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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)DescriptionActionsGraphical viewLength
    Metal bindingi60Calcium1
    Metal bindingi68Calcium1
    Metal bindingi113Calcium1
    Metal bindingi131Calcium1
    Metal bindingi132Calcium; via carbonyl oxygen1
    Metal bindingi134Calcium1
    Metal bindingi149Calcium1
    Metal bindingi150Calcium; via carbonyl oxygen1
    Metal bindingi153Calcium; via carbonyl oxygen1
    Active sitei475Charge relay system1
    Active sitei529Charge relay system1
    Active sitei632Charge relay system1

    GO - Molecular functioni

    • calcium ion binding Source: InterPro
    • 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

    BioCyciZFISH:HS00050-MONOMER.
    BRENDAi3.4.21.42. 2681.
    ReactomeiR-HSA-166663. Initial triggering of complement.
    R-HSA-173623. Classical antibody-mediated complement activation.
    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
    Proteomesi
    • UP000005640 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

    DisGeNETi716.
    MalaCardsiC1S.
    MIMi613783. phenotype.
    OpenTargetsiENSG00000182326.
    Orphaneti169147. Immunodeficiency due to an early component of complement deficiency.
    PharmGKBiPA25636.

    Chemistry databases

    ChEMBLiCHEMBL3913.
    DrugBankiDB00054. Abciximab.
    DB00051. Adalimumab.
    DB00074. Basiliximab.
    DB00002. Cetuximab.
    DB00005. Etanercept.
    DB00056. Gemtuzumab ozogamicin.
    DB00078. Ibritumomab.
    DB00075. Muromonab.
    DB00073. Rituximab.
    DB00072. Trastuzumab.
    GuidetoPHARMACOLOGYi2335.

    Polymorphism and mutation databases

    BioMutaiC1S.
    DMDMi115205.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 151 PublicationAdd BLAST15
    ChainiPRO_000002758616 – 688Complement C1s subcomponentAdd BLAST673
    ChainiPRO_000002758716 – 437Complement C1s subcomponent heavy chainAdd BLAST422
    ChainiPRO_0000027588438 – 688Complement C1s subcomponent light chainAdd BLAST251

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi65 ↔ 831 Publication
    Disulfide bondi135 ↔ 1471 Publication
    Disulfide bondi143 ↔ 1561 Publication
    Modified residuei149(3R)-3-hydroxyasparagine1 Publication1
    Disulfide bondi158 ↔ 1711 Publication
    Glycosylationi174N-linked (GlcNAc...)2 Publications1
    Disulfide bondi175 ↔ 2021 Publication
    Disulfide bondi234 ↔ 2511 Publication
    Disulfide bondi294 ↔ 3411 Publication
    Disulfide bondi321 ↔ 3541 Publication
    Disulfide bondi359 ↔ 4031 Publication
    Disulfide bondi386 ↔ 4211 Publication
    Glycosylationi406N-linked (GlcNAc...)3 Publications1
    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

    iPTMnetiP09871.
    PhosphoSitePlusiP09871.

    Miscellaneous databases

    PMAP-CutDBP09871.

    Expressioni

    Gene expression databases

    BgeeiENSG00000182326.
    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
    C1RP007364EBI-2810045,EBI-3926504

    Protein-protein interaction databases

    BioGridi107177. 8 interactors.
    IntActiP09871. 8 interactors.
    MINTiMINT-4655918.
    STRINGi9606.ENSP00000328173.

    Chemistry databases

    BindingDBiP09871.

    Structurei

    Secondary structure

    1688
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi19 – 24Combined sources6
    Turni26 – 29Combined sources4
    Beta strandi34 – 43Combined sources10
    Beta strandi48 – 58Combined sources11
    Helixi63 – 65Combined sources3
    Beta strandi67 – 73Combined sources7
    Beta strandi75 – 77Combined sources3
    Beta strandi80 – 82Combined sources3
    Beta strandi84 – 86Combined sources3
    Beta strandi96 – 112Combined sources17
    Beta strandi122 – 131Combined sources10
    Turni134 – 136Combined sources3
    Beta strandi137 – 140Combined sources4
    Beta strandi143 – 150Combined sources8
    Beta strandi153 – 157Combined sources5
    Beta strandi162 – 164Combined sources3
    Beta strandi171 – 173Combined sources3
    Beta strandi176 – 180Combined sources5
    Beta strandi182 – 188Combined sources7
    Turni190 – 193Combined sources4
    Beta strandi201 – 207Combined sources7
    Beta strandi212 – 217Combined sources6
    Helixi220 – 222Combined sources3
    Beta strandi223 – 225Combined sources3
    Beta strandi235 – 242Combined sources8
    Beta strandi245 – 250Combined sources6
    Beta strandi252 – 254Combined sources3
    Beta strandi259 – 262Combined sources4
    Beta strandi265 – 273Combined sources9
    Beta strandi282 – 291Combined sources10
    Beta strandi300 – 306Combined sources7
    Beta strandi309 – 312Combined sources4
    Beta strandi316 – 321Combined sources6
    Beta strandi325 – 331Combined sources7
    Beta strandi334 – 341Combined sources8
    Turni348 – 351Combined sources4
    Beta strandi353 – 356Combined sources4
    Beta strandi368 – 370Combined sources3
    Beta strandi381 – 386Combined sources6
    Turni388 – 390Combined sources3
    Beta strandi391 – 393Combined sources3
    Beta strandi395 – 397Combined sources3
    Beta strandi399 – 403Combined sources5
    Turni405 – 407Combined sources3
    Beta strandi409 – 411Combined sources3
    Turni412 – 414Combined sources3
    Beta strandi421 – 423Combined sources3
    Helixi446 – 448Combined sources3
    Beta strandi452 – 455Combined sources4
    Turni456 – 459Combined sources4
    Beta strandi460 – 466Combined sources7
    Beta strandi469 – 472Combined sources4
    Helixi474 – 477Combined sources4
    Beta strandi490 – 492Combined sources3
    Helixi494 – 499Combined sources6
    Beta strandi505 – 510Combined sources6
    Helixi520 – 522Combined sources3
    Beta strandi531 – 537Combined sources7
    Helixi555 – 557Combined sources3
    Beta strandi564 – 570Combined sources7
    Beta strandi576 – 578Combined sources3
    Beta strandi583 – 590Combined sources8
    Helixi592 – 596Combined sources5
    Beta strandi616 – 620Combined sources5
    Helixi627 – 629Combined sources3
    Beta strandi635 – 639Combined sources5
    Beta strandi647 – 655Combined sources9
    Beta strandi661 – 667Combined sources7
    Helixi668 – 671Combined sources4
    Helixi672 – 681Combined sources10

