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P05155

- IC1_HUMAN

UniProt

P05155 - IC1_HUMAN

Protein

Plasma protease C1 inhibitor

Gene

SERPING1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 182 (01 Oct 2014)
      Sequence version 2 (01 Feb 1991)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei465 – 4662Reactive bond for chymotrypsin
    Sitei466 – 4672Reactive bond

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. serine-type endopeptidase inhibitor activity Source: UniProtKB

    GO - Biological processi

    1. blood circulation Source: ProtInc
    2. blood coagulation Source: Reactome
    3. blood coagulation, intrinsic pathway Source: Reactome
    4. complement activation, classical pathway Source: UniProtKB-KW
    5. fibrinolysis Source: UniProtKB-KW
    6. innate immune response Source: UniProtKB-KW
    7. negative regulation of complement activation, lectin pathway Source: UniProtKB
    8. negative regulation of endopeptidase activity Source: RefGenome
    9. platelet activation Source: Reactome
    10. platelet degranulation Source: Reactome

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Keywords - Biological processi

    Blood coagulation, Complement pathway, Fibrinolysis, Hemostasis, Immunity, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_326. Intrinsic Pathway.

    Protein family/group databases

    MEROPSiI04.024.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Plasma protease C1 inhibitor
    Short name:
    C1 Inh
    Short name:
    C1Inh
    Alternative name(s):
    C1 esterase inhibitor
    C1-inhibiting factor
    Serpin G1
    Gene namesi
    Name:SERPING1
    Synonyms:C1IN, C1NH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:1228. SERPING1.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. extracellular region Source: UniProtKB
    3. extracellular space Source: UniProt
    4. extracellular vesicular exosome Source: UniProt
    5. platelet alpha granule lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Hereditary angioedema (HAE) [MIM:106100]: An autosomal dominant disorder characterized by episodic local swelling involving subcutaneous or submucous tissue of the upper respiratory and gastrointestinal tracts, face, extremities, and genitalia. Hereditary angioedema due to C1 esterase inhibitor deficiency is comprised of two clinically indistinguishable forms. In hereditary angioedema type 1, serum levels of C1 esterase inhibitor are decreased, while in type 2, the levels are normal or elevated, but the protein is non-functional.16 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti84 – 13855Missing in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_046202Add
    BLAST
    Natural varianti118 – 1181T → A in HAE. 1 Publication
    Corresponds to variant rs200534715 [ dbSNP | Ensembl ].
    VAR_068832
    Natural varianti130 – 1301C → Y in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication
    VAR_027379
    Natural varianti154 – 1541Y → C in HAE. 1 Publication
    Corresponds to variant rs281875168 [ dbSNP | Ensembl ].
    VAR_068833
    Natural varianti170 – 1701S → F in HAE. 1 Publication
    Corresponds to variant rs281875169 [ dbSNP | Ensembl ].
    VAR_068834
    Natural varianti184 – 1841G → R in HAE. 1 Publication
    Corresponds to variant rs281875170 [ dbSNP | Ensembl ].
    VAR_068835
    Natural varianti230 – 2301L → P in HAE. 1 Publication
    Corresponds to variant rs281875171 [ dbSNP | Ensembl ].
    VAR_068836
    Natural varianti232 – 2321I → K in HAE. 1 Publication
    Corresponds to variant rs281875172 [ dbSNP | Ensembl ].
    VAR_068837
    Natural varianti272 – 2721Missing in HAE. 1 Publication
    VAR_068838
    Natural varianti273 – 2731Missing in HAE; phenotype consistent with hereditary angioedema type 2; creates a new glycosylation site. 1 Publication
    VAR_007012
    Natural varianti299 – 2991W → R in HAE. 1 Publication
    Corresponds to variant rs281875173 [ dbSNP | Ensembl ].
    VAR_068839
    Natural varianti345 – 3451G → R in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication
    VAR_027376
    Natural varianti394 – 3941T → P in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication
    VAR_027380
    Natural varianti408 – 4081D → V in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication
    VAR_027381
    Natural varianti429 – 4291G → R in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007013
    Natural varianti430 – 4301L → Q in HAE. 1 Publication
    Corresponds to variant rs281875174 [ dbSNP | Ensembl ].
    VAR_068840
    Natural varianti441 – 4411M → T in HAE. 1 Publication
    Corresponds to variant rs281875175 [ dbSNP | Ensembl ].
    VAR_068841
    Natural varianti447 – 4471L → P in HAE. 1 Publication
    Corresponds to variant rs281875176 [ dbSNP | Ensembl ].
    VAR_068842
    Natural varianti454 – 4541V → E in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007014
    Natural varianti456 – 4561A → E in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007015
    Natural varianti458 – 4581A → T in HAE; phenotype consistent with hereditary angioedema type 2. 2 Publications
    VAR_007016
    Natural varianti458 – 4581A → V in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007017
    Natural varianti465 – 4651A → V in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007018
    Natural varianti466 – 4661R → C in HAE; phenotype consistent with hereditary angioedema type 2. 2 Publications
    Corresponds to variant rs28940870 [ dbSNP | Ensembl ].
    VAR_007019
    Natural varianti466 – 4661R → H in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007020
    Natural varianti466 – 4661R → L in HAE; phenotype consistent with hereditary angioedema type 2. 2 Publications
    Corresponds to variant rs121907948 [ dbSNP | Ensembl ].
    VAR_007021
    Natural varianti466 – 4661R → S in HAE; phenotype consistent with hereditary angioedema type 2. 2 Publications
    Corresponds to variant rs28940870 [ dbSNP | Ensembl ].
    VAR_007022
    Natural varianti467 – 4671T → P in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007023
    Natural varianti473 – 4731V → E in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication
    VAR_027382
    Natural varianti473 – 4731V → G in HAE. 1 Publication
    Corresponds to variant rs281875177 [ dbSNP | Ensembl ].
    VAR_068843
    Natural varianti473 – 4731V → M in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007024
    Natural varianti477 – 4771F → S in HAE; phenotype consistent with hereditary angioedema type 2.
    VAR_007026
    Natural varianti481 – 4811L → P in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007028
    Natural varianti481 – 4811L → R in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007029
    Natural varianti489 – 4891P → R in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007030
    Natural varianti493 – 4931G → E in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication
    VAR_027383
    Natural varianti497 – 4971D → G in HAE. 1 Publication
    Corresponds to variant rs281875178 [ dbSNP | Ensembl ].
    VAR_068844
    Natural varianti498 – 4981P → R in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication
    VAR_027384
    Natural varianti498 – 4981P → S in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007031

