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P06681

- CO2_HUMAN

UniProt

P06681 - CO2_HUMAN

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Protein

Complement C2

Gene

C2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. metal ion binding Source: UniProtKB-KW
  2. 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
Complete GO annotation...

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.
SABIO-RKP06681.

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
  3. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

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.
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

BgeeiP06681.
CleanExiHS_C2.
ExpressionAtlasiP06681. baseline and differential.
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.
GeneTreeiENSGT00530000063826.
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) [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

        10         20         30         40         50
MGPLMVLFCL LFLYPGLADS APSCPQNVNI SGGTFTLSHG WAPGSLLTYS
60 70 80 90 100
CPQGLYPSPA SRLCKSSGQW QTPGATRSLS KAVCKPVRCP APVSFENGIY
110 120 130 140 150
TPRLGSYPVG GNVSFECEDG FILRGSPVRQ CRPNGMWDGE TAVCDNGAGH
160 170 180 190 200
CPNPGISLGA VRTGFRFGHG DKVRYRCSSN LVLTGSSERE CQGNGVWSGT
210 220 230 240 250
EPICRQPYSY DFPEDVAPAL GTSFSHMLGA TNPTQKTKES LGRKIQIQRS
260 270 280 290 300
GHLNLYLLLD CSQSVSENDF LIFKESASLM VDRIFSFEIN VSVAIITFAS
310 320 330 340 350
EPKVLMSVLN DNSRDMTEVI SSLENANYKD HENGTGTNTY AALNSVYLMM
360 370 380 390 400
NNQMRLLGME TMAWQEIRHA IILLTDGKSN MGGSPKTAVD HIREILNINQ
410 420 430 440 450
KRNDYLDIYA IGVGKLDVDW RELNELGSKK DGERHAFILQ DTKALHQVFE
460 470 480 490 500
HMLDVSKLTD TICGVGNMSA NASDQERTPW HVTIKPKSQE TCRGALISDQ
510 520 530 540 550
WVLTAAHCFR DGNDHSLWRV NVGDPKSQWG KEFLIEKAVI SPGFDVFAKK
560 570 580 590 600
NQGILEFYGD DIALLKLAQK VKMSTHARPI CLPCTMEANL ALRRPQGSTC
610 620 630 640 650
RDHENELLNK QSVPAHFVAL NGSKLNINLK MGVEWTSCAE VVSQEKTMFP
660 670 680 690 700
NLTDVREVVT DQFLCSGTQE DESPCKGESG GAVFLERRFR FFQVGLVSWG
710 720 730 740 750
LYNPCLGSAD KNSRKRAPRS KVPPPRDFHI NLFRMQPWLR QHLGDVLNFL

PL
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]
ENST00000612228; ENSP00000482616; ENSG00000231543. [P06681-2]
ENST00000615380; ENSP00000481651; ENSG00000226560. [P06681-2]
ENST00000618254; ENSP00000483231; ENSG00000235017. [P06681-2]
ENST00000621558; ENSP00000480739; ENSG00000206372. [P06681-2]
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 ]
ENST00000612228 ; ENSP00000482616 ; ENSG00000231543 . [P06681-2 ]
ENST00000615380 ; ENSP00000481651 ; ENSG00000226560 . [P06681-2 ]
ENST00000618254 ; ENSP00000483231 ; ENSG00000235017 . [P06681-2 ]
ENST00000621558 ; ENSP00000480739 ; ENSG00000206372 . [P06681-2 ]
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.
PharmGKBi PA25637.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG306397.
GeneTreei ENSGT00530000063826.
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.
SABIO-RK P06681.

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

Bgeei P06681.
CleanExi HS_C2.
ExpressionAtlasi P06681. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 173 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