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Protein

Complement C1s subcomponent

Gene

C1S

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)1 Publication

    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

    • calcium ion binding Source: InterPro
    • identical protein binding Source: IntAct
    • serine-type endopeptidase activity Source: UniProtKB

    GO - Biological processi

    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

    BRENDAi3.4.21.42. 2681.
    ReactomeiREACT_7956. Classical antibody-mediated complement activation.
    REACT_8024. Initial triggering of complement.
    SABIO-RKP09871.

    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 Componenti: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:1247. C1S.

    Subcellular locationi

    GO - Cellular componenti

    • blood microparticle Source: UniProtKB
    • extracellular exosome Source: UniProtKB
    • extracellular region Source: Reactome
    Complete GO annotation...

    Pathology & Biotechi

    Involvement in diseasei

    Complement component C1s deficiency (C1SD)1 Publication

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

    Disease descriptionA 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.

    See also OMIM:613783

    Organism-specific databases

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

    Chemistry

    DrugBankiDB00054. Abciximab.
    DB00051. Adalimumab.
    DB00074. Basiliximab.
    DB00002. Cetuximab.
    DB00005. Etanercept.
    DB00056. Gemtuzumab ozogamicin.
    DB00078. Ibritumomab.
    DB00075. Muromonab.
    DB00073. Rituximab.
    DB00072. Trastuzumab.

    Polymorphism and mutation databases

    BioMutaiC1S.
    DMDMi115205.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 15151 PublicationAdd
    BLAST
    Chaini16 – 688673Complement C1s subcomponentPRO_0000027586Add
    BLAST
    Chaini16 – 437422Complement C1s subcomponent heavy chainPRO_0000027587Add
    BLAST
    Chaini438 – 688251Complement C1s subcomponent light chainPRO_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)PROSITE-ProRule annotation1 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.1 Publication

    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

    BgeeiP09871.
    ExpressionAtlasiP09871. baseline and differential.
    GenevisibleiP09871. HS.

    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

    1
    688
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi19 – 246Combined sources
    Turni26 – 294Combined sources
    Beta strandi34 – 4310Combined sources
    Beta strandi48 – 5811Combined sources
    Helixi63 – 653Combined sources
    Beta strandi67 – 737Combined sources
    Beta strandi75 – 773Combined sources
    Beta strandi80 – 823Combined sources
    Beta strandi84 – 863Combined sources
    Beta strandi96 – 11217Combined sources
    Beta strandi122 – 13110Combined sources
    Turni134 – 1363Combined sources
    Beta strandi137 – 1404Combined sources
    Beta strandi143 – 1508Combined sources
    Beta strandi153 – 1575Combined sources
    Beta strandi162 – 1643Combined sources
    Beta strandi171 – 1733Combined sources
    Beta strandi176 – 1805Combined sources
    Beta strandi182 – 1887Combined sources
    Turni190 – 1934Combined sources
    Beta strandi201 – 2077Combined sources
    Beta strandi212 – 2176Combined sources
    Helixi220 – 2223Combined sources
    Beta strandi223 – 2253Combined sources
    Beta strandi235 – 2428Combined sources
    Beta strandi245 – 2506Combined sources
    Beta strandi252 – 2543Combined sources
    Beta strandi259 – 2624Combined sources
    Beta strandi265 – 2739Combined sources
    Beta strandi282 – 29110Combined sources
    Beta strandi300 – 3067Combined sources
    Beta strandi309 – 3124Combined sources
    Beta strandi316 – 3216Combined sources
    Beta strandi325 – 3317Combined sources
    Beta strandi334 – 3418Combined sources
    Turni348 – 3514Combined sources
    Beta strandi353 – 3564Combined sources
    Beta strandi368 – 3703Combined sources
    Beta strandi381 – 3866Combined sources
    Turni388 – 3903Combined sources
    Beta strandi391 – 3933Combined sources
    Beta strandi395 – 3973Combined sources
    Beta strandi399 – 4035Combined sources
    Turni405 – 4073Combined sources
    Beta strandi409 – 4113Combined sources
    Turni412 – 4143Combined sources
    Beta strandi421 – 4233Combined sources
    Helixi446 – 4483Combined sources
    Beta strandi452 – 4554Combined sources
    Turni456 – 4594Combined sources
    Beta strandi460 – 4667Combined sources
    Beta strandi469 – 4724Combined sources
    Helixi474 – 4774Combined sources
    Beta strandi490 – 4923Combined sources
    Helixi494 – 4996Combined sources
    Beta strandi505 – 5106Combined sources
    Helixi520 – 5223Combined sources
    Beta strandi531 – 5377Combined sources
    Helixi555 – 5573Combined sources
    Beta strandi564 – 5707Combined sources
    Beta strandi576 – 5783Combined sources
    Beta strandi583 – 5908Combined sources
    Helixi592 – 5965Combined sources
    Beta strandi616 – 6205Combined sources
    Helixi627 – 6293Combined sources
    Beta strandi635 – 6395Combined sources
    Beta strandi647 – 6559Combined sources
    Beta strandi661 – 6677Combined sources
    Helixi668 – 6714Combined sources
    Helixi672 – 68110Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09871.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 130115CUB 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini131 – 17242EGF-like; calcium-bindingAdd
    BLAST
    Domaini175 – 290116CUB 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini292 – 35665Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini357 – 42367Sushi 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini438 – 680243Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 2 CUB domains.PROSITE-ProRule annotation
    Contains 1 EGF-like domain.Curated
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
    Contains 2 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal, Sushi

    Phylogenomic databases

    eggNOGiCOG5640.
    GeneTreeiENSGT00760000118890.
    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_dom.
    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

            10         20         30         40         50
    MWCIVLFSLL AWVYAEPTMY GEILSPNYPQ AYPSEVEKSW DIEVPEGYGI
    60 70 80 90 100
    HLYFTHLDIE LSENCAYDSV QIISGDTEEG RLCGQRSSNN PHSPIVEEFQ
    110 120 130 140 150
    VPYNKLQVIF KSDFSNEERF TGFAAYYVAT DINECTDFVD VPCSHFCNNF
    160 170 180 190 200
    IGGYFCSCPP EYFLHDDMKN CGVNCSGDVF TALIGEIASP NYPKPYPENS
    210 220 230 240 250
    RCEYQIRLEK GFQVVVTLRR EDFDVEAADS AGNCLDSLVF VAGDRQFGPY
    260 270 280 290 300
    CGHGFPGPLN IETKSNALDI IFQTDLTGQK KGWKLRYHGD PMPCPKEDTP
    310 320 330 340 350
    NSVWEPAKAK YVFRDVVQIT CLDGFEVVEG RVGATSFYST CQSNGKWSNS
    360 370 380 390 400
    KLKCQPVDCG IPESIENGKV EDPESTLFGS VIRYTCEEPY YYMENGGGGE
    410 420 430 440 450
    YHCAGNGSWV NEVLGPELPK CVPVCGVPRE PFEEKQRIIG GSDADIKNFP
    460 470 480 490 500
    WQVFFDNPWA GGALINEYWV LTAAHVVEGN REPTMYVGST SVQTSRLAKS
    510 520 530 540 550
    KMLTPEHVFI HPGWKLLEVP EGRTNFDNDI ALVRLKDPVK MGPTVSPICL
    560 570 580 590 600
    PGTSSDYNLM DGDLGLISGW GRTEKRDRAV RLKAARLPVA PLRKCKEVKV
    610 620 630 640 650
    EKPTADAEAY VFTPNMICAG GEKGMDSCKG DSGGAFAVQD PNDKTKFYAA
    660 670 680
    GLVSWGPQCG TYGLYTRVKN YVDWIMKTMQ ENSTPRED
    Length:688
    Mass (Da):76,684
    Last modified:July 1, 1989 - v1
    Checksum:i85522647A4C47205
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti294 – 2941C → K AA sequence (PubMed:3007145).Curated
    Sequence conflicti513 – 5131G → GG (PubMed:2553984).Curated
    Sequence conflicti573 – 5731T → A AA sequence (PubMed:6362661).Curated
    Sequence conflicti645 – 6462TK → GR AA sequence (PubMed:6362661).Curated

    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 databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.
    GeneIDi716.
    KEGGihsa:716.
    UCSCiuc001qsj.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    C1Sbase

    C1S mutation db

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

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

    Chemistry

    BindingDBiP09871.
    ChEMBLiCHEMBL3913.
    DrugBankiDB00054. Abciximab.
    DB00051. Adalimumab.
    DB00074. Basiliximab.
    DB00002. Cetuximab.
    DB00005. Etanercept.
    DB00056. Gemtuzumab ozogamicin.
    DB00078. Ibritumomab.
    DB00075. Muromonab.
    DB00073. Rituximab.
    DB00072. Trastuzumab.

    Protein family/group databases

    MEROPSiS01.193.

    PTM databases

    PhosphoSiteiP09871.

    Polymorphism and mutation databases

    BioMutaiC1S.
    DMDMi115205.

    2D gel databases

    SWISS-2DPAGEP09871.

    Proteomic databases

    MaxQBiP09871.
    PaxDbiP09871.
    PeptideAtlasiP09871.
    PRIDEiP09871.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000328916; ENSP00000328173; ENSG00000182326.
    ENST00000360817; ENSP00000354057; ENSG00000182326.
    ENST00000406697; ENSP00000385035; ENSG00000182326.
    GeneIDi716.
    KEGGihsa:716.
    UCSCiuc001qsj.3. human.

    Organism-specific databases

    CTDi716.
    GeneCardsiGC12P007096.
    HGNCiHGNC:1247. C1S.
    HPAiCAB016722.
    HPA018852.
    MIMi120580. gene.
    613783. phenotype.
    neXtProtiNX_P09871.
    Orphaneti169147. Immunodeficiency due to an early component of complement deficiency.
    PharmGKBiPA25636.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG5640.
    GeneTreeiENSGT00760000118890.
    HOVERGENiHBG000559.
    InParanoidiP09871.
    KOiK01331.
    OMAiPTMYGEI.
    PhylomeDBiP09871.
    TreeFamiTF330373.

    Enzyme and pathway databases

    BRENDAi3.4.21.42. 2681.
    ReactomeiREACT_7956. Classical antibody-mediated complement activation.
    REACT_8024. Initial triggering of complement.
    SABIO-RKP09871.

    Miscellaneous databases

    ChiTaRSiC1S. human.
    EvolutionaryTraceiP09871.
    GeneWikiiC1S.
    GenomeRNAii716.
    NextBioi2912.
    PMAP-CutDBP09871.
    PROiP09871.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP09871.
    ExpressionAtlasiP09871. baseline and differential.
    GenevisibleiP09871. HS.

    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_dom.
    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]
    ProtoNetiSearch...

    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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    19. "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.
    20. "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: June 24, 2015
    This is version 196 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

    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 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.