IC1_HUMAN - dbPTM
IC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IC1_HUMAN
UniProt AC P05155
Protein Name Plasma protease C1 inhibitor
Gene Name SERPING1
Organism Homo sapiens (Human).
Sequence Length 500
Subcellular Localization Secreted.
Protein 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. Inhibits chymotrypsin and kallikrein..
Protein Sequence MASRLTLLTLLLLLLAGDRASSNPNATSSSSQDPESLQDRGEGKVATTVISKMLFVEPILEVSSLPTTNSTTNSATKITANTTDEPTTQPTTEPTTQPTIQPTQPTTQLPTDSPTQPTTGSFCPGPVTLCSDLESHSTEAVLGDALVDFSLKLYHAFSAMKKVETNMAFSPFSIASLLTQVLLGAGENTKTNLESILSYPKDFTCVHQALKGFTTKGVTSVSQIFHSPDLAIRDTFVNASRTLYSSSPRVLSNNSDANLELINTWVAKNTNNKISRLLDSLPSDTRLVLLNAIYLSAKWKTTFDPKKTRMEPFHFKNSVIKVPMMNSKKYPVAHFIDQTLKAKVGQLQLSHNLSLVILVPQNLKHRLEDMEQALSPSVFKAIMEKLEMSKFQPTLLTLPRIKVTTSQDMLSIMEKLEFFDFSYDLNLCGLTEDPDLQVSAMQHQTVLELTETGVEAAAASAISVARTLLVFEVQQPFLFVLWDQQHKFPVFMGRVYDPRA
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
4Methylation----MASRLTLLTLL
----CHHHHHHHHHH		23.3524391367
22PhosphorylationLAGDRASSNPNATSS
HHCCHHHCCCCCCCC		56.1525954137
25N-linked_GlycosylationDRASSNPNATSSSSQ
CHHHCCCCCCCCCCC		61.1622171320
25N-linked_GlycosylationDRASSNPNATSSSSQ
CHHHCCCCCCCCCCC		61.1622171320
27O-linked_GlycosylationASSNPNATSSSSQDP
HHCCCCCCCCCCCCH		35.46OGP
28O-linked_GlycosylationSSNPNATSSSSQDPE
HCCCCCCCCCCCCHH		26.30OGP
28PhosphorylationSSNPNATSSSSQDPE
HCCCCCCCCCCCCHH		26.3025954137
30O-linked_GlycosylationNPNATSSSSQDPESL
CCCCCCCCCCCHHHH		31.61OGP
31O-linked_GlycosylationPNATSSSSQDPESLQ
CCCCCCCCCCHHHHH		40.32OGP
36PhosphorylationSSSQDPESLQDRGEG
CCCCCHHHHHHCCCC		36.4025954137
47O-linked_GlycosylationRGEGKVATTVISKML
CCCCHHHHHHHHHHH		25.2822171320
48O-linked_GlycosylationGEGKVATTVISKMLF
CCCHHHHHHHHHHHC		13.2022171320
48O-linked_GlycosylationGEGKVATTVISKMLF
CCCHHHHHHHHHHHC		13.2022171320
51PhosphorylationKVATTVISKMLFVEP
HHHHHHHHHHHCCCC		14.0025954137
63O-linked_GlycosylationVEPILEVSSLPTTNS
CCCEEEECCCCCCCC		19.44OGP
64O-linked_GlycosylationEPILEVSSLPTTNST
CCEEEECCCCCCCCC		43.473756141
64O-linked_GlycosylationEPILEVSSLPTTNST
CCEEEECCCCCCCCC		43.47UniProtKB CARBOHYD
67O-linked_GlycosylationLEVSSLPTTNSTTNS
EEECCCCCCCCCCCC		43.85OGP
68O-linked_GlycosylationEVSSLPTTNSTTNSA
EECCCCCCCCCCCCC		25.82OGP
69N-linked_GlycosylationVSSLPTTNSTTNSAT
ECCCCCCCCCCCCCE		39.583756141
69N-linked_GlycosylationVSSLPTTNSTTNSAT
ECCCCCCCCCCCCCE		39.5816335952
70O-linked_GlycosylationSSLPTTNSTTNSATK
CCCCCCCCCCCCCEE		34.22OGP
71O-linked_GlycosylationSLPTTNSTTNSATKI
CCCCCCCCCCCCEEE		31.873756141
71O-linked_GlycosylationSLPTTNSTTNSATKI
CCCCCCCCCCCCEEE		31.87UniProtKB CARBOHYD
72O-linked_GlycosylationLPTTNSTTNSATKIT
CCCCCCCCCCCEEEE		27.31OGP
76O-linked_GlycosylationNSTTNSATKITANTT
CCCCCCCEEEEECCC		23.85OGP
81N-linked_GlycosylationSATKITANTTDEPTT
CCEEEEECCCCCCCC		34.5619159218
81N-linked_GlycosylationSATKITANTTDEPTT
CCEEEEECCCCCCCC		34.563756141
83O-linked_GlycosylationTKITANTTDEPTTQP
EEEEECCCCCCCCCC		37.873756141
83O-linked_GlycosylationTKITANTTDEPTTQP
