MMP9_HUMAN - dbPTM
MMP9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MMP9_HUMAN
UniProt AC P14780
Protein Name Matrix metalloproteinase-9
Gene Name MMP9
Organism Homo sapiens (Human).
Sequence Length 707
Subcellular Localization Secreted, extracellular space, extracellular matrix .
Protein Description May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide..
Protein Sequence MSLWQPLVLVLLVLGCCFAAPRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEMRGESKSLGPALLLLQKQLSLPETGELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTQDGNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGGNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTTPQPTAPPTVCPTGPPTVHPSERPTAGPTGPPSAGPTGPPTAGPSTATTVPLSPVDDACNVNIFDAIAEIGNQLYLFKDGKYWRFSEGRGSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGASVLGPRRLDKLGLGADVAQVTGALRSGRGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLDTHDVFQYREKAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQCPED
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 Orthologous
Protein Cluster
2Phosphorylation------MSLWQPLVL
------CCCHHHHHH
38.0124043423
26PhosphorylationAAPRQRQSTLVLFPG
HCHHHCCCEEEECCC
26.3729083192
27PhosphorylationAPRQRQSTLVLFPGD
CHHHCCCEEEECCCC
16.7329083192
37PhosphorylationLFPGDLRTNLTDRQL
ECCCCHHCCCCCHHH
41.7124719451
38N-linked_GlycosylationFPGDLRTNLTDRQLA
CCCCHHCCCCCHHHH
34.21UniProtKB CARBOHYD
48PhosphorylationDRQLAEEYLYRYGYT
CHHHHHHHHHHHCCC
10.6724043423
50PhosphorylationQLAEEYLYRYGYTRV
HHHHHHHHHHCCCCH
10.8224043423
99S-nitrosocysteineKAMRTPRCGVPDLGR
HHHCCCCCCCCCCCC
7.30-
99S-nitrosylationKAMRTPRCGVPDLGR
HHHCCCCCCCCCCCC
7.3022178444
120N-linked_GlycosylationDLKWHHHNITYWIQN
CEEEEECCHHHHHHC
24.76UniProtKB CARBOHYD
127N-linked_GlycosylationNITYWIQNYSEDLPR
CHHHHHHCCCCCCCH
32.91UniProtKB CARBOHYD
241PhosphorylationFIFEGRSYSACTTDG
EEECCCCEEEECCCC
10.03-
262NitrationWCSTTANYDTDDRFG
CCCCCCCCCCCCCCC
20.11-
576PhosphorylationSVFEERLSKKLFFFS
HHHHHHHHCCEEEEC
33.6823909892
583PhosphorylationSKKLFFFSGRQVWVY
HCCEEEECCCEEEEE
28.1023909892
628PhosphorylationRGKMLLFSGRRLWRF
CCEEEEEECCEEEEE
31.2124719451
686PhosphorylationYWRVSSRSELNQVDQ
EEEECCHHHHCCCCC
48.6722210691
696PhosphorylationNQVDQVGYVTYDILQ
CCCCCCEEEEEEHHC
7.2622210691
698PhosphorylationVDQVGYVTYDILQCP
CCCCEEEEEEHHCCC
13.6422210691

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 MMP9_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MMP9_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 MMP9_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CXCL5_HUMANCXCL5physical
12950257
CXCL6_HUMANCXCL6physical
12950257
TGFB1_HUMANTGFB1physical
10652271
TSP1_HUMANTHBS1physical
10900205
TSP2_HUMANTHBS2physical
10900205
CLUS_HUMANCLUphysical
26716898
COCA1_HUMANCOL12A1physical
28514442
TIMP1_HUMANTIMP1physical
28514442
CO2A1_HUMANCOL2A1physical
28514442
COEA1_HUMANCOL14A1physical
28514442
CO5A1_HUMANCOL5A1physical
28514442
CO6A2_HUMANCOL6A2physical
28514442
CO4A1_HUMANCOL4A1physical
28514442
FINC_HUMANFN1physical
28514442
CO4A2_HUMANCOL4A2physical
28514442
CO6A1_HUMANCOL6A1physical
28514442
COIA1_HUMANCOL18A1physical
28514442
SCAR3_HUMANSCARA3physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
603932Intervertebral disc disease (IDD)
613073Metaphyseal anadysplasia 2 (MANDP2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MMP9_HUMAN

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Related Literatures of Post-Translational Modification

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