IDD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IDD_HUMAN
• UniProt AC: P98153
• Protein Name: Integral membrane protein DGCR2/IDD
• Gene Name: DGCR2
• Organism: Homo sapiens (Human).
• Sequence Length: 550
• Subcellular Localization: Membrane; Single-pass type I membrane protein.
• Protein Description: Putative adhesion receptor, that could be involved in cell-cell or cell-matrix interactions required for normal cell differentiation and migration..
• Protein Sequence: MVPKADSGAFLLLFLLVLTVTEPLRPELRCNPGQFACRSGTIQCIPLPWQCDGWATCEDESDEANCPEVTGEVRPHHGKEAVDPRQGRARGGDPSHFHAVNVAQPVRFSSFLGKCPTGWHHYEGTASCYRVYLSGENYWDAAQTCQRLNGSLATFSTDQELRFVLAQEWDQPERSFGWKDQRKLWVGYQYVITGRNRSLEGRWEVAFKGSSEVFLPPDPIFASAMSENDNVFCAQLQCFHFPTLRHHDLHSWHAESCYEKSSFLCKRSQTCVDIKDNVVDEGFYFTPKGDDPCLSCTCHGGEPEMCVAALCERPQGCQQYRKDPKECCKFMCLDPDGNSLFDSMASGMRLVVSCISSFLILSLLLFMVHRLRQRRRERIESLIGANLHHFNLGRRIPGFDYGPDGFGTGLTPLHLSDDGEGGTFHFHDPPPPYTAYKYPDIGQPDDPPPPYEASIHPDSVFYDPADDDAFEPVEVSLPAPGDGGSEGALLRRLEQPLPTAGASLADLEDSADSSSALLVPPDPAQSGSTPAAEALPGGGRHSRSSLNTVV

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
21	Phosphorylation	FLLVLTVTEPLRPEL HHHHHHCCCCCCHHH	27.01	24719451
90	Methylation	DPRQGRARGGDPSHF CCCCCCCCCCCCCHH	48.55	-
95	Phosphorylation	RARGGDPSHFHAVNV CCCCCCCCHHCEEEC	43.45	29978859
149	N-linked_Glycosylation	AQTCQRLNGSLATFS HHHHHHHCCCEEEEC	39.95	UniProtKB CARBOHYD
179	Ubiquitination	PERSFGWKDQRKLWV CCCCCCCCCHHHEEE	44.34	-
196	N-linked_Glycosylation	QYVITGRNRSLEGRW EEEEECCCCCCCCCE	38.96	UniProtKB CARBOHYD
260	Acetylation	HAESCYEKSSFLCKR CHHHHHHCCCEEECC	25.56	20167786
266	Acetylation	EKSSFLCKRSQTCVD HCCCEEECCCCEEEE	58.18	20167786
266	Ubiquitination	EKSSFLCKRSQTCVD HCCCEEECCCCEEEE	58.18	-
295	Phosphorylation	KGDDPCLSCTCHGGE CCCCCCEECEECCCC	17.69	-
297	Phosphorylation	DDPCLSCTCHGGEPE CCCCEECEECCCCCH	12.26	-
339	Phosphorylation	CLDPDGNSLFDSMAS EECCCCCCHHHHHHH	35.62	-
343	Phosphorylation	DGNSLFDSMASGMRL CCCCHHHHHHHCHHH	14.65	-
346	Phosphorylation	SLFDSMASGMRLVVS CHHHHHHHCHHHHHH	25.20	-
381	Phosphorylation	RRRERIESLIGANLH HHHHHHHHHHHCCCC	23.94	29255136
476	O-linked_Glycosylation	AFEPVEVSLPAPGDG CCCCEEEECCCCCCC	18.35	OGP
528	O-linked_Glycosylation	PDPAQSGSTPAAEAL CCHHHCCCCCHHHCC	36.14	OGP
542	Phosphorylation	LPGGGRHSRSSLNTV CCCCCCCCCCCCCCC	32.28	23312004
544	Phosphorylation	GGGRHSRSSLNTVV- CCCCCCCCCCCCCC-	42.04	23312004
545	Phosphorylation	GGRHSRSSLNTVV-- CCCCCCCCCCCCC--	25.24	24719451
548	Phosphorylation	HSRSSLNTVV----- CCCCCCCCCC-----	28.12	28102081

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IDD_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 IDD_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of IDD_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

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381, AND MASSSPECTROMETRY.
PubMed: 17081983