dbPTM

CH3L1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CH3L1_HUMAN
UniProt AC	P36222
Protein Name	Chitinase-3-like protein 1
Gene Name	CHI3L1
Organism	Homo sapiens (Human).
Sequence Length	383
Subcellular Localization	Secreted, extracellular space . Cytoplasm. Cytoplasm, perinuclear region. Endoplasmic reticulum.
Protein Description	Carbohydrate-binding lectin with a preference for chitin. Has no chitinase activity. May play a role in tissue remodeling and in the capacity of cells to respond to and cope with changes in their environment. Plays a role in T-helper cell type 2 (Th2) inflammatory response and IL-13-induced inflammation, regulating allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation and M2 macrophage differentiation. Facilitates invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. Mediates activation of AKT1 signaling pathway and subsequent IL8 production in colonic epithelial cells. Regulates antibacterial responses in lung by contributing to macrophage bacterial killing, controlling bacterial dissemination and augmenting host tolerance. Also regulates hyperoxia-induced injury, inflammation and epithelial apoptosis in lung..
Protein Sequence	MGVKASQTGFVVLVLLQCCSAYKLVCYYTSWSQYREGDGSCFPDALDRFLCTHIIYSFANISNDHIDTWEWNDVTLYGMLNTLKNRNPNLKTLLSVGGWNFGSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGRRDKQHFTTLIKEMKAEFIKEAQPGKKQLLLSAALSAGKVTIDSSYDIAKISQHLDFISIMTYDFHGAWRGTTGHHSPLFRGQEDASPDRFSNTDYAVGYMLRLGAPASKLVMGIPTFGRSFTLASSETGVGAPISGPGIPGRFTKEAGTLAYYEICDFLRGATVHRILGQQVPYATKGNQWVGYDDQESVKSKVQYLKDRQLAGAMVWALDLDDFQGSFCGQDLRFPLTNAIKDALAAT

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
60	N-linked_Glycosylation	HIIYSFANISNDHID HHHHHHHCCCCCCCC	35.89	12775711
113	Phosphorylation	FSKIASNTQSRRTFI HHHHHCCCCHHHHHH	25.98	28509920
115	Phosphorylation	KIASNTQSRRTFIKS HHHCCCCHHHHHHHH	22.99	28509920
175	Phosphorylation	GKKQLLLSAALSAGK CHHHHHHHHHHHCCC	16.09	29396449
179	Phosphorylation	LLLSAALSAGKVTID HHHHHHHHCCCEEEC	30.19	26437602
184	Phosphorylation	ALSAGKVTIDSSYDI HHHCCCEEECCCCCH	23.66	22167270
187	Phosphorylation	AGKVTIDSSYDIAKI CCCEEECCCCCHHHH	27.26	22167270
188	Phosphorylation	GKVTIDSSYDIAKIS CCEEECCCCCHHHHH	24.07	22167270
189	Phosphorylation	KVTIDSSYDIAKISQ CEEECCCCCHHHHHH	18.47	22167270
235	Phosphorylation	DASPDRFSNTDYAVG CCCCCCCCCCHHHHH	39.45	30206219
237	Phosphorylation	SPDRFSNTDYAVGYM CCCCCCCCHHHHHHH	29.23	30206219
239	Phosphorylation	DRFSNTDYAVGYMLR CCCCCCHHHHHHHHH	10.93	29116813
243	Phosphorylation	NTDYAVGYMLRLGAP CCHHHHHHHHHCCCC	6.08	29116813
252	Phosphorylation	LRLGAPASKLVMGIP HHCCCCHHHHHCCCC	26.01	21964256
269	Phosphorylation	GRSFTLASSETGVGA CCCEEECCCCCCCCC	31.64	28348404
270	Phosphorylation	RSFTLASSETGVGAP CCEEECCCCCCCCCC	33.30	28348404
272	Phosphorylation	FTLASSETGVGAPIS EEECCCCCCCCCCCC	38.83	28348404
321	Acetylation	QQVPYATKGNQWVGY CCCCCCCCCCCCCCC	47.93	10721027
335	Acetylation	YDDQESVKSKVQYLK CCCHHHHHHHHHHHH	54.56	10721035
342	Acetylation	KSKVQYLKDRQLAGA HHHHHHHHHHHHHHH	46.03	10721031
383	Phosphorylation	IKDALAAT------- HHHHHHCC-------	33.27	-

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 CH3L1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CH3L1_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 CH3L1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
CALR_HUMAN	CALR	physical	28514442
HSP7C_HUMAN	HSPA8	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
611960	Asthma-related traits 7 (ASRT7)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CH3L1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Structure and ligand-induced conformational change of the 39-kDaglycoprotein from human articular chondrocytes."; Houston D.R., Recklies A.D., Krupa J.C., van Aalten D.M.F.; J. Biol. Chem. 278:30206-30212(2003). Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 22-383 IN COMPLEX WITHCHITIN OLIGOMERS, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-60.	12775711 [Abstract]