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P09871

- C1S_HUMAN

UniProt

P09871 - C1S_HUMAN

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Protein
Complement C1s subcomponent
Gene
C1S
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

C1s B chain is a serine protease that combines with C1q and C1r to form C1, the first component of the classical pathway of the complement system. C1r activates C1s so that it can, in turn, activate C2 and C4.

Catalytic activityi

Cleavage of Arg-|-Ala bond in complement component C4 to form C4a and C4b, and Lys(or Arg)-|-Lys bond in complement component C2 to form C2a and C2b: the 'classical' pathway C3 convertase.1 Publication

Enzyme regulationi

Inhibited by SERPING1.1 Publication

Kineticsi

Less efficient than MASP2 in C4 cleavage.

  1. KM=12.3 µM for complement component C2 (at 37 degrees Celsius)1 Publication
  2. KM=1.9 µM for complement component C4 (at 37 degrees Celsius)

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi60 – 601Calcium
Metal bindingi68 – 681Calcium
Metal bindingi113 – 1131Calcium
Metal bindingi131 – 1311Calcium
Metal bindingi132 – 1321Calcium; via carbonyl oxygen
Metal bindingi134 – 1341Calcium
Metal bindingi149 – 1491Calcium
Metal bindingi150 – 1501Calcium; via carbonyl oxygen
Metal bindingi153 – 1531Calcium; via carbonyl oxygen
Active sitei475 – 4751Charge relay system
Active sitei529 – 5291Charge relay system
Active sitei632 – 6321Charge relay system

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. identical protein binding Source: IntAct
  3. protein binding Source: IntAct
  4. serine-type endopeptidase activity Source: UniProtKB

GO - Biological processi

  1. complement activation Source: Reactome
  2. complement activation, classical pathway Source: Reactome
  3. innate immune response Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Complement pathway, Immunity, Innate immunity

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_7956. Classical antibody-mediated complement activation.
REACT_8024. Initial triggering of complement.

Protein family/group databases

MEROPSiS01.193.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement C1s subcomponent (EC:3.4.21.42)
Alternative name(s):
C1 esterase
Complement component 1 subcomponent s
Cleaved into the following 2 chains:
Gene namesi
Name:C1S
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:1247. C1S.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. extracellular region Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Organism-specific databases

MIMi613783. phenotype.
Orphaneti169147. Immunodeficiency due to an early component of complement deficiency.
PharmGKBiPA25636.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 15151 Publication
Add
BLAST
Chaini16 – 688673Complement C1s subcomponent
PRO_0000027586Add
BLAST
Chaini16 – 437422Complement C1s subcomponent heavy chain
PRO_0000027587Add
BLAST
Chaini438 – 688251Complement C1s subcomponent light chain
PRO_0000027588Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi65 ↔ 831 Publication
Disulfide bondi135 ↔ 1471 Publication
Disulfide bondi143 ↔ 1561 Publication
Modified residuei149 – 1491(3R)-3-hydroxyasparagine1 Publication
Disulfide bondi158 ↔ 1711 Publication
Glycosylationi174 – 1741N-linked (GlcNAc...)2 Publications
Disulfide bondi175 ↔ 2021 Publication
Disulfide bondi234 ↔ 2511 Publication
Disulfide bondi294 ↔ 3411 Publication
Disulfide bondi321 ↔ 3541 Publication
Disulfide bondi359 ↔ 4031 Publication
Disulfide bondi386 ↔ 4211 Publication
Glycosylationi406 – 4061N-linked (GlcNAc...)3 Publications
Disulfide bondi425 ↔ 549Interchain (between heavy and light chains)1 Publication
Disulfide bondi595 ↔ 6181 Publication
Disulfide bondi628 ↔ 6591 Publication

Post-translational modificationi

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiP09871.
PaxDbiP09871.
PeptideAtlasiP09871.
PRIDEiP09871.

2D gel databases

SWISS-2DPAGEP09871.

PTM databases

PhosphoSiteiP09871.

Miscellaneous databases

PMAP-CutDBP09871.

Expressioni

Gene expression databases

ArrayExpressiP09871.
BgeeiP09871.
GenevestigatoriP09871.

Organism-specific databases

HPAiCAB016722.
HPA018852.

