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Protein

Plasma protease C1 inhibitor

Gene

SERPING1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Sitei465 – 466Reactive bond for chymotrypsin2
Sitei466 – 467Reactive bond2

GO - Molecular functioni

  • serine-type endopeptidase inhibitor activity Source: UniProtKB

GO - Biological processi

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

BioCyciZFISH:ENSG00000149131-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-140837. Intrinsic Pathway of Fibrin Clot Formation.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:1228. SERPING1.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: UniProtKB
  • extracellular space Source: UniProtKB
  • platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Hereditary angioedema (HAE)17 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:106100
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07170111L → R in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication1
Natural variantiVAR_04620284 – 138Missing in HAE; phenotype consistent with hereditary angioedema type 2. 1 PublicationAdd BLAST55
Natural variantiVAR_068832118T → A in HAE. 1 PublicationCorresponds to variant rs200534715dbSNPEnsembl.1
Natural variantiVAR_027379130C → Y in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication1
Natural variantiVAR_068833154Y → C in HAE. 1 PublicationCorresponds to variant rs281875168dbSNPEnsembl.1
Natural variantiVAR_068834170S → F in HAE. 1 PublicationCorresponds to variant rs281875169dbSNPEnsembl.1
Natural variantiVAR_068835184G → R in HAE. 1 PublicationCorresponds to variant rs281875170dbSNPEnsembl.1
Natural variantiVAR_068836230L → P in HAE. 1 PublicationCorresponds to variant rs281875171dbSNPEnsembl.1
Natural variantiVAR_068837232I → K in HAE. 1 PublicationCorresponds to variant rs281875172dbSNPEnsembl.1
Natural variantiVAR_071702265W → R in HAE. 1 Publication1
Natural variantiVAR_068838272Missing in HAE. 1 Publication1
Natural variantiVAR_007012273Missing in HAE; phenotype consistent with hereditary angioedema type 2; creates a new glycosylation site. 1 Publication1
Natural variantiVAR_071703274I → V in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_068839299W → R in HAE. 1 PublicationCorresponds to variant rs281875173dbSNPEnsembl.1
Natural variantiVAR_027376345G → R in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication1
Natural variantiVAR_027380394T → P in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication1
Natural variantiVAR_027381408D → V in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication1
Natural variantiVAR_007013429G → R in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_068840430L → Q in HAE. 1 PublicationCorresponds to variant rs281875174dbSNPEnsembl.1
Natural variantiVAR_068841441M → T in HAE. 1 PublicationCorresponds to variant rs281875175dbSNPEnsembl.1
Natural variantiVAR_068842447L → P in HAE. 1 PublicationCorresponds to variant rs281875176dbSNPEnsembl.1
Natural variantiVAR_007014454V → E in HAE; phenotype consistent with hereditary angioedema type 2. 1 PublicationCorresponds to variant rs121907949dbSNPEnsembl.1
Natural variantiVAR_007015456A → E in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_007016458A → T in HAE; phenotype consistent with hereditary angioedema type 2. 3 PublicationsCorresponds to variant rs121907947dbSNPEnsembl.1
Natural variantiVAR_007017458A → V in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_007018465A → V in HAE; phenotype consistent with hereditary angioedema type 2. 1 PublicationCorresponds to variant rs121907950dbSNPEnsembl.1
Natural variantiVAR_007019466R → C in HAE; phenotype consistent with hereditary angioedema type 2. 3 PublicationsCorresponds to variant rs28940870dbSNPEnsembl.1
Natural variantiVAR_007020466R → H in HAE; phenotype consistent with hereditary angioedema type 2. 2 PublicationsCorresponds to variant rs121907948dbSNPEnsembl.1
Natural variantiVAR_007021466R → L in HAE; phenotype consistent with hereditary angioedema type 2. 2 PublicationsCorresponds to variant rs121907948dbSNPEnsembl.1
Natural variantiVAR_007022466R → S in HAE; phenotype consistent with hereditary angioedema type 2. 2 PublicationsCorresponds to variant rs28940870dbSNPEnsembl.1
Natural variantiVAR_007023467T → P in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_027382473V → E in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication1
Natural variantiVAR_068843473V → G in HAE. 1 PublicationCorresponds to variant rs281875177dbSNPEnsembl.1
Natural variantiVAR_007024473V → M in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_007026477F → S in HAE; phenotype consistent with hereditary angioedema type 2. 1
Natural variantiVAR_007028481L → P in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_007029481L → R in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_007030489P → R in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_027383493G → E in HAE; phenotype consistent with hereditary angioedema type 1. 2 Publications1
Natural variantiVAR_071704493G → R in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_068844497D → G in HAE. 1 PublicationCorresponds to variant rs281875178dbSNPEnsembl.1
Natural variantiVAR_027384498P → R in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication1
Natural variantiVAR_007031498P → S in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi710.
MalaCardsiSERPING1.
MIMi106100. phenotype.
OpenTargetsiENSG00000149131.
Orphaneti100050. Hereditary angioedema type 1.
100051. Hereditary angioedema type 2.
169147. Immunodeficiency due to an early component of complement deficiency.
PharmGKBiPA35029.

