PCDBC_HUMAN - dbPTM
PCDBC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCDBC_HUMAN
UniProt AC Q9Y5F1
Protein Name Protocadherin beta-12
Gene Name PCDHB12
Organism Homo sapiens (Human).
Sequence Length 795
Subcellular Localization Cell membrane
Single-pass type I membrane protein.
Protein Description Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain..
Protein Sequence MENGGAGTLQIRQVLLFFVLLGMSQAGSETGNFLVMEELQSGSFVGNLAKTLGLEVSELSSRGARVVSNDNKECLQLDTNTGDLLLREMLDREELCGSNEPCVLYFQVLMKNPTQFLQIELQVRDINDHSPVFLEKEMLLEIPENSPVGAVFLLESAKDLDVGINAVKSYTINPNSHFHVKIRVNPDNRKYPELVLDKALDYEERPELSFILTALDGGSPPRSGTALVRVVVVDINDNSPEFEQAFYEVKILENSILGSLVVTVSAWDLDSGTNSELSYTFSHASEDIRKTFEINQKSGDITLTAPLDFEAIESYSIIIQATDGGGLFGKSTVRIQVMDVNDNAPEITVSSITSPIPENTPETVVMVFRIRDRDSGDNGKMVCSIPEDIPFVLKSSVNNYYTLETERPLDRESRAEYNITITVTDLGTPRLKTEHNITVLVSDVNDNAPAFTQTSYALFVRENNSPALHIGSISATDRDSGTNAQVNYSLLPSQDPHLPLASLVSINADNGHLFALRSLDYEALQGFQFRVGATDHGSPALSSEALVRVLVLDANDNSPFVLYPLQNGSAPCTELVPWAAEPGYLVTKVVAVDGDSGQNAWLSYQLLKATEPGLFGVWAHNGEVRTARLLSERDAAKHRLVVLVKDNGEPPRSATATLHVLLVDGFSQPYLPLPEAAPAQAQADSLTVYLVVALASVSSLFLFSVLLFVAVRLCRRSRAAPVGRCSVPEGPFPGHLVDVSGTGTLSQSYHYEVCVTGGSRSNKFKFLKPIIPNFLPQSTGSEVEENPPFQNNLGF
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
8PhosphorylationMENGGAGTLQIRQVL
CCCCCCCHHHHHHHH
18.2422210691
68PhosphorylationSRGARVVSNDNKECL
HCCCEEECCCCCCEE
35.29-
105PhosphorylationSNEPCVLYFQVLMKN
CCCCEEEEEEEEECC
3.30-
223PhosphorylationDGGSPPRSGTALVRV
CCCCCCCCCCEEEEE
46.3923403867
225PhosphorylationGSPPRSGTALVRVVV
CCCCCCCCEEEEEEE
20.3323403867
247PhosphorylationPEFEQAFYEVKILEN
HHHHHHHHHHHHHHC
23.8722817900
413PhosphorylationERPLDRESRAEYNIT
CCCCCCCCCCEEEEE
37.3718669648
418N-linked_GlycosylationRESRAEYNITITVTD
CCCCCEEEEEEEEEC
19.21UniProtKB CARBOHYD
420PhosphorylationSRAEYNITITVTDLG
CCCEEEEEEEEECCC
13.6318669648
428PhosphorylationITVTDLGTPRLKTEH
EEEECCCCCCCCCCC
16.7218669648
436N-linked_GlycosylationPRLKTEHNITVLVSD
CCCCCCCCEEEEEEC
25.95UniProtKB CARBOHYD
487N-linked_GlycosylationSGTNAQVNYSLLPSQ
CCCCCEEEEECCCCC
14.48UniProtKB CARBOHYD
567N-linked_GlycosylationFVLYPLQNGSAPCTE
EEEEECCCCCCCCCC
54.81UniProtKB CARBOHYD
717PhosphorylationAVRLCRRSRAAPVGR
HHHHHHHCCCCCCCC
13.61-

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 PCDBC_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCDBC_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 PCDBC_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PCDBC_HUMAN !!

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 PCDBC_HUMAN

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Related Literatures of Post-Translational Modification

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