dbPTM

CADH5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CADH5_HUMAN
UniProt AC	P33151
Protein Name	Cadherin-5
Gene Name	CDH5
Organism	Homo sapiens (Human).
Sequence Length	784
Subcellular Localization	Cell junction . Cell membrane Single-pass type I membrane protein . Found at cell-cell boundaries and probably at cell-matrix boundaries. KRIT1 and CDH5 reciprocally regulate their localization to endothelial cell-cell junctions.
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. This cadherin may play a important role in endothelial cell biology through control of the cohesion and organization of the intercellular junctions. It associates with alpha-catenin forming a link to the cytoskeleton. Acts in concert with KRIT1 to establish and maintain correct endothelial cell polarity and vascular lumen. These effects are mediated by recruitment and activation of the Par polarity complex and RAP1B. Required for activation of PRKCZ and for the localization of phosphorylated PRKCZ, PARD3, TIAM1 and RAP1B to the cell junction..
Protein Sequence	MQRLMMLLATSGACLGLLAVAAVAAAGANPAQRDTHSLLPTHRRQKRDWIWNQMHIDEEKNTSLPHHVGKIKSSVSRKNAKYLLKGEYVGKVFRVDAETGDVFAIERLDRENISEYHLTAVIVDKDTGENLETPSSFTIKVHDVNDNWPVFTHRLFNASVPESSAVGTSVISVTAVDADDPTVGDHASVMYQILKGKEYFAIDNSGRIITITKSLDREKQARYEIVVEARDAQGLRGDSGTATVLVTLQDINDNFPFFTQTKYTFVVPEDTRVGTSVGSLFVEDPDEPQNRMTKYSILRGDYQDAFTIETNPAHNEGIIKPMKPLDYEYIQQYSFIVEATDPTIDLRYMSPPAGNRAQVIINITDVDEPPIFQQPFYHFQLKENQKKPLIGTVLAMDPDAARHSIGYSIRRTSDKGQFFRVTKKGDIYNEKELDREVYPWYNLTVEAKELDSTGTPTGKESIVQVHIEVLDENDNAPEFAKPYQPKVCENAVHGQLVLQISAIDKDITPRNVKFKFILNTENNFTLTDNHDNTANITVKYGQFDREHTKVHFLPVVISDNGMPSRTGTSTLTVAVCKCNEQGEFTFCEDMAAQVGVSIQAVVAILLCILTITVITLLIFLRRRLRKQARAHGKSVPEIHEQLVTYDEEGGGEMDTTSYDVSVLNSVRRGGAKPPRPALDARPSLYAQVQKPPRHAPGAHGGPGEMAAMIEVKKDEADHDGDGPPYDTLHIYGYEGSESIAESLSSLGTDSSDSDVDYDFLNDWGPRFKMLAELYGSDPREELLY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
61	N-linked_Glycosylation	MHIDEEKNTSLPHHV CCCCCCCCCCCCCCH	37.87	21269602
62	Phosphorylation	HIDEEKNTSLPHHVG CCCCCCCCCCCCCHH	42.58	24719451
63	Phosphorylation	IDEEKNTSLPHHVGK CCCCCCCCCCCCHHH	49.66	24719451
82	Phosphorylation	VSRKNAKYLLKGEYV CCCCCHHHEECCEEE	18.17	-
112	N-linked_Glycosylation	IERLDRENISEYHLT EEECCCCCCCCEEEE	43.94	19139490
157	N-linked_Glycosylation	VFTHRLFNASVPESS EEEEEEECCCCCCHH	35.58	21269602
212	Phosphorylation	SGRIITITKSLDREK CCCEEEEECCCCHHH	13.11	-
223	Phosphorylation	DREKQARYEIVVEAR CHHHHHCEEEEEEEE	17.02	-
362	N-linked_Glycosylation	NRAQVIINITDVDEP CCEEEEEEEECCCCC	21.71	21269602
392	Phosphorylation	QKKPLIGTVLAMDPD CCCCCEEEEEEECHH	12.83	-
408	Phosphorylation	ARHSIGYSIRRTSDK HHHHHCEEEEECCCC	12.38	24719451
442	N-linked_Glycosylation	REVYPWYNLTVEAKE CCCCCEEEEEEEEEE	25.93	19139490
523	N-linked_Glycosylation	FILNTENNFTLTDNH EEEECCCCEEECCCC	25.66	16335952
535	N-linked_Glycosylation	DNHDNTANITVKYGQ CCCCCCEEEEEEEEE	28.55	16335952
658	Phosphorylation	GEMDTTSYDVSVLNS CCCCCCCCCHHHHHH	20.48	16027153
665	Phosphorylation	YDVSVLNSVRRGGAK CCHHHHHHHHCCCCC	16.91	22817900
683	Phosphorylation	PALDARPSLYAQVQK CCCCCCCCHHEECCC	28.58	28442448
685	Phosphorylation	LDARPSLYAQVQKPP CCCCCCHHEECCCCC	10.18	16909109
725	Phosphorylation	HDGDGPPYDTLHIYG CCCCCCCCCEEEEEC	25.37	-
731	Phosphorylation	PYDTLHIYGYEGSES CCCEEEEECCCCCHH	11.69	16027153
733	Phosphorylation	DTLHIYGYEGSESIA CEEEEECCCCCHHHH	10.51	22817900
774	Phosphorylation	FKMLAELYGSDPREE HHHHHHHHCCCCHHH	13.19	23403867
776	Phosphorylation	MLAELYGSDPREELL HHHHHHCCCCHHHHC	30.77	23403867
784	Phosphorylation	DPREELLY------- CCHHHHCC-------	29.18	27642862

