dbPTM

PCDB2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PCDB2_HUMAN
UniProt AC	Q9Y5E7
Protein Name	Protocadherin beta-2
Gene Name	PCDHB2
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	MEAGEGKERVPKQRQVLIFFVLLGIAQASCQPRHYSVAEETESGSFVANLLKDLGLEIGELAVRGARVVSKGKKMHLQFDRQTGDLLLNEKLDREELCGPTEPCVLPFQVLLENPLQFFQAELRIRDVNDHSPVFLDKEILLKIPESITPGTTFLIERAQDLDVGTNSLQNYTISPNFHFHLNLQDSLDGIILPQLVLNRALDREEQPEIRLTLTALDGGSPPRSGTALVRIEVVDINDNVPEFAKLLYEVQIPEDSPVGSQVAIVSARDLDIGTNGEISYAFSQASEDIRKTFRLSAKSGELLLRQKLDFESIQTYTVNIQATDGGGLSGTCVVFVQVMDLNDNPPELTMSTLINQIPENLQDTLIAVFSVSDPDSGDNGRMVCSIQDDLPFFLKPSVENFYTLVISTALDRETRSEYNITITVTDFGTPRLKTEHNITVLVSDVNDNAPAFTQTSYTLFVRENNSPALHIGSVSATDRDSGTNAQVTYSLLPPQDPHLPLASLVSINADNGHLFALQSLDYEALQAFEFRVGAADRGSPALSSEALVRVLVLDANDNSPFVLYPLQNGSAPCTELVPRAAEPGYLVTKVVAVDGDSGQNAWLSYQLLKATEPGLFGVWAHNGEVRTARLLRERDAAKQRLVVLVKDNGEPPRSATATLHVLLVDGFSQPYLLLPEAAPAQAQADLLTVYLVVALASVSSLFLFSVLLFVAVRLCRRSRAASVGRCSVPEGPFPGQMVDVSGTGTLSQSYQYEVCLTGGSGTNEFKFLKPIIPNFVAQGAERVSEANPSFRKSFEFT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
29	Phosphorylation	LLGIAQASCQPRHYS HHHHHHHCCCCCCCC	10.95	-
43	Phosphorylation	SVAEETESGSFVANL CCCCCCCCCCHHHHH	47.35	-
171	N-linked_Glycosylation	VGTNSLQNYTISPNF CCCCCCCCEEECCCE	41.00	UniProtKB CARBOHYD
225	Phosphorylation	DGGSPPRSGTALVRI CCCCCCCCCEEEEEE	46.39	23403867
227	Phosphorylation	GSPPRSGTALVRIEV CCCCCCCEEEEEEEE	20.33	23403867
299	Acetylation	KTFRLSAKSGELLLR HHHHHCHHCCCCEEE	56.47	19608861
420	N-linked_Glycosylation	RETRSEYNITITVTD CCCCCCEEEEEEEEC	22.37	UniProtKB CARBOHYD
438	N-linked_Glycosylation	PRLKTEHNITVLVSD CCCCCCCCEEEEEEC	25.95	UniProtKB CARBOHYD
569	N-linked_Glycosylation	FVLYPLQNGSAPCTE EEEEECCCCCCCCCC	54.81	UniProtKB CARBOHYD
770	Ubiquitination	TNEFKFLKPIIPNFV CCCEECCCCCCCHHH	36.98	-
790	Phosphorylation	RVSEANPSFRKSFEF HHHCCCHHHHHHCCC	37.17	24719451
798	Phosphorylation	FRKSFEFT------- HHHHCCCC-------	30.42	24719451

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 PCDB2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PCDB2_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 PCDB2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PCDB2_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 PCDB2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-299, AND MASS SPECTROMETRY.	19608861 [Abstract]