MATN2_HUMAN - dbPTM
MATN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MATN2_HUMAN
UniProt AC O00339
Protein Name Matrilin-2
Gene Name MATN2
Organism Homo sapiens (Human).
Sequence Length 956
Subcellular Localization Secreted.
Protein Description Involved in matrix assembly..
Protein Sequence MEKMLAGCFLLILGQIVLLPAEARERSRGRSISRGRHARTHPQTALLESSCENKRADLVFIIDSSRSVNTHDYAKVKEFIVDILQFLDIGPDVTRVGLLQYGSTVKNEFSLKTFKRKSEVERAVKRMRHLSTGTMTGLAIQYALNIAFSEAEGARPLRENVPRVIMIVTDGRPQDSVAEVAAKARDTGILIFAIGVGQVDFNTLKSIGSEPHEDHVFLVANFSQIETLTSVFQKKLCTAHMCSTLEHNCAHFCINIPGSYVCRCKQGYILNSDQTTCRIQDLCAMEDHNCEQLCVNVPGSFVCQCYSGYALAEDGKRCVAVDYCASENHGCEHECVNADGSYLCQCHEGFALNPDKKTCTKIDYCASSNHGCQHECVNTDDSYSCHCLKGFTLNPDKKTCRRINYCALNKPGCEHECVNMEESYYCRCHRGYTLDPNGKTCSRVDHCAQQDHGCEQLCLNTEDSFVCQCSEGFLINEDLKTCSRVDYCLLSDHGCEYSCVNMDRSFACQCPEGHVLRSDGKTCAKLDSCALGDHGCEHSCVSSEDSFVCQCFEGYILREDGKTCRRKDVCQAIDHGCEHICVNSDDSYTCECLEGFRLAEDGKRCRRKDVCKSTHHGCEHICVNNGNSYICKCSEGFVLAEDGRRCKKCTEGPIDLVFVIDGSKSLGEENFEVVKQFVTGIIDSLTISPKAARVGLLQYSTQVHTEFTLRNFNSAKDMKKAVAHMKYMGKGSMTGLALKHMFERSFTQGEGARPLSTRVPRAAIVFTDGRAQDDVSEWASKAKANGITMYAVGVGKAIEEELQEIASEPTNKHLFYAEDFSTMDEISEKLKKGICEALEDSDGRQDSPAGELPKTVQQPTESEPVTINIQDLLSCSNFAVQHRYLFEEDNLLRSTQKLSHSTKPSGSPLEEKHDQCKCENLIMFQNLANEEVRKLTQRLEEMTQRMEALENRLRYR
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
40O-linked_GlycosylationSRGRHARTHPQTALL
CCCCCCCCCCCHHHH		38.4055827747
101PhosphorylationTRVGLLQYGSTVKNE
CEEEEEECCCCCCCE		17.02-
110PhosphorylationSTVKNEFSLKTFKRK
CCCCCEEECHHHCCH		23.8324719451
115AcetylationEFSLKTFKRKSEVER
EEECHHHCCHHHHHH		65.2419822859
118PhosphorylationLKTFKRKSEVERAVK
CHHHCCHHHHHHHHH		51.4023532336
125AcetylationSEVERAVKRMRHLST
HHHHHHHHHHHHCCC		39.2219822867
134PhosphorylationMRHLSTGTMTGLAIQ
HHHCCCCHHHHHHHH		16.20-
136PhosphorylationHLSTGTMTGLAIQYA
HCCCCHHHHHHHHHH		28.96-
149PhosphorylationYALNIAFSEAEGARP
HHHHHHHHHCCCCCC		27.20-
169PhosphorylationPRVIMIVTDGRPQDS
CEEEEEEECCCCCCC		23.08-
221N-linked_GlycosylationDHVFLVANFSQIETL
CCEEEEEEHHHHHHH		29.62UniProtKB CARBOHYD
432PhosphorylationYCRCHRGYTLDPNGK
EEEECCCEEECCCCC		12.23-
686PhosphorylationTGIIDSLTISPKAAR
HHHHHHCCCCHHHHH		24.3025332170
688PhosphorylationIIDSLTISPKAARVG
HHHHCCCCHHHHHEE		18.3424719451
705PhosphorylationQYSTQVHTEFTLRNF
EEECCCCCHHHHCCC		33.66-
708PhosphorylationTQVHTEFTLRNFNSA
CCCCCHHHHCCCCCH		20.6924719451
714PhosphorylationFTLRNFNSAKDMKKA
HHHCCCCCHHHHHHH		32.3419369195
727PhosphorylationKAVAHMKYMGKGSMT
HHHHHHHHCCCCCHH		11.9729759185
730AcetylationAHMKYMGKGSMTGLA
HHHHHCCCCCHHHHH		31.147925245
732PhosphorylationMKYMGKGSMTGLALK
HHHCCCCCHHHHHHH		19.3629978859
734PhosphorylationYMGKGSMTGLALKHM
HCCCCCHHHHHHHHH		30.6429978859
767PhosphorylationPRAAIVFTDGRAQDD
CCEEEEEECCCCCCC		27.0128796482
780PhosphorylationDDVSEWASKAKANGI
CCHHHHHHHHHHCCC		33.9326074081
788PhosphorylationKAKANGITMYAVGVG
HHHHCCCEEEEEEHH		12.9126074081
790PhosphorylationKANGITMYAVGVGKA
HHCCCEEEEEEHHHH		6.8926074081
847PhosphorylationDSDGRQDSPAGELPK
CCCCCCCCCCCCCCC		14.3323403867
860O-linked_GlycosylationPKTVQQPTESEPVTI
CCCCCCCCCCCCEEE		48.05OGP
866O-linked_GlycosylationPTESEPVTINIQDLL
CCCCCCEEEEHHHHH		21.01OGP
894PhosphorylationEEDNLLRSTQKLSHS
HHCCHHHHHHHHCCC		34.8517525332
895PhosphorylationEDNLLRSTQKLSHST
HCCHHHHHHHHCCCC		24.2417525332
901PhosphorylationSTQKLSHSTKPSGSP
HHHHHCCCCCCCCCC		34.45-
901O-linked_GlycosylationSTQKLSHSTKPSGSP
HHHHHCCCCCCCCCC		34.4555831353
902PhosphorylationTQKLSHSTKPSGSPL
HHHHCCCCCCCCCCC		41.36-
902O-linked_GlycosylationTQKLSHSTKPSGSPL
HHHHCCCCCCCCCCC		41.3655831359
905O-linked_GlycosylationLSHSTKPSGSPLEEK
HCCCCCCCCCCCHHH		54.1655831365
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 MATN2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MATN2_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 MATN2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MATN2_HUMANMATN2physical
12180907
FBN2_HUMANFBN2physical
12180907
CO1A1_HUMANCOL1A1physical
12180907
MATN4_HUMANMATN4physical
11896063
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.
Regulatory Network of MATN2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-894 AND THR-895, ANDMASS SPECTROMETRY.

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