MASP1_HUMAN - dbPTM
MASP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MASP1_HUMAN
UniProt AC P48740
Protein Name Mannan-binding lectin serine protease 1
Gene Name MASP1
Organism Homo sapiens (Human).
Sequence Length 699
Subcellular Localization Secreted .
Protein Description Functions in the lectin pathway of complement, which performs a key role in innate immunity by recognizing pathogens through patterns of sugar moieties and neutralizing them. The lectin pathway is triggered upon binding of mannan-binding lectin (MBL) and ficolins to sugar moieties which leads to activation of the associated proteases MASP1 and MASP2. Functions as an endopeptidase and may activate MASP2 or C2 or directly activate C3 the key component of complement reaction. Isoform 2 may have an inhibitory effect on the activation of the lectin pathway of complement or may cleave IGFBP5. Also plays a role in development. [PubMed: 21258343]
Protein Sequence MRWLLLYYALCFSLSKASAHTVELNNMFGQIQSPGYPDSYPSDSEVTWNITVPDGFRIKLYFMHFNLESSYLCEYDYVKVETEDQVLATFCGRETTDTEQTPGQEVVLSPGSFMSITFRSDFSNEERFTGFDAHYMAVDVDECKEREDEELSCDHYCHNYIGGYYCSCRFGYILHTDNRTCRVECSDNLFTQRTGVITSPDFPNPYPKSSECLYTIELEEGFMVNLQFEDIFDIEDHPEVPCPYDYIKIKVGPKVLGPFCGEKAPEPISTQSHSVLILFHSDNSGENRGWRLSYRAAGNECPELQPPVHGKIEPSQAKYFFKDQVLVSCDTGYKVLKDNVEMDTFQIECLKDGTWSNKIPTCKIVDCRAPGELEHGLITFSTRNNLTTYKSEIKYSCQEPYYKMLNNNTGIYTCSAQGVWMNKVLGRSLPTCLPVCGLPKFSRKLMARIFNGRPAQKGTTPWIAMLSHLNGQPFCGGSLLGSSWIVTAAHCLHQSLDPEDPTLRDSDLLSPSDFKIILGKHWRLRSDENEQHLGVKHTTLHPQYDPNTFENDVALVELLESPVLNAFVMPICLPEGPQQEGAMVIVSGWGKQFLQRFPETLMEIEIPIVDHSTCQKAYAPLKKKVTRDMICAGEKEGGKDACAGDSGGPMVTLNRERGQWYLVGTVSWGDDCGKKDRYGVYSYIHHNKDWIQRVTGVRN
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
49N-linked_GlycosylationSDSEVTWNITVPDGF
CCCCCEEEEECCCCE		15.6416335952
61PhosphorylationDGFRIKLYFMHFNLE
CCEEEEEEEEECCCC		8.2125072903
69PhosphorylationFMHFNLESSYLCEYD
EEECCCCCCEEEECC		27.7025072903
70PhosphorylationMHFNLESSYLCEYDY
EECCCCCCEEEECCE		16.8525072903
71PhosphorylationHFNLESSYLCEYDYV
ECCCCCCEEEECCEE		25.3425072903
75PhosphorylationESSYLCEYDYVKVET
CCCEEEECCEEEEEC		16.1625072903
77PhosphorylationSYLCEYDYVKVETED
CEEEECCEEEEECHH		10.9825072903
82PhosphorylationYDYVKVETEDQVLAT
CCEEEEECHHEEEEE		48.0925072903
89PhosphorylationTEDQVLATFCGRETT
CHHEEEEECCCCCCC		18.4625072903
96PhosphorylationTFCGRETTDTEQTPG
ECCCCCCCCCCCCCC		35.8522210691
115PhosphorylationLSPGSFMSITFRSDF
ECCCCEEEEEECCCC		19.2322210691
117PhosphorylationPGSFMSITFRSDFSN
CCCEEEEEECCCCCC		12.9922210691
123PhosphorylationITFRSDFSNEERFTG
EEECCCCCCCCCCCC		48.6124505115
129PhosphorylationFSNEERFTGFDAHYM
CCCCCCCCCCCEEEE		43.0628060719
135PhosphorylationFTGFDAHYMAVDVDE
CCCCCEEEEEECHHH		6.6228060719
159HydroxylationSCDHYCHNYIGGYYC
