PCDBE_HUMAN - dbPTM
PCDBE_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PCDBE_HUMAN
UniProt AC Q9Y5E9
Protein Name Protocadherin beta-14
Gene Name PCDHB14
Organism Homo sapiens (Human).
Sequence Length 798
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 MEIRGALDLRKRQVLIFLVLLGLSRAGTESAHYSVAEETEIGSFVANLARDLGLGVEELSSREARVVSDDNKKYLHLDLLTGNLLLNEKLDRDELCGSTEPCVLHFQVVLENPLQFFRFELCVKDINDHSPTFLDKEILIKISEGTTVGATFLMESAQDLDVGSNSLQNYTISPNSHFYIKIPDSSDRKIYPELVLDRALDYEQEAELRLTLTAVDGGSPPKSGTTLVLIKVLDINDNAPEFPQSLYEVQVPEDRPLGSWIATISAKDLDAGNYGKISYTFFHASEDIRKTFEINPISGEVNLRSPLDFEVIQSYTINIQATDGGGLSGKCTLLVKVMDINDNPPEVTISSITKRIPENASETLVALFSILDQDSGDNGRMICSIQDNLPFFLKPTFKNFFTLVSEKALDRESQAEYNITITVTDLGTPRLKTEYNITVLLSDVNDNAPTFTQTSYTLFVRENNSPALHIGSVSATDRDSGTNAQVNYSLLPPQDRHLPLASLVSINADNGHLFALRSLDYEALQEFEFRVGATDRGSPALSSEALVRVLVLDANDNSPFVLYPLQNGSAPCTELVPRAAEPGYLVTKVVAVDGDSGQNAWLSYQLLKATEPGLFGVWAHNGEVRTARLLSERDAAKHRLVVLVKDNGEPPRSATATLHVLLVDGFSQPYLPLPEAAPAQAQADSLTVYLVVALASVSSLFLFSVLLFVAVRLCRRSRAASVGRCSVPEGPFPGHLVDVSGTGTLSQSYQYEVCLTGGSGTNEFKFLKPIIPNFQVHDTGRNMGEIENFRNSFGLNIQ
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
33PhosphorylationAGTESAHYSVAEETE
CCCCCCCCCCCCHHH
12.4521253578
169N-linked_GlycosylationVGSNSLQNYTISPNS
CCCCCCCCEEECCCC
41.00UniProtKB CARBOHYD
202PhosphorylationVLDRALDYEQEAELR
HHHHHCCHHHHHEEE
21.9919658100
219PhosphorylationLTAVDGGSPPKSGTT
EEEECCCCCCCCCCE
43.49-
359N-linked_GlycosylationITKRIPENASETLVA
HHCCCCCCHHHHHHH
43.33UniProtKB CARBOHYD
418N-linked_GlycosylationRESQAEYNITITVTD
CHHHCEEEEEEEEEE
19.21UniProtKB CARBOHYD
436N-linked_GlycosylationPRLKTEYNITVLLSD
CCCEEEEEEEEEEEC
19.75UniProtKB CARBOHYD
487N-linked_GlycosylationSGTNAQVNYSLLPPQ
CCCCCEEEEECCCCC
14.48UniProtKB CARBOHYD
567N-linked_GlycosylationFVLYPLQNGSAPCTE
EEEEECCCCCCCCCC
54.81UniProtKB CARBOHYD
765UbiquitinationGSGTNEFKFLKPIIP
CCCCCCEEECCCCCC
43.5423000965
768UbiquitinationTNEFKFLKPIIPNFQ
CCCEEECCCCCCCEE
36.9823000965

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 PCDBE_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PCDBE_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 PCDBE_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBY1F_HUMANRBMY1Fphysical
25416956

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 PCDBE_HUMAN

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Related Literatures of Post-Translational Modification

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