dbPTM

SUSD1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SUSD1_HUMAN
UniProt AC	Q6UWL2
Protein Name	Sushi domain-containing protein 1
Gene Name	SUSD1
Organism	Homo sapiens (Human).
Sequence Length	747
Subcellular Localization	Membrane Single-pass type I membrane protein .
Protein Description
Protein Sequence	MGRGPWDAGPSRRLLPLLLLLGLARGAAGAPGPDGLDVCATCHEHATCQQREGKKICICNYGFVGNGRTQCVDKNECQFGATLVCGNHTSCHNTPGGFYCICLEGYRATNNNKTFIPNDGTFCTDIDECEVSGLCRHGGRCVNTHGSFECYCMDGYLPRNGPEPFHPTTDATSCTEIDCGTPPEVPDGYIIGNYTSSLGSQVRYACREGFFSVPEDTVSSCTGLGTWESPKLHCQEINCGNPPEMRHAILVGNHSSRLGGVARYVCQEGFESPGGKITSVCTEKGTWRESTLTCTEILTKINDVSLFNDTCVRWQINSRRINPKISYVISIKGQRLDPMESVREETVNLTTDSRTPEVCLALYPGTNYTVNISTAPPRRSMPAVIGFQTAEVDLLEDDGSFNISIFNETCLKLNRRSRKVGSEHMYQFTVLGQRWYLANFSHATSFNFTTREQVPVVCLDLYPTTDYTVNVTLLRSPKRHSVQITIATPPAVKQTISNISGFNETCLRWRSIKTADMEEMYLFHIWGQRWYQKEFAQEMTFNISSSSRDPEVCLDLRPGTNYNVSLRALSSELPVVISLTTQITEPPLPEVEFFTVHRGPLPRLRLRKAKEKNGPISSYQVLVLPLALQSTFSCDSEGASSFFSNASDADGYVAAELLAKDVPDDAMEIPIGDRLYYGEYYNAPLKRGSDYCIILRITSEWNKVRRHSCAVWAQVKDSSLMLLQMAGVGLGSLAVVIILTFLSFSAV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Phosphorylation	GPWDAGPSRRLLPLL CCCCCCHHHCHHHHH	29.16	-
87	N-linked_Glycosylation	GATLVCGNHTSCHNT CCEEEECCCCCCCCC	30.09	UniProtKB CARBOHYD
112	N-linked_Glycosylation	GYRATNNNKTFIPND CEEEECCCCEECCCC	46.98	UniProtKB CARBOHYD
193	N-linked_Glycosylation	PDGYIIGNYTSSLGS CCCEEECCCCCCCCH	26.88	UniProtKB CARBOHYD
212	Phosphorylation	ACREGFFSVPEDTVS HHHCCCCCCCCCCCC	34.20	22468782
253	N-linked_Glycosylation	RHAILVGNHSSRLGG CEEEEECCCHHHHHH	25.12	16263699
284	Ubiquitination	ITSVCTEKGTWREST EEEEECCCCCCCCCE	43.41	-
284 (in isoform 2)	Ubiquitination	-	43.41	-
290	Phosphorylation	EKGTWRESTLTCTEI CCCCCCCCEEEHHHH	21.83	30576142
293	Phosphorylation	TWRESTLTCTEILTK CCCCCEEEHHHHHHH	19.92	30576142
299	Phosphorylation	LTCTEILTKINDVSL EEHHHHHHHHCCEEC	35.22	30576142
330	Phosphorylation	PKISYVISIKGQRLD CCEEEEEEECCEECC	14.27	24719451
346	Phosphorylation	MESVREETVNLTTDS CHHHCEEEEECCCCC	15.22	22210691
348	N-linked_Glycosylation	SVREETVNLTTDSRT HHCEEEEECCCCCCC	38.81	UniProtKB CARBOHYD
353	Phosphorylation	TVNLTTDSRTPEVCL EEECCCCCCCCCEEE	35.64	22210691
367	N-linked_Glycosylation	LALYPGTNYTVNIST EEECCCCCEEEEEEC	36.07	UniProtKB CARBOHYD
368	Phosphorylation	ALYPGTNYTVNISTA EECCCCCEEEEEECC	16.35	-
369	Phosphorylation	LYPGTNYTVNISTAP ECCCCCEEEEEECCC	14.78	-
548	Dimethylation	FNISSSSRDPEVCLD EECCCCCCCCCEEEE	66.50	-
548	Methylation	FNISSSSRDPEVCLD EECCCCCCCCCEEEE	66.50	30763241
560	Phosphorylation	CLDLRPGTNYNVSLR EEECCCCCCCEEEHH	36.89	29978859
562	Phosphorylation	DLRPGTNYNVSLRAL ECCCCCCCEEEHHHH	19.44	29978859
563	N-linked_Glycosylation	LRPGTNYNVSLRALS CCCCCCCEEEHHHHC	20.97	UniProtKB CARBOHYD
565	Phosphorylation	PGTNYNVSLRALSSE CCCCCEEEHHHHCCC	14.43	29978859
686 (in isoform 2)	Ubiquitination	-	54.37	21890473
686	Ubiquitination	EYYNAPLKRGSDYCI EECCCCCCCCCCEEE	54.37	21890473
686 (in isoform 1)	Ubiquitination	-	54.37	21890473
686 (in isoform 3)	Ubiquitination	-	54.37	21890473

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
Oops, there are no upstream regulatory protein records of SUSD1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SUSD1_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 SUSD1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of SUSD1_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.

Regulatory Network of SUSD1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Elucidation of N-glycosylation sites on human platelet proteins: aglycoproteomic approach."; Lewandrowski U., Moebius J., Walter U., Sickmann A.; Mol. Cell. Proteomics 5:226-233(2006). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-253, AND MASSSPECTROMETRY.	16263699 [Abstract]