Interactioni

Subunit structurei

C1 is a calcium-dependent trimolecular complex of C1q, C1r and C1s in the molar ration of 1:2:2. Activated C1s is an disulfide-linked heterodimer of a heavy chain and a light chain.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-2810045,EBI-2810045
C1RP007363EBI-2810045,EBI-3926504

Protein-protein interaction databases

BioGridi107177. 7 interactions.
IntActiP09871. 8 interactions.
MINTiMINT-4655918.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi19 – 246
Turni26 – 294
Beta strandi34 – 4310
Beta strandi48 – 5811
Helixi63 – 653
Beta strandi67 – 737
Beta strandi80 – 823
Beta strandi84 – 863
Beta strandi96 – 11217
Beta strandi122 – 13110
Turni134 – 1363
Beta strandi137 – 1404
Beta strandi143 – 1508
Beta strandi153 – 1575
Beta strandi162 – 1643
Beta strandi171 – 1733
Beta strandi176 – 1805
Beta strandi182 – 1887
Turni190 – 1934
Beta strandi201 – 2077
Beta strandi212 – 2176
Helixi220 – 2223
Beta strandi223 – 2253
Beta strandi235 – 2428
Beta strandi245 – 2506
Beta strandi252 – 2543
Beta strandi259 – 2624
Beta strandi265 – 2739
Beta strandi282 – 29110
Beta strandi300 – 3067
Beta strandi309 – 3124
Beta strandi316 – 3216
Beta strandi325 – 3317
Beta strandi334 – 3418
Turni348 – 3514
Beta strandi353 – 3564
Beta strandi368 – 3703
Beta strandi381 – 3866
Turni388 – 3903
Beta strandi391 – 3933
Beta strandi395 – 3973
Beta strandi399 – 4035
Turni405 – 4073
Beta strandi409 – 4113
Turni412 – 4143
Beta strandi421 – 4233
Helixi446 – 4483
Beta strandi452 – 4554
Turni456 – 4594
Beta strandi460 – 4667
Beta strandi469 – 4724
Helixi474 – 4774
Beta strandi490 – 4923
Helixi494 – 4996
Beta strandi505 – 5106
Helixi520 – 5223
Beta strandi531 – 5377
Helixi555 – 5573
Beta strandi564 – 5707
Beta strandi576 – 5783
Beta strandi583 – 5908
Helixi592 – 5965
Beta strandi616 – 6205
Helixi627 – 6293
Beta strandi635 – 6395
Beta strandi647 – 6559
Beta strandi661 – 6677
Helixi668 – 6714
Helixi672 – 68110

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ELVX-ray1.70A356-688[»]
1NZIX-ray1.50A/B16-174[»]
4J1YX-ray2.66A/B292-688[»]
4LMFX-ray2.92A/B/C/D17-292[»]
4LORX-ray2.50A17-292[»]
4LOSX-ray2.00A172-358[»]
4LOTX-ray2.92A175-423[»]
ProteinModelPortaliP09871.
SMRiP09871. Positions 17-684.

Miscellaneous databases

EvolutionaryTraceiP09871.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 130115CUB 1
Add
BLAST
Domaini131 – 17242EGF-like; calcium-binding
Add
BLAST
Domaini175 – 290116CUB 2
Add
BLAST
Domaini292 – 35665Sushi 1
Add
BLAST
Domaini357 – 42367Sushi 2
Add
BLAST
Domaini438 – 680243Peptidase S1
Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.
Contains 2 CUB domains.
Contains 1 EGF-like domain.

Keywords - Domaini

EGF-like domain, Repeat, Signal, Sushi

Phylogenomic databases

eggNOGiCOG5640.
HOVERGENiHBG000559.
InParanoidiP09871.
KOiK01331.
OMAiPTMYGEI.
PhylomeDBiP09871.
TreeFamiTF330373.

Family and domain databases

Gene3Di2.60.120.290. 2 hits.
InterProiIPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024175. Pept_S1A_C1r/C1S/mannan-bd.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamiPF00431. CUB. 2 hits.
PF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001155. C1r_C1s_MASP. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00032. CCP. 2 hits.
SM00042. CUB. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF49854. SSF49854. 2 hits.
SSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEiPS00010. ASX_HYDROXYL. 1 hit.
PS01180. CUB. 2 hits.
PS01187. EGF_CA. 1 hit.
PS50923. SUSHI. 2 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P09871-1 [UniParc]FASTAAdd to Basket

