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P06681

- CO2_HUMAN

UniProt

P06681 - CO2_HUMAN

Protein

Complement C2

Gene

C2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 172 (01 Oct 2014)
      Sequence version 2 (15 Dec 1998)
      Previous versions | rss
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    Functioni

    Component C2 which is part of the classical pathway of the complement system is cleaved by activated factor C1 into two fragments: C2b and C2a. C2a, a serine protease, then combines with complement factor C4b to generate the C3 or C5 convertase.

    Catalytic activityi

    Selective cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to form C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha-chain to form C5a and C5b.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi262 – 2621Divalent metal cation
    Metal bindingi264 – 2641Divalent metal cation
    Metal bindingi337 – 3371Divalent metal cation
    Active sitei507 – 5071Charge relay system1 Publication
    Active sitei561 – 5611Charge relay system1 Publication
    Active sitei679 – 6791Charge relay system1 Publication

    GO - Molecular functioni

    1. serine-type endopeptidase activity Source: InterPro

    GO - Biological processi

    1. complement activation Source: BHF-UCL
    2. complement activation, classical pathway Source: ProtInc
    3. innate immune response Source: Reactome
    4. positive regulation of apoptotic cell clearance Source: BHF-UCL
    5. regulation of complement activation Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Biological processi

    Complement pathway, Immunity, Innate immunity

    Keywords - Ligandi

    Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_118707. Regulation of Complement cascade.
    REACT_7972. Activation of C3 and C5.
    REACT_8024. Initial triggering of complement.

    Protein family/group databases

    MEROPSiS01.194.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Complement C2 (EC:3.4.21.43)
    Alternative name(s):
    C3/C5 convertase
    Cleaved into the following 2 chains:
    Gene namesi
    Name:C2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:1248. C2.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: ProtInc

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Complement component 2 deficiency (C2D) [MIM:217000]: A rare defect of the complement classical pathway associated with the development of autoimmune disorders, mainly systemic lupus erythematosus. Skin and joint manifestations are common and renal disease is relatively rare. Patients with complement component 2 deficiency are also reported to have recurrent invasive infections.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti131 – 1311C → Y in C2D. 1 Publication
    VAR_008544
    Natural varianti209 – 2091S → F in C2D. 1 Publication
    Corresponds to variant rs28934590 [ dbSNP | Ensembl ].
    VAR_008545
    Natural varianti464 – 4641G → R in C2D. 1 Publication
    VAR_008546

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi217000. phenotype.
    603075. phenotype.
    Orphaneti169147. Immunodeficiency due to an early component of complement deficiency.
    536. Systemic lupus erythematosus.
    PharmGKBiPA25637.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20202 PublicationsAdd
    BLAST
    Chaini21 – 752732Complement C2PRO_0000027610Add
    BLAST
    Chaini21 – 243223Complement C2b fragmentPRO_0000027611Add
    BLAST
    Chaini244 – 752509Complement C2a fragmentPRO_0000027612Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi24 ↔ 64
    Glycosylationi29 – 291N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi51 ↔ 84
    Disulfide bondi89 ↔ 131
    Glycosylationi112 – 1121N-linked (GlcNAc...)2 Publications
    Disulfide bondi117 ↔ 144
    Disulfide bondi151 ↔ 191
    Disulfide bondi177 ↔ 204
    Glycosylationi290 – 2901N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi333 – 3331N-linked (GlcNAc...)3 Publications
    Glycosylationi467 – 4671N-linked (GlcNAc...)2 Publications
    Glycosylationi471 – 4711N-linked (GlcNAc...)1 Publication
    Disulfide bondi492 ↔ 508By similarity
    Glycosylationi621 – 6211N-linked (GlcNAc...)2 Publications
    Glycosylationi651 – 6511N-linked (GlcNAc...) (complex)1 Publication
    Disulfide bondi675 ↔ 705By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP06681.
    PaxDbiP06681.
    PRIDEiP06681.

    PTM databases

    PhosphoSiteiP06681.

    Miscellaneous databases

    PMAP-CutDBP06681.