CCCCCCHHHHCCCEE		26.93-
178N-linked_GlycosylationGYILHTDNRTCRVEC
EEEEECCCCEEEEEE		42.1718596036
178N-linked_GlycosylationGYILHTDNRTCRVEC
EEEEECCCCEEEEEE		42.1716335952
371 (in isoform 3)Phosphorylation-51.6528270605
375 (in isoform 3)Phosphorylation-49.3227130503
379 (in isoform 3)Phosphorylation-19.3128270605
385N-linked_GlycosylationITFSTRNNLTTYKSE
EEEECCCCCCEEHHH		35.1616335952
387PhosphorylationFSTRNNLTTYKSEIK
EECCCCCCEEHHHEE		30.1529523821
388PhosphorylationSTRNNLTTYKSEIKY
ECCCCCCEEHHHEEE		31.9229523821
389PhosphorylationTRNNLTTYKSEIKYS
CCCCCCEEHHHEEEE		13.7929523821
391PhosphorylationNNLTTYKSEIKYSCQ
CCCCEEHHHEEEECC		33.8529523821
394 (in isoform 4)Phosphorylation-27.3627273156
395PhosphorylationTYKSEIKYSCQEPYY
EEHHHEEEECCCCHH		21.9725884760
401PhosphorylationKYSCQEPYYKMLNNN
EEECCCCHHHHHCCC		18.2425884760
407N-linked_GlycosylationPYYKMLNNNTGIYTC
CHHHHHCCCCCEEEE		43.4016335952
409PhosphorylationYKMLNNNTGIYTCSA
HHHHCCCCCEEEECC		27.38-
413PhosphorylationNNNTGIYTCSAQGVW
CCCCCEEEECCCCEE		9.69-
422 (in isoform 4)Phosphorylation-18.64-
507 (in isoform 2)Phosphorylation-56.7927273156
533 (in isoform 2)N-linked_Glycosylation-9.3616335952
535 (in isoform 2)Phosphorylation-5.30-
599 (in isoform 2)N-linked_Glycosylation-52.4316335952
618PhosphorylationHSTCQKAYAPLKKKV
HHHCHHHHHCCCCCC		18.7824114839
652PhosphorylationDSGGPMVTLNRERGQ
CCCCCEEEEECCCCC		16.4429396449
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 MASP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MASP1_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 MASP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MASP2_HUMANMASP2physical
10878362
FCN2_HUMANFCN2physical
12421953
PDC6I_HUMANPDCD6IPphysical
12771190
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
2579203MC syndrome 1 (3MC1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MASP1_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 andidentification of its interaction sites with mannan-binding lectin andficolins.";
Teillet F., Gaboriaud C., Lacroix M., Martin L., Arlaud G.J.,Thielens N.M.;
J. Biol. Chem. 283:25715-25724(2008).
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 20-295 IN COMPLEX WITHCALCIUM IONS, HOMODIMERIZATION, GLYCOSYLATION AT ASN-178, DISULFIDEBONDS, CALCIUM-BINDING SITES, INTERACTION WITH FCN2; FCN3 AND MBL2,AND MUTAGENESIS OF GLU-68; TYR-77; GLU-99; ASP-121; PHE-122; SER-123;GLU-125; HIS-237; GLU-239; TYR-244; GLU-262; SER-274; ASN-283 ANDGLU-286.
"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-49; ASN-178; ASN-385;ASN-407 (ISOFORM 1), GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-533AND ASN-599 (ISOFORM 2), AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory