPVEIVVRSPTPLNDDQWHRVTAERNVKQASLQVDRLPQQIRKAPTEGHTRLELYSQLFVGGAGGQQGFLGCIRSLRMNGVTLDLEERAKVTSGFISGCSGHCTSYGTNCENGGKCLERYHGYSCDCSNTAYDGTFCNKDVGAFFEEGMWLRYNFQAPATNARDSSSRVDNAPDQQNSHPDLAQEEIRFSFSTTKAPCILLYISSFTTDFLAVLVKPTGSLQIRYNLGGTREPYNIDVDHRNMANGQPHSVNITRHEKTIFLKLDHYPSVSYHLPSSSDTLFNSPKSLFLGKVIETGKIDQEIHKYNTPGFTGCLSRVQFNQIAPLKAALRQTNASAHVHIQGELVESNCGASPLTLSPMSSATDPWHLDHLDSASADFPYNPGQGQAIRNGVNRNSAIIGGVIAVVIFTILCTLVFLIRYMFRHKGTYHTNEAKGAESAESADAAIMNNDPNFTETIDESKKEWLI
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 Orthologous
Protein Cluster
100PhosphorylationKQISAIATQGRYSSS
HEEEEEEECCCCCCC		25.99-
183PhosphorylationIEVYGCSYWADVINF
EEEEEECEEEEEEEE		14.53-
287PhosphorylationVIERQGRSINLTLDR
EEEECCCEEEEEEEH		23.7423403867
289N-linked_GlycosylationERQGRSINLTLDRSM
EECCCEEEEEEEHHH		28.37UniProtKB CARBOHYD
346N-linked_GlycosylationSINYNGVNITDLARR
HHCCCCCCHHHHHHH		32.61UniProtKB CARBOHYD
348PhosphorylationNYNGVNITDLARRKK
CCCCCCHHHHHHHCC		21.54-
363N-linked_GlycosylationLEPSNVGNLSFSCVE
CCCCCCCCCEEEECC		28.38UniProtKB CARBOHYD
379N-linked_GlycosylationYTVPVFFNATSYLEV
CEEEEEEECCCCEEC		30.74UniProtKB CARBOHYD
429PhosphorylationVEIDLTESKVGVHIN
EEEECCCCEEEEEEE		27.66-
436N-linked_GlycosylationSKVGVHINITQTKMS
CEEEEEEEECCCCCC		19.17UniProtKB CARBOHYD
506N-linked_GlycosylationGGFLNQMNNSSHSVL
HHHHHHCCCCCCCCC		35.15UniProtKB CARBOHYD
507N-linked_GlycosylationGFLNQMNNSSHSVLQ
HHHHHCCCCCCCCCC		39.28UniProtKB CARBOHYD
546N-linked_GlycosylationRKPGSFANVSIDMCA
CCCCCCCCCEEEEEH		26.51UniProtKB CARBOHYD
579PhosphorylationTWDSFKCTCDETGYS
CCCCEEEEECCCCCC		24.4719690332
583PhosphorylationFKCTCDETGYSGATC
EEEEECCCCCCCCCC		28.3319690332
589PhosphorylationETGYSGATCHNSIYE
CCCCCCCCCCCCCCC		20.1619690332
595PhosphorylationATCHNSIYEPSCEAY
CCCCCCCCCCCHHHH		22.9319690332
630N-linked_GlycosylationGPLKVYCNMTEDKVW
CCEEEEEECCCCCEE		23.79UniProtKB CARBOHYD
638PhosphorylationMTEDKVWTIVSHDLQ
CCCCCEEEEEECCCC		17.94-
641PhosphorylationDKVWTIVSHDLQMQT
CCEEEEEECCCCCCC		13.87-
658PhosphorylationVGYNPEKYSVTQLVY
CCCCHHHCCEEEEEE		13.5025907765
659PhosphorylationGYNPEKYSVTQLVYS
CCCHHHCCEEEEEEE		29.7425907765
661PhosphorylationNPEKYSVTQLVYSAS
CHHHCCEEEEEEECC		15.3925907765
665PhosphorylationYSVTQLVYSASMDQI
CCEEEEEEECCHHHH		13.7025907765
666PhosphorylationSVTQLVYSASMDQIS
CEEEEEEECCHHHHH		13.3425907765
668PhosphorylationTQLVYSASMDQISAI
EEEEEECCHHHHHHH		19.5625907765
673PhosphorylationSASMDQISAITDSAE
ECCHHHHHHHHCCHH		14.1625907765
676PhosphorylationMDQISAITDSAEYCE
HHHHHHHHCCHHHHH		24.5025907765
678PhosphorylationQISAITDSAEYCEQY
HHHHHHCCHHHHHHH		17.8525907765