    Expressioni

    Gene expression databases

    ArrayExpressiP06681.
    BgeeiP06681.
    CleanExiHS_C2.
    GenevestigatoriP06681.

    Organism-specific databases

    HPAiCAB016775.

    Interactioni

    Subunit structurei

    C2a interacts with Schistosoma haematobium TOR (via N-terminal extracellular domain). This results in inhibition of the classical and lectin pathway of complement activation, probably due to interference with binding of C2a to C4b such that C3 convertase cannot be formed. This infers resistance to complement-mediated cell lysis, allowing parasite survival and infection.1 Publication

    Protein-protein interaction databases

    BioGridi107178. 1 interaction.
    IntActiP06681. 1 interaction.
    STRINGi9606.ENSP00000372853.

    Structurei

    Secondary structure

    1
    752
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 396
    Beta strandi46 – 505
    Beta strandi55 – 595
    Beta strandi61 – 644
    Beta strandi83 – 864
    Beta strandi88 – 903
    Beta strandi98 – 1025
    Beta strandi105 – 1084
    Beta strandi112 – 1176
    Beta strandi122 – 1254
    Beta strandi127 – 1315
    Beta strandi137 – 1393
    Beta strandi143 – 1453
    Beta strandi149 – 1513
    Beta strandi160 – 1634
    Beta strandi172 – 1776
    Beta strandi182 – 1854
    Beta strandi187 – 1915
    Beta strandi197 – 1993
    Beta strandi203 – 2053
    Helixi207 – 2115
    Beta strandi249 – 26012
    Helixi267 – 28418
    Turni285 – 2873
    Beta strandi291 – 30616
    Helixi311 – 3144
    Helixi316 – 3249
    Helixi328 – 3314
    Helixi339 – 35719
    Beta strandi359 – 3613
    Helixi362 – 3654
    Beta strandi367 – 3759
    Beta strandi381 – 3833
    Helixi386 – 39510
    Helixi403 – 4053
    Beta strandi406 – 4138
    Helixi420 – 4267
    Beta strandi436 – 4405
    Helixi442 – 45110
    Helixi474 – 4774
    Beta strandi481 – 4855
    Beta strandi492 – 50413
    Helixi506 – 5094
    Helixi515 – 5173
    Beta strandi519 – 5224
    Beta strandi531 – 5333
    Beta strandi535 – 5406
    Helixi546 – 5527
    Beta strandi563 – 5697
    Beta strandi574 – 5763
    Helixi586 – 5916
    Helixi600 – 6078
    Beta strandi610 – 6189
    Beta strandi623 – 6308
    Helixi632 – 6398
    Helixi640 – 6445
    Helixi655 – 6573
    Beta strandi663 – 6664
    Helixi676 – 6783
    Beta strandi682 – 6876
    Beta strandi690 – 70112
    Turni704 – 7074
    Beta strandi720 – 7234
    Beta strandi727 – 7315
    Helixi732 – 7354
    Helixi736 – 7438
    Turni744 – 7463

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2I6QX-ray2.10A244-752[»]
    2I6SX-ray2.70A244-752[»]
    2ODPX-ray1.90A244-752[»]
    2ODQX-ray2.30A244-752[»]
    3ERBX-ray1.80A21-243[»]
    ProteinModelPortaliP06681.
    SMRiP06681. Positions 23-217, 244-752.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06681.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 8665Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini87 – 14660Sushi 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini149 – 20658Sushi 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini254 – 452199VWFAPROSITE-ProRule annotationAdd
    BLAST
    Domaini464 – 744281Peptidase S1PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi260 – 2645MIDAS-like motif

    Domaini

    The MIDAS-like motif in the VWFA domain binds divalent metal cations.

    Sequence similaritiesi

    Belongs to the peptidase S1 family.PROSITE-ProRule annotation
    Contains 1 peptidase S1 domain.PROSITE-ProRule annotation
    Contains 3 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation
    Contains 1 VWFA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Sushi

    Phylogenomic databases

    eggNOGiNOG306397.
    HOGENOMiHOG000038034.
    HOVERGENiHBG002567.
    InParanoidiP06681.
    KOiK01332.
    OMAiRDMTEVI.
    PhylomeDBiP06681.
    TreeFamiTF330194.

    Family and domain databases

    Gene3Di3.40.50.410. 1 hit.
    InterProiIPR011360. Compl_C2_B.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR000436. Sushi_SCR_CCP.
    IPR009003. Trypsin-like_Pept_dom.
    IPR002035. VWF_A.
    [Graphical view]
    PfamiPF00084. Sushi. 2 hits.
    PF00089. Trypsin. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001154. Compl_C2_B. 1 hit.
    PRINTSiPR00722. CHYMOTRYPSIN.
    SMARTiSM00032. CCP. 3 hits.
    SM00020. Tryp_SPc. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF50494. SSF50494. 1 hit.
    SSF53300. SSF53300. 1 hit.
    SSF57535. SSF57535. 3 hits.
    PROSITEiPS50923. SUSHI. 3 hits.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    PS50234. VWFA. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P06681-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGPLMVLFCL LFLYPGLADS APSCPQNVNI SGGTFTLSHG WAPGSLLTYS    50
    CPQGLYPSPA SRLCKSSGQW QTPGATRSLS KAVCKPVRCP APVSFENGIY 100
    TPRLGSYPVG GNVSFECEDG FILRGSPVRQ CRPNGMWDGE TAVCDNGAGH 150
    CPNPGISLGA VRTGFRFGHG DKVRYRCSSN LVLTGSSERE CQGNGVWSGT 200
    EPICRQPYSY DFPEDVAPAL GTSFSHMLGA TNPTQKTKES LGRKIQIQRS 250
    GHLNLYLLLD CSQSVSENDF LIFKESASLM VDRIFSFEIN VSVAIITFAS 300
    EPKVLMSVLN DNSRDMTEVI SSLENANYKD HENGTGTNTY AALNSVYLMM 350
    NNQMRLLGME TMAWQEIRHA IILLTDGKSN MGGSPKTAVD HIREILNINQ 400
    KRNDYLDIYA IGVGKLDVDW RELNELGSKK DGERHAFILQ DTKALHQVFE 450
    HMLDVSKLTD TICGVGNMSA NASDQERTPW HVTIKPKSQE TCRGALISDQ 500
    WVLTAAHCFR DGNDHSLWRV NVGDPKSQWG KEFLIEKAVI SPGFDVFAKK 550
    NQGILEFYGD DIALLKLAQK VKMSTHARPI CLPCTMEANL ALRRPQGSTC 600
    RDHENELLNK QSVPAHFVAL NGSKLNINLK MGVEWTSCAE VVSQEKTMFP 650
    NLTDVREVVT DQFLCSGTQE DESPCKGESG GAVFLERRFR FFQVGLVSWG 700
    LYNPCLGSAD KNSRKRAPRS KVPPPRDFHI NLFRMQPWLR QHLGDVLNFL 750
    PL 752
    Length:752
    Mass (Da):83,268
    Last modified:December 15, 1998 - v2
    Checksum:i5A96A13E700CF444
    GO
    Isoform 2 (identifier: P06681-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-147: MGPLMVLFCL...DGETAVCDNG → MRALCIRETCSSELGFSRNWSRRK
         238-328: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:538
    Mass (Da):60,318
    Checksum:iDAD9613AAAF483E8
    GO
    Isoform 3 (identifier: P06681-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         16-147: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:620
    Mass (Da):69,444
    Checksum:iFC295E99940BE04D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti30 – 301I → L AA sequence (PubMed:6922702)Curated
    Sequence conflicti34 – 341T → S AA sequence (PubMed:6922702)Curated
    Sequence conflicti211 – 2111D → G in BAG62532. (PubMed:14702039)Curated
    Sequence conflicti249 – 2491R → S AA sequence (PubMed:6922702)Curated
    Sequence conflicti253 – 2531L → K AA sequence (PubMed:6922702)Curated

    Polymorphismi

    The variant Asp-318 is associated with a reduced risk of age-related macular degeneration (ARMD) [MIMi:603075]. ARMD is a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti131 – 1311C → Y in C2D. 1 Publication
    VAR_008544
    Natural varianti209 – 2091S → F in C2D. 1 Publication
    Corresponds to variant rs28934590 [ dbSNP | Ensembl ].
    VAR_008545
    Natural varianti318 – 3181E → D.2 Publications
    Corresponds to variant rs9332739 [ dbSNP | Ensembl ].
    VAR_019158
    Natural varianti464 – 4641G → R in C2D. 1 Publication
    VAR_008546
    Natural varianti533 – 5331F → L.
    Corresponds to variant rs1042664 [ dbSNP | Ensembl ].
    VAR_011772
    Natural varianti734 – 7341R → C.1 Publication
    Corresponds to variant rs4151648 [ dbSNP | Ensembl ].
    VAR_019159

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 147147MGPLM…VCDNG → MRALCIRETCSSELGFSRNW SRRK in isoform 2. 1 PublicationVSP_043038Add
    BLAST
    Alternative sequencei16 – 147132Missing in isoform 3. 1 PublicationVSP_046103Add
    BLAST
    Alternative sequencei238 – 32891Missing in isoform 2. 1 PublicationVSP_043039Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04481 mRNA. Translation: CAA28169.1.
    M26301 mRNA. Translation: AAA35614.1.
    L09708, L09706, L09707 Genomic DNA. Translation: AAB97607.1.
    AF019413 Genomic DNA. Translation: AAB67975.1.
    AY349611 Genomic DNA. Translation: AAQ15273.1.
    AK298311 mRNA. Translation: BAG60565.1.
    AK300892 mRNA. Translation: BAG62532.1.
    AL645922 Genomic DNA. No translation available.
    AL662834 Genomic DNA. No translation available.
    AL662849 Genomic DNA. No translation available.
    AL671762 Genomic DNA. No translation available.
    AL844853 Genomic DNA. No translation available.
    BX005143 Genomic DNA. No translation available.
    CR388219 Genomic DNA. No translation available.
    CR759782 Genomic DNA. No translation available.
    CR759784 Genomic DNA. No translation available.
    CR933857 Genomic DNA. No translation available.
    BC043484 mRNA. Translation: AAH43484.1.
    M15549 Genomic DNA. Translation: AAA59649.1.
    M15082 Genomic DNA. Translation: AAA59624.1.
    CCDSiCCDS4728.1. [P06681-1]
    CCDS54991.1. [P06681-3]
    CCDS56416.1. [P06681-2]
    PIRiA25971. C2HU.
    RefSeqiNP_000054.2. NM_000063.5. [P06681-1]
    NP_001139375.1. NM_001145903.2. [P06681-3]
    NP_001171534.1. NM_001178063.2. [P06681-2]
    UniGeneiHs.408903.

    Genome annotation databases

    EnsembliENST00000299367; ENSP00000299367; ENSG00000166278. [P06681-1]
    ENST00000375510; ENSP00000364660; ENSG00000204364. [P06681-1]
    ENST00000383362; ENSP00000372853; ENSG00000206372. [P06681-1]
    ENST00000411803; ENSP00000402278; ENSG00000235696. [P06681-1]
    ENST00000413548; ENSP00000407961; ENSG00000231543. [P06681-1]
    ENST00000416252; ENSP00000405800; ENSG00000235017. [P06681-1]
    ENST00000442278; ENSP00000395683; ENSG00000166278. [P06681-3]
    ENST00000448206; ENSP00000392835; ENSG00000226560. [P06681-1]
    ENST00000452323; ENSP00000392322; ENSG00000166278. [P06681-2]
    ENST00000548973; ENSP00000446728; ENSG00000206372. [P06681-3]
    ENST00000548995; ENSP00000449286; ENSG00000204364. [P06681-3]
    ENST00000549972; ENSP00000447632; ENSG00000235696. [P06681-3]
    ENST00000550682; ENSP00000446639; ENSG00000231543. [P06681-3]
    ENST00000551081; ENSP00000450387; ENSG00000235017. [P06681-3]
    ENST00000551648; ENSP00000449715; ENSG00000226560. [P06681-3]
    GeneIDi717.
    KEGGihsa:717.
    UCSCiuc003nyf.3. human. [P06681-1]
    uc010jtk.3. human.
    uc011dop.2. human. [P06681-2]

    Polymorphism databases

    DMDMi3915642.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    C2base

    C2 mutation db

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04481 mRNA. Translation: CAA28169.1 .
    M26301 mRNA. Translation: AAA35614.1 .
    L09708 , L09706 , L09707 Genomic DNA. Translation: AAB97607.1 .
    AF019413 Genomic DNA. Translation: AAB67975.1 .
    AY349611 Genomic DNA. Translation: AAQ15273.1 .
    AK298311 mRNA. Translation: BAG60565.1 .
    AK300892 mRNA. Translation: BAG62532.1 .
    AL645922 Genomic DNA. No translation available.
    AL662834 Genomic DNA. No translation available.
    AL662849 Genomic DNA. No translation available.
    AL671762 Genomic DNA. No translation available.
    AL844853 Genomic DNA. No translation available.
    BX005143 Genomic DNA. No translation available.
    CR388219 Genomic DNA. No translation available.
    CR759782 Genomic DNA. No translation available.
    CR759784 Genomic DNA. No translation available.
    CR933857 Genomic DNA. No translation available.
    BC043484 mRNA. Translation: AAH43484.1 .
    M15549 Genomic DNA. Translation: AAA59649.1 .
    M15082 Genomic DNA. Translation: AAA59624.1 .
    CCDSi CCDS4728.1. [P06681-1 ]
    CCDS54991.1. [P06681-3 ]
    CCDS56416.1. [P06681-2 ]
    PIRi A25971. C2HU.
    RefSeqi NP_000054.2. NM_000063.5. [P06681-1 ]
    NP_001139375.1. NM_001145903.2. [P06681-3 ]
    NP_001171534.1. NM_001178063.2. [P06681-2 ]
    UniGenei Hs.408903.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2I6Q X-ray 2.10 A 244-752 [» ]
    2I6S X-ray 2.70 A 244-752 [» ]
    2ODP X-ray 1.90 A 244-752 [» ]
    2ODQ X-ray 2.30 A 244-752 [» ]
    3ERB X-ray 1.80 A 21-243 [» ]
    ProteinModelPortali P06681.
    SMRi P06681. Positions 23-217, 244-752.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107178. 1 interaction.
    IntActi P06681. 1 interaction.
    STRINGi 9606.ENSP00000372853.

    Protein family/group databases

    MEROPSi S01.194.

    PTM databases

    PhosphoSitei P06681.

    Polymorphism databases

    DMDMi 3915642.

    Proteomic databases

    MaxQBi P06681.
    PaxDbi P06681.
    PRIDEi P06681.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000299367 ; ENSP00000299367 ; ENSG00000166278 . [P06681-1 ]
    ENST00000375510 ; ENSP00000364660 ; ENSG00000204364 . [P06681-1 ]
    ENST00000383362 ; ENSP00000372853 ; ENSG00000206372 . [P06681-1 ]
    ENST00000411803 ; ENSP00000402278 ; ENSG00000235696 . [P06681-1 ]
    ENST00000413548 ; ENSP00000407961 ; ENSG00000231543 . [P06681-1 ]
    ENST00000416252 ; ENSP00000405800 ; ENSG00000235017 . [P06681-1 ]
    ENST00000442278 ; ENSP00000395683 ; ENSG00000166278 . [P06681-3 ]
    ENST00000448206 ; ENSP00000392835 ; ENSG00000226560 . [P06681-1 ]
    ENST00000452323 ; ENSP00000392322 ; ENSG00000166278 . [P06681-2 ]
    ENST00000548973 ; ENSP00000446728 ; ENSG00000206372 . [P06681-3 ]
    ENST00000548995 ; ENSP00000449286 ; ENSG00000204364 . [P06681-3 ]
    ENST00000549972 ; ENSP00000447632 ; ENSG00000235696 . [P06681-3 ]
    ENST00000550682 ; ENSP00000446639 ; ENSG00000231543 . [P06681-3 ]
    ENST00000551081 ; ENSP00000450387 ; ENSG00000235017 . [P06681-3 ]
    ENST00000551648 ; ENSP00000449715 ; ENSG00000226560 . [P06681-3 ]
    GeneIDi 717.
    KEGGi hsa:717.
    UCSCi uc003nyf.3. human. [P06681-1 ]
    uc010jtk.3. human.
    uc011dop.2. human. [P06681-2 ]

