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P05155

- IC1_HUMAN

UniProt

P05155 - IC1_HUMAN

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Protein

Plasma protease C1 inhibitor

Gene
SERPING1, C1IN, C1NH
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.16 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti84 – 13855Missing in HAE; phenotype consistent with hereditary angioedema type 2.
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).7 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.

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.

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]

Sequencei

Sequence statusi: Complete.

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

P05155-1 [UniParc]FASTAAdd to Basket

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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

Sequence cautioni

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

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.
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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1031T → S in BAF85743. 1 Publication
Sequence conflicti187 – 1871E → Q in AAB59387. 1 Publication
Sequence conflicti306 – 3061K → R in AAA35613. 1 Publication
Sequence conflicti314 – 3207HFKNSVI → QLQKLSY AA sequence 1 Publication
Sequence conflicti322 – 3221V → M AA sequence 1 Publication
Sequence conflicti332 – 3321V → L AA sequence 1 Publication
Sequence conflicti370 – 3756MEQALS → TGTGSQ AA sequence 1 Publication
Sequence conflicti417 – 4171E → V AA sequence 1 Publication
Sequence conflicti439 – 4391S → F AA sequence 1 Publication

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.
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.
GeneIDi710.
KEGGihsa:710.
UCSCiuc001nkp.1. human.

Polymorphism databases

DMDMi124096.

Keywords - Coding sequence diversityi

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 .
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 .
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

« Hide 'large scale' publications
  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].
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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].
  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].
    Tissue: Heart 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], 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], 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], 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.
  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.
  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, 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, 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: September 3, 2014
This is version 181 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

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