| Tag | Content |
|---|
| CPLM ID | CPLM-005709 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Murinoglobulin-2 |
Protein Synonyms/Alias | MuG2 |
Gene Name | Mug2 |
Gene Synonyms/Alias | Mug-2 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 258 | CGKYTYGKPVPGQVK | ubiquitination | [1] | | 365 | KVRLVDIKGDPIPNE | ubiquitination | [1] | | 559 | IEKCLRNKVDLSFSS | ubiquitination | [1] | | 667 | YVEDMDLKAFTNLKI | ubiquitination | [1] | | 994 | YVLKYLDKTQQLTQK | ubiquitination | [1] | | 1001 | KTQQLTQKIKTKALG | ubiquitination | [1] | | 1139 | ALAGNQDKRNEILKS | ubiquitination | [1] | | 1313 | RYNMHLEKQQSAFAL | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | A proteinase activates the inhibitor by specific proteolysis in the bait region, which, by an unknown mechanism leads to reaction at the cysteinyl-glutamyl internal thiol ester site and to a conformational change, whereby the proteinase is trapped and/or covalently bound to the inhibitor. While in the tetrameric proteinase inhibitors steric inhibition is sufficiently strong, monomeric forms need a covalent linkage between the activated glutamyl residue of the original thiol ester and a terminal amino group of a lysine or another nucleophilic group on the proteinase, for inhibition to be effective. |
Sequence Annotation | REGION 677 734 Bait region.
CARBOHYD 55 55 N-linked (GlcNAc...) (Potential).
CARBOHYD 294 294 N-linked (GlcNAc...) (Potential).
CARBOHYD 313 313 N-linked (GlcNAc...) (Potential).
CARBOHYD 500 500 N-linked (GlcNAc...) (Potential).
CARBOHYD 749 749 N-linked (GlcNAc...) (Potential).
CARBOHYD 776 776 N-linked (GlcNAc...) (Potential).
CARBOHYD 871 871 N-linked (GlcNAc...) (Potential).
CARBOHYD 1401 1401 N-linked (GlcNAc...) (Potential).
DISULFID 48 86 By similarity.
DISULFID 251 276 By similarity.
DISULFID 269 288 By similarity.
DISULFID 461 555 By similarity.
DISULFID 587 773 By similarity.
DISULFID 634 680 By similarity.
DISULFID 849 885 By similarity.
DISULFID 923 1274 By similarity.
DISULFID 1081 1104 By similarity.
DISULFID 1298 1444 By similarity.
CROSSLNK 974 977 Isoglutamyl cysteine thioester (Cys-Gln) |
Keyword | Bait region; Complete proteome; Disulfide bond; Glycoprotein; Protease inhibitor; Reference proteome; Secreted; Serine protease inhibitor; Signal; Thioester bond. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1451 AA |
Protein Sequence | MWKSRRAQLC LFSVLLAFLP SASSLNGDSK YMVLVPSQLY TETPEKICLH LYHLNETVTV 60
TASLVSQTGR RNLFDELVVD KDLFQCVSFI IPTLNSPDEE EFLYVDIKGP THEFSKRNAV 120
LVKNKESVVF VQTDKPVYKP GQSVKFRVVS MDKTLRPLNE LLPLAYIEDP KKNRIMQWRD 180
IKTENGLKQM SFSLAAEPIQ GPYKIVVHKQ SGVKEEHSFT VMEFVLPRFN VDLKVPNAIS 240
VNDEVLQVTV CGKYTYGKPV PGQVKISICH ETEAGCKEVN SKLDNNGCST QEVNITELQS 300
KKRNYEVQLF HVNATVTEEG TGLEFNGYGT TKIERITNKL IFLKADSHFR HGIPFFVKVR 360
LVDIKGDPIP NERVFIKAQV LGYTSATTTD QHGLAKFSID TAGFSGSSLH IKVNHKGKDS 420
CYFFYCMEER YASAEHVAYA VYSLSKSYIY LVKETSSILP CNQIHTVQAH FILKGDLGVL 480
KELVFYYLVM AQGSIIQTGN HTHQVEPGEA PVKGNFDLEI PVEFSMAPMA KMLIYTILPD 540
GEVIADSVNF EIEKCLRNKV DLSFSSSQSL PASQTRLQVT ASPQSLCGLR AVDQSVLLLK 600
PEDELSPSWI YNLPGMQHNK FIPSSSLSED REDCILYSSW VAEKHTDWVP HGREKDVYRY 660
VEDMDLKAFT NLKIKLPKIC FDSAPMSGPR GKFDLAFSSE VSGTLQKGSS KRPQPEEPPR 720
EDPPPKDPLA ETIRKYFPET WVWDIVTVNS TGVAEVEMTV PDTITEWKAG ALCLSNDTGL 780
GLSSVVPLQA FQPFFVEVSL PYSVVRGEAF MLKATVMNYL PTSMRMSVQL EASPDFTAVP 840
VGDDHDSYCL SANGRHTSSW LVTPKSLGNV NFSVSVEAQQ SSEPCGSEVA TVPETGRKDT 900
VVKVLIVEPE GIKQEHTFNS LFCASDAEIS EKMSLVLPPT VVKDSARAHF SVMGDILSSA 960
IKNTQNLLHM PYGCGEQNMV LFAPNIYVLK YLDKTQQLTQ KIKTKALGFL RAGYQRELNY 1020
KHKDGSYSAF GDQNGEREGN TWLTAFVLKS FAQARAFIFI DESHITHAFT WLSQQQKDNG 1080
CFRSSGSLFH NDIKHPVVSK ALSCLESSWK TIEQGRNANF VYTKALMAYA FALAGNQDKR 1140
NEILKSLDEE AIKEDNSIHW ERPQKPRKSE HNLYKPQASS VEVEMNAYVV LARLTAQPAP 1200
SPEDLTLSRS TIMWLTKQQN SNGGFSSTQD TVVALDALSK YGAVTFSRRQ KTSLVTIQST 1260
GSFSQKFQVE NSNCLLLQQV PLPDIPGDYT ISVSGEGCVY AQTTLRYNMH LEKQQSAFAL 1320
RVQTVPLTCN NPKGHNSFQI SLEISYTGSR PASNMVIADV KMLSGFIPLK PTVKKLERLE 1380
HISRTEVSNN NVLLYLDQVT NQTLAFSFII QQDISVRNLQ PAIVKVYDYY ETDEVAYAEY 1440
SSPCSSDKQN V 1451 |
Gene Ontology | GO:0005615; C:extracellular space; IEA:InterPro. GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW. GO:0010951; P:negative regulation of endopeptidase activity; IEA:GOC. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |