SHRPN_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SHRPN_HUMAN
• UniProt AC: Q9H0F6
• Protein Name: Sharpin
• Gene Name: SHARPIN
• Organism: Homo sapiens (Human).
• Sequence Length: 387
• Subcellular Localization: Cytoplasm, cytosol . Cell junction, synapse. Enriched at synaptic sites in mature neurons where it colocalizes with SHANK1..
• Protein Description: Component of the LUBAC complex which conjugates linear polyubiquitin chains in a head-to-tail manner to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis..
• Protein Sequence: MAPPAGGAAAAASDLGSAAVLLAVHAAVRPLGAGPDAEAQLRRLQLSADPERPGRFRLELLGAGPGAVNLEWPLESVSYTIRGPTQHELQPPPGGPGTLSLHFLNPQEAQRWAVLVRGATVEGQNGSKSNSPPALGPEACPVSLPSPPEASTLKGPPPEADLPRSPGNLTEREELAGSLARAIAGGDEKGAAQVAAVLAQHRVALSVQLQEACFPPGPIRLQVTLEDAASAASAASSAHVALQVHPHCTVAALQEQVFSELGFPPAVQRWVIGRCLCVPERSLASYGVRQDGDPAFLYLLSAPREAPATGPSPQHPQKMDGELGRLFPPSLGLPPGPQPAASSLPSPLQPSWSCPSCTFINAPDRPGCEMCSTQRPCTWDPLAAAST

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
29	Methylation	LAVHAAVRPLGAGPD HHHHHHHCCCCCCCC	18.92	24384663
80	Phosphorylation	PLESVSYTIRGPTQH CHHHCEEEEECCCCC	9.19	24719451
127	Phosphorylation	TVEGQNGSKSNSPPA EEECCCCCCCCCCCC	40.22	28348404
129	Phosphorylation	EGQNGSKSNSPPALG ECCCCCCCCCCCCCC	44.21	30278072
131	Phosphorylation	QNGSKSNSPPALGPE CCCCCCCCCCCCCCC	39.07	30278072
143	Phosphorylation	GPEACPVSLPSPPEA CCCCCCCCCCCCCCC	21.50	30206219
146	Phosphorylation	ACPVSLPSPPEASTL CCCCCCCCCCCCCCC	59.38	25159151
151	Phosphorylation	LPSPPEASTLKGPPP CCCCCCCCCCCCCCC	32.39	22199227
152	Phosphorylation	PSPPEASTLKGPPPE CCCCCCCCCCCCCCC	39.27	30576142
154	Ubiquitination	PPEASTLKGPPPEAD CCCCCCCCCCCCCCC	70.25	-
165	Phosphorylation	PEADLPRSPGNLTER CCCCCCCCCCCCCHH	34.91	29255136
170	Phosphorylation	PRSPGNLTEREELAG CCCCCCCCHHHHHHH	36.68	23927012
178	Phosphorylation	EREELAGSLARAIAG HHHHHHHHHHHHHHC	17.16	23927012
189	Ubiquitination	AIAGGDEKGAAQVAA HHHCCCHHHHHHHHH	59.60	21890473
189 (in isoform 1)	Ubiquitination	-	59.60	21890473
189	Ubiquitination	AIAGGDEKGAAQVAA HHHCCCHHHHHHHHH	59.60	21890473
189 (in isoform 2)	Ubiquitination	-	59.60	21890473
189	Ubiquitination	AIAGGDEKGAAQVAA HHHCCCHHHHHHHHH	59.60	22053931
224	Phosphorylation	GPIRLQVTLEDAASA CCEEEEEEHHHHHHH	16.09	-
282	Phosphorylation	CLCVPERSLASYGVR CEEECHHHHHHCCCC	26.99	27251275
301	Phosphorylation	PAFLYLLSAPREAPA CEEEEEEECCCCCCC	33.36	24719451
309	Phosphorylation	APREAPATGPSPQHP CCCCCCCCCCCCCCC	48.87	28450419
312	Phosphorylation	EAPATGPSPQHPQKM CCCCCCCCCCCCCCC	38.24	25159151
318	Ubiquitination	PSPQHPQKMDGELGR CCCCCCCCCCCCHHH	43.33	21890473
318 (in isoform 1)	Ubiquitination	-	43.33	21890473
318	Ubiquitination	PSPQHPQKMDGELGR CCCCCCCCCCCCHHH	43.33	21890473

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SHRPN_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 SHRPN_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SHRPN_HUMAN	SHARPIN	physical	11178875
PTEN_HUMAN	PTEN	physical	20458142
TNAP3_HUMAN	TNFAIP3	physical	23032186
HOIL1_HUMAN	RBCK1	physical	23032186
RNF31_HUMAN	RNF31	physical	23032186
RNF31_HUMAN	RNF31	physical	23746843
OTUL_HUMAN	OTULIN	physical	23746843
TNR1A_HUMAN	TNFRSF1A	physical	23746843
THIOM_HUMAN	TXN2	physical	21988832
RNF31_HUMAN	RNF31	physical	24726327
HOIL1_HUMAN	RBCK1	physical	24726327
HOIL1_HUMAN	RBCK1	physical	21455180
RNF31_HUMAN	RNF31	physical	21455180
ITAL_HUMAN	ITGAL	physical	24210817
PTEN_HUMAN	PTEN	physical	25152374
NEMO_HUMAN	IKBKG	physical	21455180
IKKA_HUMAN	CHUK	physical	21455180
IKKB_HUMAN	IKBKB	physical	21455180
ITAL_HUMAN	ITGAL	physical	26600301
ITB2_HUMAN	ITGB2	physical	26600301
ITA5_HUMAN	ITGA5	physical	26600301
RNF31_HUMAN	RNF31	physical	26600301
TRAF1_HUMAN	TRAF1	physical	25996949
HOIL1_HUMAN	RBCK1	physical	26670046
CYLD_HUMAN	CYLD	physical	26670046
RNF31_HUMAN	RNF31	physical	26670046
MDM2_HUMAN	MDM2	physical	28063307
TRAF1_HUMAN	TRAF1	physical	27893701
NEMO_HUMAN	IKBKG	physical	27893701
RNF31_HUMAN	RNF31	physical	27591049
CYLD_HUMAN	CYLD	physical	27591049
OTUL_HUMAN	OTULIN	physical	27591049
SPAT2_HUMAN	SPATA2	physical	27591049

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

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND MASSSPECTROMETRY.
PubMed: 18669648