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P00736

- C1R_HUMAN

UniProt

P00736 - C1R_HUMAN

Protein

Complement C1r subcomponent

Gene

C1R

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 181 (01 Oct 2014)
      Sequence version 2 (16 Dec 2008)
      Previous versions | rss
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    Functioni

    C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system.

    Catalytic activityi

    Selective cleavage of Lys(or Arg)-|-Ile bond in complement subcomponent C1s to form the active form of C1s (EC 3.4.21.42).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei502 – 5021Charge relay system
    Active sitei557 – 5571Charge relay system
    Active sitei654 – 6541Charge relay system

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. protein binding Source: IntAct
    3. serine-type endopeptidase activity Source: Reactome
    4. serine-type peptidase activity Source: ProtInc

    GO - Biological processi

    1. complement activation Source: Reactome
    2. complement activation, classical pathway Source: Reactome
    3. immune response Source: ProtInc
    4. innate immune response Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Complement pathway, Immunity, Innate immunity

    Enzyme and pathway databases

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

    Protein family/group databases

    MEROPSiS01.192.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Complement C1r subcomponent (EC:3.4.21.41)
    Alternative name(s):
    Complement component 1 subcomponent r
    Cleaved into the following 2 chains:
    Gene namesi
    Name:C1R
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:1246. C1R.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. extracellular region Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    MIMi216950. phenotype.
    Orphaneti169147. Immunodeficiency due to an early component of complement deficiency.
    PharmGKBiPA25635.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 17171 PublicationAdd
    BLAST
    Chaini18 – 705688Complement C1r subcomponentPRO_0000027577Add
    BLAST
    Chaini18 – 463446Complement C1r subcomponent heavy chainPRO_0000027578Add
    BLAST
    Chaini464 – 705242Complement C1r subcomponent light chainPRO_0000027579Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi71 ↔ 89Curated
    Glycosylationi125 – 1251N-linked (GlcNAc...)1 Publication
    Disulfide bondi146 ↔ 165
    Disulfide bondi161 ↔ 174
    Modified residuei167 – 1671(3R)-3-hydroxyasparagine1 Publication
    Disulfide bondi176 ↔ 189
    Disulfide bondi193 ↔ 220Curated
    Modified residuei206 – 2061Phosphoserine; by CK21 Publication
    Glycosylationi221 – 2211N-linked (GlcNAc...)1 Publication
    Disulfide bondi250 ↔ 268Curated
    Disulfide bondi309 ↔ 358
    Disulfide bondi338 ↔ 371
    Disulfide bondi376 ↔ 429
    Disulfide bondi406 ↔ 447
    Disulfide bondi451 ↔ 577Interchain (between heavy and light chains)
    Glycosylationi514 – 5141N-linked (GlcNAc...)2 Publications
    Glycosylationi581 – 5811N-linked (GlcNAc...)
    Disulfide bondi620 ↔ 639
    Disulfide bondi650 ↔ 680

    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, Phosphoprotein

    Proteomic databases

    PaxDbiP00736.
    PeptideAtlasiP00736.
    PRIDEiP00736.

    PTM databases

    PhosphoSiteiP00736.

    Expressioni

    Gene expression databases

    BgeeiP00736.
    CleanExiHS_C1R.
    GenevestigatoriP00736.

    Organism-specific databases

    HPAiHPA001551.

    Interactioni

    Subunit structurei

    C1 is a calcium-dependent trimolecular complex of C1q, C1r and C1s in the molar ration of 1:2:2. C1r is a dimer of identical chains, each of which is activated by cleavage into two chains, A and B, connected by disulfide bonds.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    C1SP098713EBI-3926504,EBI-2810045

    Protein-protein interaction databases

    BioGridi107176. 6 interactions.
    IntActiP00736. 3 interactions.
    MINTiMINT-8045732.
    STRINGi9606.ENSP00000290575.