« Hide

MWCIVLFSLL AWVYAEPTMY GEILSPNYPQ AYPSEVEKSW DIEVPEGYGI    50
HLYFTHLDIE LSENCAYDSV QIISGDTEEG RLCGQRSSNN PHSPIVEEFQ 100
VPYNKLQVIF KSDFSNEERF TGFAAYYVAT DINECTDFVD VPCSHFCNNF 150
IGGYFCSCPP EYFLHDDMKN CGVNCSGDVF TALIGEIASP NYPKPYPENS 200
RCEYQIRLEK GFQVVVTLRR EDFDVEAADS AGNCLDSLVF VAGDRQFGPY 250
CGHGFPGPLN IETKSNALDI IFQTDLTGQK KGWKLRYHGD PMPCPKEDTP 300
NSVWEPAKAK YVFRDVVQIT CLDGFEVVEG RVGATSFYST CQSNGKWSNS 350
KLKCQPVDCG IPESIENGKV EDPESTLFGS VIRYTCEEPY YYMENGGGGE 400
YHCAGNGSWV NEVLGPELPK CVPVCGVPRE PFEEKQRIIG GSDADIKNFP 450
WQVFFDNPWA GGALINEYWV LTAAHVVEGN REPTMYVGST SVQTSRLAKS 500
KMLTPEHVFI HPGWKLLEVP EGRTNFDNDI ALVRLKDPVK MGPTVSPICL 550
PGTSSDYNLM DGDLGLISGW GRTEKRDRAV RLKAARLPVA PLRKCKEVKV 600
EKPTADAEAY VFTPNMICAG GEKGMDSCKG DSGGAFAVQD PNDKTKFYAA 650
GLVSWGPQCG TYGLYTRVKN YVDWIMKTMQ ENSTPRED 688
Length:688
Mass (Da):76,684
Last modified:July 1, 1989 - v1
Checksum:i85522647A4C47205
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti119 – 1191R → H.
Corresponds to variant rs12146727 [ dbSNP | Ensembl ].
VAR_033643
Natural varianti327 – 3271V → L.
Corresponds to variant rs2239170 [ dbSNP | Ensembl ].
VAR_033644
Natural varianti383 – 3831R → H.
Corresponds to variant rs20573 [ dbSNP | Ensembl ].
VAR_014565

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti294 – 2941C → K AA sequence 1 Publication
Sequence conflicti513 – 5131G → GG1 Publication
Sequence conflicti573 – 5731T → A AA sequence 1 Publication
Sequence conflicti645 – 6462TK → GR AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06596 mRNA. Translation: CAA29817.1.
M18767 mRNA. Translation: AAA51853.1.
J04080 mRNA. Translation: AAA51852.1.
CH471116 Genomic DNA. Translation: EAW88689.1.
CH471116 Genomic DNA. Translation: EAW88690.1.
BC056903 mRNA. Translation: AAH56903.1.
AB009076 Genomic DNA. Translation: BAA86864.1.
CCDSiCCDS31735.1.
PIRiA40496. C1HUS.
RefSeqiNP_001725.1. NM_001734.3.
NP_958850.1. NM_201442.2.
XP_005253817.1. XM_005253760.1.
UniGeneiHs.458355.

Genome annotation databases

EnsembliENST00000328916; ENSP00000328173; ENSG00000182326.
ENST00000360817; ENSP00000354057; ENSG00000182326.
ENST00000406697; ENSP00000385035; ENSG00000182326.
ENST00000594877; ENSP00000471707; ENSG00000269882.
ENST00000595575; ENSP00000469947; ENSG00000269882.
ENST00000600933; ENSP00000469899; ENSG00000269882.
GeneIDi716.
KEGGihsa:716.
UCSCiuc001qsj.3. human.

Polymorphism databases

DMDMi115205.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

C1Sbase

C1S mutation db

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X06596 mRNA. Translation: CAA29817.1 .
M18767 mRNA. Translation: AAA51853.1 .
J04080 mRNA. Translation: AAA51852.1 .
CH471116 Genomic DNA. Translation: EAW88689.1 .
CH471116 Genomic DNA. Translation: EAW88690.1 .
BC056903 mRNA. Translation: AAH56903.1 .
AB009076 Genomic DNA. Translation: BAA86864.1 .
CCDSi CCDS31735.1.
PIRi A40496. C1HUS.
RefSeqi NP_001725.1. NM_001734.3.
NP_958850.1. NM_201442.2.
XP_005253817.1. XM_005253760.1.
UniGenei Hs.458355.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ELV X-ray 1.70 A 356-688 [» ]
1NZI X-ray 1.50 A/B 16-174 [» ]
4J1Y X-ray 2.66 A/B 292-688 [» ]
4LMF X-ray 2.92 A/B/C/D 17-292 [» ]
4LOR X-ray 2.50 A 17-292 [» ]
4LOS X-ray 2.00 A 172-358 [» ]
4LOT X-ray 2.92 A 175-423 [» ]
ProteinModelPortali P09871.
SMRi P09871. Positions 17-684.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107177. 7 interactions.
IntActi P09871. 8 interactions.
MINTi MINT-4655918.

