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P0C0L5

- CO4B_HUMAN

UniProt

P0C0L5 - CO4B_HUMAN

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Protein
Complement C4-B
Gene
C4B, CO4, CPAMD3
C4B_2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Non-enzymatic component of the C3 and C5 convertases and thus essential for the propagation of the classical complement pathway. Covalently binds to immunoglobulins and immune complexes and enhances the solubilization of immune aggregates and the clearance of IC through CR1 on erythrocytes. C4A isotype is responsible for effective binding to form amide bonds with immune aggregates or protein antigens, while C4B isotype catalyzes the transacylation of the thioester carbonyl group to form ester bonds with carbohydrate antigens.2 Publications
Derived from proteolytic degradation of complement C4, C4a anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes.2 Publications

GO - Molecular functioni

  1. carbohydrate binding Source: BHF-UCL
  2. complement binding Source: BHF-UCL
  3. endopeptidase inhibitor activity Source: InterPro
Complete GO annotation...

GO - Biological processi

  1. complement activation Source: BHF-UCL
  2. complement activation, classical pathway Source: UniProtKB-KW
  3. detection of molecule of bacterial origin Source: BHF-UCL
  4. inflammatory response Source: UniProtKB-KW
  5. innate immune response Source: Reactome
  6. opsonization Source: BHF-UCL
  7. positive regulation of apoptotic cell clearance Source: BHF-UCL
  8. regulation of complement activation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Blood group antigen

Keywords - Biological processi

Complement pathway, Immunity, Inflammatory response, Innate immunity

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

MEROPSiI39.951.

Names & Taxonomyi

Organism-specific databases

Protein namesi
Recommended name:
Complement C4-B
Alternative name(s):
Basic complement C4
C3 and PZP-like alpha-2-macroglobulin domain-containing protein 3
Cleaved into the following 6 chains:
Gene namesi
Name:C4B
Synonyms:CO4, CPAMD3
AND
Name:C4B_2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6
HGNCiHGNC:1324. C4B.
HGNC:42398. C4B_2.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. extracellular region Source: Reactome
  3. extracellular space Source: BHF-UCL
  4. extracellular vesicular exosome Source: UniProt
  5. other organism cell Source: BHF-UCL
  6. plasma membrane Source: Reactome

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Systemic lupus erythematosus (SLE) [MIM:152700]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Interindividual copy-number variation (CNV) of complement component C4 and associated polymorphisms result in different susceptibilities to SLE. The risk of SLE susceptibility has been shown to be significantly increased among subjects with only two copies of total C4. A high copy number is a protective factor against SLE.3 Publications
Complement component 4B deficiency (C4BD) [MIM:614379]: A rare defect of the complement classical pathway associated with the development of autoimmune disorders, mainly systemic lupus with or without associated glomerulonephritis.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1120 – 11201L → P: No effect on hemolytic activity, nor on C1-dependent binding to IgG. 1 Publication
Mutagenesisi1121 – 11211S → C: 30-40% decrease in hemolytic activity and C1-dependent binding to IgG. 1 Publication
Mutagenesisi1124 – 11241I → A: 50-60% decrease in hemolytic activity and C1-dependent binding to IgG. 1 Publication
Mutagenesisi1125 – 11251H → A: 20% decrease in hemolytic activity, 2-fold increase in C1-dependent binding to IgG. 1 Publication
Mutagenesisi1125 – 11251H → D: 2.5-3 fold-decrease in hemolytic activity, 3-fold increase in C1-dependent binding to IgG. 1 Publication