    Structurei

    Secondary structure

    1
    705
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni145 – 1473
    Turni150 – 1523
    Beta strandi156 – 1583
    Beta strandi162 – 1687
    Beta strandi171 – 1755
    Beta strandi319 – 3224
    Beta strandi326 – 3283
    Beta strandi333 – 3386
    Beta strandi342 – 3465
    Beta strandi349 – 3524
    Beta strandi355 – 3584
    Beta strandi364 – 3663
    Beta strandi370 – 3734
    Beta strandi385 – 3928
    Beta strandi401 – 4066
    Turni408 – 4103
    Beta strandi411 – 4133
    Beta strandi426 – 4294
    Beta strandi433 – 4375
    Turni438 – 4403
    Beta strandi447 – 4493
    Beta strandi478 – 49215
    Turni493 – 4953
    Beta strandi496 – 4994
    Helixi501 – 5044
    Beta strandi518 – 5225
    Helixi526 – 5327
    Beta strandi537 – 5426
    Beta strandi548 – 5525
    Beta strandi559 – 5657
    Beta strandi571 – 5733
    Helixi582 – 5854
    Beta strandi590 – 5956
    Beta strandi600 – 6023
    Beta strandi608 – 6147
    Helixi617 – 62610
    Beta strandi637 – 6415
    Helixi643 – 6508
    Turni651 – 6555
    Beta strandi657 – 6615
    Turni663 – 6653
    Beta strandi668 – 6769
    Beta strandi678 – 6836
    Beta strandi685 – 6895
    Helixi690 – 6934
    Helixi694 – 7007

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1APQNMR-A140-192[»]
    1GPZX-ray2.90A/B307-705[»]
    1MD7X-ray3.20A375-702[»]
    1MD8X-ray2.80A375-703[»]
    2QY0X-ray2.60A/C309-463[»]
    B/D464-705[»]
    DisProtiDP00621.
    ProteinModelPortaliP00736.
    SMRiP00736. Positions 25-703.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00736.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 141124CUB 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini142 – 19049EGF-like; calcium-bindingSequence AnalysisAdd
    BLAST
    Domaini193 – 305113CUB 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini307 – 37367Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini374 – 44976Sushi 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini464 – 702239Peptidase 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.
    KOiK01330.
    OrthoDBiEOG7W6WK4.
    PhylomeDBiP00736.
    TreeFamiTF330373.

    Family and domain databases

    Gene3Di2.60.120.290. 2 hits.
    InterProiIPR000859. CUB_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    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.
    PS01186. EGF_2. 1 hit.
    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.

    P00736-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWLLYLLVPA LFCRAGGSIP IPQKLFGEVT SPLFPKPYPN NFETTTVITV    50
    PTGYRVKLVF QQFDLEPSEG CFYDYVKISA DKKSLGRFCG QLGSPLGNPP 100
    GKKEFMSQGN KMLLTFHTDF SNEENGTIMF YKGFLAYYQA VDLDECASRS 150
    KSGEEDPQPQ CQHLCHNYVG GYFCSCRPGY ELQEDTHSCQ AECSSELYTE 200
    ASGYISSLEY PRSYPPDLRC NYSIRVERGL TLHLKFLEPF DIDDHQQVHC 250
    PYDQLQIYAN GKNIGEFCGK QRPPDLDTSS NAVDLLFFTD ESGDSRGWKL 300
    RYTTEIIKCP QPKTLDEFTI IQNLQPQYQF RDYFIATCKQ GYQLIEGNQV 350
    LHSFTAVCQD DGTWHRAMPR CKIKDCGQPR NLPNGDFRYT TTMGVNTYKA 400
    RIQYYCHEPY YKMQTRAGSR ESEQGVYTCT AQGIWKNEQK GEKIPRCLPV 450
    CGKPVNPVEQ RQRIIGGQKA KMGNFPWQVF TNIHGRGGGA LLGDRWILTA 500
    AHTLYPKEHE AQSNASLDVF LGHTNVEELM KLGNHPIRRV SVHPDYRQDE 550
    SYNFEGDIAL LELENSVTLG PNLLPICLPD NDTFYDLGLM GYVSGFGVME 600
    EKIAHDLRFV RLPVANPQAC ENWLRGKNRM DVFSQNMFCA GHPSLKQDAC 650
    QGDSGGVFAV RDPNTDRWVA TGIVSWGIGC SRGYGFYTKV LNYVDWIKKE 700
    MEEED 705
    Length:705
    Mass (Da):80,119
    Last modified:December 16, 2008 - v2
    Checksum:iB45D120201061462
    GO

    Polymorphismi

    Complement component C1r deficiency [MIMi:216950] leads to the failure of the classical complement system activation pathway (C1 deficiency). Individuals with C1 deficiency are highly susceptible to infections by microorganisms and have greater risk in developing autoimmune diseases such as systemic lupus erythematosus (SLE).