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP09871.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini16 – 130CUB 1PROSITE-ProRule annotationAdd BLAST115
    Domaini131 – 172EGF-like; calcium-bindingAdd BLAST42
    Domaini175 – 290CUB 2PROSITE-ProRule annotationAdd BLAST116
    Domaini292 – 356Sushi 1PROSITE-ProRule annotationAdd BLAST65
    Domaini357 – 423Sushi 2PROSITE-ProRule annotationAdd BLAST67
    Domaini438 – 680Peptidase S1PROSITE-ProRule annotationAdd BLAST243

    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

    eggNOGiKOG3627. Eukaryota.
    COG5640. LUCA.
    GeneTreeiENSGT00760000118890.
    HOVERGENiHBG000559.
    InParanoidiP09871.
    KOiK01331.
    OMAiFGPYCGN.
    OrthoDBiEOG091G02DS.
    PhylomeDBiP09871.
    TreeFamiTF330373.

    Family and domain databases

    CDDicd00033. CCP. 2 hits.
    cd00041. CUB. 2 hits.
    cd00190. Tryp_SPc. 1 hit.
    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.
    IPR009003. Peptidase_S1_PA.
    IPR001314. Peptidase_S1A.
    IPR000436. Sushi_SCR_CCP_dom.
    IPR001254. Trypsin_dom.
    IPR033116. TRYPSIN_SER.
    [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)DescriptionActionsGraphical viewLength
    Sequence conflicti294C → K AA sequence (PubMed:3007145).Curated1
    Sequence conflicti513G → GG (PubMed:2553984).Curated1
    Sequence conflicti573T → A AA sequence (PubMed:6362661).Curated1
    Sequence conflicti645 – 646TK → GR AA sequence (PubMed:6362661).Curated2

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_033643119R → H.Corresponds to variant rs12146727dbSNPEnsembl.1
    Natural variantiVAR_033644327V → L.Corresponds to variant rs2239170dbSNPEnsembl.1
    Natural variantiVAR_014565383R → H.Corresponds to variant rs20573dbSNPEnsembl.1

    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.4. 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
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi107177. 8 interactors.
    IntActiP09871. 8 interactors.
    MINTiMINT-4655918.
    STRINGi9606.ENSP00000328173.

    Chemistry databases

    BindingDBiP09871.
    ChEMBLiCHEMBL3913.
    DrugBankiDB00054. Abciximab.
    DB00051. Adalimumab.
    DB00074. Basiliximab.
    DB00002. Cetuximab.
    DB00005. Etanercept.
    DB00056. Gemtuzumab ozogamicin.
    DB00078. Ibritumomab.
    DB00075. Muromonab.
    DB00073. Rituximab.
    DB00072. Trastuzumab.
    GuidetoPHARMACOLOGYi2335.

    Protein family/group databases

    MEROPSiS01.193.

    PTM databases

    iPTMnetiP09871.
    PhosphoSitePlusiP09871.

    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.4. human.

    Organism-specific databases

    CTDi716.
    DisGeNETi716.
    GeneCardsiC1S.
    HGNCiHGNC:1247. C1S.
    HPAiCAB016722.
    HPA018852.
    MalaCardsiC1S.
    MIMi120580. gene.
    613783. phenotype.
    neXtProtiNX_P09871.
    OpenTargetsiENSG00000182326.
    Orphaneti169147. Immunodeficiency due to an early component of complement deficiency.
    PharmGKBiPA25636.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG3627. Eukaryota.
    COG5640. LUCA.
    GeneTreeiENSGT00760000118890.
    HOVERGENiHBG000559.
    InParanoidiP09871.
    KOiK01331.
    OMAiFGPYCGN.
    OrthoDBiEOG091G02DS.
    PhylomeDBiP09871.
    TreeFamiTF330373.

    Enzyme and pathway databases

    BioCyciZFISH:HS00050-MONOMER.
    BRENDAi3.4.21.42. 2681.
    ReactomeiR-HSA-166663. Initial triggering of complement.
    R-HSA-173623. Classical antibody-mediated complement activation.
    SABIO-RKP09871.

    Miscellaneous databases

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

    Gene expression databases

    BgeeiENSG00000182326.
    ExpressionAtlasiP09871. baseline and differential.
    GenevisibleiP09871. HS.

    Family and domain databases

    CDDicd00033. CCP. 2 hits.
    cd00041. CUB. 2 hits.
    cd00190. Tryp_SPc. 1 hit.
    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.
    IPR009003. Peptidase_S1_PA.
    IPR001314. Peptidase_S1A.
    IPR000436. Sushi_SCR_CCP_dom.
    IPR001254. Trypsin_dom.
    IPR033116. TRYPSIN_SER.
    [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...

    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: November 30, 2016
    This is version 210 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

    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.