Keywords - Diseasei

Systemic lupus erythematosus

Organism-specific databases

MIMi152700. phenotype.
614374. phenotype.
614379. phenotype.
Orphaneti169147. Immunodeficiency due to an early component of complement deficiency.
536. Systemic lupus erythematosus.
PharmGKBiPA25904.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919
Add
BLAST
Chaini20 – 675656Complement C4 beta chain
PRO_0000042699Add
BLAST
Propeptidei676 – 6794
PRO_0000042700
Chaini680 – 1446767Complement C4-B alpha chain
PRO_0000042701Add
BLAST
Chaini680 – 75677C4a anaphylatoxin
PRO_0000042702Add
BLAST
Chaini757 – 1446690C4b-B
PRO_0000042703Add
BLAST
Chaini957 – 1336380C4d-B
PRO_0000042704Add
BLAST
Propeptidei1447 – 14537
PRO_0000042705
Chaini1454 – 1744291Complement C4 gamma chain
PRO_0000042706Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi226 – 2261N-linked (GlcNAc...)1 Publication
Disulfide bondi702 ↔ 728 By similarity
Disulfide bondi703 ↔ 735 By similarity
Disulfide bondi716 ↔ 736 By similarity
Glycosylationi862 – 8621N-linked (GlcNAc...) Reviewed prediction
Cross-linki1010 ↔ 1013Isoglutamyl cysteine thioester (Cys-Gln)
Glycosylationi1328 – 13281N-linked (GlcNAc...)1 Publication
Glycosylationi1391 – 13911N-linked (GlcNAc...)1 Publication
Modified residuei1417 – 14171Sulfotyrosine1 Publication
Modified residuei1420 – 14201Sulfotyrosine1 Publication
Modified residuei1422 – 14221Sulfotyrosine1 Publication
Disulfide bondi1595 ↔ 1673 By similarity
Disulfide bondi1618 ↔ 1742 By similarity

Post-translational modificationi

Prior to secretion, the single-chain precursor is enzymatically cleaved to yield non-identical chains alpha, beta and gamma. During activation, the alpha chain is cleaved by C1 into C4a and C4b, and C4b stays linked to the beta and gamma chains. Further degradation of C4b by C1 into the inactive fragments C4c and C4d blocks the generation of C3 convertase. The proteolytic cleavages often are incomplete so that many structural forms can be found in plasma.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Sulfation, Thioester bond

Proteomic databases

MaxQBiP0C0L5.
PaxDbiP0C0L5.
PRIDEiP0C0L5.

2D gel databases

SWISS-2DPAGEP0C0L5.

PTM databases

PhosphoSiteiP0C0L5.

Expressioni

Tissue specificityi

Complement component C4 is expressed at highest levels in the liver, at moderate levels in the adrenal cortex, adrenal medulla, thyroid gland,and the kidney, and at lowest levels in the heart, ovary, small intestine, thymus, pancreas and spleen. The extra-hepatic sites of expression may be important for the local protection and inflammatory response.1 Publication

Gene expression databases

GenevestigatoriP0C0L5.

Interactioni

Subunit structurei

Circulates in blood as a disulfide-linked trimer of alpha, beta and gamma chains.

Protein-protein interaction databases

BioGridi107182. 1 interaction.
DIPiDIP-47260N.
IntActiP0C0L5. 1 interaction.
STRINGi9606.ENSP00000412786.

Structurei

3D structure databases

ProteinModelPortaliP0C0L5.
SMRiP0C0L5. Positions 20-670, 681-1420, 1455-1744.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini702 – 73635Anaphylatoxin-like
Add
BLAST
Domaini1595 – 1742148NTR
Add
BLAST

Sequence similaritiesi

Contains 1 NTR domain.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2373.
HOVERGENiHBG107123.
InParanoidiP0C0L5.
KOiK03989.
OMAiYAPRQTV.
PhylomeDBiP0C0L5.
TreeFamiTF313285.

Family and domain databases

Gene3Di1.20.91.20. 1 hit.
1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProiIPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR000020. Anaphylatoxin/fibulin.
IPR018081. Anaphylatoxin_comp_syst.
IPR001840. Anaphylatoxn_comp_syst_dom.
IPR001599. Macroglobln_a2.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
IPR001134. Netrin_domain.
IPR018933. Netrin_module_non-TIMP.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008993. TIMP-like_OB-fold.
[Graphical view]
PfamiPF00207. A2M. 1 hit.
PF07678. A2M_comp. 1 hit.
PF01835. A2M_N. 1 hit.
PF07703. A2M_N_2. 1 hit.
PF07677. A2M_recep. 1 hit.
PF01821. ANATO. 1 hit.
PF01759. NTR. 1 hit.
PF10569. Thiol-ester_cl. 1 hit.
[Graphical view]
PRINTSiPR00004. ANAPHYLATOXN.
SMARTiSM00104. ANATO. 1 hit.
SM00643. C345C. 1 hit.
[Graphical view]
SUPFAMiSSF47686. SSF47686. 1 hit.
SSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF50242. SSF50242. 1 hit.
PROSITEiPS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
PS01177. ANAPHYLATOXIN_1. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0C0L5-1 [UniParc]FASTAAdd to Basket

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MRLLWGLIWA SSFFTLSLQK PRLLLFSPSV VHLGVPLSVG VQLQDVPRGQ     50
VVKGSVFLRN PSRNNVPCSP KVDFTLSSER DFALLSLQVP LKDAKSCGLH 100
QLLRGPEVQL VAHSPWLKDS LSRTTNIQGI NLLFSSRRGH LFLQTDQPIY 150
NPGQRVRYRV FALDQKMRPS TDTITVMVEN SHGLRVRKKE VYMPSSIFQD 200
DFVIPDISEP GTWKISARFS DGLESNSSTQ FEVKKYVLPN FEVKITPGKP 250
YILTVPGHLD EMQLDIQARY IYGKPVQGVA YVRFGLLDED GKKTFFRGLE 300
SQTKLVNGQS HISLSKAEFQ DALEKLNMGI TDLQGLRLYV AAAIIESPGG 350
EMEEAELTSW YFVSSPFSLD LSKTKRHLVP GAPFLLQALV REMSGSPASG 400
IPVKVSATVS SPGSVPEVQD IQQNTDGSGQ VSIPIIIPQT ISELQLSVSA 450
GSPHPAIARL TVAAPPSGGP GFLSIERPDS RPPRVGDTLN LNLRAVGSGA 500
TFSHYYYMIL SRGQIVFMNR EPKRTLTSVS VFVDHHLAPS FYFVAFYYHG 550
DHPVANSLRV DVQAGACEGK LELSVDGAKQ YRNGESVKLH LETDSLALVA 600
LGALDTALYA AGSKSHKPLN MGKVFEAMNS YDLGCGPGGG DSALQVFQAA 650
GLAFSDGDQW TLSRKRLSCP KEKTTRKKRN VNFQKAINEK LGQYASPTAK 700
RCCQDGVTRL PMMRSCEQRA ARVQQPDCRE PFLSCCQFAE SLRKKSRDKG 750
QAGLQRALEI LQEEDLIDED DIPVRSFFPE NWLWRVETVD RFQILTLWLP 800
DSLTTWEIHG LSLSKTKGLC VATPVQLRVF REFHLHLRLP MSVRRFEQLE 850
LRPVLYNYLD KNLTVSVHVS PVEGLCLAGG GGLAQQVLVP AGSARPVAFS 900
VVPTAATAVS LKVVARGSFE FPVGDAVSKV LQIEKEGAIH REELVYELNP 950
LDHRGRTLEI PGNSDPNMIP DGDFNSYVRV TASDPLDTLG SEGALSPGGV 1000
ASLLRLPRGC GEQTMIYLAP TLAASRYLDK TEQWSTLPPE TKDHAVDLIQ 1050
KGYMRIQQFR KADGSYAAWL SRGSSTWLTA FVLKVLSLAQ EQVGGSPEKL 1100
QETSNWLLSQ QQADGSFQDL SPVIHRSMQG GLVGNDETVA LTAFVTIALH 1150
HGLAVFQDEG AEPLKQRVEA SISKASSFLG EKASAGLLGA HAAAITAYAL 1200
TLTKAPADLR GVAHNNLMAM AQETGDNLYW GSVTGSQSNA VSPTPAPRNP 1250
SDPMPQAPAL WIETTAYALL HLLLHEGKAE MADQAAAWLT RQGSFQGGFR 1300
STQDTVIALD ALSAYWIASH TTEERGLNVT LSSTGRNGFK SHALQLNNRQ 1350
IRGLEEELQF SLGSKINVKV GGNSKGTLKV LRTYNVLDMK NTTCQDLQIE 1400
VTVKGHVEYT MEANEDYEDY EYDELPAKDD PDAPLQPVTP LQLFEGRRNR 1450
RRREAPKVVE EQESRVHYTV CIWRNGKVGL SGMAIADVTL LSGFHALRAD 1500
LEKLTSLSDR YVSHFETEGP HVLLYFDSVP TSRECVGFEA VQEVPVGLVQ 1550
PASATLYDYY NPERRCSVFY GAPSKSRLLA TLCSAEVCQC AEGKCPRQRR 1600
ALERGLQDED GYRMKFACYY PRVEYGFQVK VLREDSRAAF RLFETKITQV 1650
LHFTKDVKAA ANQMRNFLVR ASCRLRLEPG KEYLIMGLDG ATYDLEGHPQ 1700
YLLDSNSWIE EMPSERLCRS TRQRAACAQL NDFLQEYGTQ GCQV 1744
Length:1,744
Mass (Da):192,751
Last modified:April 3, 2013 - v2
Checksum:iE724B85F7FA673C5
GO

Sequence cautioni

The sequence AAA99717.1 differs from that shown. Reason: Erroneous gene model prediction.

Polymorphismi

The complement component C4 is the most polymorphic protein of the complement system. It is the product of 2 closely linked and highly homologous genes, C4A and C4B. Once polymorphic variation is discounted, the 2 isotypes differ by only 4 amino acids at positions 1120-1125: PCPVLD for C4A and LSPVIH for C4B. The 2 isotypes bear several antigenic determinants defining Chido/Rodgers blood group system [MIMi:614374]. Rodgers determinants are generally associated with C4A allotypes, and Chido with C4B. Variations at these loci involve not only nucleotide polymorphisms, but also gene number and gene size. The second copy of C4B gene present in some individuals has been called C4B_2 by the HUGO Gene Nomenclature Committee (HGNC). Some individuals may lack either C4A, or C4B gene. Partial deficiency of C4A or C4B is the most commonly inherited immune deficiency known in humans with a combined frequency over 31% in the normal Caucasian population (1 Publication).

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti347 – 3471S → Y in allotype C4B-long. 2 Publications
Corresponds to variant rs139889867 [ dbSNP | Ensembl ].
VAR_023729
Natural varianti478 – 4781P → L in allotype C4B1-hi.
VAR_069160
Natural varianti907 – 9071T → A in allotype C4B-long and allotype C4B2. 3 Publications
VAR_023730
Natural varianti1073 – 10731G → D in allotype C4B2 and allotype C4B5-Rg1. 2 Publications
VAR_023731
Natural varianti1176 – 11761S → N in allotype C4B1a. 1 Publication
Corresponds to variant rs2746414 [ dbSNP | Ensembl ].
VAR_023732
Natural varianti1207 – 12071A → V in allotype C4B5-Rg1. 1 Publication
Corresponds to variant rs200888163 [ dbSNP | Ensembl ].
VAR_023734
Natural varianti1210 – 12101R → L in allotype C4B5-Rg1. 1 Publication
Corresponds to variant rs112683215 [ dbSNP | Ensembl ].
VAR_023735
Natural varianti1317 – 13171I → F in allotype C4B1-SC01. 1 Publication
VAR_069161

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti714 – 7141R → S in AAR89101. 1 Publication
Sequence conflicti729 – 7291R → Q in AAR89127. 1 Publication
Sequence conflicti980 – 9812VT → LQ in AAA99717. 1 Publication
Sequence conflicti1013 – 10131Q → E AA sequence 1 Publication
Sequence conflicti1013 – 10131Q → E AA sequence 1 Publication
Sequence conflicti1013 – 10131Q → E AA sequence 1 Publication
Sequence conflicti1109 – 11102SQ → IA AA sequence 1 Publication
Sequence conflicti1271 – 12711H → V AA sequence 1 Publication
Sequence conflicti1271 – 12711H → V AA sequence 1 Publication
Sequence conflicti1300 – 13001R → V AA sequence 1 Publication
Sequence conflicti1300 – 13001R → V AA sequence 1 Publication
Sequence conflicti1654 – 16541T → RA in AAA99717. 1 Publication
Sequence conflicti1698 – 16981H → Q in AAA99717. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U24578 Genomic DNA. Translation: AAA99717.1. Sequence problems.
AF019413 Genomic DNA. Translation: AAB67980.1.
AY379860 Genomic DNA. Translation: AAR89087.1.
AY379862 Genomic DNA. Translation: AAR89089.1.
AY379864 Genomic DNA. Translation: AAR89091.1.
AY379866 Genomic DNA. Translation: AAR89093.1.
AY379868 Genomic DNA. Translation: AAR89095.1.
AY379870 Genomic DNA. Translation: AAR89097.1.
AY379872 Genomic DNA. Translation: AAR89099.1.
AY379874 Genomic DNA. Translation: AAR89101.1.
AY379876 Genomic DNA. Translation: AAR89103.1.
AY379878 Genomic DNA. Translation: AAR89105.1.
AY379880 Genomic DNA. Translation: AAR89107.1.
AY379882 Genomic DNA. Translation: AAR89109.1.
AY379884 Genomic DNA. Translation: AAR89111.1.
AY379886 Genomic DNA. Translation: AAR89113.1.
AY379888 Genomic DNA. Translation: AAR89115.1.
AY379890 Genomic DNA. Translation: AAR89117.1.
AY379892 Genomic DNA. Translation: AAR89119.1.
AY379894 Genomic DNA. Translation: AAR89121.1.
AY379896 Genomic DNA. Translation: AAR89123.1.
AY379898 Genomic DNA. Translation: AAR89125.1.
AY379900 Genomic DNA. Translation: AAR89127.1.
AY379902 Genomic DNA. Translation: AAR89130.1.
AY379904 Genomic DNA. Translation: AAR89132.1.
AY379906 Genomic DNA. Translation: AAR89134.1.
AY379908 Genomic DNA. Translation: AAR89136.1.
AY379910 Genomic DNA. Translation: AAR89138.1.
AY379912 Genomic DNA. Translation: AAR89139.1.
AY379914 Genomic DNA. Translation: AAR89142.1.
AY379916 Genomic DNA. Translation: AAR89144.1.
AY379918 Genomic DNA. Translation: AAR89145.1.
AY379920 Genomic DNA. Translation: AAR89148.1.
AY379922 Genomic DNA. Translation: AAR89150.1.
AY379924 Genomic DNA. Translation: AAR89151.1.
AY379959
, AY379936, AY379937, AY379938, AY379939, AY379940, AY379941, AY379942, AY379943, AY379944, AY379945, AY379946, AY379947, AY379948, AY379949, AY379950, AY379951, AY379952, AY379953, AY379954, AY379955, AY379956, AY379957, AY379958 Genomic DNA. Translation: AAR89163.1.
AL049547 Genomic DNA. Translation: CAB89302.1.
BX679671 Genomic DNA. No translation available.
K02404 mRNA. Translation: AAA59651.1.
U77887 Genomic DNA. Translation: AAK49811.1.
AY343497 Genomic DNA. Translation: AAQ99144.1.
CCDSiCCDS47405.1.
PIRiB20807.
RefSeqiNP_001002029.3. NM_001002029.3.
NP_001229752.1. NM_001242823.2.
UniGeneiHs.534847.
Hs.720022.

Genome annotation databases

EnsembliENST00000375177; ENSP00000364321; ENSG00000228454.
ENST00000411583; ENSP00000407942; ENSG00000228267.
ENST00000435363; ENSP00000415941; ENSG00000224389.
ENST00000435500; ENSP00000412786; ENSG00000233312.
ENST00000449788; ENSP00000414200; ENSG00000236625.
GeneIDi100293534.
721.
KEGGihsa:100293534.
hsa:721.
UCSCiuc011doy.2. human.

Polymorphism databases

DMDMi476007828.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

dbRBC/BGMUT

Blood group antigen gene mutation database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U24578 Genomic DNA. Translation: AAA99717.1 . Sequence problems.
AF019413 Genomic DNA. Translation: AAB67980.1 .
AY379860 Genomic DNA. Translation: AAR89087.1 .
AY379862 Genomic DNA. Translation: AAR89089.1 .
AY379864 Genomic DNA. Translation: AAR89091.1 .
AY379866 Genomic DNA. Translation: AAR89093.1 .
AY379868 Genomic DNA. Translation: AAR89095.1 .
AY379870 Genomic DNA. Translation: AAR89097.1 .
AY379872 Genomic DNA. Translation: AAR89099.1 .
AY379874 Genomic DNA. Translation: AAR89101.1 .
AY379876 Genomic DNA. Translation: AAR89103.1 .
AY379878 Genomic DNA. Translation: AAR89105.1 .
AY379880 Genomic DNA. Translation: AAR89107.1 .
AY379882 Genomic DNA. Translation: AAR89109.1 .
AY379884 Genomic DNA. Translation: AAR89111.1 .
AY379886 Genomic DNA. Translation: AAR89113.1 .
AY379888 Genomic DNA. Translation: AAR89115.1 .
AY379890 Genomic DNA. Translation: AAR89117.1 .
AY379892 Genomic DNA. Translation: AAR89119.1 .
AY379894 Genomic DNA. Translation: AAR89121.1 .
AY379896 Genomic DNA. Translation: AAR89123.1 .
AY379898 Genomic DNA. Translation: AAR89125.1 .
AY379900 Genomic DNA. Translation: AAR89127.1 .
AY379902 Genomic DNA. Translation: AAR89130.1 .
AY379904 Genomic DNA. Translation: AAR89132.1 .
AY379906 Genomic DNA. Translation: AAR89134.1 .
AY379908 Genomic DNA. Translation: AAR89136.1 .
AY379910 Genomic DNA. Translation: AAR89138.1 .
AY379912 Genomic DNA. Translation: AAR89139.1 .
AY379914 Genomic DNA. Translation: AAR89142.1 .
AY379916 Genomic DNA. Translation: AAR89144.1 .
AY379918 Genomic DNA. Translation: AAR89145.1 .
AY379920 Genomic DNA. Translation: AAR89148.1 .
AY379922 Genomic DNA. Translation: AAR89150.1 .
AY379924 Genomic DNA. Translation: AAR89151.1 .
AY379959
, AY379936 , AY379937 , AY379938 , AY379939 , AY379940 , AY379941 , AY379942 , AY379943 , AY379944 , AY379945 , AY379946 , AY379947 , AY379948 , AY379949 , AY379950 , AY379951 , AY379952 , AY379953 , AY379954 , AY379955 , AY379956 , AY379957 , AY379958 Genomic DNA. Translation: AAR89163.1 .
AL049547 Genomic DNA. Translation: CAB89302.1 .
BX679671 Genomic DNA. No translation available.
K02404 mRNA. Translation: AAA59651.1 .
U77887 Genomic DNA. Translation: AAK49811.1 .
AY343497 Genomic DNA. Translation: AAQ99144.1 .
CCDSi CCDS47405.1.
PIRi B20807.
RefSeqi NP_001002029.3. NM_001002029.3.
NP_001229752.1. NM_001242823.2.
UniGenei Hs.534847.
Hs.720022.

3D structure databases

ProteinModelPortali P0C0L5.
SMRi P0C0L5. Positions 20-670, 681-1420, 1455-1744.
ModBasei Search...

Protein-protein interaction databases

BioGridi 107182. 1 interaction.
DIPi DIP-47260N.
IntActi P0C0L5. 1 interaction.
STRINGi 9606.ENSP00000412786.

Protein family/group databases

MEROPSi I39.951.

PTM databases

PhosphoSitei P0C0L5.

Polymorphism databases

DMDMi 476007828.

2D gel databases

SWISS-2DPAGE P0C0L5.