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti131 – 1311Y → H.1 Publication
    VAR_018667
    Natural varianti152 – 1521S → L Common polymorphism. 4 Publications
    Corresponds to variant rs1801046 [ dbSNP | Ensembl ].
    VAR_016103
    Natural varianti163 – 1631H → Y.1 Publication
    VAR_018668
    Natural varianti184 – 1841E → K Polymorphism confirmed at protein level. 2 Publications
    Corresponds to variant rs1126605 [ dbSNP | Ensembl ].
    VAR_018669
    Natural varianti186 – 1861T → R.4 Publications
    Corresponds to variant rs4519167 [ dbSNP | Ensembl ].
    VAR_047933
    Natural varianti261 – 2611G → R Polymorphism confirmed at protein level. 2 Publications
    Corresponds to variant rs3813728 [ dbSNP | Ensembl ].
    VAR_018670

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14058 mRNA. Translation: AAA51851.1.
    X04701 mRNA. Translation: CAA28407.1.
    AB083037 Genomic DNA. Translation: BAC19850.2.
    AC094008 Genomic DNA. No translation available.
    AC140077 Genomic DNA. No translation available.
    CR749540 mRNA. Translation: CAH18343.1.
    BC035220 mRNA. Translation: AAH35220.1.
    PIRiA24170. C1HURB.
    RefSeqiNP_001724.3. NM_001733.4.
    UniGeneiHs.524224.

    Genome annotation databases

    EnsembliENST00000290575; ENSP00000290575; ENSG00000159403.
    GeneIDi715.
    KEGGihsa:715.

    Polymorphism databases

    DMDMi218511956.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14058 mRNA. Translation: AAA51851.1 .
    X04701 mRNA. Translation: CAA28407.1 .
    AB083037 Genomic DNA. Translation: BAC19850.2 .
    AC094008 Genomic DNA. No translation available.
    AC140077 Genomic DNA. No translation available.
    CR749540 mRNA. Translation: CAH18343.1 .
    BC035220 mRNA. Translation: AAH35220.1 .
    PIRi A24170. C1HURB.
    RefSeqi NP_001724.3. NM_001733.4.
    UniGenei Hs.524224.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1APQ NMR - A 140-192 [» ]
    1GPZ X-ray 2.90 A/B 307-705 [» ]
    1MD7 X-ray 3.20 A 375-702 [» ]
    1MD8 X-ray 2.80 A 375-703 [» ]
    2QY0 X-ray 2.60 A/C 309-463 [» ]
    B/D 464-705 [» ]
    DisProti DP00621.
    ProteinModelPortali P00736.
    SMRi P00736. Positions 25-703.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107176. 6 interactions.
    IntActi P00736. 3 interactions.
    MINTi MINT-8045732.
    STRINGi 9606.ENSP00000290575.

    Chemistry

    BindingDBi P00736.
    ChEMBLi CHEMBL4611.
    DrugBanki DB00054. Abciximab.
    DB00051. Adalimumab.
    DB00092. Alefacept.
    DB00087. Alemtuzumab.
    DB00074. Basiliximab.
    DB00112. Bevacizumab.
    DB00002. Cetuximab.
    DB00111. Daclizumab.
    DB00095. Efalizumab.
    DB00005. Etanercept.
    DB00056. Gemtuzumab ozogamicin.
    DB00078. Ibritumomab.
    DB00028. Immune globulin.
    DB00075. Muromonab.
    DB00108. Natalizumab.
    DB00110. Palivizumab.
    DB00073. Rituximab.
    DB00081. Tositumomab.
    DB00072. Trastuzumab.
    GuidetoPHARMACOLOGYi 2334.

    Protein family/group databases

    MEROPSi S01.192.

    PTM databases

    PhosphoSitei P00736.

    Polymorphism databases

    DMDMi 218511956.

    Proteomic databases

    PaxDbi P00736.
    PeptideAtlasi P00736.
    PRIDEi P00736.

    Protocols and materials databases

    DNASUi 715.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000290575 ; ENSP00000290575 ; ENSG00000159403 .
    GeneIDi 715.
    KEGGi hsa:715.

    Organism-specific databases

    CTDi 715.
    GeneCardsi GC12M007187.
    HGNCi HGNC:1246. C1R.
    HPAi HPA001551.
    MIMi 216950. phenotype.
    613785. gene.
    neXtProti NX_P00736.
    Orphaneti 169147. Immunodeficiency due to an early component of complement deficiency.
    PharmGKBi PA25635.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5640.
    HOVERGENi HBG000559.
    KOi K01330.
    OrthoDBi EOG7W6WK4.
    PhylomeDBi P00736.
    TreeFami TF330373.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi C1R. human.
    EvolutionaryTracei P00736.
    GeneWikii C1R_(gene).
    GenomeRNAii 715.
    NextBioi 2906.
    PROi P00736.
    SOURCEi Search...

    Gene expression databases

    Bgeei P00736.
    CleanExi HS_C1R.
    Genevestigatori P00736.

    Family and domain databases

    Gene3Di 2.60.120.290. 2 hits.
    InterProi IPR000859. CUB_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR013032. EGF-like_CS.
    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.
    PS01186. EGF_2. 1 hit.
    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. "Nucleotide sequence of the cDNA coding for human complement C1r."
      Leytus S.P., Kurachi K., Sakariassen K.S., Davie E.W.
      Biochemistry 25:4855-4863(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-186.
    2. "Cloning and sequencing of full-length cDNA encoding the precursor of human complement component C1r."
      Journet A., Tosi M.
      Biochem. J. 240:783-787(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-152 AND ARG-186.
    3. "The human complement component C1R gene: the exon-intron structure and the molecular basis of allelic diversity."
      Nakagawa M., Yuasa I., Irizawa Y., Umetsu K.
      Ann. Hum. Genet. 67:207-215(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-131; LEU-152; TYR-163; LYS-184; ARG-186 AND ARG-261.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Colon endothelium.
    5. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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], VARIANTS LEU-152 AND ARG-186.
      Tissue: Skin.
    7. "Complete amino acid sequence of the A chain of human complement-classical-pathway enzyme C1r."
      Arlaud G.J., Willis A.C., Gagnon J.
      Biochem. J. 241:711-720(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 18-463.
    8. "Complete amino acid sequence of the catalytic chain of human complement subcomponent C1-r."
      Arlaud G.J., Gagnon J.
      Biochemistry 22:1758-1764(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 464-705.
    9. "Identification of erythro-beta-hydroxyasparagine in the EGF-like domain of human C1r."
      Arlaud G.J., van Dorsselaer A., Bell A., Mancini M., Aude C., Gagnon J.
      FEBS Lett. 222:129-134(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 152-186, HYDROXYLATION AT ASN-167.
    10. "Identification of a cryptic protein kinase CK2 phosphorylation site in human complement protease Clr, and its use to probe intramolecular interaction."
      Pelloux S., Thielens N.M., Hudry-Clergeon G., Petillot Y., Filhol O., Arlaud G.J.
      FEBS Lett. 386:15-20(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 133-137; 187-211 AND 609-613, PHOSPHORYLATION AT SER-206 BY CK2.
    11. "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-125; ASN-221 AND ASN-514.
      Tissue: Plasma.
    12. "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-514.
      Tissue: Liver.
    13. "Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family."
      Bersch B., Hernandez J.-F., Marion D., Arlaud G.J.
      Biochemistry 37:1204-1214(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 140-192.
    14. "The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex."
      Budayova-Spano M., Lacroix M., Thielens N.M., Arlaud G.J., Fontecilla-Camps J.-C., Gaboriaud C.
      EMBO J. 21:231-239(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 307-702.
    15. "Monomeric structures of the zymogen and active catalytic domain of complement protease c1r: further insights into the c1 activation mechanism."
      Budayova-Spano M., Grabarse W., Thielens N.M., Hillen H., Lacroix M., Schmidt M., Fontecilla-Camps J.-C., Arlaud G.J., Gaboriaud C.
      Structure 10:1509-1519(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 375-702.
    16. "A common amino acid polymorphism in complement component C1R."
      Nothen M.M., Dewald G.
      Hum. Mol. Genet. 3:217-217(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LEU-152.
    17. "Quantitative detection of single amino acid polymorphisms by targeted proteomics."
      Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H., Lin X., Zeng R., Wu J.R.
      J. Mol. Cell Biol. 3:309-315(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS LYS-184 AND ARG-261, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiC1R_HUMAN
    AccessioniPrimary (citable) accession number: P00736
    Secondary accession number(s): A6NJQ8, Q68D77, Q8J012
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 181 of the entry and version 2 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