CADH2_HUMAN - dbPTM
CADH2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CADH2_HUMAN
UniProt AC P19022
Protein Name Cadherin-2
Gene Name CDH2
Organism Homo sapiens (Human).
Sequence Length 906
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Cell membrane, sarcolemma . Cell junction . Cell surface . Colocalizes with TMEM65 at the intercalated disk in cardiomyocytes. Colocalizes with OBSCN at the intercalated disk and at sarcolemma in
Protein Description Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem cells to ependymocytes in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated anchorage is affected, leading to modulate neural stem cell quiescence. CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density (By similarity)..
Protein Sequence MCRIAGALRTLLPLLAALLQASVEASGEIALCKTGFPEDVYSAVLSKDVHEGQPLLNVKFSNCNGKRKVQYESSEPADFKVDEDGMVYAVRSFPLSSEHAKFLIYAQDKETQEKWQVAVKLSLKPTLTEESVKESAEVEEIVFPRQFSKHSGHLQRQKRDWVIPPINLPENSRGPFPQELVRIRSDRDKNLSLRYSVTGPGADQPPTGIFIINPISGQLSVTKPLDREQIARFHLRAHAVDINGNQVENPIDIVINVIDMNDNRPEFLHQVWNGTVPEGSKPGTYVMTVTAIDADDPNALNGMLRYRIVSQAPSTPSPNMFTINNETGDIITVAAGLDREKVQQYTLIIQATDMEGNPTYGLSNTATAVITVTDVNDNPPEFTAMTFYGEVPENRVDIIVANLTVTDKDQPHTPAWNAVYRISGGDPTGRFAIQTDPNSNDGLVTVVKPIDFETNRMFVLTVAAENQVPLAKGIQHPPQSTATVSVTVIDVNENPYFAPNPKIIRQEEGLHAGTMLTTFTAQDPDRYMQQNIRYTKLSDPANWLKIDPVNGQITTIAVLDRESPNVKNNIYNATFLASDNGIPPMSGTGTLQIYLLDINDNAPQVLPQEAETCETPDPNSINITALDYDIDPNAGPFAFDLPLSPVTIKRNWTITRLNGDFAQLNLKIKFLEAGIYEVPIIITDSGNPPKSNISILRVKVCQCDSNGDCTDVDRIVGAGLGTGAIIAILLCIIILLILVLMFVVWMKRRDKERQAKQLLIDPEDDVRDNILKYDEEGGGEEDQDYDLSQLQQPDTVEPDAIKPVGIRRMDERPIHAEPQYPVRSAAPHPGDIGDFINEGLKAADNDPTAPPYDSLLVFDYEGSGSTAGSLSSLNSSSSGGEQDYDYLNDWGPRFKKLADMYGGGDD
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
61PhosphorylationPLLNVKFSNCNGKRK
EEEEEEEECCCCEEE		34.45-
71PhosphorylationNGKRKVQYESSEPAD
CCEEEEEEECCCCCC		22.2922210691
73PhosphorylationKRKVQYESSEPADFK
EEEEEEECCCCCCEE		34.7622210691
96PhosphorylationAVRSFPLSSEHAKFL
EEEECCCCHHHCEEE		33.6426091039
135PhosphorylationTEESVKESAEVEEIV
CHHHHHHHEEEEEEE		24.8229255136
190N-linked_GlycosylationIRSDRDKNLSLRYSV
ECCCCCCCEEEEEEE		38.87UniProtKB CARBOHYD
273N-linked_GlycosylationEFLHQVWNGTVPEGS
HHHHHHHCCCCCCCC		37.0819159218
325N-linked_GlycosylationPNMFTINNETGDIIT
CCEEEECCCCCCEEE		44.34UniProtKB CARBOHYD
327PhosphorylationMFTINNETGDIITVA
EEEECCCCCCEEEEE		42.1323879269
332PhosphorylationNETGDIITVAAGLDR
CCCCCEEEEEECCCH		12.3923879269
402N-linked_GlycosylationRVDIIVANLTVTDKD
CEEEEEEECEECCCC		25.9219159218
417UbiquitinationQPHTPAWNAVYRISG
CCCCCCCEEEEEECC		22.95-
439PhosphorylationAIQTDPNSNDGLVTV
EEECCCCCCCCCEEE		41.5129507054
448UbiquitinationDGLVTVVKPIDFETN
CCCEEEEEEECCCCC		31.74-
454PhosphorylationVKPIDFETNRMFVLT
EEEECCCCCCEEEEE		28.28-
461PhosphorylationTNRMFVLTVAAENQV
CCCEEEEEEEECCCC		11.6430301811
496PhosphorylationIDVNENPYFAPNPKI
EECCCCCCCCCCHHH		24.7725884760
505UbiquitinationAPNPKIIRQEEGLHA
CCCHHHEECCCCCCC		41.13-
536UbiquitinationQQNIRYTKLSDPANW
HHHCCEEECCCCCCC		36.74-
538PhosphorylationNIRYTKLSDPANWLK
HCCEEECCCCCCCEE		43.0030266825
572N-linked_GlycosylationNVKNNIYNATFLASD
CCCCCEEEEEEEEEC		28.8019159218
651N-linked_GlycosylationSPVTIKRNWTITRLN
CCEEEECCEEEEEEC		34.93UniProtKB CARBOHYD
667UbiquitinationDFAQLNLKIKFLEAG
CEEEEEEEEEEHHCC		42.66-
683PhosphorylationYEVPIIITDSGNPPK
EEEEEEEECCCCCCC		17.44-
685PhosphorylationVPIIITDSGNPPKSN
EEEEEECCCCCCCCC		31.64-
692N-linked_GlycosylationSGNPPKSNISILRVK
CCCCCCCCEEEEEEE		37.8519159218
725UbiquitinationAGLGTGAIIAILLCI
CCCHHHHHHHHHHHH		2.0121890473
741UbiquitinationILLILVLMFVVWMKR
HHHHHHHHHHHHHHH		1.54-
756UbiquitinationRDKERQAKQLLIDPE
CCHHHHHHHHCCCCC		32.8921890473
756UbiquitinationRDKERQAKQLLIDPE
