PCDB6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PCDB6_HUMAN
• UniProt AC: Q9Y5E3
• Protein Name: Protocadherin beta-6 {ECO:0000305}
• Gene Name: PCDHB6 {ECO:0000312|HGNC:HGNC:8691}
• Organism: Homo sapiens (Human).
• Sequence Length: 794
• Subcellular Localization: Cell membrane ; Single-pass type I membrane protein .
• Protein Description: Calcium-dependent cell-adhesion protein involved in cells self-recognition and non-self discrimination. Thereby, it is involved in the establishment and maintenance of specific neuronal connections in the brain..
• Protein Sequence: MMQTKVQNKKRQVAFFILLMLWGEVGSESIQYSVLEETESGTFVANLTKDLGLRVGELASRGARVVFKGNRQHLQFDPQTHDLLLNEKLDREELCGSTEPCVLPFQVLLENPLQFFQASLRVRDINDHAPEFPAREMLLKISEITMPGKIFPLKMAHDLDTGSNGLQRYTISSNPHFHVLTRNRSEGRKFPELVLDKPLDREEQPQLRLTLIALDGGSPPRSGTSEIQIQVLDINDNVPEFAQELYEAQVPENNPLGSLVITVSARDLDAGSFGKVSYALFQVDDVNQPFEINAITGEIRLRKALDFEEIQSYDVDVEATDGGGLSGKCSLVVRVLDVNDNAPELTMSFFISLIPENLPEITVAVFSVSDADSGHNQQVICSIENNLPFLLRPSVENFYTLVTEGALDRESRAEYNITITVTDLGTPRLKTQQSITVQVSDVNDNVPAFTQTSYTLFVRENNSPALHIGSVSATDRDSGINAQVTYSLLPPQDPHLPLSSLVSINADNGHLFALRSLDYEALQSFEFRVGATDRGSPALSSEALVRLLVLDANDNSPFVLYPLQNGSAPCTELVPRAAEPGYLVTKVVAVDGDSGQNAWLSYQLLKATELGLFGVWAHNGEVRTARLLSERDAAKHRLVVLVKDNGEPPRSATATLHVLLVDGFSQPYLPLPEAAPAQAQADSLTVYLVVALASVSSLFLFSVLLFVAVRLCRRSRAASVGRYSVPEGPFPGHLVDVSGTGTLSQSYQYKVCLTGGSETNEFKFLKPIMPNFPPQGTEREMEETPTSRNSFPFS

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
5	Acetylation	---MMQTKVQNKKRQ ---CCCCHHCHHHHH	25.57	19824457
9	Acetylation	MQTKVQNKKRQVAFF CCCHHCHHHHHHHHH	32.04	19824463
46	N-linked_Glycosylation	ESGTFVANLTKDLGL CCCEEEEEHHHHHCC	42.83	UniProtKB CARBOHYD
60	Phosphorylation	LRVGELASRGARVVF CCHHHHHHCCCEEEE	43.82	-
169	Phosphorylation	GSNGLQRYTISSNPH CCCCCEEEECCCCCC	8.75	22210691
170	Phosphorylation	SNGLQRYTISSNPHF CCCCEEEECCCCCCE	19.30	22210691
172	Phosphorylation	GLQRYTISSNPHFHV CCEEEECCCCCCEEE	19.10	22210691
183	N-linked_Glycosylation	HFHVLTRNRSEGRKF CEEEEECCCCCCCCC	46.74	UniProtKB CARBOHYD
394	Phosphorylation	LPFLLRPSVENFYTL CCEEECCCHHHHHHH	35.31	26270265
399	Phosphorylation	RPSVENFYTLVTEGA CCCHHHHHHHHHCCC	15.67	26270265
400	Phosphorylation	PSVENFYTLVTEGAL CCHHHHHHHHHCCCC	15.60	26270265
403	Phosphorylation	ENFYTLVTEGALDRE HHHHHHHHCCCCCCC	31.64	26270265
411	Phosphorylation	EGALDRESRAEYNIT CCCCCCCCCCEEEEE	37.37	18669648
416	N-linked_Glycosylation	RESRAEYNITITVTD CCCCCEEEEEEEEEE	19.21	UniProtKB CARBOHYD
418	Phosphorylation	SRAEYNITITVTDLG CCCEEEEEEEEEECC	13.63	18669648
426	Phosphorylation	ITVTDLGTPRLKTQQ EEEEECCCCCCEECC	16.72	18669648
565	N-linked_Glycosylation	FVLYPLQNGSAPCTE EEEEECCCCCCCCCC	54.81	UniProtKB CARBOHYD

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PCDB6_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PCDB6_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PCDB6_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of PCDB6_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.

Related Literatures of Post-Translational Modification

Phosphorylation

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; THR-418 ANDTHR-426, AND MASS SPECTROMETRY.
PubMed: 18669648