CHIT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CHIT1_HUMAN
• UniProt AC: Q13231
• Protein Name: Chitotriosidase-1
• Gene Name: CHIT1
• Organism: Homo sapiens (Human).
• Sequence Length: 466
• Subcellular Localization: Secreted. Lysosome. A small proportion is lysosomal.
• Protein Description: Degrades chitin, chitotriose and chitobiose. May participate in the defense against nematodes and other pathogens. Isoform 3 has no enzymatic activity..
• Protein Sequence: MVRSVAWAGFMVLLMIPWGSAAKLVCYFTNWAQYRQGEARFLPKDLDPSLCTHLIYAFAGMTNHQLSTTEWNDETLYQEFNGLKKMNPKLKTLLAIGGWNFGTQKFTDMVATANNRQTFVNSAIRFLRKYSFDGLDLDWEYPGSQGSPAVDKERFTTLVQDLANAFQQEAQTSGKERLLLSAAVPAGQTYVDAGYEVDKIAQNLDFVNLMAYDFHGSWEKVTGHNSPLYKRQEESGAAASLNVDAAVQQWLQKGTPASKLILGMPTYGRSFTLASSSDTRVGAPATGSGTPGPFTKEGGMLAYYEVCSWKGATKQRIQDQKVPYIFRDNQWVGFDDVESFKTKVSYLKQKGLGGAMVWALDLDDFAGFSCNQGRYPLIQTLRQELSLPYLPSGTPELEVPKPGQPSEPEHGPSPGQDTFCQGKADGLYPNPRERSSFYSCAAGRLFQQSCPTGLVFSNSCKCCTWN

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
27	Phosphorylation	SAAKLVCYFTNWAQY CHHHHHHHHCCHHHH	13.12	29083192
29	Phosphorylation	AKLVCYFTNWAQYRQ HHHHHHHCCHHHHHC	11.90	29083192
100	N-linked_Glycosylation	LLAIGGWNFGTQKFT HHHCCCCCCCCCHHH	28.83	19725875
122	Phosphorylation	NRQTFVNSAIRFLRK CHHHHHHHHHHHHHH	21.55	-
255	Phosphorylation	QQWLQKGTPASKLIL HHHHHHCCCHHHHHC	23.79	28270605
258	Phosphorylation	LQKGTPASKLILGMP HHHCCCHHHHHCCCC	29.24	28270605
266	Phosphorylation	KLILGMPTYGRSFTL HHHCCCCCCCCCEEE	29.71	28270605
267	Phosphorylation	LILGMPTYGRSFTLA HHCCCCCCCCCEEEC	12.50	28270605
270	Phosphorylation	GMPTYGRSFTLASSS CCCCCCCCEEECCCC	20.44	22210691
272	Phosphorylation	PTYGRSFTLASSSDT CCCCCCEEECCCCCC	23.74	28270605
275	Phosphorylation	GRSFTLASSSDTRVG CCCEEECCCCCCEEC	33.22	28270605
276	Phosphorylation	RSFTLASSSDTRVGA CCEEECCCCCCEECC	26.99	28270605
277	Phosphorylation	SFTLASSSDTRVGAP CEEECCCCCCEECCC	40.27	28270605
279	Phosphorylation	TLASSSDTRVGAPAT EECCCCCCEECCCCC	29.24	28270605
392	O-linked_Glycosylation	LSLPYLPSGTPELEV HCCCCCCCCCCCCCC	53.34	OGP

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

Oops, there are no upstream regulatory protein records of CHIT1_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CHIT1_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 CHIT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VHL_HUMAN	VHL	physical	28514442
RMD1_HUMAN	RMDN1	physical	28514442
RL11_HUMAN	RPL11	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.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Common G102S polymorphism in chitotriosidase differentially affectsactivity towards 4-methylumbelliferyl substrates.";
Bussink A.P., Verhoek M., Vreede J., Ghauharali-van der Vlugt K.,Donker-Koopman W.E., Sprenger R.R., Hollak C.E., Aerts J.M.,Boot R.G.;
FEBS J. 276:5678-5688(2009).
Cited for: CHARACTERIZATION OF VARIANT SER-102, SUBCELLULAR LOCATION, CATALYTICACTIVITY, AND GLYCOSYLATION AT ASN-100.
PubMed: 19725875