MMP23_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MMP23_HUMAN
• UniProt AC: O75900
• Protein Name: Matrix metalloproteinase-23
• Gene Name: MMP23A
• Organism: Homo sapiens (Human).
• Sequence Length: 390
• Subcellular Localization: Endoplasmic reticulum membrane; Single-pass type II membrane protein. Membrane ; Single-pass type II membrane protein . A secreted form produced by proteolytic cleavage may also exist.
• Protein Description: Protease. May regulate the surface expression of some potassium channels by retaining them in the endoplasmic reticulum (By similarity)..
• Protein Sequence: MGRGARVPSEAPGAGVERRWLGAALVALCLLPALVLLARLGAPAVPAWSAAQGDVAALGLSAVPPTRVPGPLAPRRRRYTLTPARLRWDHFNLTYRILSFPRNLLSPRETRRALAAAFRMWSDVSPFSFREVAPEQPSDLRIGFYPINHTDCLVSALHHCFDGPTGELAHAFFPPHGGIHFDDSEYWVLGPTRYSWKKGVWLTDLVHVAAHEIGHALGLMHSQHGRALMHLNATLRGWKALSQDELWGLHRLYGCLDRLFVCASWARRGFCDARRRLMKRLCPSSCDFCYEFPFPTVATTPPPPRTKTRLVPEGRNVTFRCGQKILHKKGKVYWYKDQEPLEFSYPGYLALGEAHLSIIANAVNEGTYTCVVRRQQRVLTTYSWRVRVRG

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
79	Phosphorylation	LAPRRRRYTLTPARL CCCCCCCEEECCCHH	12.32	24043423
80	Phosphorylation	APRRRRYTLTPARLR CCCCCCEEECCCHHC	23.50	24043423
82	Phosphorylation	RRRRYTLTPARLRWD CCCCEEECCCHHCCC	13.70	24043423
92	N-linked_Glycosylation	RLRWDHFNLTYRILS HHCCCCCCCHHHHHH	28.22	UniProtKB CARBOHYD
95	Phosphorylation	WDHFNLTYRILSFPR CCCCCCHHHHHHCCH	9.98	-
99	Phosphorylation	NLTYRILSFPRNLLS CCHHHHHHCCHHCCC	30.73	24719451
106	Phosphorylation	SFPRNLLSPRETRRA HCCHHCCCHHHHHHH	25.69	18669648
128	Phosphorylation	WSDVSPFSFREVAPE HHCCCCCCHHHCCCC	27.12	24719451
138	Phosphorylation	EVAPEQPSDLRIGFY HCCCCCCCCCEEEEE	49.31	22817900
148	N-linked_Glycosylation	RIGFYPINHTDCLVS EEEEEECCHHHHHHH	27.74	UniProtKB CARBOHYD
232	N-linked_Glycosylation	GRALMHLNATLRGWK HHHHHHHHHHHHHHH	19.05	UniProtKB CARBOHYD
285	Phosphorylation	MKRLCPSSCDFCYEF HHHHCCCCCCCCEEC	11.66	23879269
299	Phosphorylation	FPFPTVATTPPPPRT CCCCCCCCCCCCCCC	35.18	23879269
300	Phosphorylation	PFPTVATTPPPPRTK CCCCCCCCCCCCCCC	24.86	23879269
316	N-linked_Glycosylation	RLVPEGRNVTFRCGQ EECCCCCCEEEECCC	48.30	UniProtKB CARBOHYD
318	Phosphorylation	VPEGRNVTFRCGQKI CCCCCCEEEECCCEE	14.65	24719451
328	Acetylation	CGQKILHKKGKVYWY CCCEEEEECCCEEEE	60.83	21466224
329	Acetylation	GQKILHKKGKVYWYK CCEEEEECCCEEEEC	53.90	21466224
331	Acetylation	KILHKKGKVYWYKDQ EEEEECCCEEEECCC	40.82	21466224
336	Acetylation	KGKVYWYKDQEPLEF CCCEEEECCCCCCCC	38.50	7339507

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

Oops, there are no upstream regulatory protein records of MMP23_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MMP23_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 MMP23_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of MMP23_HUMAN !!

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

Phosphorylation

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND MASSSPECTROMETRY.
PubMed: 18669648