EEEEECCCCCCCCCC		37.87UniProtKB CARBOHYD
88O-linked_GlycosylationNTTDEPTTQPTTEPT
CCCCCCCCCCCCCCC		43.18UniProtKB CARBOHYD
88O-linked_GlycosylationNTTDEPTTQPTTEPT
CCCCCCCCCCCCCCC		43.183756141
92O-linked_GlycosylationEPTTQPTTEPTTQPT
CCCCCCCCCCCCCCC		46.80UniProtKB CARBOHYD
92O-linked_GlycosylationEPTTQPTTEPTTQPT
CCCCCCCCCCCCCCC		46.803756141
96O-linked_GlycosylationQPTTEPTTQPTIQPT
CCCCCCCCCCCCCCC		43.18UniProtKB CARBOHYD
96O-linked_GlycosylationQPTTEPTTQPTIQPT
CCCCCCCCCCCCCCC		43.183756141
113O-linked_GlycosylationTTQLPTDSPTQPTTG
CCCCCCCCCCCCCCC		32.12OGP
115O-linked_GlycosylationQLPTDSPTQPTTGSF
CCCCCCCCCCCCCCC		51.65OGP
118O-linked_GlycosylationTDSPTQPTTGSFCPG
CCCCCCCCCCCCCCC		33.69OGP
119O-linked_GlycosylationDSPTQPTTGSFCPGP
CCCCCCCCCCCCCCC		37.20OGP
176PhosphorylationFSPFSIASLLTQVLL
CCHHHHHHHHHHHHH		23.4224719451
179PhosphorylationFSIASLLTQVLLGAG
HHHHHHHHHHHHCCC		23.1724719451
189PhosphorylationLLGAGENTKTNLESI
HHCCCCCCCCCHHHH		34.6424719451
198PhosphorylationTNLESILSYPKDFTC
CCHHHHHCCCCCCHH		37.4117192257
199PhosphorylationNLESILSYPKDFTCV
CHHHHHCCCCCCHHH		15.7423312004
238N-linked_GlycosylationAIRDTFVNASRTLYS
CHHHHCCCHHHHHHC		28.1817488724
238N-linked_GlycosylationAIRDTFVNASRTLYS
CHHHHCCCHHHHHHC		28.1817488724
253N-linked_GlycosylationSSPRVLSNNSDANLE
CCCCHHCCCCCCCHH		48.1117623646
253N-linked_GlycosylationSSPRVLSNNSDANLE
CCCCHHCCCCCCCHH		48.1118638581
272N-linked_GlycosylationWVAKNTNNKISRLLD
HHHHHCCCHHHHHHH		40.79UniProtKB CARBOHYD
294PhosphorylationLVLLNAIYLSAKWKT
HHHHHHHHHHHCCCC		7.68-
296PhosphorylationLLNAIYLSAKWKTTF
HHHHHHHHHCCCCCC		15.72-
316AcetylationRMEPFHFKNSVIKVP
CCCCCCCCCCEEEEE		39.48164205
321AcetylationHFKNSVIKVPMMNSK
CCCCCEEEEECCCCC		37.82164209
350PhosphorylationKVGQLQLSHNLSLVI
HHCEEECCCCEEEEE		9.4329888752
352N-linked_GlycosylationGQLQLSHNLSLVILV
CEEECCCCEEEEEEE		28.1317623646
352N-linked_GlycosylationGQLQLSHNLSLVILV
CEEECCCCEEEEEEE		28.1319838169
354PhosphorylationLQLSHNLSLVILVPQ
EECCCCEEEEEEEEC		26.3829888752
375PhosphorylationEDMEQALSPSVFKAI
HHHHHHHCHHHHHHH		20.39-
385AcetylationVFKAIMEKLEMSKFQ
HHHHHHHHHHHHCCC		32.1627178108
389PhosphorylationIMEKLEMSKFQPTLL
HHHHHHHHCCCCCEE		22.4229396449
397PhosphorylationKFQPTLLTLPRIKVT
CCCCCEECCCCEEEE		37.5224719451
460PhosphorylationGVEAAAASAISVART
HHHHHHHHHHHHHHH		22.7824275569
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 IC1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IC1_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 IC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LYAM2_HUMANSELEphysical
14568956
LYAM3_HUMANSELPphysical
14568956
C1S_HUMANC1Sphysical
6604523
MASP1_HUMANMASP1physical
10946292
MASP2_HUMANMASP2physical
10946292
TPA_HUMANPLATphysical
28514442
ARFG2_HUMANARFGAP2physical
28514442
GRN_HUMANGRNphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