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi106100. phenotype.
    Orphaneti100050. Hereditary angioedema type 1.
    100051. Hereditary angioedema type 2.
    169147. Immunodeficiency due to an early component of complement deficiency.
    PharmGKBiPA35029.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Chaini23 – 500478Plasma protease C1 inhibitor1 PublicationPRO_0000032514Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi25 – 251N-linked (GlcNAc...) (complex)5 Publications
    Glycosylationi47 – 471O-linked (GalNAc...)2 Publications
    Glycosylationi48 – 481O-linked (GalNAc...)3 Publications
    Glycosylationi64 – 641O-linked (GalNAc...)1 Publication
    Glycosylationi69 – 691N-linked (GlcNAc...)3 Publications
    Glycosylationi71 – 711O-linked (GalNAc...)1 Publication
    Glycosylationi81 – 811N-linked (GlcNAc...)2 Publications
    Glycosylationi83 – 831O-linked (GalNAc...)1 Publication
    Glycosylationi88 – 881O-linked (GalNAc...)1 Publication
    Glycosylationi92 – 921O-linked (GalNAc...)1 Publication
    Glycosylationi96 – 961O-linked (GalNAc...)1 Publication
    Disulfide bondi123 ↔ 4282 Publications
    Disulfide bondi130 ↔ 2052 Publications
    Glycosylationi238 – 2381N-linked (GlcNAc...) (complex)6 Publications
    Glycosylationi253 – 2531N-linked (GlcNAc...) (complex)6 Publications
    Glycosylationi272 – 2721N-linked (GlcNAc...); in variant TA
    Glycosylationi352 – 3521N-linked (GlcNAc...) (complex)6 Publications

    Post-translational modificationi

    Highly glycosylated (49%) with N- and O-glycosylation. O-glycosylated with core 1 or possibly core 8 glycans. N-glycan heterogeneity at Asn-25: Hex5HexNAc4 (minor), dHex1Hex5HexNAc4 (minor), Hex6HexNAc5 (major) and dHex1Hex6HexNAc5 (minor).11 Publications
    Can be proteolytically cleaved by E.coli stcE.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP05155.
    PaxDbiP05155.
    PeptideAtlasiP05155.
    PRIDEiP05155.

    PTM databases

    PhosphoSiteiP05155.

    Miscellaneous databases

    PMAP-CutDBP05155.

    Expressioni

    Gene expression databases

    ArrayExpressiP05155.
    BgeeiP05155.
    GenevestigatoriP05155.

    Organism-specific databases

    HPAiCAB026161.
    HPA048738.

    Interactioni

    Subunit structurei

    Binds to E.coli stcE which allows localization of SERPING1 to cell membranes thus protecting the bacteria against complement-mediated lysis. Interacts with MASP1.3 Publications

    Protein-protein interaction databases

    BioGridi107171. 12 interactions.
    DIPiDIP-45635N.
    IntActiP05155. 6 interactions.

    Structurei

    Secondary structure

    1
    500
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi135 – 15723
    Beta strandi167 – 1693
    Helixi171 – 18313
    Helixi187 – 19711
    Helixi206 – 2116
    Beta strandi216 – 22611
    Helixi234 – 24411
    Helixi255 – 26814
    Turni269 – 2724
    Beta strandi287 – 30115
    Beta strandi309 – 3135
    Beta strandi320 – 33718
    Turni338 – 3414
    Beta strandi342 – 3509
    Beta strandi353 – 36210
    Helixi367 – 3737
    Helixi376 – 38712
    Beta strandi391 – 3999
    Beta strandi402 – 4087
    Helixi409 – 4135
    Helixi414 – 4163
    Beta strandi417 – 4193
    Helixi421 – 4244
    Turni428 – 4303
    Beta strandi441 – 4499
    Beta strandi451 – 46313
    Beta strandi468 – 4703
    Beta strandi477 – 4837
    Turni484 – 4874
    Beta strandi488 – 4958

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1M6Qmodel-A138-500[»]
    2OAYX-ray2.35A119-500[»]
    ProteinModelPortaliP05155.
    SMRiP05155. Positions 102-498.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05155.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati85 – 8841
    Repeati89 – 9242
    Repeati93 – 9643
    Repeati97 – 10044
    Repeati101 – 10445
    Repeati105 – 10846
    Repeati116 – 11947

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni85 – 119357 X 4 AA tandem repeats of [QE]-P-T-[TQ]Add
    BLAST

    Sequence similaritiesi

    Belongs to the serpin family.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG4826.
    HOVERGENiHBG104060.
    KOiK04001.
    PhylomeDBiP05155.
    TreeFamiTF317350.

    Family and domain databases

    InterProiIPR015553. C1-inh.
    IPR023795. Serpin_CS.
    IPR023796. Serpin_dom.
    IPR000215. Serpin_fam.
    [Graphical view]
    PANTHERiPTHR11461. PTHR11461. 1 hit.
    PTHR11461:SF156. PTHR11461:SF156. 1 hit.
    PfamiPF00079. Serpin. 1 hit.
    [Graphical view]
    SMARTiSM00093. SERPIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF56574. SSF56574. 1 hit.
    PROSITEiPS00284. SERPIN. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P05155-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASRLTLLTL LLLLLAGDRA SSNPNATSSS SQDPESLQDR GEGKVATTVI    50
    SKMLFVEPIL EVSSLPTTNS TTNSATKITA NTTDEPTTQP TTEPTTQPTI 100
    QPTQPTTQLP TDSPTQPTTG SFCPGPVTLC SDLESHSTEA VLGDALVDFS 150
    LKLYHAFSAM KKVETNMAFS PFSIASLLTQ VLLGAGENTK TNLESILSYP 200
    KDFTCVHQAL KGFTTKGVTS VSQIFHSPDL AIRDTFVNAS RTLYSSSPRV 250
    LSNNSDANLE LINTWVAKNT NNKISRLLDS LPSDTRLVLL NAIYLSAKWK 300
    TTFDPKKTRM EPFHFKNSVI KVPMMNSKKY PVAHFIDQTL KAKVGQLQLS 350
    HNLSLVILVP QNLKHRLEDM EQALSPSVFK AIMEKLEMSK FQPTLLTLPR 400
    IKVTTSQDML SIMEKLEFFD FSYDLNLCGL TEDPDLQVSA MQHQTVLELT 450
    ETGVEAAAAS AISVARTLLV FEVQQPFLFV LWDQQHKFPV FMGRVYDPRA 500
    Length:500
    Mass (Da):55,154
    Last modified:February 1, 1991 - v2
    Checksum:i8B5E874833EA6C05
    GO
    Isoform 2 (identifier: P05155-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-52: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:448
    Mass (Da):49,757
    Checksum:iC3BA362232FA47AB
    GO
    Isoform 3 (identifier: P05155-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         17-17: G → GFLEPQ

    Note: No experimental confirmation available.

    Show »
    Length:505
    Mass (Da):55,769
    Checksum:i6AAEEB52FEE89B80
    GO

    Sequence cautioni

    The sequence AAA53096.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti103 – 1031T → S in BAF85743. (PubMed:14702039)Curated
    Sequence conflicti187 – 1871E → Q in AAB59387. (PubMed:3756141)Curated
    Sequence conflicti306 – 3061K → R in AAA35613. (PubMed:3488058)Curated
    Sequence conflicti314 – 3207HFKNSVI → QLQKLSY AA sequence (PubMed:3458172)Curated
    Sequence conflicti322 – 3221V → M AA sequence (PubMed:3458172)Curated
    Sequence conflicti332 – 3321V → L AA sequence (PubMed:3458172)Curated
    Sequence conflicti370 – 3756MEQALS → TGTGSQ AA sequence (PubMed:3458172)Curated
    Sequence conflicti417 – 4171E → V AA sequence (PubMed:3458172)Curated
    Sequence conflicti439 – 4391S → F AA sequence (PubMed:3458172)Curated

    Polymorphismi

    Chymotrypsin uses Ala-465 as its reactive site in normal plasma protease C1 inhibitor, and His-466 as its reactive site in the variant His-466.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti39 – 391D → E.
    Corresponds to variant rs11229062 [ dbSNP | Ensembl ].
    VAR_027374
    Natural varianti56 – 561V → A.2 Publications
    Corresponds to variant rs11546660 [ dbSNP | Ensembl ].
    VAR_027375
    Natural varianti84 – 13855Missing in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_046202Add
    BLAST
    Natural varianti118 – 1181T → A in HAE. 1 Publication
    Corresponds to variant rs200534715 [ dbSNP | Ensembl ].
    VAR_068832
    Natural varianti130 – 1301C → Y in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication
    VAR_027379
    Natural varianti154 – 1541Y → C in HAE. 1 Publication
    Corresponds to variant rs281875168 [ dbSNP | Ensembl ].
    VAR_068833
    Natural varianti170 – 1701S → F in HAE. 1 Publication
    Corresponds to variant rs281875169 [ dbSNP | Ensembl ].
    VAR_068834
    Natural varianti184 – 1841G → R in HAE. 1 Publication
    Corresponds to variant rs281875170 [ dbSNP | Ensembl ].
    VAR_068835
    Natural varianti230 – 2301L → P in HAE. 1 Publication
    Corresponds to variant rs281875171 [ dbSNP | Ensembl ].
    VAR_068836
    Natural varianti232 – 2321I → K in HAE. 1 Publication
    Corresponds to variant rs281875172 [ dbSNP | Ensembl ].
    VAR_068837
    Natural varianti272 – 2721Missing in HAE. 1 Publication
    VAR_068838
    Natural varianti273 – 2731Missing in HAE; phenotype consistent with hereditary angioedema type 2; creates a new glycosylation site. 1 Publication
    VAR_007012
    Natural varianti299 – 2991W → R in HAE. 1 Publication
    Corresponds to variant rs281875173 [ dbSNP | Ensembl ].
    VAR_068839
    Natural varianti308 – 3081T → S.
    Corresponds to variant rs1803212 [ dbSNP | Ensembl ].
    VAR_011751
    Natural varianti345 – 3451G → R in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication
    VAR_027376
    Natural varianti394 – 3941T → P in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication
    VAR_027380
    Natural varianti408 – 4081D → V in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication
    VAR_027381
    Natural varianti429 – 4291G → R in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007013
    Natural varianti430 – 4301L → Q in HAE. 1 Publication
    Corresponds to variant rs281875174 [ dbSNP | Ensembl ].
    VAR_068840
    Natural varianti441 – 4411M → T in HAE. 1 Publication
    Corresponds to variant rs281875175 [ dbSNP | Ensembl ].
    VAR_068841
    Natural varianti447 – 4471L → P in HAE. 1 Publication
    Corresponds to variant rs281875176 [ dbSNP | Ensembl ].
    VAR_068842
    Natural varianti454 – 4541V → E in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007014
    Natural varianti456 – 4561A → E in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007015
    Natural varianti458 – 4581A → T in HAE; phenotype consistent with hereditary angioedema type 2. 2 Publications
    VAR_007016
    Natural varianti458 – 4581A → V in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007017
    Natural varianti465 – 4651A → V in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007018
    Natural varianti466 – 4661R → C in HAE; phenotype consistent with hereditary angioedema type 2. 2 Publications
    Corresponds to variant rs28940870 [ dbSNP | Ensembl ].
    VAR_007019
    Natural varianti466 – 4661R → H in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007020
    Natural varianti466 – 4661R → L in HAE; phenotype consistent with hereditary angioedema type 2. 2 Publications
    Corresponds to variant rs121907948 [ dbSNP | Ensembl ].
    VAR_007021
    Natural varianti466 – 4661R → S in HAE; phenotype consistent with hereditary angioedema type 2. 2 Publications
    Corresponds to variant rs28940870 [ dbSNP | Ensembl ].
    VAR_007022
    Natural varianti467 – 4671T → P in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007023
    Natural varianti473 – 4731V → E in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication
    VAR_027382
    Natural varianti473 – 4731V → G in HAE. 1 Publication
    Corresponds to variant rs281875177 [ dbSNP | Ensembl ].
    VAR_068843
    Natural varianti473 – 4731V → M in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007024
    Natural varianti474 – 4741Q → E.
    VAR_007025
    Natural varianti477 – 4771F → S in HAE; phenotype consistent with hereditary angioedema type 2.
    VAR_007026
    Natural varianti480 – 4801V → M.6 Publications
    Corresponds to variant rs4926 [ dbSNP | Ensembl ].
    VAR_007027
    Natural varianti481 – 4811L → P in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007028
    Natural varianti481 – 4811L → R in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007029
    Natural varianti489 – 4891P → R in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007030
    Natural varianti493 – 4931G → E in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication
    VAR_027383
    Natural varianti497 – 4971D → G in HAE. 1 Publication
    Corresponds to variant rs281875178 [ dbSNP | Ensembl ].
    VAR_068844
    Natural varianti498 – 4981P → R in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication
    VAR_027384
    Natural varianti498 – 4981P → S in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication
    VAR_007031