Chemistry databases

DrugBankiDB06404. C1 Esterase Inhibitor (Human).

Polymorphism and mutation databases

BioMutaiSERPING1.
DMDMi124096.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 221 PublicationAdd BLAST22
ChainiPRO_000003251423 – 500Plasma protease C1 inhibitor1 PublicationAdd BLAST478

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi25N-linked (GlcNAc...) (complex)5 Publications1
Glycosylationi47O-linked (GalNAc...)2 Publications1
Glycosylationi48O-linked (GalNAc...)3 Publications1
Glycosylationi64O-linked (GalNAc...)1 Publication1
Glycosylationi69N-linked (GlcNAc...)3 Publications1
Glycosylationi71O-linked (GalNAc...)1 Publication1
Glycosylationi81N-linked (GlcNAc...)2 Publications1
Glycosylationi83O-linked (GalNAc...)1 Publication1
Glycosylationi88O-linked (GalNAc...)1 Publication1
Glycosylationi92O-linked (GalNAc...)1 Publication1
Glycosylationi96O-linked (GalNAc...)1 Publication1
Disulfide bondi123 ↔ 4282 Publications
Disulfide bondi130 ↔ 2052 Publications
Glycosylationi238N-linked (GlcNAc...) (complex)6 Publications1
Glycosylationi253N-linked (GlcNAc...) (complex)6 Publications1
Glycosylationi272N-linked (GlcNAc...); in variant TA1
Glycosylationi352N-linked (GlcNAc...) (complex)6 Publications1

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

PaxDbiP05155.
PeptideAtlasiP05155.
PRIDEiP05155.
TopDownProteomicsiP05155-1. [P05155-1]

PTM databases

iPTMnetiP05155.
PhosphoSitePlusiP05155.
UniCarbKBiP05155.

Miscellaneous databases

PMAP-CutDBP05155.

Expressioni

Gene expression databases

BgeeiENSG00000149131.
ExpressionAtlasiP05155. baseline and differential.
GenevisibleiP05155. HS.

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. 17 interactors.
DIPiDIP-45635N.
IntActiP05155. 7 interactors.
STRINGi9606.ENSP00000278407.

Structurei

Secondary structure

1500
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi132 – 137Combined sources6
Helixi139 – 160Combined sources22
Beta strandi167 – 169Combined sources3
Helixi171 – 182Combined sources12
Helixi187 – 197Combined sources11
Helixi206 – 212Combined sources7
Beta strandi218 – 226Combined sources9
Helixi234 – 244Combined sources11
Helixi255 – 269Combined sources15
Turni270 – 272Combined sources3
Beta strandi287 – 295Combined sources9
Beta strandi299 – 301Combined sources3
Helixi305 – 307Combined sources3
Beta strandi309 – 315Combined sources7
Beta strandi318 – 337Combined sources20
Turni338 – 341Combined sources4
Beta strandi342 – 350Combined sources9
Beta strandi353 – 362Combined sources10
Helixi367 – 373Combined sources7
Helixi376 – 387Combined sources12
Beta strandi392 – 399Combined sources8
Beta strandi401 – 408Combined sources8
Helixi409 – 415Combined sources7
Beta strandi417 – 419Combined sources3
Turni420 – 422Combined sources3
Turni428 – 430Combined sources3
Beta strandi440 – 449Combined sources10
Beta strandi453 – 455Combined sources3
Helixi458 – 461Combined sources4
Beta strandi469 – 472Combined sources4
Beta strandi477 – 483Combined sources7
Turni484 – 487Combined sources4
Beta strandi488 – 496Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M6Qmodel-A138-500[»]
2OAYX-ray2.35A119-500[»]
5DU3X-ray2.10A/B119-500[»]
5DUQX-ray2.90A/B118-500[»]
ProteinModelPortaliP05155.
SMRiP05155.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05155.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati85 – 8814
Repeati89 – 9224
Repeati93 – 9634
Repeati97 – 10044
Repeati101 – 10454
Repeati105 – 10864
Repeati116 – 11974

