dbPTM

DLK1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DLK1_MOUSE
UniProt AC	Q09163
Protein Name	Protein delta homolog 1
Gene Name	Dlk1
Organism	Mus musculus (Mouse).
Sequence Length	385
Subcellular Localization	Membrane Single-pass type I membrane protein.
Protein Description	May have a role in neuroendocrine differentiation. Inhibits adipocyte differentiation..
Protein Sequence	MIATGALLRVLLLLLAFGHSTYGAECDPPCDPQYGFCEADNVCRCHVGWEGPLCDKCVTAPGCVNGVCKEPWQCICKDGWDGKFCEIDVRACTSTPCANNGTCVDLEKGQYECSCTPGFSGKDCQHKAGPCVINGSPCQHGGACVDDEGQASHASCLCPPGFSGNFCEIVAATNSCTPNPCENDGVCTDIGGDFRCRCPAGFVDKTCSRPVSNCASGPCQNGGTCLQHTQVSFECLCKPPFMGPTCAKKRGASPVQVTHLPSGYGLTYRLTPGVHELPVQQPEQHILKVSMKELNKSTPLLTEGQAICFTILGVLTSLVVLGTVAIVFLNKCETWVSNLRYNHTFRKKKNLLLQYNSGEELAVNIIFPEKIDMTTFNKEAGDEEI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MIATGALLRVL ----CCHHHHHHHHH	16.44	28059163
94	O-linked_Glycosylation	IDVRACTSTPCANNG EEEEEECCCCCCCCC	30.18	9118998
100	N-linked_Glycosylation	TSTPCANNGTCVDLE CCCCCCCCCEEEECC	28.73	9118998
165	N-linked_Glycosylation	CPPGFSGNFCEIVAA CCCCCCCCCCEEEEE	36.88	9118998
174	N-linked_Glycosylation	CEIVAATNSCTPNPC CEEEEECCCCCCCCC	30.29	9118998
216	O-linked_Glycosylation	RPVSNCASGPCQNGG CCCCCCCCCCCCCCC	45.53	9118998
224	O-linked_Glycosylation	GPCQNGGTCLQHTQV CCCCCCCCCCCCCEE	16.08	9118998
258	O-linked_Glycosylation	GASPVQVTHLPSGYG CCCCCEEEECCCCCC	10.70	9118998
262	Phosphorylation	VQVTHLPSGYGLTYR CEEEECCCCCCCEEE	51.51	24719451
264	Phosphorylation	VTHLPSGYGLTYRLT EEECCCCCCCEEEEC	17.19	-
267	O-linked_Glycosylation	LPSGYGLTYRLTPGV CCCCCCCEEEECCCC	11.39	9118998
268	Phosphorylation	PSGYGLTYRLTPGVH CCCCCCEEEECCCCC	14.52	24719451
271	O-linked_Glycosylation	YGLTYRLTPGVHELP CCCEEEECCCCCCCC	14.70	9118998
295	N-linked_Glycosylation	KVSMKELNKSTPLLT EEEHHHHHCCCCCCC	37.01	-
355	Phosphorylation	KKNLLLQYNSGEELA CCEEEEEECCCCCEE	15.97	26643407
357	Phosphorylation	NLLLQYNSGEELAVN EEEEEECCCCCEEEE	42.52	26643407
375	Phosphorylation	PEKIDMTTFNKEAGD CCCCCCCEECCCCCC	20.69	29514104

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	Stub1	Q9WUD1	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DLK1_MOUSE !!

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 DLK1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of DLK1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of DLK1_MOUSE

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Glycosylation analysis and protein structure determination of murinefetal antigen 1 (mFA1) -- the circulating gene product of the delta-like protein (dlk), preadipocyte factor 1 (Pref-1) and stromal-cell-derived protein 1 (SCP-1) cDNAs."; Krogh T.N., Bachmann E., Teisner B., Skjoedt K., Hoejrup P.; Eur. J. Biochem. 244:334-342(1997). Cited for: GLYCOSYLATION AT SER-94; ASN-100; ASN-165; ASN-174; SER-216; THR-224;THR-258; THR-267 AND THR-271, AND STRUCTURE OF CARBOHYDRATE.	9118998 [Abstract]
O-linked Glycosylation
Reference	PubMed
"Glycosylation analysis and protein structure determination of murinefetal antigen 1 (mFA1) -- the circulating gene product of the delta-like protein (dlk), preadipocyte factor 1 (Pref-1) and stromal-cell-derived protein 1 (SCP-1) cDNAs."; Krogh T.N., Bachmann E., Teisner B., Skjoedt K., Hoejrup P.; Eur. J. Biochem. 244:334-342(1997). Cited for: GLYCOSYLATION AT SER-94; ASN-100; ASN-165; ASN-174; SER-216; THR-224;THR-258; THR-267 AND THR-271, AND STRUCTURE OF CARBOHYDRATE.	9118998 [Abstract]