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
658	Y	Phosphorylation	Kinase	SRC	P12931	PSP
685	Y	Phosphorylation	Kinase	SRC	P12931	PSP
685	Y	Phosphorylation	Kinase	SRC-FAMILY	-	GPS
731	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CADH5_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 CADH5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CTNA1_HUMAN	CTNNA1	physical	9434630
CTNB1_HUMAN	CTNNB1	physical	9434630
PLAK_HUMAN	JUP	physical	9434630
CTND1_HUMAN	CTNND1	physical	11855855
PKP4_HUMAN	PKP4	physical	12426320
CTND1_HUMAN	CTNND1	physical	9378757
CTNA1_HUMAN	CTNNA1	physical	12003790
CTNB1_HUMAN	CTNNB1	physical	12003790
PLAK_HUMAN	JUP	physical	12003790
VIME_HUMAN	VIM	physical	12003790
FIBA_HUMAN	FGA	physical	11900554
CTNB1_HUMAN	CTNNB1	physical	23243000
ARVC_HUMAN	ARVCF	physical	28514442
PKP4_HUMAN	PKP4	physical	28514442
SCML1_HUMAN	SCML1	physical	28514442
CTNA2_HUMAN	CTNNA2	physical	28514442
CTNB1_HUMAN	CTNNB1	physical	28514442
RBFA_HUMAN	RBFA	physical	28514442
CTNA1_HUMAN	CTNNA1	physical	28514442
SARAF_HUMAN	SARAF	physical	28514442
PLD1_HUMAN	PLD1	physical	28514442
TMTC3_HUMAN	TMTC3	physical	28514442
ZMYM1_HUMAN	ZMYM1	physical	28514442
GPAT1_HUMAN	GPAM	physical	28514442
KCJ11_HUMAN	KCNJ11	physical	28514442
EXOG_HUMAN	EXOG	physical	28514442
MYO5A_HUMAN	MYO5A	physical	28514442
TNFL9_HUMAN	TNFSF9	physical	28514442
SGPL1_HUMAN	SGPL1	physical	28514442
WDR75_HUMAN	WDR75	physical	28514442
IQCB1_HUMAN	IQCB1	physical	28514442
KEAP1_HUMAN	KEAP1	physical	28514442
MYO5C_HUMAN	MYO5C	physical	28514442
CAN15_HUMAN	CAPN15	physical	28514442
TIGD5_HUMAN	TIGD5	physical	28514442
RPP29_HUMAN	POP4	physical	28514442
VANG2_HUMAN	VANGL2	physical	28514442
DNJC1_HUMAN	DNAJC1	physical	28514442
ST7_HUMAN	ST7	physical	28514442
MTMR5_HUMAN	SBF1	physical	28514442
ECHB_HUMAN	HADHB	physical	28514442
TSSC4_HUMAN	TSSC4	physical	28514442
MICU2_HUMAN	MICU2	physical	28514442
DAG1_HUMAN	DAG1	physical	28514442
CEP57_HUMAN	CEP57	physical	28514442
SRBP2_HUMAN	SREBF2	physical	28514442
ATF6A_HUMAN	ATF6	physical	28514442
PLD2_HUMAN	PLD2	physical	28514442
MCRS1_HUMAN	MCRS1	physical	28514442
OSBP1_HUMAN	OSBP	physical	28514442
CTND1_HUMAN	CTNND1	physical	28514442
ACD11_HUMAN	ACAD11	physical	28514442
LTBP1_HUMAN	LTBP1	physical	28514442
RPC1_HUMAN	POLR3A	physical	28514442
VTI1B_HUMAN	VTI1B	physical	28514442
LRFN1_HUMAN	LRFN1	physical	28514442
MACOI_HUMAN	TMEM57	physical	28514442
ZNHI2_HUMAN	ZNHIT2	physical	28514442
ASPM_HUMAN	ASPM	physical	28514442
PTPRU_HUMAN	PTPRU	physical	28514442
MYO9B_HUMAN	MYO9B	physical	28514442
MICU1_HUMAN	MICU1	physical	28514442
PK3CB_HUMAN	PIK3CB	physical	28514442
PKN3_HUMAN	PKN3	physical	28514442
U520_HUMAN	SNRNP200	physical	28514442
MYO1B_HUMAN	MYO1B	physical	28514442
KCNJ8_HUMAN	KCNJ8	physical	28514442
PLPL6_HUMAN	PNPLA6	physical	28514442
RYK_HUMAN	RYK	physical	28514442
TIP_HUMAN	ITFG1	physical	28514442
UTP15_HUMAN	UTP15	physical	28514442
KDIS_HUMAN	KIDINS220	physical	28514442
MYO1D_HUMAN	MYO1D	physical	28514442
ECHA_HUMAN	HADHA	physical	28514442
TBL2_HUMAN	TBL2	physical	28514442
RPA1_HUMAN	POLR1A	physical	28514442
RRP1_HUMAN	RRP1	physical	28514442
P121A_HUMAN	POM121	physical	28514442
PDZD8_HUMAN	PDZD8	physical	28514442
TM39A_HUMAN	TMEM39A	physical	28514442
FAK1_HUMAN	PTK2	physical	22720799
CTNB1_HUMAN	CTNNB1	physical	22720799

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
DB00480	Lenalidomide

Regulatory Network of CADH5_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-112; ASN-442; ASN-523 ANDASN-535, AND MASS SPECTROMETRY.	16335952 [Abstract]
Phosphorylation
Reference	PubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-685, AND MASSSPECTROMETRY.	18083107 [Abstract]