Chemistry

BindingDBi P09871.
ChEMBLi CHEMBL3913.
DrugBanki DB00054. Abciximab.
DB00051. Adalimumab.
DB00074. Basiliximab.
DB00002. Cetuximab.
DB00005. Etanercept.
DB00056. Gemtuzumab ozogamicin.
DB00078. Ibritumomab.
DB00028. Immune globulin.
DB00075. Muromonab.
DB00073. Rituximab.
DB00072. Trastuzumab.

Protein family/group databases

MEROPSi S01.193.

PTM databases

PhosphoSitei P09871.

Polymorphism databases

DMDMi 115205.

2D gel databases

SWISS-2DPAGE P09871.

Proteomic databases

MaxQBi P09871.
PaxDbi P09871.
PeptideAtlasi P09871.
PRIDEi P09871.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000328916 ; ENSP00000328173 ; ENSG00000182326 .
ENST00000360817 ; ENSP00000354057 ; ENSG00000182326 .
ENST00000406697 ; ENSP00000385035 ; ENSG00000182326 .
ENST00000594877 ; ENSP00000471707 ; ENSG00000269882 .
ENST00000595575 ; ENSP00000469947 ; ENSG00000269882 .
ENST00000600933 ; ENSP00000469899 ; ENSG00000269882 .
GeneIDi 716.
KEGGi hsa:716.
UCSCi uc001qsj.3. human.

Organism-specific databases

CTDi 716.
GeneCardsi GC12P007096.
HGNCi HGNC:1247. C1S.
HPAi CAB016722.
HPA018852.
MIMi 120580. gene.
613783. phenotype.
neXtProti NX_P09871.
Orphaneti 169147. Immunodeficiency due to an early component of complement deficiency.
PharmGKBi PA25636.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5640.
HOVERGENi HBG000559.
InParanoidi P09871.
KOi K01331.
OMAi PTMYGEI.
PhylomeDBi P09871.
TreeFami TF330373.

Enzyme and pathway databases

Reactomei REACT_7956. Classical antibody-mediated complement activation.
REACT_8024. Initial triggering of complement.

Miscellaneous databases

ChiTaRSi C1S. human.
EvolutionaryTracei P09871.
GeneWikii C1S.
GenomeRNAii 716.
NextBioi 2912.
PMAP-CutDB P09871.
PROi P09871.
SOURCEi Search...

Gene expression databases

ArrayExpressi P09871.
Bgeei P09871.
Genevestigatori P09871.