681PhosphorylationAITDSAEYCEQYVSY
HHHCCHHHHHHHHHH		10.8725907765
685PhosphorylationSAEYCEQYVSYFCKM
CHHHHHHHHHHHHHH		2.9725907765
687PhosphorylationEYCEQYVSYFCKMSR
HHHHHHHHHHHHHHH		13.9325907765
688PhosphorylationYCEQYVSYFCKMSRL
HHHHHHHHHHHHHHH		11.7125907765
735N-linked_GlycosylationCACGIERNCTDPKYY
CCCCCCCCCCCCCCC		21.91UniProtKB CARBOHYD
760PhosphorylationRKDAGFLSYKDHLPV
HHHCCCCCCCCCCCH		28.0724114839
852PhosphorylationFIKLELKSATEVSFS
EEEEEECCCCEEEEE		53.71-
854PhosphorylationKLELKSATEVSFSFD
EEEECCCCEEEEEEE		43.97-
857PhosphorylationLKSATEVSFSFDVGN
ECCCCEEEEEEECCC		14.67-
859PhosphorylationSATEVSFSFDVGNGP
CCCEEEEEEECCCCC		17.03-
1017PhosphorylationEEGMWLRYNFQAPAT
CCCCEEEEEEECCCC		20.4029978859
1071PhosphorylationLLYISSFTTDFLAVL
EEEEECCCCCEEHHH		27.66-
1072PhosphorylationLYISSFTTDFLAVLV
EEEECCCCCEEHHHC		23.81-
1116N-linked_GlycosylationNGQPHSVNITRHEKT
CCCCCEEECEECCEE		32.69UniProtKB CARBOHYD
1198N-linked_GlycosylationKAALRQTNASAHVHI
HHHHHHCCCCCEEEE		24.45UniProtKB CARBOHYD
1285PhosphorylationTLVFLIRYMFRHKGT
HHHHHHHHHHHHCCC		8.1328270605
1292PhosphorylationYMFRHKGTYHTNEAK
HHHHHCCCCCCCCCC		19.5528270605
1293PhosphorylationMFRHKGTYHTNEAKG
HHHHCCCCCCCCCCC		18.4728270605
1295PhosphorylationRHKGTYHTNEAKGAE
HHCCCCCCCCCCCCC		25.0828270605
1303PhosphorylationNEAKGAESAESADAA
CCCCCCCCHHHHCHH		36.4820363803
1306PhosphorylationKGAESAESADAAIMN
CCCCCHHHHCHHHHC		31.0319413330
1319PhosphorylationMNNDPNFTETIDESK
HCCCCCCCCCCCHHH		38.5725002506
1321PhosphorylationNDPNFTETIDESKKE
CCCCCCCCCCHHHHH		30.5825002506
1325PhosphorylationFTETIDESKKEWLI-
CCCCCCHHHHHHCC-		45.3325002506
1326UbiquitinationTETIDESKKEWLI--
CCCCCHHHHHHCC--		53.30-
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 CNTP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNTP2_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 CNTP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CNTN2_HUMANCNTN2physical
12975355
E41L3_HUMANEPB41L3physical
12542678
CSKP_HUMANCASKphysical
12093160
CTR9_HUMANCTR9physical
12421765
ZMIZ1_HUMANZMIZ1physical
12421765
MACF1_HUMANMACF1physical
12421765
MEOX2_HUMANMEOX2physical
24722188
Drug and Disease Associations
Kegg Disease
H00756 Pitt-Hopkins syndrome, including: Pitt-Hopkins syndrome; Pitt-Hopkins-like syndrome
OMIM Disease
610042Cortical dysplasia-focal epilepsy syndrome (CDFES)
612100Autism 15 (AUTS15)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CNTP2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1303 AND SER-1306, ANDMASS SPECTROMETRY.

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