SIGL5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SIGL5_HUMAN
• UniProt AC: O15389
• Protein Name: Sialic acid-binding Ig-like lectin 5
• Gene Name: SIGLEC5
• Organism: Homo sapiens (Human).
• Sequence Length: 551
• Subcellular Localization: Membrane; Single-pass type I membrane protein.
• Protein Description: Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface..
• Protein Sequence: MLPLLLLPLLWGGSLQEKPVYELQVQKSVTVQEGLCVLVPCSFSYPWRSWYSSPPLYVYWFRDGEIPYYAEVVATNNPDRRVKPETQGRFRLLGDVQKKNCSLSIGDARMEDTGSYFFRVERGRDVKYSYQQNKLNLEVTALIEKPDIHFLEPLESGRPTRLSCSLPGSCEAGPPLTFSWTGNALSPLDPETTRSSELTLTPRPEDHGTNLTCQMKRQGAQVTTERTVQLNVSYAPQTITIFRNGIALEILQNTSYLPVLEGQALRLLCDAPSNPPAHLSWFQGSPALNATPISNTGILELRRVRSAEEGGFTCRAQHPLGFLQIFLNLSVYSLPQLLGPSCSWEAEGLHCRCSFRARPAPSLCWRLEEKPLEGNSSQGSFKVNSSSAGPWANSSLILHGGLSSDLKVSCKAWNIYGSQSGSVLLLQGRSNLGTGVVPAALGGAGVMALLCICLCLIFFLIVKARRKQAAGRPEKMDDEDPIMGTITSGSRKKPWPDSPGDQASPPGDAPPLEEQKELHYASLSFSEMKSREPKDQEAPSTTEYSEIKTSK

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
100	N-linked_Glycosylation	LGDVQKKNCSLSIGD CHHHHHCCCEEEECC	27.87	UniProtKB CARBOHYD
128	Phosphorylation	ERGRDVKYSYQQNKL ECCCCCCEEECCCCC	16.68	29083192
129	Phosphorylation	RGRDVKYSYQQNKLN CCCCCCEEECCCCCC	15.67	29083192
130	Phosphorylation	GRDVKYSYQQNKLNL CCCCCEEECCCCCCE	15.84	29083192
201	Phosphorylation	RSSELTLTPRPEDHG CCCEEECCCCCCCCC	16.41	24719451
210	N-linked_Glycosylation	RPEDHGTNLTCQMKR CCCCCCCCCEEEEEE	37.63	UniProtKB CARBOHYD
231	N-linked_Glycosylation	TERTVQLNVSYAPQT EEEEEEEECCCCCCE	12.00	UniProtKB CARBOHYD
253	N-linked_Glycosylation	IALEILQNTSYLPVL EEHHHHHCCCCCCEE	27.78	UniProtKB CARBOHYD
328	N-linked_Glycosylation	GFLQIFLNLSVYSLP CEEHHHHCCHHCCHH	21.37	UniProtKB CARBOHYD
375	N-linked_Glycosylation	EEKPLEGNSSQGSFK EECCCCCCCCCCCEE	29.16	UniProtKB CARBOHYD
384	N-linked_Glycosylation	SQGSFKVNSSSAGPW CCCCEEECCCCCCCC	36.44	UniProtKB CARBOHYD
393	N-linked_Glycosylation	SSAGPWANSSLILHG CCCCCCCCCEEEECC	28.41	UniProtKB CARBOHYD
485	Phosphorylation	DEDPIMGTITSGSRK CCCCCCCEECCCCCC	12.05	-
487	Phosphorylation	DPIMGTITSGSRKKP CCCCCEECCCCCCCC	27.20	-
488	Phosphorylation	PIMGTITSGSRKKPW CCCCEECCCCCCCCC	30.81	26434552
490	Phosphorylation	MGTITSGSRKKPWPD CCEECCCCCCCCCCC	40.47	25003641
520	Phosphorylation	EEQKELHYASLSFSE HHHHHHHEEEECHHH	15.54	-
522	Phosphorylation	QKELHYASLSFSEMK HHHHHEEEECHHHHH	19.85	27251275
524	Phosphorylation	ELHYASLSFSEMKSR HHHEEEECHHHHHCC	25.00	27251275
544	Phosphorylation	EAPSTTEYSEIKTSK CCCCCCCHHHHCCCC	14.98	25587033
545	Phosphorylation	APSTTEYSEIKTSK- CCCCCCHHHHCCCC-	26.98	19060867

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

Oops, there are no upstream regulatory protein records of SIGL5_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SIGL5_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
490	Phosphorylation	499 (9)	P ⇒ T;A;S	rs3829655	Cerebrospinal fluid biomarker levels	28031287

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PCH2_HUMAN	TRIP13	physical	16189514
SIGL5_HUMAN	SIGLEC5	physical	9731071
PCH2_HUMAN	TRIP13	physical	25416956
VAC14_HUMAN	VAC14	physical	25416956
LG3BP_HUMAN	LGALS3BP	physical	25320078
PTN11_HUMAN	PTPN11	physical	28514442
KLHL8_HUMAN	KLHL8	physical	28514442
CIP4_HUMAN	TRIP10	physical	28514442
INT4_HUMAN	INTS4	physical	28514442
GPN3_HUMAN	GPN3	physical	28514442
MET13_HUMAN	METTL13	physical	28514442
UFSP2_HUMAN	UFSP2	physical	28514442

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.