106100Hereditary angioedema (HAE)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IC1_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"C1 inhibitor serpin domain structure reveals the likely mechanism ofheparin potentiation and conformational disease.";
Beinrohr L., Harmat V., Dobo J., Loerincz Z., Gal P., Zavodszky P.;
J. Biol. Chem. 282:21100-21109(2007).
Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 119-500, DISULFIDE BONDS,AND GLYCOSYLATION AT ASN-238.
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT ASN-25; THR-47 AND THR-48, STRUCTURE OFCARBOHYDRATES, AND MASS SPECTROMETRY.
"Enrichment of glycopeptides for glycan structure and attachment siteidentification.";
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,Brinkmalm G., Larson G.;
Nat. Methods 6:809-811(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352, STRUCTURE OFCARBOHYDRATES, AND MASS SPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-81; ASN-238;ASN-253 AND ASN-352, AND MASS SPECTROMETRY.
"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-25; ASN-69; ASN-238;ASN-253 AND ASN-352, AND MASS SPECTROMETRY.
"N-linked glycosylation at Asn3 and the positively charged residueswithin the amino-terminal domain of the c1 inhibitor are required forinteraction of the C1 Inhibitor with Salmonella enterica serovartyphimurium lipopolysaccharide and lipid A.";
Liu D., Cramer C.C., Scafidi J., Davis A.E. III;
Infect. Immun. 73:4478-4487(2005).
Cited for: GLYCOSYLATION AT ASN-25.
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Proteomics 4:454-465(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-25; ASN-238; ASN-253 ANDASN-352, AND MASS SPECTROMETRY.
"Identification and quantification of N-linked glycoproteins usinghydrazide chemistry, stable isotope labeling and mass spectrometry.";
Zhang H., Li X.-J., Martin D.B., Aebersold R.;
Nat. Biotechnol. 21:660-666(2003).
Cited for: GLYCOSYLATION AT ASN-253.
"Human C1 inhibitor: primary structure, cDNA cloning, and chromosomallocalization.";
Bock S.C., Skriver K., Nielsen E., Thoegersen H.-C., Wiman B.,Donaldson V.H., Eddy R.L., Marrinan J., Radziejewska E., Huber R.,Shows T.B., Magnusson S.;
Biochemistry 25:4292-4301(1986).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ANDGLYCOSYLATION AT ASN-25; THR-48; SER-64; ASN-69; THR-71; ASN-81;THR-83; THR-88; THR-92; THR-96; ASN-238; ASN-253 AND ASN-352.
O-linked Glycosylation
ReferencePubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT ASN-25; THR-47 AND THR-48, STRUCTURE OFCARBOHYDRATES, AND MASS SPECTROMETRY.
"Human C1 inhibitor: primary structure, cDNA cloning, and chromosomallocalization.";
Bock S.C., Skriver K., Nielsen E., Thoegersen H.-C., Wiman B.,Donaldson V.H., Eddy R.L., Marrinan J., Radziejewska E., Huber R.,Shows T.B., Magnusson S.;
Biochemistry 25:4292-4301(1986).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, ANDGLYCOSYLATION AT ASN-25; THR-48; SER-64; ASN-69; THR-71; ASN-81;THR-83; THR-88; THR-92; THR-96; ASN-238; ASN-253 AND ASN-352.

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