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni85 – 1197 X 4 AA tandem repeats of [QE]-P-T-[TQ]Add BLAST35

Sequence similaritiesi

Belongs to the serpin family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG2392. Eukaryota.
COG4826. LUCA.
GeneTreeiENSGT00850000132312.
HOGENOMiHOG000231936.
HOVERGENiHBG104060.
InParanoidiP05155.
KOiK04001.
PhylomeDBiP05155.
TreeFamiTF317350.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 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. AlignAdd to basket

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

        10         20         30         40         50
MASRLTLLTL LLLLLAGDRA SSNPNATSSS SQDPESLQDR GEGKVATTVI
60 70 80 90 100
SKMLFVEPIL EVSSLPTTNS TTNSATKITA NTTDEPTTQP TTEPTTQPTI
110 120 130 140 150
QPTQPTTQLP TDSPTQPTTG SFCPGPVTLC SDLESHSTEA VLGDALVDFS
160 170 180 190 200
LKLYHAFSAM KKVETNMAFS PFSIASLLTQ VLLGAGENTK TNLESILSYP
210 220 230 240 250
KDFTCVHQAL KGFTTKGVTS VSQIFHSPDL AIRDTFVNAS RTLYSSSPRV
260 270 280 290 300
LSNNSDANLE LINTWVAKNT NNKISRLLDS LPSDTRLVLL NAIYLSAKWK
310 320 330 340 350
TTFDPKKTRM EPFHFKNSVI KVPMMNSKKY PVAHFIDQTL KAKVGQLQLS
360 370 380 390 400
HNLSLVILVP QNLKHRLEDM EQALSPSVFK AIMEKLEMSK FQPTLLTLPR
410 420 430 440 450
IKVTTSQDML SIMEKLEFFD FSYDLNLCGL TEDPDLQVSA MQHQTVLELT
460 470 480 490 500
ETGVEAAAAS AISVARTLLV FEVQQPFLFV LWDQQHKFPV FMGRVYDPRA
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 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti103T → S in BAF85743 (PubMed:14702039).Curated1
Sequence conflicti187E → Q in AAB59387 (PubMed:3756141).Curated1
Sequence conflicti306K → R in AAA35613 (PubMed:3488058).Curated1
Sequence conflicti314 – 320HFKNSVI → QLQKLSY AA sequence (PubMed:3458172).Curated7
Sequence conflicti322V → M AA sequence (PubMed:3458172).Curated1
Sequence conflicti332V → L AA sequence (PubMed:3458172).Curated1
Sequence conflicti370 – 375MEQALS → TGTGSQ AA sequence (PubMed:3458172).Curated6
Sequence conflicti417E → V AA sequence (PubMed:3458172).Curated1
Sequence conflicti439S → F AA sequence (PubMed:3458172).Curated1

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_07170111L → R in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication1
Natural variantiVAR_02737439D → E.Corresponds to variant rs11229062dbSNPEnsembl.1
Natural variantiVAR_02737556V → A.2 PublicationsCorresponds to variant rs11546660dbSNPEnsembl.1
Natural variantiVAR_04620284 – 138Missing in HAE; phenotype consistent with hereditary angioedema type 2. 1 PublicationAdd BLAST55
Natural variantiVAR_068832118T → A in HAE. 1 PublicationCorresponds to variant rs200534715dbSNPEnsembl.1
Natural variantiVAR_027379130C → Y in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication1
Natural variantiVAR_068833154Y → C in HAE. 1 PublicationCorresponds to variant rs281875168dbSNPEnsembl.1
Natural variantiVAR_068834170S → F in HAE. 1 PublicationCorresponds to variant rs281875169dbSNPEnsembl.1
Natural variantiVAR_068835184G → R in HAE. 1 PublicationCorresponds to variant rs281875170dbSNPEnsembl.1
Natural variantiVAR_068836230L → P in HAE. 1 PublicationCorresponds to variant rs281875171dbSNPEnsembl.1
Natural variantiVAR_068837232I → K in HAE. 1 PublicationCorresponds to variant rs281875172dbSNPEnsembl.1
Natural variantiVAR_071702265W → R in HAE. 1 Publication1
Natural variantiVAR_068838272Missing in HAE. 1 Publication1
Natural variantiVAR_007012273Missing in HAE; phenotype consistent with hereditary angioedema type 2; creates a new glycosylation site. 1 Publication1
Natural variantiVAR_071703274I → V in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_068839299W → R in HAE. 1 PublicationCorresponds to variant rs281875173dbSNPEnsembl.1
Natural variantiVAR_011751308T → S.Corresponds to variant rs1803212dbSNPEnsembl.1
Natural variantiVAR_027376345G → R in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication1
Natural variantiVAR_027380394T → P in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication1
Natural variantiVAR_027381408D → V in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication1
Natural variantiVAR_007013429G → R in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_068840430L → Q in HAE. 1 PublicationCorresponds to variant rs281875174dbSNPEnsembl.1
Natural variantiVAR_068841441M → T in HAE. 1 PublicationCorresponds to variant rs281875175dbSNPEnsembl.1
Natural variantiVAR_068842447L → P in HAE. 1 PublicationCorresponds to variant rs281875176dbSNPEnsembl.1
Natural variantiVAR_007014454V → E in HAE; phenotype consistent with hereditary angioedema type 2. 1 PublicationCorresponds to variant rs121907949dbSNPEnsembl.1
Natural variantiVAR_007015456A → E in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_007016458A → T in HAE; phenotype consistent with hereditary angioedema type 2. 3 PublicationsCorresponds to variant rs121907947dbSNPEnsembl.1
Natural variantiVAR_007017458A → V in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_007018465A → V in HAE; phenotype consistent with hereditary angioedema type 2. 1 PublicationCorresponds to variant rs121907950dbSNPEnsembl.1
Natural variantiVAR_007019466R → C in HAE; phenotype consistent with hereditary angioedema type 2. 3 PublicationsCorresponds to variant rs28940870dbSNPEnsembl.1
Natural variantiVAR_007020466R → H in HAE; phenotype consistent with hereditary angioedema type 2. 2 PublicationsCorresponds to variant rs121907948dbSNPEnsembl.1
Natural variantiVAR_007021466R → L in HAE; phenotype consistent with hereditary angioedema type 2. 2 PublicationsCorresponds to variant rs121907948dbSNPEnsembl.1
Natural variantiVAR_007022466R → S in HAE; phenotype consistent with hereditary angioedema type 2. 2 PublicationsCorresponds to variant rs28940870dbSNPEnsembl.1
Natural variantiVAR_007023467T → P in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_027382473V → E in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication1
Natural variantiVAR_068843473V → G in HAE. 1 PublicationCorresponds to variant rs281875177dbSNPEnsembl.1
Natural variantiVAR_007024473V → M in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_007025474Q → E.1
Natural variantiVAR_007026477F → S in HAE; phenotype consistent with hereditary angioedema type 2. 1
Natural variantiVAR_007027480V → M.6 PublicationsCorresponds to variant rs4926dbSNPEnsembl.1
Natural variantiVAR_007028481L → P in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_007029481L → R in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_007030489P → R in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_027383493G → E in HAE; phenotype consistent with hereditary angioedema type 1. 2 Publications1
Natural variantiVAR_071704493G → R in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1
Natural variantiVAR_068844497D → G in HAE. 1 PublicationCorresponds to variant rs281875178dbSNPEnsembl.1
Natural variantiVAR_027384498P → R in HAE; phenotype consistent with hereditary angioedema type 1. 1 Publication1
Natural variantiVAR_007031498P → S in HAE; phenotype consistent with hereditary angioedema type 2. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0566621 – 52Missing in isoform 2. 1 PublicationAdd BLAST52
Alternative sequenceiVSP_05666317G → GFLEPQ in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [P05155-1]
PIRiS15386. ITHUC1.
RefSeqiNP_000053.2. NM_000062.2. [P05155-1]
NP_001027466.1. NM_001032295.1. [P05155-1]
UniGeneiHs.384598.

Genome annotation databases

EnsembliENST00000278407; ENSP00000278407; ENSG00000149131. [P05155-1]
ENST00000378323; ENSP00000367574; ENSG00000149131. [P05155-3]
ENST00000378324; ENSP00000367575; ENSG00000149131. [P05155-2]
GeneIDi710.
KEGGihsa:710.
UCSCiuc001nkp.2. human. [P05155-1]

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:
EMBLi
GenBanki
DDBJi
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. [P05155-1]
PIRiS15386. ITHUC1.
RefSeqiNP_000053.2. NM_000062.2. [P05155-1]
NP_001027466.1. NM_001032295.1. [P05155-1]
UniGeneiHs.384598.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1M6Qmodel-A138-500[»]
2OAYX-ray2.35A119-500[»]
5DU3X-ray2.10A/B119-500[»]
5DUQX-ray2.90A/B118-500[»]
ProteinModelPortaliP05155.
SMRiP05155.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107171. 17 interactors.
DIPiDIP-45635N.
IntActiP05155. 7 interactors.
STRINGi9606.ENSP00000278407.

Chemistry databases

DrugBankiDB06404. C1 Esterase Inhibitor (Human).

Protein family/group databases

MEROPSiI04.024.

PTM databases

iPTMnetiP05155.
PhosphoSitePlusiP05155.
UniCarbKBiP05155.

Polymorphism and mutation databases

BioMutaiSERPING1.
DMDMi124096.

Proteomic databases

PaxDbiP05155.
PeptideAtlasiP05155.
PRIDEiP05155.
TopDownProteomicsiP05155-1. [P05155-1]

Protocols and materials databases

DNASUi710.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000278407; ENSP00000278407; ENSG00000149131. [P05155-1]
ENST00000378323; ENSP00000367574; ENSG00000149131. [P05155-3]
ENST00000378324; ENSP00000367575; ENSG00000149131. [P05155-2]
GeneIDi710.
KEGGihsa:710.
UCSCiuc001nkp.2. human. [P05155-1]

Organism-specific databases

CTDi710.
DisGeNETi710.
GeneCardsiSERPING1.
HGNCiHGNC:1228. SERPING1.
HPAiCAB026161.
HPA048738.
MalaCardsiSERPING1.
MIMi106100. phenotype.
606860. gene.
neXtProtiNX_P05155.
OpenTargetsiENSG00000149131.
Orphaneti100050. Hereditary angioedema type 1.
100051. Hereditary angioedema type 2.
169147. Immunodeficiency due to an early component of complement deficiency.
PharmGKBiPA35029.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2392. Eukaryota.
COG4826. LUCA.
GeneTreeiENSGT00850000132312.
HOGENOMiHOG000231936.
HOVERGENiHBG104060.
InParanoidiP05155.
KOiK04001.
PhylomeDBiP05155.
TreeFamiTF317350.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000149131-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-140837. Intrinsic Pathway of Fibrin Clot Formation.

Miscellaneous databases

ChiTaRSiSERPING1. human.
EvolutionaryTraceiP05155.
GeneWikiiC1-inhibitor.
GenomeRNAii710.
PMAP-CutDBP05155.
PROiP05155.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000149131.
ExpressionAtlasiP05155. baseline and differential.
GenevisibleiP05155. HS.

Family and domain databases

InterProiIPR023795. Serpin_CS.
IPR023796. Serpin_dom.
IPR000215. Serpin_fam.
[Graphical view]
PANTHERiPTHR11461. PTHR11461. 1 hit.
PfamiPF00079. Serpin. 1 hit.
[Graphical view]
SMARTiSM00093. SERPIN. 1 hit.
[Graphical view]
SUPFAMiSSF56574. SSF56574. 1 hit.
PROSITEiPS00284. SERPIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 206 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.