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P06681 (CO2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 170. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Complement C2

EC=3.4.21.43
Alternative name(s):
C3/C5 convertase

Cleaved into the following 2 chains:

  1. Complement C2b fragment
  2. Complement C2a fragment
Gene names
Name:C2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length752 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 4b to generate the C3 or C5 convertase.

Catalytic activity

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.

Subunit structure

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. Ref.11

Subcellular location

Secreted.

Polymorphism

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19 Ref.20

Miscellaneous

C2 is a major histocompatibility complex class-III protein.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 peptidase S1 domain.

Contains 3 Sushi (CCP/SCR) domains.

Contains 1 VWFA domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P06681-1)

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.
Isoform 2 (identifier: P06681-2)

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.
Isoform 3 (identifier: P06681-3)

The sequence of this isoform differs from the canonical sequence as follows:
     16-147: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Ref.9 Ref.11
Chain21 – 752732Complement C2
PRO_0000027610
Chain21 – 243223Complement C2b fragment
PRO_0000027611
Chain244 – 752509Complement C2a fragment
PRO_0000027612

Regions

Domain22 – 8665Sushi 1
Domain87 – 14660Sushi 2
Domain149 – 20658Sushi 3
Domain254 – 452199VWFA
Domain464 – 744281Peptidase S1

Sites

Active site5071Charge relay system By similarity
Active site5611Charge relay system By similarity
Active site6791Charge relay system By similarity

Amino acid modifications

Glycosylation291N-linked (GlcNAc...) Potential
Glycosylation1121N-linked (GlcNAc...) Ref.16 Ref.17
Glycosylation2901N-linked (GlcNAc...) Potential
Glycosylation3331N-linked (GlcNAc...) Ref.16 Ref.17
Glycosylation4671N-linked (GlcNAc...) Ref.16
Glycosylation4711N-linked (GlcNAc...) Ref.16
Glycosylation6211N-linked (GlcNAc...) Ref.16
Glycosylation6511N-linked (GlcNAc...) (complex) Ref.16
Disulfide bond24 ↔ 64 Ref.18
Disulfide bond51 ↔ 84 Ref.18
Disulfide bond89 ↔ 131 Ref.18
Disulfide bond117 ↔ 144 Ref.18
Disulfide bond151 ↔ 191 Ref.18
Disulfide bond177 ↔ 204 Ref.18
Disulfide bond492 ↔ 508 By similarity
Disulfide bond675 ↔ 705 By similarity

Natural variations

Alternative sequence1 – 147147MGPLM…VCDNG → MRALCIRETCSSELGFSRNW SRRK in isoform 2.
VSP_043038
Alternative sequence16 – 147132Missing in isoform 3.
VSP_046103
Alternative sequence238 – 32891Missing in isoform 2.
VSP_043039
Natural variant1311C → Y in C2D. Ref.20
VAR_008544
Natural variant2091S → F in C2D. Ref.19
Corresponds to variant rs28934590 [ dbSNP | Ensembl ].
VAR_008545
Natural variant3181E → D. Ref.5 Ref.21
Corresponds to variant rs9332739 [ dbSNP | Ensembl ].
VAR_019158
Natural variant4641G → R in C2D. Ref.19
VAR_008546
Natural variant5331F → L.
Corresponds to variant rs1042664 [ dbSNP | Ensembl ].
VAR_011772
Natural variant7341R → C. Ref.5
Corresponds to variant rs4151648 [ dbSNP | Ensembl ].
VAR_019159

Experimental info

Sequence conflict301I → L AA sequence Ref.9
Sequence conflict341T → S AA sequence Ref.9
Sequence conflict2111D → G in BAG62532. Ref.6
Sequence conflict2491R → S AA sequence Ref.9
Sequence conflict2531L → K AA sequence Ref.9

Secondary structure

................................................................................................................................ 752
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 5A96A13E700CF444

FASTA75283,268
        10         20         30         40         50         60 
MGPLMVLFCL LFLYPGLADS APSCPQNVNI SGGTFTLSHG WAPGSLLTYS CPQGLYPSPA 

        70         80         90        100        110        120 
SRLCKSSGQW QTPGATRSLS KAVCKPVRCP APVSFENGIY TPRLGSYPVG GNVSFECEDG 

       130        140        150        160        170        180 
FILRGSPVRQ CRPNGMWDGE TAVCDNGAGH CPNPGISLGA VRTGFRFGHG DKVRYRCSSN 

       190        200        210        220        230        240 
LVLTGSSERE CQGNGVWSGT EPICRQPYSY DFPEDVAPAL GTSFSHMLGA TNPTQKTKES 

       250        260        270        280        290        300 
LGRKIQIQRS GHLNLYLLLD CSQSVSENDF LIFKESASLM VDRIFSFEIN VSVAIITFAS 

       310        320        330        340        350        360 
EPKVLMSVLN DNSRDMTEVI SSLENANYKD HENGTGTNTY AALNSVYLMM NNQMRLLGME 

