SIGL7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SIGL7_HUMAN
• UniProt AC: Q9Y286
• Protein Name: Sialic acid-binding Ig-like lectin 7
• Gene Name: SIGLEC7
• Organism: Homo sapiens (Human).
• Sequence Length: 467
• Subcellular Localization: Membrane; Single-pass type I membrane protein.
• Protein Description: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,3- and alpha-2,6-linked sialic acid. Also binds disialogangliosides (disialogalactosyl globoside, disialyl lactotetraosylceramide and disialyl GalNAc lactotetraoslylceramide). The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Mediates inhibition of natural killer cells cytotoxicity. May play a role in hemopoiesis. Inhibits differentiation of CD34+ cell precursors towards myelomonocytic cell lineage and proliferation of leukemic myeloid cells (in vitro)..
• Protein Sequence: MLLLLLLPLLWGRERVEGQKSNRKDYSLTMQSSVTVQEGMCVHVRCSFSYPVDSQTDSDPVHGYWFRAGNDISWKAPVATNNPAWAVQEETRDRFHLLGDPQTKNCTLSIRDARMSDAGRYFFRMEKGNIKWNYKYDQLSVNVTALTHRPNILIPGTLESGCFQNLTCSVPWACEQGTPPMISWMGTSVSPLHPSTTRSSVLTLIPQPQHHGTSLTCQVTLPGAGVTTNRTIQLNVSYPPQNLTVTVFQGEGTASTALGNSSSLSVLEGQSLRLVCAVDSNPPARLSWTWRSLTLYPSQPSNPLVLELQVHLGDEGEFTCRAQNSLGSQHVSLNLSLQQEYTGKMRPVSGVLLGAVGGAGATALVFLSFCVIFIVVRSCRKKSARPAADVGDIGMKDANTIRGSASQGNLTESWADDNPRHHGLAAHSSGEEREIQYAPLSFHKGEPQDLSGQEATNNEYSEIKIPK

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
105	N-linked_Glycosylation	LGDPQTKNCTLSIRD CCCCCCCCCEEEEEE	27.65	16895906
109	Phosphorylation	QTKNCTLSIRDARMS CCCCCEEEEEEECHH	9.45	24719451
142	N-linked_Glycosylation	KYDQLSVNVTALTHR EECEEEEEEEEECCC	23.26	UniProtKB CARBOHYD
165	N-linked_Glycosylation	LESGCFQNLTCSVPW CCCCCCCCCEECCCC	19.64	UniProtKB CARBOHYD
229	N-linked_Glycosylation	PGAGVTTNRTIQLNV CCCCCEECCEEEEEE	29.72	UniProtKB CARBOHYD
235	N-linked_Glycosylation	TNRTIQLNVSYPPQN ECCEEEEEEECCCCC	12.33	UniProtKB CARBOHYD
242	N-linked_Glycosylation	NVSYPPQNLTVTVFQ EEECCCCCEEEEEEE	43.37	UniProtKB CARBOHYD
260	N-linked_Glycosylation	TASTALGNSSSLSVL CCEEECCCCCCEEEE	39.30	UniProtKB CARBOHYD
334	N-linked_Glycosylation	GSQHVSLNLSLQQEY CCCEEEEEEEEEEHH	21.78	UniProtKB CARBOHYD
349	Phosphorylation	TGKMRPVSGVLLGAV CCCCCCCCCEEHHCC	26.35	-
362	Phosphorylation	AVGGAGATALVFLSF CCCHHHHHHHHHHHH	21.43	-
400	Phosphorylation	IGMKDANTIRGSASQ CCCCCCCCCCCCCCC	17.48	27486199
404	Phosphorylation	DANTIRGSASQGNLT CCCCCCCCCCCCCCC	18.20	26657352
406	Phosphorylation	NTIRGSASQGNLTES CCCCCCCCCCCCCCC	40.07	28355574
411	Phosphorylation	SASQGNLTESWADDN CCCCCCCCCCCCCCC	31.79	28450419
413	Phosphorylation	SQGNLTESWADDNPR CCCCCCCCCCCCCCC	23.48	28450419
428	Phosphorylation	HHGLAAHSSGEEREI CCCCCCCCCCCCEEE	35.00	24275569
429	Phosphorylation	HGLAAHSSGEEREIQ CCCCCCCCCCCEEEE	40.12	16895906
437	Phosphorylation	GEEREIQYAPLSFHK CCCEEEEEECCEECC	18.82	28258704
441	Phosphorylation	EIQYAPLSFHKGEPQ EEEEECCEECCCCCC	25.01	28258704
460	Phosphorylation	QEATNNEYSEIKIPK CCCCCCCCCCCCCCC	17.46	25587033
461	Phosphorylation	EATNNEYSEIKIPK- CCCCCCCCCCCCCC-	27.02	-

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	SOCS3	O14543	PMID:17138568

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SIGL7_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 SIGL7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LG3BP_HUMAN	LGALS3BP	physical	25320078
WDR89_HUMAN	WDR89	physical	28514442
LEG1_HUMAN	LGALS1	physical	28514442
PTN6_HUMAN	PTPN6	physical	15703304
PTN11_HUMAN	PTPN11	physical	15703304

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

N-linked Glycosylation

"Siglec-7 undergoes a major conformational change when complexed withthe alpha(2,8)-disialylganglioside GT1b.";
Attrill H., Imamura A., Sharma R.S., Kiso M., Crocker P.R.,van Aalten D.M.;
J. Biol. Chem. 281:32774-32783(2006).
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 18-144 IN COMPLEX WITHALPHA(2,8)-DISIALYLATED LIGAND GT1B, GLYCOSYLATION AT ASN-105, ANDDISULFIDE BOND.
PubMed: 16895906

"The structure of siglec-7 in complex with sialosides: leads forrational structure-based inhibitor design.";
Attrill H., Takazawa H., Witt S., Kelm S., Isecke R., Brossmer R.,Ando T., Ishida H., Kiso M., Crocker P.R., van Aalten D.M.;
Biochem. J. 397:271-278(2006).
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 18-144 IN COMPLEX WITHSIALYLATED LIGAND, GLYCOSYLATION AT ASN-105, AND DISULFIDE BOND.
PubMed: 16623661