    Organism-specific databases

    CTDi 717.
    GeneCardsi GC06P031865.
    GC06Pj31853.
    GC06Pk31847.
    GC06Pl31927.
    GC06Pm31942.
    GC06Pn31855.
    GC06Po31879.
    HGNCi HGNC:1248. C2.
    HPAi CAB016775.
    MIMi 217000. phenotype.
    603075. phenotype.
    613927. gene.
    neXtProti NX_P06681.
    Orphaneti 169147. Immunodeficiency due to an early component of complement deficiency.
    536. Systemic lupus erythematosus.
    PharmGKBi PA25637.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG306397.
    HOGENOMi HOG000038034.
    HOVERGENi HBG002567.
    InParanoidi P06681.
    KOi K01332.
    OMAi RDMTEVI.
    PhylomeDBi P06681.
    TreeFami TF330194.

    Enzyme and pathway databases

    Reactomei REACT_118707. Regulation of Complement cascade.
    REACT_7972. Activation of C3 and C5.
    REACT_8024. Initial triggering of complement.

    Miscellaneous databases

    ChiTaRSi C2. human.
    EvolutionaryTracei P06681.
    GeneWikii Complement_component_2.
    GenomeRNAii 717.
    NextBioi 2918.
    PMAP-CutDB P06681.
    PROi P06681.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P06681.
    Bgeei P06681.
    CleanExi HS_C2.
    Genevestigatori P06681.