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5252Missing in isoform 2. 1 PublicationVSP_056662Add
    BLAST
    Alternative sequencei17 – 171G → GFLEPQ in isoform 3. 1 PublicationVSP_056663

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13690 mRNA. Translation: AAA35613.1.
    M13656 mRNA. Translation: AAB59387.1.
    X07427
    , X07428, X07429, X07430, X07431, X07432, X07433 Genomic DNA. Translation: CAA30314.1.
    X07577 mRNA. Translation: CAA30469.1.
    X54486 Genomic DNA. Translation: CAA38358.1.
    AF435921 Genomic DNA. Translation: AAM21515.1.
    AK293054 mRNA. Translation: BAF85743.1.
    AK303809 mRNA. Translation: BAG64762.1.
    AK303840 mRNA. Translation: BAG64784.1.
    AK312626 mRNA. Translation: BAG35512.1.
    BT006966 mRNA. Translation: AAP35612.1.
    AB209826 mRNA. Translation: BAD93063.1.
    AY904027 Genomic DNA. Translation: AAW69393.1.
    AP000662 Genomic DNA. No translation available.
    AP002893 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW73764.1.
    BC011171 mRNA. Translation: AAH11171.1.
    AY291075 Genomic DNA. Translation: AAQ19269.1.
    M30688 Genomic DNA. Translation: AAA53096.1. Sequence problems.
    M14036 mRNA. Translation: AAA51848.1.
    M13203 mRNA. Translation: AAA51849.1.
    S76944 Genomic DNA. Translation: AAB33044.2.
    CCDSiCCDS7962.1.
    PIRiS15386. ITHUC1.
    RefSeqiNP_000053.2. NM_000062.2.
    NP_001027466.1. NM_001032295.1.
    UniGeneiHs.384598.

    Genome annotation databases

    EnsembliENST00000278407; ENSP00000278407; ENSG00000149131.
    ENST00000378323; ENSP00000367574; ENSG00000149131.
    ENST00000378324; ENSP00000367575; ENSG00000149131.
    GeneIDi710.
    KEGGihsa:710.
    UCSCiuc001nkp.1. human.

    Polymorphism databases

    DMDMi124096.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    C1-inhibitor entry

    SERPING1base

    SERPING1 mutation db

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13690 mRNA. Translation: AAA35613.1 .
    M13656 mRNA. Translation: AAB59387.1 .
    X07427
    , X07428 , X07429 , X07430 , X07431 , X07432 , X07433 Genomic DNA. Translation: CAA30314.1 .
    X07577 mRNA. Translation: CAA30469.1 .
    X54486 Genomic DNA. Translation: CAA38358.1 .
    AF435921 Genomic DNA. Translation: AAM21515.1 .
    AK293054 mRNA. Translation: BAF85743.1 .
    AK303809 mRNA. Translation: BAG64762.1 .
    AK303840 mRNA. Translation: BAG64784.1 .
    AK312626 mRNA. Translation: BAG35512.1 .
    BT006966 mRNA. Translation: AAP35612.1 .
    AB209826 mRNA. Translation: BAD93063.1 .
    AY904027 Genomic DNA. Translation: AAW69393.1 .
    AP000662 Genomic DNA. No translation available.
    AP002893 Genomic DNA. No translation available.
    CH471076 Genomic DNA. Translation: EAW73764.1 .
    BC011171 mRNA. Translation: AAH11171.1 .
    AY291075 Genomic DNA. Translation: AAQ19269.1 .
    M30688 Genomic DNA. Translation: AAA53096.1 . Sequence problems.
    M14036 mRNA. Translation: AAA51848.1 .
    M13203 mRNA. Translation: AAA51849.1 .
    S76944 Genomic DNA. Translation: AAB33044.2 .
    CCDSi CCDS7962.1.
    PIRi S15386. ITHUC1.
    RefSeqi NP_000053.2. NM_000062.2.
    NP_001027466.1. NM_001032295.1.
    UniGenei Hs.384598.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M6Q model - A 138-500 [» ]
    2OAY X-ray 2.35 A 119-500 [» ]
    ProteinModelPortali P05155.
    SMRi P05155. Positions 102-498.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107171. 12 interactions.
    DIPi DIP-45635N.
    IntActi P05155. 6 interactions.

    Protein family/group databases

    MEROPSi I04.024.

    PTM databases

    PhosphoSitei P05155.

    Polymorphism databases

    DMDMi 124096.

    Proteomic databases

    MaxQBi P05155.
    PaxDbi P05155.
    PeptideAtlasi P05155.
    PRIDEi P05155.

    Protocols and materials databases

    DNASUi 710.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000278407 ; ENSP00000278407 ; ENSG00000149131 .
    ENST00000378323 ; ENSP00000367574 ; ENSG00000149131 .
    ENST00000378324 ; ENSP00000367575 ; ENSG00000149131 .
    GeneIDi 710.
    KEGGi hsa:710.
    UCSCi uc001nkp.1. human.

    Organism-specific databases

    CTDi 710.
    GeneCardsi GC11P057364.
    HGNCi HGNC:1228. SERPING1.
    HPAi CAB026161.
    HPA048738.
    MIMi 106100. phenotype.
    606860. gene.
    neXtProti NX_P05155.
    Orphaneti 100050. Hereditary angioedema type 1.
    100051. Hereditary angioedema type 2.
    169147. Immunodeficiency due to an early component of complement deficiency.
    PharmGKBi PA35029.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4826.
    HOVERGENi HBG104060.
    KOi K04001.
    PhylomeDBi P05155.
    TreeFami TF317350.

    Enzyme and pathway databases

    Reactomei REACT_326. Intrinsic Pathway.

    Miscellaneous databases

    ChiTaRSi SERPING1. human.
    EvolutionaryTracei P05155.
    GeneWikii C1-inhibitor.
    GenomeRNAii 710.
    NextBioi 2886.
    PMAP-CutDB P05155.
    PROi P05155.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05155.
    Bgeei P05155.
    Genevestigatori P05155.

    Family and domain databases

    InterProi IPR015553. C1-inh.
    IPR023795. Serpin_CS.
    IPR023796. Serpin_dom.
    IPR000215. Serpin_fam.
    [Graphical view ]
    PANTHERi PTHR11461. PTHR11461. 1 hit.
    PTHR11461:SF156. PTHR11461:SF156. 1 hit.
    Pfami PF00079. Serpin. 1 hit.
    [Graphical view ]
    SMARTi SM00093. SERPIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56574. SSF56574. 1 hit.
    PROSITEi PS00284. SERPIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and analysis of a cDNA coding for human C1 inhibitor."
      Que B.G., Petra P.H.
      Biochem. Biophys. Res. Commun. 137:620-625(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION 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.
    3. "Genomic and cDNA cloning of the human C1 inhibitor. Intron-exon junctions and comparison with other serpins."
      Carter P.E., Dunbar B., Fothergill J.E.
      Eur. J. Biochem. 173:163-169(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    4. "Complete nucleotide sequence of the gene for human C1 inhibitor with an unusually high density of Alu elements."
      Carter P.E., Duponchel C., Tosi M., Fothergill J.E.
      Eur. J. Biochem. 197:301-308(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "Production of recombinant human C1 inhibitor in milk of transgenic rabbits for potential use in enzyme replacement therapy for hereditary angioedema."
      Heus J., Platenburg-Kootwijk E., Meershoek E., De Winter R., Knijnenburg J., Kupers L., Habex H., Renaers I., Samuel C., Bonnarens L., Hoffman S., Brouwer M., Hack E., Horbach D., Timmermans M., Nuijens J., Pieper F.
      Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Foreskin.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
      Tissue: Heart, Liver, Ovary and Uterus.
    7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT MET-480.
    8. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT MET-480.
      Tissue: Brain.
    9. SeattleSNPs variation discovery resource
      Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-480.
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT MET-480.
      Tissue: Brain.
    13. "Molecular cloning of the cDNA coding for human C1 inhibitor."
      Rauth G., Schumacher G., Buckel P., Mueller-Esterl W.
      Protein Seq. Data Anal. 1:251-257(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-500 (ISOFORM 1).
    14. "The functional integrity of the serpin domain of C1-inhibitor depends on the unique N-terminal domain, as revealed by a pathological mutant."
      Bos I.G.A., Lubbers Y.T.P., Roem D., Abrahams J.P., Hack C.E., Eldering E.
      J. Biol. Chem. 278:29463-29470(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-188, VARIANT HAE 84-ASP--THR-138 DEL.
      Tissue: Blood.
    15. "Human C1 inhibitor: improved isolation and preliminary structural characterization."
      Harrison R.A.
      Biochemistry 22:5001-5007(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-62.
    16. "Clusters of intragenic Alu repeats predispose the human C1 inhibitor locus to deleterious rearrangements."
      Stoppa-Lyonnet D., Carter P.E., Meo T., Tosi M.
      Proc. Natl. Acad. Sci. U.S.A. 87:1551-1555(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-228.
    17. "Molecular cloning of human C1 inhibitor: sequence homologies with alpha 1-antitrypsin and other members of the serpins superfamily."
      Tosi M., Duponchel C., Bourgarel P., Colomb M., Meo T.
      Gene 42:265-272(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 213-500 (ISOFORM 1/2/3).
    18. "Molecular weights and isoelectric points of sperm antigens relevant to autoimmune infertility in men."
      Pillai S., Wright D., Gupta A., Zhou G., Hull G., Jiang H., Zhang H.
      J. Urol. 155:1928-1933(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 217-233.
    19. "Human inhibitor of the first component of complement, C1: characterization of cDNA clones and localization of the gene to chromosome 11."
      Davis A.E. III, Whitehead A.S., Harrison R.A., Dauphinias A., Bruns G.A., Cicardi M., Rosen F.S.
      Proc. Natl. Acad. Sci. U.S.A. 83:3161-3165(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 241-458 (ISOFORM 1/2/3), PARTIAL PROTEIN SEQUENCE.
    20. "Crucial residues in the carboxy-terminal end of C1 inhibitor revealed by pathogenic mutants impaired in secretion or function."
      Verpy E., Couture-Tosi E., Eldering E., Lopez-Trascasa M., Spath P., Meo T., Tosi M.
      J. Clin. Invest. 95:350-359(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 418-500, VARIANTS HAE MET-473; ARG-481; PRO-481; ARG-489 AND SER-498.
    21. "Chymotrypsin inhibitory activity of normal C1-inhibitor and a P1 Arg to His mutant: evidence for the presence of overlapping reactive centers."
      Aulak K.S., Davis A.E. III, Donaldson V.H., Harrison R.A.
      Protein Sci. 2:727-732(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 464-481, FUNCTION, REACTIVE SITE FOR CHYMOTRYPSIN.
      Tissue: Plasma.
    22. "Proteolytic activities of two types of mannose-binding lectin-associated serine protease."
      Matsushita M., Thiel S., Jensenius J.C., Terai I., Fujita T.
      J. Immunol. 165:2637-2642(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MASP1.
    23. "StcE, a metalloprotease secreted by Escherichia coli O157:H7, specifically cleaves C1 esterase inhibitor."
      Lathem W.W., Grys T.E., Witowski S.E., Torres A.G., Kaper J.B., Tarr P.I., Welch R.A.
      Mol. Microbiol. 45:277-288(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH E.COLI STCE, PROTEOLYTIC PROCESSING BY E.COLI STCE.
    24. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
      Zhang H., Li X.-J., Martin D.B., Aebersold R.
      Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-253.
    25. "Potentiation of C1 esterase inhibitor by StcE, a metalloprotease secreted by Escherichia coli O157:H7."
      Lathem W.W., Bergsbaken T., Welch R.A.
      J. Exp. Med. 199:1077-1087(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH E.COLI STCE, PROTEOLYTIC PROCESSING BY E.COLI STCE.
    26. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
      Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
      Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-25; ASN-238; ASN-253 AND ASN-352.
      Tissue: Plasma.
    27. "N-linked glycosylation at Asn3 and the positively charged residues within the amino-terminal domain of the c1 inhibitor are required for interaction of the C1 Inhibitor with Salmonella enterica serovar typhimurium lipopolysaccharide and lipid A."
      Liu D., Cramer C.C., Scafidi J., Davis A.E. III
