LUM_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LUM_HUMAN
• UniProt AC: P51884
• Protein Name: Lumican
• Gene Name: LUM
• Organism: Homo sapiens (Human).
• Sequence Length: 338
• Subcellular Localization: Secreted, extracellular space, extracellular matrix.
• Protein Sequence: MSLSAFTLFLALIGGTSGQYYDYDFPLSIYGQSSPNCAPECNCPESYPSAMYCDELKLKSVPMVPPGIKYLYLRNNQIDHIDEKAFENVTDLQWLILDHNLLENSKIKGRVFSKLKQLKKLHINHNNLTESVGPLPKSLEDLQLTHNKITKLGSFEGLVNLTFIHLQHNRLKEDAVSAAFKGLKSLEYLDLSFNQIARLPSGLPVSLLTLYLDNNKISNIPDEYFKRFNALQYLRLSHNELADSGIPGNSFNVSSLVELDLSYNKLKNIPTVNENLENYYLEVNQLEKFDIKSFCKILGPLSYSKIKHLRLDGNRISETSLPPDMYECLRVANEVTLN

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
19	Pyrrolidone_carboxylic_acid	LIGGTSGQYYDYDFP HHHCCCCCCCCCCCC	33.12	14551184
19	Pyrrolidone_carboxylic_acid	LIGGTSGQYYDYDFP HHHCCCCCCCCCCCC	33.12	14551184
19	Pyrrolidone_carboxylic_acid	LIGGTSGQYYDYDFP HHHCCCCCCCCCCCC	33.12	-
20	Sulfation	IGGTSGQYYDYDFPL HHCCCCCCCCCCCCE	11.22	-
20	Sulfation	IGGTSGQYYDYDFPL HHCCCCCCCCCCCCE	11.22	17558413
21	Sulfation	GGTSGQYYDYDFPLS HCCCCCCCCCCCCEE	10.51	-
21	Sulfation	GGTSGQYYDYDFPLS HCCCCCCCCCCCCEE	10.51	17558413
23	Sulfation	TSGQYYDYDFPLSIY CCCCCCCCCCCEEEE	11.90	-
23	Sulfation	TSGQYYDYDFPLSIY CCCCCCCCCCCEEEE	11.90	17558413
30	Sulfation	YDFPLSIYGQSSPNC CCCCEEEECCCCCCC	13.02	-
30	Sulfation	YDFPLSIYGQSSPNC CCCCEEEECCCCCCC	13.02	-
88	N-linked_Glycosylation	IDEKAFENVTDLQWL CCHHHHCCCCHHHHH	35.22	14760718
88	N-linked_Glycosylation	IDEKAFENVTDLQWL CCHHHHCCCCHHHHH	35.22	17623646
127	N-linked_Glycosylation	KLHINHNNLTESVGP HHCCCCCCCCCCCCC	40.57	17623646
127	N-linked_Glycosylation	KLHINHNNLTESVGP HHCCCCCCCCCCCCC	40.57	UniProtKB CARBOHYD
138	Phosphorylation	SVGPLPKSLEDLQLT CCCCCCCCHHHHHCC	34.74	23911959
145	Phosphorylation	SLEDLQLTHNKITKL CHHHHHCCCCCCHHC	15.50	23911959
150	Phosphorylation	QLTHNKITKLGSFEG HCCCCCCHHCCCHHH	23.09	27251275
160	N-linked_Glycosylation	GSFEGLVNLTFIHLQ CCHHHHHCCEEEECC	38.10	17623646
160	N-linked_Glycosylation	GSFEGLVNLTFIHLQ CCHHHHHCCEEEECC	38.10	14760718
177	Phosphorylation	RLKEDAVSAAFKGLK CCHHHHHHHHHHCCC	18.66	23911959
181	Acetylation	DAVSAAFKGLKSLEY HHHHHHHHCCCHHCE	59.62	7668479
192	Phosphorylation	SLEYLDLSFNQIARL HHCEEECCHHHHHCC	23.09	27251275
201	Phosphorylation	NQIARLPSGLPVSLL HHHHCCCCCCCCEEE	58.51	27251275
201	O-linked_Glycosylation	NQIARLPSGLPVSLL HHHHCCCCCCCCEEE	58.51	29351928
209	Phosphorylation	GLPVSLLTLYLDNNK CCCCEEEEEEECCCC	20.74	-
209	O-linked_Glycosylation	GLPVSLLTLYLDNNK CCCCEEEEEEECCCC	20.74	29351928
211	Phosphorylation	PVSLLTLYLDNNKIS CCEEEEEEECCCCCC	13.53	-
224	Phosphorylation	ISNIPDEYFKRFNAL CCCCCHHHHHHHHHH	23.06	-
226	Acetylation	NIPDEYFKRFNALQY CCCHHHHHHHHHHHH	56.00	27178108
233	Phosphorylation	KRFNALQYLRLSHNE HHHHHHHHHHCCCHH	8.47	-
252	N-linked_Glycosylation	GIPGNSFNVSSLVEL CCCCCCCCHHHHEEE	32.36	UniProtKB CARBOHYD
292	Acetylation	QLEKFDIKSFCKILG HHHHCCHHHHHHHHC	39.05	27178108
293	Phosphorylation	LEKFDIKSFCKILGP HHHCCHHHHHHHHCC	35.89	30631047
302	Phosphorylation	CKILGPLSYSKIKHL HHHHCCCCHHHCEEE	30.41	24719451
304	Phosphorylation	ILGPLSYSKIKHLRL HHCCCCHHHCEEEEE	25.24	30631047
320	O-linked_Glycosylation	GNRISETSLPPDMYE CCCCCCCCCCCHHHH	34.52	OGP
320	Phosphorylation	GNRISETSLPPDMYE CCCCCCCCCCCHHHH	34.52	27251275

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LUM_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 LUM_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
LRC40_HUMAN	LRRC40	physical	28514442
THUM1_HUMAN	THUMPD1	physical	28514442
PTN11_HUMAN	PTPN11	physical	28514442
RHOA_HUMAN	RHOA	physical	28514442
CGL_HUMAN	CTH	physical	28514442
RSRC1_HUMAN	RSRC1	physical	27173435

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

"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-88; ASN-127; ASN-160 ANDASN-252, AND MASS SPECTROMETRY.
PubMed: 19159218

"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-88; ASN-127; ASN-160 ANDASN-252, AND MASS SPECTROMETRY.
PubMed: 16335952

"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Proteomics 4:454-465(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-88 AND ASN-160, AND MASSSPECTROMETRY.
PubMed: 14760718