C1S
entrez
716
canonical
uniprot
P09871
canonical
ensembl
ENSG00000182326
resolver
ensp
ENSP00000328173
resolver
ensp
ENSP00000354057
resolver
ensp
ENSP00000384171
resolver
ensp
ENSP00000385035
resolver
ensp
ENSP00000527975
resolver
ensp
ENSP00000527982
resolver
ensp
ENSP00000527984
resolver
ensp
ENSP00000626078
resolver
ensp
ENSP00000626079
resolver
ensp
ENSP00000626080
resolver
enst
ENST00000328916
resolver
enst
ENST00000360817
resolver
enst
ENST00000402681
resolver
enst
ENST00000406697
resolver
enst
ENST00000857916
resolver
enst
ENST00000857923
resolver
enst
ENST00000857925
resolver
enst
ENST00000956019
resolver
enst
ENST00000956020
resolver
enst
ENST00000956021
resolver
genesymbol
C1S
resolver
hgnc
HGNC:1247
resolver
uniprot
D3DUT4
resolver
uniprot
F8WCZ6
resolver
uniprot
Q9UCU7
resolver
uniprot
Q9UCU8
resolver
uniprot
Q9UCU9
resolver
uniprot
Q9UCV0
resolver
uniprot
Q9UCV1
resolver
uniprot
Q9UCV2
resolver
uniprot
Q9UCV3
resolver
uniprot
Q9UCV4
resolver
uniprot
Q9UCV5
resolver
uniprot
Q9UM14
resolver
uniprot_entry
C1S_HUMAN
resolver
uniprot_entry
F8WCZ6_HUMAN
resolver
uniprot_sec
D3DUT4
resolver
uniprot_sec
Q9UCU7
resolver
uniprot_sec
Q9UCU8
resolver
uniprot_sec
Q9UCU9
resolver
uniprot_sec
Q9UCV0
resolver
uniprot_sec
Q9UCV1
resolver
uniprot_sec
Q9UCV2
resolver
uniprot_sec
Q9UCV3
resolver
uniprot_sec
Q9UCV4
resolver
uniprot_sec
Q9UCV5
resolver
uniprot_sec
Q9UM14
resolver
activity_regulation
ACTIVITY REGULATION: Cleaved and activated by C1R (PubMed:11445589, PubMed:6271784). Immunoglobulin-binding promotes autoactivation of C1R, which results in the cleavage of the Arg-Ile bond in the catalytic domain (PubMed:11445589, PubMed:6271784). Inhibited by C1 inhibitor (SERPING1) (PubMed:11527969). {ECO:0000269|PubMed:11445589, ECO:0000269|PubMed:11527969, ECO:0000269|PubMed:6271784}.
uniprot
proteins
amino_acid_sequence
MWCIVLFSLLAWVYAEPTMYGEILSPNYPQAYPSEVEKSWDIEVPEGYGIHLYFTHLDIELSENCAYDSVQIISGDTEEGRLCGQRSSNNPHSPIVEEFQVPYNKLQVIFKSDFSNEERFTGFAAYYVATDINECTDFVDVPCSHFCNNFIGGYFCSCPPEYFLHDDMKNCGVNCSGDVFTALIGEIASPNYPKPYPENSRCEYQIRLEKGFQVVVTLRREDFDVEAADSAGNCLDSLVFVAGDRQFGPYCGHGFPGPLNIETKSNALDIIFQTDLTGQKKGWKLRYHGDPMPCPKEDTPNSVWEPAKAKYVFRDVVQITCLDGFEVVEGRVGATSFYSTCQSNGKWSNSKLKCQPVDCGIPESIENGKVEDPESTLFGSVIRYTCEEPYYYMENGGGGEYHCAGNGSWVNEVLGPELPKCVPVCGVPREPFEEKQRIIGGSDADIKNFPWQVFFDNPWAGGALINEYWVLTAAHVVEGNREPTMYVGSTSVQTSRLAKSKMLTPEHVFIHPGWKLLEVPEGRTNFDNDIALVRLKDPVKMGPTVSPICLPGTSSDYNLMDGDLGLISGWGRTEKRDRAVRLKAARLPVAPLRKCKEVKVEKPTADAEAYVFTPNMICAGGEKGMDSCKGDSGGAFAVQDPNDKTKFYAAGLVSWGPQCGTYGLYTRVKNYVDWIMKTMQENSTPRED
uniprot
proteins
disease_involvement
DISEASE: Complement component C1s deficiency (C1SD) [MIM:613783]: A rare defect resulting in C1 deficiency and impaired activation of the complement classical pathway. C1 deficiency generally leads to severe immune complex disease with features of systemic lupus erythematosus and glomerulonephritis. {ECO:0000269|PubMed:11390518}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Ehlers-Danlos syndrome, periodontal type, 2 (EDSPD2) [MIM:617174]: A form of Ehlers-Danlos syndrome, a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDSPD2 is characterized by the association of typical features of Ehlers-Danlos syndrome with gingival recession and severe early-onset periodontal disease, leading to premature loss of permanent teeth. EDSPD2 transmission pattern is consistent with autosomal dominant inheritance. {ECO:0000269|PubMed:27745832}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.4.21.42
uniprot
proteins
function
FUNCTION: Component of the complement C1 complex, a multiprotein complex that initiates the classical pathway of the complement system, a cascade of proteins that leads to phagocytosis and breakdown of pathogens and signaling that strengthens the adaptive immune system (PubMed:11445589, PubMed:16169853, PubMed:417728, PubMed:467643, PubMed:6271784, PubMed:6282646, PubMed:6319179, PubMed:70787, PubMed:9422791). C1S is activated following association of the C1 complex with immunoglobulins (IgG or IgM) complexed with antigens to form antigen-antibody complexes on the surface of pathogens (PubMed:34155115). C1S is cleaved and activated by C1R to generate C1s subcomponent heavy and light chains (PubMed:11445589, PubMed:6271784). C1s subcomponent light chain then cleaves and activates C2 and C4, the next components of the classical complement pathway (PubMed:16169853, PubMed:467643, PubMed:6282646, PubMed:6319179, PubMed:6906228, PubMed:70787, PubMed:9422791). {ECO:0000269|PubMed:11445589, ECO:0000269|PubMed:16169853, ECO:0000269|PubMed:34155115, ECO:0000269|PubMed:417728, ECO:0000269|PubMed:467643, ECO:0000269|PubMed:6271784, ECO:0000269|PubMed:6282646, ECO:0000269|PubMed:6319179, ECO:0000269|PubMed:6906228, ECO:0000269|PubMed:70787, ECO:0000269|PubMed:9422791}.; FUNCTION: [Complement C1s subcomponent light chain]: Serine protease component of the complement C1 complex, which catalyzes cleavage and activation of C2 and C4, the next components of the classical complement pathway (PubMed:16169853, PubMed:22949645, PubMed:417728, PubMed:467643, PubMed:6282646, PubMed:6319179, PubMed:70787, PubMed:9422791). Also able to cleave C1 inhibitor (SERPING1) in vitro; additional evidence is however required to confirm this result in vivo (PubMed:16169853). Also cleaves IGFBP5 and thereby inhibits the trophic effects of IGF1 (PubMed:18930415). {ECO:0000269|PubMed:16169853, ECO:0000269|PubMed:18930415, ECO:0000269|PubMed:22949645, ECO:0000269|PubMed:417728, ECO:0000269|PubMed:467643, ECO:0000269|PubMed:6282646, ECO:0000269|PubMed:6319179, ECO:0000269|PubMed:70787, ECO:0000269|PubMed:9422791}.
uniprot
proteins
mass_dalton
76684
uniprot
proteins
mutagenesis
MUTAGEN 35; /note="E->A: Does not affect association with the C1Q subcomplex."; /evidence="ECO:0000269|PubMed:19473974"; MUTAGEN 60; /note="E->A: Slightly decreased association with the C1Q subcomplex."; /evidence="ECO:0000269|PubMed:19473974"; MUTAGEN 63; /note="E->A: Does not affect association with the C1Q subcomplex."; /evidence="ECO:0000269|PubMed:19473974"; MUTAGEN 67; /note="Y->A: Does not affect association with the C1Q subcomplex."; /evidence="ECO:0000269|PubMed:19473974"; MUTAGEN 113; /note="D->A: Slightly decreased association with the C1Q subcomplex."; /evidence="ECO:0000269|PubMed:19473974"; MUTAGEN 226; /note="E->A: Does not affect association with the C1Q subcomplex."; /evidence="ECO:0000269|PubMed:19473974"; MUTAGEN 275; /note="D->A: Does not affect association with the C1Q subcomplex."; /evidence="ECO:0000269|PubMed:19473974
uniprot
proteins
post_translational_modification
PTM: Cleaved and activated by C1R to generate Complement C1s subcomponent heavy and light chains. {ECO:0000269|PubMed:11445589, ECO:0000269|PubMed:6271784}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:2141278}.
uniprot
proteins
protein_family
Peptidase S1 family
uniprot
proteins
pubmed
10775260
uniprot
proteins
pubmed
11390518
uniprot
proteins
pubmed
11445589
uniprot
proteins
pubmed
11527969
uniprot
proteins
pubmed
12788922
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16169853
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
1854725
uniprot
proteins
pubmed
18930415
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19473974
uniprot
proteins
pubmed
2007122
uniprot
proteins
pubmed
2141278
uniprot
proteins
pubmed
22949645
uniprot
proteins
pubmed
23592783
uniprot
proteins
pubmed
23922389
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2459702
uniprot
proteins
pubmed
2553984
uniprot
proteins
pubmed
27745832
uniprot
proteins
pubmed
28104818
uniprot
proteins
pubmed
2831944
uniprot
proteins
pubmed
29311313
uniprot
proteins
pubmed
2988513
uniprot
proteins
pubmed
2989825
uniprot
proteins
pubmed
3007145
uniprot
proteins
pubmed
34155115
uniprot
proteins
pubmed
3500856
uniprot
proteins
pubmed
417728
uniprot
proteins
pubmed
467643
uniprot
proteins
pubmed
6271784
uniprot
proteins
pubmed
6282646
uniprot
proteins
pubmed
6319179
uniprot
proteins
pubmed
6362661
uniprot
proteins
pubmed
6906228
uniprot
proteins
pubmed
6952210
uniprot
proteins
pubmed
70787
uniprot
proteins
pubmed
7779774
uniprot
proteins
pubmed
869924
uniprot
proteins
pubmed
9422791
uniprot
proteins
pubmed
9794427
uniprot
proteins
sequence_length
688
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3007145}. Cell surface {ECO:0000269|PubMed:34155115}. Note=Recruited to the surface of pathogens by the C1Q subcomplex. {ECO:0000269|PubMed:34155115}.
uniprot
proteins