    Family and domain databases

    Gene3Di 3.40.50.410. 1 hit.
    InterProi IPR011360. Compl_C2_B.
    IPR001254. Peptidase_S1.
    IPR018114. Peptidase_S1_AS.
    IPR001314. Peptidase_S1A.
    IPR000436. Sushi_SCR_CCP.
    IPR009003. Trypsin-like_Pept_dom.
    IPR002035. VWF_A.
    [Graphical view ]
    Pfami PF00084. Sushi. 2 hits.
    PF00089. Trypsin. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001154. Compl_C2_B. 1 hit.
    PRINTSi PR00722. CHYMOTRYPSIN.
    SMARTi SM00032. CCP. 3 hits.
    SM00020. Tryp_SPc. 1 hit.
    SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50494. SSF50494. 1 hit.
    SSF53300. SSF53300. 1 hit.
    SSF57535. SSF57535. 3 hits.
    PROSITEi PS50923. SUSHI. 3 hits.
    PS50240. TRYPSIN_DOM. 1 hit.
    PS00134. TRYPSIN_HIS. 1 hit.
    PS00135. TRYPSIN_SER. 1 hit.
    PS50234. VWFA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of human complement component C2. Homology to two unrelated protein families."
      Bentley D.R.
      Biochem. J. 239:339-345(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. "cDNA cloning and expression of human complement component C2."
      Horiuchi T., Macon K.J., Kidd V.J., Volanakis J.E.
      J. Immunol. 142:2105-2111(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    3. "Structure of the human C2 gene."
      Ishii Y., Zhu Z.B., Macon K.J., Volanakis J.E.
      J. Immunol. 151:170-174(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Sequence determination of 300 kilobases of the human class III MHC locus."
      Rowen L., Dankers C., Baskin D., Faust J., Loretz C., Ahearn M.E., Banta A., Swartzell S., Smith T.M., Spies T., Hood L.
      Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. SeattleSNPs variation discovery resource
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASP-318 AND CYS-734.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
      Tissue: Kidney and Small intestine.
    7. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 1).
      Tissue: Brain.
    9. "The purification and properties of the second component of guinea-pig complement."
      Kerr M.A., Gagnon J.
      Biochem. J. 205:59-67(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-46 AND 244-256.
    10. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-46.
    11. "A Schistosoma protein, Sh-TOR, is a novel inhibitor of complement which binds human C2."
      Inal J.M., Sim R.B.
      FEBS Lett. 470:131-134(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-28, INTERACTION WITH SCHISTOSOMA HAEMATOBIUM TOR.
    12. "Structure and activation of complement components C2 and factor B."
      Gagnon J.
      Philos. Trans. R. Soc. Lond., B, Biol. Sci. 306:301-309(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 137-171; 454-466 AND 574-717.
    13. "The reaction of iodine and thiol-blocking reagents with human complement components C2 and factor B. Purification and N-terminal amino acid sequence of a peptide from C2a containing a free thiol group."
      Parkes C., Gagnon J., Kerr M.A.
      Biochem. J. 213:201-209(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 244-269.
    14. "Isolation of cDNA clones for human complement component C2."
      Bentley D.R., Porter R.R.
      Proc. Natl. Acad. Sci. U.S.A. 81:1212-1215(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 588-717 (ISOFORM 1).
    15. "Cell-specific expression of the human complement protein factor B gene: evidence for the role of two distinct 5'-flanking elements."
      Wu L.C., Morley B.J., Campbell R.D.
      Cell 48:331-342(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 694-752.
    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-112; ASN-333; ASN-467; ASN-471; ASN-621 AND ASN-651.
      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-112 AND ASN-333.
      Tissue: Liver.
    18. "Structure of complement component C2A: implications for convertase formation and substrate binding."
      Milder F.J., Raaijmakers H.C., Vandeputte M.D., Schouten A., Huizinga E.G., Romijn R.A., Hemrika W., Roos A., Daha M.R., Gros P.
      Structure 14:1587-1597(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 244-752, GLYCOSYLATION AT ASN-333; ASN-467 AND ASN-621, MIDAS-LIKE MOTIF, METAL-BINDING SITES, ACTIVE SITE, DISULFIDE BONDS.
    19. "The structure of C2b, a fragment of complement component C2 produced during C3 convertase formation."
      Krishnan V., Xu Y., Macon K., Volanakis J.E., Narayana S.V.
      Acta Crystallogr. D 65:266-274(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 21-243, DISULFIDE BONDS.
    20. "Type II human complement C2 deficiency. Allele-specific amino acid substitutions (Ser189 --> Phe; Gly444 --> Arg) cause impaired C2 secretion."
      Wetsel R.A., Kulics J., Lokki M.L., Kiepiela P., Akama H., Johnson C.A., Densen P., Colten H.R.
      J. Biol. Chem. 271:5824-5831(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS C2D PHE-209 AND ARG-464.
    21. "A novel type II complement C2 deficiency allele in an African-American family."
      Zhu Z.B., Atkinson T.P., Volanakis J.E.
      J. Immunol. 161:578-584(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT C2D TYR-131.
    22. "Variation in factor B (BF) and complement component 2 (C2) genes is associated with age-related macular degeneration."
      Gold B., Merriam J.E., Zernant J., Hancox L.S., Taiber A.J., Gehrs K., Cramer K., Neel J., Bergeron J., Barile G.R., Smith R.T., Hageman G.S., Dean M., Allikmets R.
      Nat. Genet. 38:458-462(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ASP-318, INVOLVEMENT IN REDUCED RISK OF ARMD.

    Entry informationi

    Entry nameiCO2_HUMAN
    AccessioniPrimary (citable) accession number: P06681
    Secondary accession number(s): B4DPF3
    , B4DV20, E9PFN7, O19694, Q13904
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 172 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

    Miscellaneous

    C2 is a major histocompatibility complex class-III protein.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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