CCHHHHHHHHCCCCC		32.8921890473
771UbiquitinationDDVRDNILKYDEEGG
CHHHHHCCCCCCCCC		5.43-
772UbiquitinationDVRDNILKYDEEGGG
HHHHHCCCCCCCCCC		47.02-
773PhosphorylationVRDNILKYDEEGGGE
HHHHCCCCCCCCCCC		25.7429978859
785PhosphorylationGGEEDQDYDLSQLQQ
CCCCCCCCCHHHCCC		17.1028796482
788PhosphorylationEDQDYDLSQLQQPDT
CCCCCCHHHCCCCCC		26.4121955146
795PhosphorylationSQLQQPDTVEPDAIK
HHCCCCCCCCCCCCC		33.1921955146
802UbiquitinationTVEPDAIKPVGIRRM
CCCCCCCCCCCEEEC		35.06-
820PhosphorylationPIHAEPQYPVRSAAP
CCCCCCCCCCCCCCC		17.8916371504
824PhosphorylationEPQYPVRSAAPHPGD
CCCCCCCCCCCCCCC		29.0825850435
852PhosphorylationNDPTAPPYDSLLVFD
CCCCCCCCCEEEEEE		19.6616371504
860PhosphorylationDSLLVFDYEGSGSTA
CEEEEEEECCCCCCC		15.6616371504
884PhosphorylationSSGGEQDYDYLNDWG
CCCCCCCHHHHHCCC		13.2416371504
886PhosphorylationGGEQDYDYLNDWGPR
CCCCCHHHHHCCCHH		10.9416371504
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
96SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
135SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
820YPhosphorylationKinaseSRCP12931
PSP
852YPhosphorylationKinaseSRCP12931
PSP
852YPhosphorylationKinaseSRC64-PhosphoELM
860YPhosphorylationKinaseSRCP12931
PSP
884YPhosphorylationKinaseSRCP12931
PSP
884YPhosphorylationKinaseSRC64-PhosphoELM
886YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CADH2_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 CADH2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GNA12_HUMANGNA12physical
11136230
GNA13_HUMANGNA13physical
11136230
ACTS_HUMANACTA1physical
12438242
CTNA1_HUMANCTNNA1physical
14625392
CTNB1_HUMANCTNNB1physical
14625392
PLAK_HUMANJUPphysical
14625392
CTND1_HUMANCTNND1physical
14625392
CAD11_HUMANCDH11physical
14625392
CTNA1_HUMANCTNNA1physical
12604612
CTNB1_HUMANCTNNB1physical
12604612
CTND1_HUMANCTNND1physical
12604612
PLAK_HUMANJUPphysical
7650039
CTNB1_HUMANCTNNB1physical
11835406
CTNB1_HUMANCTNNB1physical
12077367
CTNA1_HUMANCTNNA1physical
22939629
PLAK_HUMANJUPphysical
22939629
PERI_HUMANPRPHphysical
22939629
RL32_HUMANRPL32physical
22939629
CAVN3_HUMANPRKCDBPphysical
22939629
RM23_HUMANMRPL23physical
22939629
PYC_HUMANPCphysical
22939629
SPT5H_HUMANSUPT5Hphysical
22939629
SSRD_HUMANSSR4physical
22939629
RL21_HUMANRPL21physical
22939629
RL3_HUMANRPL3physical
22939629
RL8_HUMANRPL8physical
22939629
ICT1_HUMANICT1physical
22939629
RS26_HUMANRPS26physical
22939629
RL14_HUMANRPL14physical
22939629
RS16_HUMANRPS16physical
22939629
KTN1_HUMANKTN1physical
22939629
LYAG_HUMANGAAphysical
22939629
TPM4_HUMANTPM4physical
22939629
RM49_HUMANMRPL49physical
22939629
PTBP3_HUMANPTBP3physical
22939629
SPTB2_HUMANSPTBN1physical
22939629
TM256_HUMANTMEM256physical
22939629
NENF_HUMANNENFphysical
22939629
SYSM_HUMANSARS2physical
22939629
PPT2_HUMANPPT2physical
22939629
SYIM_HUMANIARS2physical
22939629
NACA2_HUMANNACA2physical
22939629
DREB_HUMANDBN1physical
22939629
PDIA4_HUMANPDIA4physical
22939629
EXOC5_HUMANEXOC5physical
21988832
FBSP1_HUMANFBXO45physical
25143387
CTNB1_HUMANCTNNB1physical
25143387
SKP1_HUMANSKP1physical
25143387
CCNA2_HUMANCCNA2physical
22152476
EGFR_HUMANEGFRphysical
19033391
ERBB2_HUMANERBB2physical
19033391
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CADH2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-273; ASN-402; ASN-572 ANDASN-692, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of HeLa cells using stable isotope labelingwith amino acids in cell culture (SILAC).";
Amanchy R., Kalume D.E., Iwahori A., Zhong J., Pandey A.;
J. Proteome Res. 4:1661-1671(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-785, AND MASSSPECTROMETRY.

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