      Infect. Immun. 73:4478-4487(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-25.
    28. "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) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-25; ASN-69; ASN-238; ASN-253 AND ASN-352.
      Tissue: Plasma.
    29. "Glycoproteomics analysis of human liver tissue by combination of multiple 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) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-69; ASN-81; ASN-238; ASN-253 AND ASN-352.
      Tissue: Liver.
    30. Cited for: GLYCOSYLATION AT ASN-238; ASN-253 AND ASN-352.
    31. "Enrichment of glycopeptides for glycan structure and attachment site identification."
      Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
      Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352, STRUCTURE OF CARBOHYDRATES.
      Tissue: Cerebrospinal fluid.
    32. "Human urinary glycoproteomics; attachment site specific analysis of N-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) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-25; THR-47 AND THR-48, STRUCTURE OF CARBOHYDRATES, IDENTIFICATION BY MASS SPECTROMETRY.
    33. "LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
      Halim A., Ruetschi U., Larson G., Nilsson J.
      J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-47 AND THR-48, IDENTIFICATION BY MASS SPECTROMETRY.
    34. "C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease."
      Beinrohr L., Harmat V., Dobo J., Loerincz Z., Gal P., Zavodszky P.
      J. Biol. Chem. 282:21100-21109(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 119-500, DISULFIDE BONDS, GLYCOSYLATION AT ASN-238.
    35. "What do dysfunctional serpins tell us about molecular mobility and disease?"
      Stein P.E., Carrell R.W.
      Nat. Struct. Biol. 2:96-113(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS.
    36. "Dysfunctional C1-inhibitor(At), isolated from a type II hereditary-angio-oedema plasma, contains a P1 'reactive centre' (Arg444-->His) mutation."
      Aulak K.S., Pemberton P.A., Rosen F.S., Carrell R.W., Lachmann P.J., Harrison R.A.
      Biochem. J. 253:615-618(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HAE HIS-466.
    37. "Identification of a new P1 residue mutation (444Arg-->Ser) in a dysfunctional C1 inhibitor protein contained in a type II hereditary angioedema plasma."
      Aulak K.S., Cicardi M., Harrison R.A.
      FEBS Lett. 266:13-16(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HAE SER-466.
    38. "Type II hereditary angioneurotic edema that may result from a single nucleotide change in the codon for alanine-436 in the C1 inhibitor gene."
      Levy N.J., Ramesh N., Cicardi M., Harrison R.A., Davis A.E. III
      Proc. Natl. Acad. Sci. U.S.A. 87:265-268(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HAE THR-458.
    39. "Dysfunctional C1 inhibitor Ta: deletion of Lys-251 results in acquisition of an N-glycosylation site."
      Parad R.B., Kramer J., Strunk R.C., Rosen F.S., Davis A.E. III
      Proc. Natl. Acad. Sci. U.S.A. 87:6786-6790(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HAE LYS-273 DEL.
    40. "Identification of type II hereditary angio-oedema (HAE) mutations."
      Siddique Z.M., McPhaden A.R., Whaley K.
      Clin. Exp. Immunol. 86:11-12(1991)
      Cited for: VARIANTS HAE GLU-456 AND VAL-458.
    41. "A dysfunctional C1 inhibitor protein with a new reactive center mutation (Arg-444-->Leu)."
      Frange D., Aulak K.S., Cicardi M., Harrison R.A., Davis A.E. III
      FEBS Lett. 301:34-36(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HAE LEU-466.
    42. "C1 inhibitor hinge region mutations produce dysfunction by different mechanisms."
      Davis A.E. III, Aulak K., Parad R.B., Stecklein H.P., Eldering E., Hack C.E., Kramer J., Strunk R.C., Bissler J., Rosen F.S.
      Nat. Genet. 1:354-358(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HAE GLU-454 AND THR-458.
    43. "Mutations in the C1 inhibitor gene that result in hereditary angioneurotic edema."
      Davis A.E. III, Bissler J.J., Cicardi M.
      Behring Inst. Mitt. 93:313-320(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HAE ARG-429.
    44. "Unique C1 inhibitor dysfunction in a kindred without angioedema. II. Identification of an Ala443-->Val substitution and functional analysis of the recombinant mutant protein."
      Zahedi R., Bissler J.J., Davis A.E. III, Andreadis C., Wisnieski J.J.
      J. Clin. Invest. 95:1299-1305(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HAE VAL-465.
    45. "A mutation unique in serine protease inhibitors (serpins) identified in a family with type II hereditary angioneurotic edema."
      Ocejo-Vinyals J.G., Leyva-Cobian F., Fernandez-Luna J.L.
      Mol. Med. 1:700-705(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HAE PRO-467.
    46. "Exhaustive mutation scanning by fluorescence-assisted mismatch analysis discloses new genotype-phenotype correlations in angiodema."
      Verpy E., Biasotto M., Brai M., Misiano G., Meo T., Tosi M.
      Am. J. Hum. Genet. 59:308-319(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HAE.
    47. "Mutation screening of the C1 inhibitor gene among Hungarian patients with hereditary angioedema."
      Kalmar L., Bors A., Farkas H., Vas S., Fandl B., Varga L., Fuest G., Tordai A.
      Hum. Mutat. 22:498-498(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HAE TYR-130; PRO-394; VAL-408; CYS-466; GLU-473; GLU-493 AND ARG-498.
    48. "Normal C1 inhibitor mRNA expression level in type I hereditary angioedema patients: newly found C1 inhibitor gene mutations."
      Kang H.-R., Yim E.-Y., Oh S.-Y., Chang Y.-S., Kim Y.-K., Cho S.-H., Min K.-U., Kim Y.-Y.
      Allergy 61:260-264(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HAE ARG-345, VARIANTS ALA-56 AND MET-480.
    49. "Mutational spectrum and geno-phenotype correlation in Chinese families with Hereditary Angioedema."
      Xu Y.Y., Zhi Y.X., Yin J., Wang L.L., Wen L.P., Gu J.Q., Guan K., Craig T., Zhang H.Y.
      Allergy 67:1430-1436(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HAE ALA-118; CYS-154; PHE-170; ARG-184; PRO-230; LYS-232; ASN-272 DEL; ARG-299; GLN-430; THR-441; PRO-447; SER-466; CYS-466; LEU-466; GLY-473 AND GLY-497, VARIANTS ALA-56 AND MET-480.

    Entry informationi

    Entry nameiIC1_HUMAN
    AccessioniPrimary (citable) accession number: P05155
    Secondary accession number(s): A6NMU0
    , A8KAI9, B2R6L5, B4E1F0, B4E1H2, Q16304, Q547W3, Q59EI5, Q7Z455, Q96FE0, Q9UC49, Q9UCF9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 182 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3