Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P09871

- C1S_HUMAN

UniProt

P09871 - C1S_HUMAN

Protein

Complement C1s subcomponent

Gene

C1S

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 188 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    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

    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.1 Publication
    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 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)1 PublicationPROSITE-ProRule annotation
    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

    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

    1
    688
    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.
    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.
    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

    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:
    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.
    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 .
    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

    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: October 1, 2014
    This is version 188 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