LAMC2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LAMC2_HUMAN
• UniProt AC: Q13753
• Protein Name: Laminin subunit gamma-2
• Gene Name: LAMC2
• Organism: Homo sapiens (Human).
• Sequence Length: 1193
• Subcellular Localization: Secreted, extracellular space, extracellular matrix, basement membrane. Major component.
• Protein Description: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Ladsin exerts cell-scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells..
• Protein Sequence: MPALWLGCCLCFSLLLPAARATSRREVCDCNGKSRQCIFDRELHRQTGNGFRCLNCNDNTDGIHCEKCKNGFYRHRERDRCLPCNCNSKGSLSARCDNSGRCSCKPGVTGARCDRCLPGFHMLTDAGCTQDQRLLDSKCDCDPAGIAGPCDAGRCVCKPAVTGERCDRCRSGYYNLDGGNPEGCTQCFCYGHSASCRSSAEYSVHKITSTFHQDVDGWKAVQRNGSPAKLQWSQRHQDVFSSAQRLDPVYFVAPAKFLGNQQVSYGQSLSFDYRVDRGGRHPSAHDVILEGAGLRITAPLMPLGKTLPCGLTKTYTFRLNEHPSNNWSPQLSYFEYRRLLRNLTALRIRATYGEYSTGYIDNVTLISARPVSGAPAPWVEQCICPVGYKGQFCQDCASGYKRDSARLGPFGTCIPCNCQGGGACDPDTGDCYSGDENPDIECADCPIGFYNDPHDPRSCKPCPCHNGFSCSVMPETEEVVCNNCPPGVTGARCELCADGYFGDPFGEHGPVRPCQPCQCNNNVDPSASGNCDRLTGRCLKCIHNTAGIYCDQCKAGYFGDPLAPNPADKCRACNCNPMGSEPVGCRSDGTCVCKPGFGGPNCEHGAFSCPACYNQVKIQMDQFMQQLQRMEALISKAQGGDGVVPDTELEGRMQQAEQALQDILRDAQISEGASRSLGLQLAKVRSQENSYQSRLDDLKMTVERVRALGSQYQNRVRDTHRLITQMQLSLAESEASLGNTNIPASDHYVGPNGFKSLAQEATRLAESHVESASNMEQLTRETEDYSKQALSLVRKALHEGVGSGSGSPDGAVVQGLVEKLEKTKSLAQQLTREATQAEIEADRSYQHSLRLLDSVSRLQGVSDQSFQVEEAKRIKQKADSLSSLVTRHMDEFKRTQKNLGNWKEEAQQLLQNGKSGREKSDQLLSRANLAKSRAQEALSMGNATFYEVESILKNLREFDLQVDNRKAEAEEAMKRLSYISQKVSDASDKTQQAERALGSAAADAQRAKNGAGEALEISSEIEQEIGSLNLEANVTADGALAMEKGLASLKSEMREVEGELERKELEFDTNMDAVQMVITEAQKVDTRAKNAGVTIQDTLNTLDGLLHLMDQPLSVDEEGLVLLEQKLSRAKTQINSQLRPMMSELEERARQQRGHLHLLETSIDGILADVKNLENIRDNLPPGCYNTQALEQQ

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
250	Phosphorylation	AQRLDPVYFVAPAKF HCCCCCEEEEEEHHH	9.57	22817900
265	Phosphorylation	LGNQQVSYGQSLSFD HCCCCCCCCCCCEEE	21.96	22817900
273	Phosphorylation	GQSLSFDYRVDRGGR CCCCEEEEEECCCCC	15.55	22817900
297	Phosphorylation	EGAGLRITAPLMPLG CCCCCEEECCEECCC	18.78	29083192
342	N-linked_Glycosylation	EYRRLLRNLTALRIR HHHHHHHHHHHHHHH	41.53	UniProtKB CARBOHYD
344	Phosphorylation	RRLLRNLTALRIRAT HHHHHHHHHHHHHHH	27.48	24719451
362	N-linked_Glycosylation	YSTGYIDNVTLISAR CCCCEEECEEEEEEE	21.08	UniProtKB CARBOHYD
578	Sulfoxidation	RACNCNPMGSEPVGC CCCCCCCCCCCCCCC	6.00	28465586
636 (in isoform 2)	Ubiquitination	-	37.42	21906983
636 (in isoform 1)	Ubiquitination	-	37.42	21906983
636	Ubiquitination	RMEALISKAQGGDGV HHHHHHHHHHCCCCC	37.42	22817900
686	Phosphorylation	LQLAKVRSQENSYQS HHHHHHHHCCCCHHH	44.85	23898821
690	Phosphorylation	KVRSQENSYQSRLDD HHHHCCCCHHHHHHH	24.64	23898821
762	O-linked_Glycosylation	KSLAQEATRLAESHV HHHHHHHHHHHHHHH	26.01	55831393
762	Phosphorylation	KSLAQEATRLAESHV HHHHHHHHHHHHHHH	26.01	-
767	Phosphorylation	EATRLAESHVESASN HHHHHHHHHHHHHHC	27.50	-
771	Phosphorylation	LAESHVESASNMEQL HHHHHHHHHHCHHHH	35.59	-
773	Phosphorylation	ESHVESASNMEQLTR HHHHHHHHCHHHHHH	46.09	-
779	Phosphorylation	ASNMEQLTRETEDYS HHCHHHHHHHCHHHH	26.59	-
787	Acetylation	RETEDYSKQALSLVR HHCHHHHHHHHHHHH	33.10	7974711
791	Phosphorylation	DYSKQALSLVRKALH HHHHHHHHHHHHHHH	28.03	24719451
803	Phosphorylation	ALHEGVGSGSGSPDG HHHCCCCCCCCCCCH	27.64	26091039
805	Phosphorylation	HEGVGSGSGSPDGAV HCCCCCCCCCCCHHH	37.48	26091039
807	Phosphorylation	GVGSGSGSPDGAVVQ CCCCCCCCCCHHHHH	22.86	26091039
819	Malonylation	VVQGLVEKLEKTKSL HHHHHHHHHHHHHHH	55.24	26320211
819	Acetylation	VVQGLVEKLEKTKSL HHHHHHHHHHHHHHH	55.24	178226349
831	O-linked_Glycosylation	KSLAQQLTREATQAE HHHHHHHHHHHHHHH	23.33	73397645
886	O-linked_Glycosylation	DSLSSLVTRHMDEFK HHHHHHHHHCHHHHH	21.83	55825213
925	Phosphorylation	EKSDQLLSRANLAKS HHHHHHHHHHHHHHH	37.63	29888752
932	Phosphorylation	SRANLAKSRAQEALS HHHHHHHHHHHHHHH	27.52	28102081
942	N-linked_Glycosylation	QEALSMGNATFYEVE HHHHHCCCCCHHHHH	27.45	UniProtKB CARBOHYD
950	Phosphorylation	ATFYEVESILKNLRE CCHHHHHHHHHHHHH	38.09	24719451
977	Phosphorylation	EEAMKRLSYISQKVS HHHHHHHHHHHHHHC	25.18	22817900
987	Phosphorylation	SQKVSDASDKTQQAE HHHHCCCCHHHHHHH	44.63	22817900
999	Phosphorylation	QAERALGSAAADAQR HHHHHHHHHHHHHHH	18.65	28355574
1033	N-linked_Glycosylation	GSLNLEANVTADGAL CCCCEEEEEEHHHHH	23.46	UniProtKB CARBOHYD

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

Oops, there are no upstream regulatory protein records of LAMC2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LAMC2_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 LAMC2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SLAP2_HUMAN	SLA2	physical	17353186
TYY1_HUMAN	YY1	physical	16624538

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 226700: Epidermolysis bullosa, junctional, Herlitz type (H-JEB)
• 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

Phosphorylation

"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-250; TYR-265 ANDTYR-273, AND MASS SPECTROMETRY.
PubMed: 18083107