Family and domain databases

Gene3Di 2.60.120.290. 2 hits.
InterProi IPR000859. CUB_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR024175. Pept_S1A_C1r/C1S/mannan-bd.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view ]
Pfami PF00431. CUB. 2 hits.
PF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PIRSFi PIRSF001155. C1r_C1s_MASP. 1 hit.
PRINTSi PR00722. CHYMOTRYPSIN.
SMARTi SM00032. CCP. 2 hits.
SM00042. CUB. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF49854. SSF49854. 2 hits.
SSF50494. SSF50494. 1 hit.
SSF57535. SSF57535. 2 hits.
PROSITEi PS00010. ASX_HYDROXYL. 1 hit.
PS01180. CUB. 2 hits.
PS01187. EGF_CA. 1 hit.
PS50923. SUSHI. 2 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of cDNA for human complement component C1s. The complete amino acid sequence."
    McKinnon C.M., Carter P.E., Smyth S.J., Dunbar B., Fothergill J.E.
    Eur. J. Biochem. 169:547-553(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Complete cDNA sequence of human complement Cls and close physical linkage of the homologous genes Cls and Clr."
    Tosi M., Duponchel C., Meo T., Julier C.
    Biochemistry 26:8516-8524(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Human genes for complement components C1r and C1s in a close tail-to-tail arrangement."
    Kusumoto H., Hirosawa S., Salier J.-P., Hagen F.S., Kurachi K.
    Proc. Natl. Acad. Sci. U.S.A. 85:7307-7311(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: PNS.
  6. "Two lineages of mannose-binding lectin-associated serine protease (MASP) in vertebrates."
    Endo Y., Takahashi M., Nakao M., Saiga H., Sekine H., Matsushita M., Nonaka M., Fujita T.
    J. Immunol. 161:4924-4930(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-329.
    Tissue: Peripheral blood leukocyte.
  7. "Complement genes C1r and C1s feature an intronless serine protease domain closely related to haptoglobin."
    Tosi M., Duponchel C., Meo T., Couture-Tosi E.
    J. Mol. Biol. 208:709-714(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 291-688.
  8. "Human complement component C1s. Partial sequence determination of the heavy chain and identification of the peptide bond cleaved during activation."
    Spycher S.E., Nick H., Rickli E.E.
    Eur. J. Biochem. 156:49-57(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 16-61; 168-219; 287-334 AND 384-445.
  9. "The serine proteinase chain of human complement component C1s. Cyanogen bromide cleavage and N-terminal sequences of the fragments."
    Carter P.E., Dunbar B., Fothergill J.E.
    Biochem. J. 215:565-571(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 438-500; 503-534; 542-601; 617-623 AND 626-656.
  10. "Chemical and functional characterization of a fragment of C1-s containing the epidermal growth factor homology region."
    Thielens N.M., van Dorsselaer A., Gagnon J., Arlaud G.J.
    Biochemistry 29:3570-3578(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT ASN-174, HYDROXYLATION AT ASN-149.
  11. "Effect of lactoperoxidase-catalyzed iodination on the Ca(2+)-dependent interactions of human C1s. Location of the iodination sites."
    Illy C., Thielens N.M., Gagnon J., Arlaud G.J.
    Biochemistry 30:7135-7141(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Plasma.
  12. "Identification of the disulfide bonds of human complement C1s."
    Hess D., Schaller J., Rickli E.E.
    Biochemistry 30:2827-2833(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISULFIDE BONDS.
  13. "Structure of the catalytic region of human complement protease C1s: study by chemical cross-linking and three-dimensional homology modeling."
    Rossi V., Gaboriaud C., Lacroix M., Ulrich J., Fontecilla-Camps J.-C., Gagnon J., Arlaud G.J.
    Biochemistry 34:7311-7321(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, 3D-STRUCTURE MODELING OF CATALYTIC DOMAIN.
  14. "Substrate specificities of recombinant mannan-binding lectin-associated serine proteases-1 and -2."
    Rossi V., Cseh S., Bally I., Thielens N.M., Jensenius J.C., Arlaud G.J.
    J. Biol. Chem. 276:40880-40887(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
  15. "Molecular basis of a selective C1s deficiency associated with early onset multiple autoimmune diseases."
    Dragon-Durey M.-A., Quartier P., Fremeaux-Bacchi V., Blouin J., de Barace C., Prieur A.-M., Weiss L., Fridman W.-H.
    J. Immunol. 166:7612-7616(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN COMPLEMENT COMPONENT C1S DEFICIENCY.
  16. "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-406.
    Tissue: Plasma.
  17. "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-174 AND ASN-406.
    Tissue: Liver.
  18. "Crystal structure of the catalytic domain of human complement c1s: a serine protease with a handle."
    Gaboriaud C., Rossi V., Bally I., Arlaud G.J., Fontecilla-Camps J.-C.
    EMBO J. 19:1755-1765(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 358-688.
  19. "X-ray structure of the Ca2+-binding interaction domain of C1s. Insights into the assembly of the C1 complex of complement."
    Gregory L.A., Thielens N.M., Arlaud G.J., Fontecilla-Camps J.-C., Gaboriaud C.
    J. Biol. Chem. 278:32157-32164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 16-174, CALCIUM-BINDING SITES, GLYCOSYLATION AT ASN-406.

Entry informationi

Entry nameiC1S_HUMAN
AccessioniPrimary (citable) accession number: P09871
Secondary accession number(s): D3DUT4
, Q9UCU7, Q9UCU8, Q9UCU9, Q9UCV0, Q9UCV1, Q9UCV2, Q9UCV3, Q9UCV4, Q9UCV5, Q9UM14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: September 3, 2014
This is version 187 of the entry and version 1 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 12
    Human chromosome 12: 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. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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