       370        380        390        400        410        420 
TMAWQEIRHA IILLTDGKSN MGGSPKTAVD HIREILNINQ KRNDYLDIYA IGVGKLDVDW 

       430        440        450        460        470        480 
RELNELGSKK DGERHAFILQ DTKALHQVFE HMLDVSKLTD TICGVGNMSA NASDQERTPW 

       490        500        510        520        530        540 
HVTIKPKSQE TCRGALISDQ WVLTAAHCFR DGNDHSLWRV NVGDPKSQWG KEFLIEKAVI 

       550        560        570        580        590        600 
SPGFDVFAKK NQGILEFYGD DIALLKLAQK VKMSTHARPI CLPCTMEANL ALRRPQGSTC 

       610        620        630        640        650        660 
RDHENELLNK QSVPAHFVAL NGSKLNINLK MGVEWTSCAE VVSQEKTMFP NLTDVREVVT 

       670        680        690        700        710        720 
DQFLCSGTQE DESPCKGESG GAVFLERRFR FFQVGLVSWG LYNPCLGSAD KNSRKRAPRS 

       730        740        750 
KVPPPRDFHI NLFRMQPWLR QHLGDVLNFL PL 

« Hide

Isoform 2 [UniParc].

Checksum: DAD9613AAAF483E8
Show »

FASTA53860,318
Isoform 3 [UniParc].

Checksum: FC295E99940BE04D
Show »

FASTA62069,444

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"DNA polymorphism of the C2 locus."
Bentley D.R., Campbell R.D., Cross S.J.
Immunogenetics 22:377-390(1985) [PubMed] [Europe PMC] [Abstract]
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]"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.
[19]"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.
[20]"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.
[21]"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.
+Additional computationally mapped references.

Web resources

C2base

C2 mutation db

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS4728.1. [P06681-1]
CCDS54991.1. [P06681-3]
CCDS56416.1. [P06681-2]
PIRC2HU. A25971.
RefSeqNP_000054.2. NM_000063.5. [P06681-1]
NP_001139375.1. NM_001145903.2. [P06681-3]
NP_001171534.1. NM_001178063.2. [P06681-2]
UniGeneHs.408903.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2I6QX-ray2.10A244-752[»]
2I6SX-ray2.70A244-752[»]
2ODPX-ray1.90A244-752[»]
2ODQX-ray2.30A244-752[»]
3ERBX-ray1.80A21-243[»]
ProteinModelPortalP06681.
SMRP06681. Positions 23-217, 244-752.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107178. 1 interaction.
IntActP06681. 1 interaction.
STRING9606.ENSP00000372853.

Protein family/group databases

MEROPSS01.194.

PTM databases

PhosphoSiteP06681.

Polymorphism databases

DMDM3915642.

Proteomic databases

MaxQBP06681.
PaxDbP06681.
PRIDEP06681.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299367; 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]
GeneID717.
KEGGhsa:717.
UCSCuc003nyf.3. human. [P06681-1]
uc010jtk.3. human.
uc011dop.2. human. [P06681-2]

Organism-specific databases

CTD717.
GeneCardsGC06P031865.
GC06Pj31853.
GC06Pk31847.
GC06Pl31927.
GC06Pm31942.
GC06Pn31855.
GC06Po31879.
HGNCHGNC:1248. C2.
HPACAB016775.
MIM217000. phenotype.
603075. phenotype.
613927. gene.
neXtProtNX_P06681.
Orphanet169147. Immunodeficiency due to an early component of complement deficiency.
536. Systemic lupus erythematosus.
PharmGKBPA25637.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG306397.
HOGENOMHOG000038034.
HOVERGENHBG002567.
InParanoidP06681.
KOK01332.
OMARDMTEVI.
PhylomeDBP06681.
TreeFamTF330194.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressP06681.
BgeeP06681.
CleanExHS_C2.
GenevestigatorP06681.

Family and domain databases

Gene3D3.40.50.410. 1 hit.
InterProIPR011360. 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]
PfamPF00084. Sushi. 2 hits.
PF00089. Trypsin. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]
PIRSFPIRSF001154. Compl_C2_B. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00032. CCP. 3 hits.
SM00020. Tryp_SPc. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF57535. SSF57535. 3 hits.
PROSITEPS50923. SUSHI. 3 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSC2. human.
EvolutionaryTraceP06681.
GeneWikiComplement_component_2.
GenomeRNAi717.
NextBio2918.
PMAP-CutDBP06681.
PROP06681.
SOURCESearch...

Entry information

Entry nameCO2_HUMAN
AccessionPrimary (citable) accession number: P06681
Secondary accession number(s): B4DPF3 expand/collapse secondary AC list , B4DV20, E9PFN7, O19694, Q13904
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: December 15, 1998
Last modified: July 9, 2014
This is version 170 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM