| Tag | Content |
|---|
| CPLM ID | CPLM-010615 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Plasma protease C1 inhibitor |
Protein Synonyms/Alias | C1 Inh; C1Inh; C1 esterase inhibitor; C1-inhibiting factor; Serpin G1 |
Gene Name | Serping1 |
Gene Synonyms/Alias | C1nh |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 221 | ALKGFSSKGVTSVSQ | ubiquitination | [1] | | 278 | VAENTNHKIRKLLDS | ubiquitination | [1] | | 320 | MMAPFFYKNSMIKVP | ubiquitination | [1] | | 376 | HQLKDVEKALNPTVF | 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 | Activation of the C1 complex is under control of the C1- inhibitor. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases. May play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. Very efficient inhibitor of FXIIa. May inhibit chymotrypsin and kallikrein. |
Sequence Annotation | MOD_RES 41 41 Phosphoserine.
CARBOHYD 75 75 N-linked (GlcNAc...) (Potential).
CARBOHYD 83 83 N-linked (GlcNAc...) (Potential).
CARBOHYD 107 107 N-linked (GlcNAc...) (Potential).
CARBOHYD 243 243 N-linked (GlcNAc...).
CARBOHYD 356 356 N-linked (GlcNAc...) (Potential).
DISULFID 128 432 By similarity.
DISULFID 135 210 By similarity. |
Keyword | Blood coagulation; Complement pathway; Complete proteome; Disulfide bond; Fibrinolysis; Glycoprotein; Hemostasis; Immunity; Innate immunity; Phosphoprotein; Protease inhibitor; Reference proteome; Secreted; Serine protease inhibitor; Signal. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 504 AA |
Protein Sequence | MASRLTPLTL LLLLLAGDRA FSDPEATSHS TQDPLEAQAK SRESFPERDD SWSPPEPTVL 60
PSTWPTTSVA ITITNDTMGK VANESFSQHS QPAAQLPTDS PGQPPLNSSS QPSTASDLPT 120
QATTEPFCPE PLAQCSDSDR DSSEAKLSEA LTDFSVKLYH AFSATKMAKT NMAFSPFSIA 180
SLLTQVLLGA GDSTKSNLES ILSYPKDFAC VHQALKGFSS KGVTSVSQIF HSPDLAIRDT 240
YVNASQSLYG SSPRVLGPDS AANLELINTW VAENTNHKIR KLLDSLPSDT CLVLLNAVYL 300
SAKWKITFEP KKMMAPFFYK NSMIKVPMMS SVKYPVAQFD DHTLKAKVGQ LQLSHNLSFV 360
IVVPVFPKHQ LKDVEKALNP TVFKAIMKKL ELSKFLPTYL TMPHIKVKSS QDMLSVMEKL 420
EFFDFTYDLN LCGLTEDPDL QVSAMKHETV LELTESGVEA AAASAISFGR SLPIFEVQRP 480
FLFLLWDQQH RFPVFMGRVY DPRG 504 |
Gene Ontology | GO:0005615; C:extracellular space; IDA:MGI. GO:0004867; F:serine-type endopeptidase inhibitor activity; ISS:UniProtKB. GO:0007596; P:blood coagulation; IEA:UniProtKB-KW. GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW. GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW. GO:0045087; P:innate immune response; IEA:UniProtKB-KW. GO:0001869; P:negative regulation of complement activation, lectin pathway; ISS:UniProtKB. GO:0030162; P:regulation of proteolysis; IBA:RefGenome. |
Interpro | |
Pfam | |
SMART | |
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PRINTS | |