dbPTM

CAD13_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CAD13_HUMAN
UniProt AC	P55290
Protein Name	Cadherin-13
Gene Name	CDH13
Organism	Homo sapiens (Human).
Sequence Length	713
Subcellular Localization	Cell membrane Lipid-anchor, GPI-anchor.
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. May act as a negative regulator of neural cell growth..
Protein Sequence	MQPRTPLVLCVLLSQVLLLTSAEDLDCTPGFQQKVFHINQPAEFIEDQSILNLTFSDCKGNDKLRYEVSSPYFKVNSDGGLVALRNITAVGKTLFVHARTPHAEDMAELVIVGGKDIQGSLQDIFKFARTSPVPRQKRSIVVSPILIPENQRQPFPRDVGKVVDSDRPERSKFRLTGKGVDQEPKGIFRINENTGSVSVTRTLDREVIAVYQLFVETTDVNGKTLEGPVPLEVIVIDQNDNRPIFREGPYIGHVMEGSPTGTTVMRMTAFDADDPATDNALLRYNIRQQTPDKPSPNMFYIDPEKGDIVTVVSPALLDRETLENPKYELIIEAQDMAGLDVGLTGTATATIMIDDKNDHSPKFTKKEFQATVEEGAVGVIVNLTVEDKDDPTTGAWRAAYTIINGNPGQSFEIHTNPQTNEGMLSVVKPLDYEISAFHTLLIKVENEDPLVPDVSYGPSSTATVHITVLDVNEGPVFYPDPMMVTRQEDLSVGSVLLTVNATDPDSLQHQTIRYSVYKDPAGWLNINPINGTVDTTAVLDRESPFVDNSVYTALFLAIDSGNPPATGTGTLLITLEDVNDNAPFIYPTVAEVCDDAKNLSVVILGASDKDLHPNTDPFKFEIHKQAVPDKVWKISKINNTHALVSLLQNLNKANYNLPIMVTDSGKPPMTNITDLRVQVCSCRNSKVDCNAAGALRFSLPSVLLLSLFSLACL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
52	N-linked_Glycosylation	IEDQSILNLTFSDCK CCCCCEEEEEEECCC	35.05	UniProtKB CARBOHYD
66	Phosphorylation	KGNDKLRYEVSSPYF CCCCEEEEEECCCEE	30.99	23403867
69	Phosphorylation	DKLRYEVSSPYFKVN CEEEEEECCCEEEEC	17.41	23403867
70	Phosphorylation	KLRYEVSSPYFKVNS EEEEEECCCEEEECC	28.88	23403867
72	Phosphorylation	RYEVSSPYFKVNSDG EEEECCCEEEECCCC	20.27	29759185
86	N-linked_Glycosylation	GGLVALRNITAVGKT CCEEEEEEEEECCCE	36.49	16335952
120	Phosphorylation	GGKDIQGSLQDIFKF CCCCCCCCHHHHHHH	13.39	29759185
167	Dimethylation	GKVVDSDRPERSKFR CEECCCCCCCHHCEE	38.64	-
167	Methylation	GKVVDSDRPERSKFR CEECCCCCCCHHCEE	38.64	-
170	Methylation	VDSDRPERSKFRLTG CCCCCCCHHCEEEEC	48.07	-
170	Dimethylation	VDSDRPERSKFRLTG CCCCCCCHHCEEEEC	48.07	-
196	Phosphorylation	RINENTGSVSVTRTL EEECCCCEEEEEEEC	14.80	-
200	Phosphorylation	NTGSVSVTRTLDREV CCCEEEEEEECCHHH	15.49	-
200	O-linked_Glycosylation	NTGSVSVTRTLDREV CCCEEEEEEECCHHH	15.49	55830453
258	Phosphorylation	IGHVMEGSPTGTTVM EEEEECCCCCCCEEE	13.14	-
382	N-linked_Glycosylation	GAVGVIVNLTVEDKD CCEEEEEEEEECCCC	20.90	UniProtKB CARBOHYD
500	N-linked_Glycosylation	GSVLLTVNATDPDSL CEEEEEEECCCHHHH	31.71	16335952
530	N-linked_Glycosylation	WLNINPINGTVDTTA CEEEECCCCEEEECE	41.14	19159218
598	N-linked_Glycosylation	EVCDDAKNLSVVILG HHCCCCCCEEEEEEC	38.99	UniProtKB CARBOHYD
600	O-linked_Glycosylation	CDDAKNLSVVILGAS CCCCCCEEEEEECCC	24.59	28657654
638	N-linked_Glycosylation	VWKISKINNTHALVS EEEEEEECCHHHHHH	51.59	16335952
662	Phosphorylation	YNLPIMVTDSGKPPM CCCCEEEECCCCCCC	13.68	27251275
664	Phosphorylation	LPIMVTDSGKPPMTN CCEEEECCCCCCCCC	39.07	27251275
671	N-linked_Glycosylation	SGKPPMTNITDLRVQ CCCCCCCCCCEEEEE	28.98	UniProtKB CARBOHYD
693	GPI-anchor	KVDCNAAGALRFSLP CCCCCHHHHHCCCHH	23.80	16602701

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
-	K	Ubiquitination	E3 ubiquitin ligase	FZR1	Q9UM11	PMID:17631504

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CAD13_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 CAD13_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
S14L1_HUMAN	SEC14L1	physical	28514442
PLCE_HUMAN	AGPAT5	physical	28514442
INSI1_HUMAN	INSIG1	physical	28514442
DUSTY_HUMAN	DSTYK	physical	28514442
RRAGB_HUMAN	RRAGB	physical	28514442
ERMP1_HUMAN	ERMP1	physical	28514442
VMP1_HUMAN	VMP1	physical	28514442
UQCC1_HUMAN	UQCC1	physical	28514442
TBB3_HUMAN	TUBB3	physical	28514442
CHPT1_HUMAN	CHPT1	physical	28514442
TBB8_HUMAN	TUBB8	physical	28514442
GHITM_HUMAN	GHITM	physical	28514442
ARF5_HUMAN	ARF5	physical	28514442
PIGU_HUMAN	PIGU	physical	28514442
TMX4_HUMAN	TMX4	physical	28514442
RL23_HUMAN	RPL23	physical	28514442

Drug and Disease Associations

Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CAD13_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-530 AND ASN-638, AND MASSSPECTROMETRY.	19159218 [Abstract]
"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-86; ASN-500 AND ASN-638,AND MASS SPECTROMETRY.	16335952 [Abstract]