SIG10_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SIG10_HUMAN
• UniProt AC: Q96LC7
• Protein Name: Sialic acid-binding Ig-like lectin 10
• Gene Name: SIGLEC10
• Organism: Homo sapiens (Human).
• Sequence Length: 697
• Subcellular Localization: Isoform 1: Cell membrane; Single-pass type I membrane protein.; Isoform 2: Cell membrane; Single-pass type I membrane protein.; Isoform 3: Cell membrane; Single-pass type I membrane protein.; Isoform 4: Cell 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- or alpha-2,6-linked sialic acid (By similarity). The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, seems to 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. [PubMed: 11284738]
• Protein Sequence: MLLPLLLSSLLGGSQAMDGRFWIRVQESVMVPEGLCISVPCSFSYPRQDWTGSTPAYGYWFKAVTETTKGAPVATNHQSREVEMSTRGRFQLTGDPAKGNCSLVIRDAQMQDESQYFFRVERGSYVRYNFMNDGFFLKVTALTQKPDVYIPETLEPGQPVTVICVFNWAFEECPPPSFSWTGAALSSQGTKPTTSHFSVLSFTPRPQDHNTDLTCHVDFSRKGVSAQRTVRLRVAYAPRDLVISISRDNTPALEPQPQGNVPYLEAQKGQFLRLLCAADSQPPATLSWVLQNRVLSSSHPWGPRPLGLELPGVKAGDSGRYTCRAENRLGSQQRALDLSVQYPPENLRVMVSQANRTVLENLGNGTSLPVLEGQSLCLVCVTHSSPPARLSWTQRGQVLSPSQPSDPGVLELPRVQVEHEGEFTCHARHPLGSQHVSLSLSVHYSPKLLGPSCSWEAEGLHCSCSSQASPAPSLRWWLGEELLEGNSSQDSFEVTPSSAGPWANSSLSLHGGLSSGLRLRCEAWNVHGAQSGSILQLPDKKGLISTAFSNGAFLGIGITALLFLCLALIIMKILPKRRTQTETPRPRFSRHSTILDYINVVPTAGPLAQKRNQKATPNSPRTPLPPGAPSPESKKNQKKQYQLPSFPEPKSSTQAPESQESQEELHYATLNFPGVRPRPEARMPKGTQADYAEVKFQ

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
8	Phosphorylation	MLLPLLLSSLLGGSQ CCHHHHHHHHHCCCC	20.93	24043423
9	Phosphorylation	LLPLLLSSLLGGSQA CHHHHHHHHHCCCCC	27.81	24043423
14	Phosphorylation	LSSLLGGSQAMDGRF HHHHHCCCCCCCCCE	16.99	24043423
38	Phosphorylation	VPEGLCISVPCSFSY ECCCEEEEEECCCCC	21.00	-
57	Phosphorylation	WTGSTPAYGYWFKAV CCCCCCCCEEEEEEE	16.38	-
100	N-linked_Glycosylation	TGDPAKGNCSLVIRD CCCCCCCCEEEEEEE	16.11	UniProtKB CARBOHYD
250	Phosphorylation	ISISRDNTPALEPQP EEEECCCCCCCCCCC	17.77	-
298	Phosphorylation	QNRVLSSSHPWGPRP HCCHHCCCCCCCCCC	30.14	18767875
322	Phosphorylation	AGDSGRYTCRAENRL CCCCCCEEECCCCCC	8.31	-
331	Phosphorylation	RAENRLGSQQRALDL CCCCCCCCCCEEEEE	27.94	-
339	Phosphorylation	QQRALDLSVQYPPEN CCEEEEEECCCCCCH	13.57	-
355	N-linked_Glycosylation	RVMVSQANRTVLENL EEEEEHHCCHHHHHC	32.30	UniProtKB CARBOHYD
364	N-linked_Glycosylation	TVLENLGNGTSLPVL HHHHHCCCCCCCCEE	54.45	UniProtKB CARBOHYD
486	N-linked_Glycosylation	GEELLEGNSSQDSFE CHHHHCCCCCCCCEE	29.16	UniProtKB CARBOHYD
495	Phosphorylation	SQDSFEVTPSSAGPW CCCCEEECCCCCCCC	15.40	22210691
504	N-linked_Glycosylation	SSAGPWANSSLSLHG CCCCCCCCCCEEECC	28.41	UniProtKB CARBOHYD
506	Phosphorylation	AGPWANSSLSLHGGL CCCCCCCCEEECCCC	23.06	22210691
508	Phosphorylation	PWANSSLSLHGGLSS CCCCCCEEECCCCCC	21.92	22210691
589	Phosphorylation	ETPRPRFSRHSTILD CCCCCCCCCCCCHHH	30.29	28857561
592	Phosphorylation	RPRFSRHSTILDYIN CCCCCCCCCHHHHHE	18.94	28857561
593	Phosphorylation	PRFSRHSTILDYINV CCCCCCCCHHHHHEE	21.31	26657352
597	Phosphorylation	RHSTILDYINVVPTA CCCCHHHHHEECCCC	7.31	28857561
630	Phosphorylation	PLPPGAPSPESKKNQ CCCCCCCCHHHHHCC	40.54	28857561
641	Phosphorylation	KKNQKKQYQLPSFPE HHCCCCCCCCCCCCC	22.39	28674151
645	Phosphorylation	KKQYQLPSFPEPKSS CCCCCCCCCCCCCCC	63.12	25159151
667	Phosphorylation	ESQEELHYATLNFPG HHHHHHHHEECCCCC	17.57	12163025
691	Phosphorylation	PKGTQADYAEVKFQ- CCCCCCCCEECCCC-	14.00	22817900

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
597	Y	Phosphorylation	Kinase	ITK	Q08881	PSP
597	Y	Phosphorylation	Kinase	JAK3	P52333	PSP
597	Y	Phosphorylation	Kinase	LCK	P06239	PSP
667	Y	Phosphorylation	Kinase	FYN	P06241	PSP
667	Y	Phosphorylation	Kinase	ITK	Q08881	PSP
667	Y	Phosphorylation	Kinase	JAK3	P52333	PSP
667	Y	Phosphorylation	Kinase	LCK	P06239	PSP
691	Y	Phosphorylation	Kinase	JAK3	P52333	PSP
691	Y	Phosphorylation	Kinase	LCK	P06239	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SIG10_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 SIG10_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LG3BP_HUMAN	LGALS3BP	physical	25320078
PTH2_HUMAN	PTRH2	physical	28514442
T132A_HUMAN	TMEM132A	physical	28514442
GRP78_HUMAN	HSPA5	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.