Proteomic databases

MaxQBi P0C0L5.
PaxDbi P0C0L5.
PRIDEi P0C0L5.

Protocols and materials databases

DNASUi 721.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375177 ; ENSP00000364321 ; ENSG00000228454 .
ENST00000411583 ; ENSP00000407942 ; ENSG00000228267 .
ENST00000435363 ; ENSP00000415941 ; ENSG00000224389 .
ENST00000435500 ; ENSP00000412786 ; ENSG00000233312 .
ENST00000449788 ; ENSP00000414200 ; ENSG00000236625 .
GeneIDi 100293534.
721.
KEGGi hsa:100293534.
hsa:721.
UCSCi uc011doy.2. human.

Organism-specific databases

CTDi 100293534.
721.
GeneCardsi GC06P031982.
GC06P031985.
H-InvDB HIX0164690.
HIX0164691.
HIX0166073.
HIX0166340.
HIX0166869.
HIX0167127.
HIX0167359.
HIX0167360.
HGNCi HGNC:1324. C4B.
HGNC:42398. C4B_2.
MIMi 120820. gene.
152700. phenotype.
614374. phenotype.
614379. phenotype.
neXtProti NX_P0C0L5.
Orphaneti 169147. Immunodeficiency due to an early component of complement deficiency.
536. Systemic lupus erythematosus.
PharmGKBi PA25904.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2373.
HOVERGENi HBG107123.
InParanoidi P0C0L5.
KOi K03989.
OMAi YAPRQTV.
PhylomeDBi P0C0L5.
TreeFami TF313285.

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

GeneWikii Complement_component_4B.
NextBioi 20783275.
PROi P0C0L5.
SOURCEi Search...

Gene expression databases

Genevestigatori P0C0L5.

Family and domain databases

Gene3Di 1.20.91.20. 1 hit.
1.50.10.20. 1 hit.
2.60.40.690. 1 hit.
InterProi IPR009048. A-macroglobulin_rcpt-bd.
IPR011626. A2M_comp.
IPR002890. A2M_N.
IPR011625. A2M_N_2.
IPR000020. Anaphylatoxin/fibulin.
IPR018081. Anaphylatoxin_comp_syst.
IPR001840. Anaphylatoxn_comp_syst_dom.
IPR001599. Macroglobln_a2.
IPR019742. MacrogloblnA2_CS.
IPR019565. MacrogloblnA2_thiol-ester-bond.
IPR001134. Netrin_domain.
IPR018933. Netrin_module_non-TIMP.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008993. TIMP-like_OB-fold.
[Graphical view ]
Pfami PF00207. A2M. 1 hit.
PF07678. A2M_comp. 1 hit.
PF01835. A2M_N. 1 hit.
PF07703. A2M_N_2. 1 hit.
PF07677. A2M_recep. 1 hit.
PF01821. ANATO. 1 hit.
PF01759. NTR. 1 hit.
PF10569. Thiol-ester_cl. 1 hit.
[Graphical view ]
PRINTSi PR00004. ANAPHYLATOXN.
SMARTi SM00104. ANATO. 1 hit.
SM00643. C345C. 1 hit.
[Graphical view ]
SUPFAMi SSF47686. SSF47686. 1 hit.
SSF48239. SSF48239. 1 hit.
SSF49410. SSF49410. 1 hit.
SSF50242. SSF50242. 1 hit.
PROSITEi PS00477. ALPHA_2_MACROGLOBULIN. 1 hit.
PS01177. ANAPHYLATOXIN_1. 1 hit.
PS01178. ANAPHYLATOXIN_2. 1 hit.
PS50189. NTR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete sequence of the complement C4 gene from the HLA-A1, B8, C4AQ0, C4B1, DR3 haplotype."
    Ulgiati D., Townend D.C., Christiansen F.T., Dawkins R.L., Abraham L.J.
    Immunogenetics 43:250-252(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-1317.
    Tissue: Blood.
  2. "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 (OCT-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TYR-347 AND ALA-907.
  3. "Molecular genetics of complement C4: implications for MHC evolution and disease susceptibility gene mapping."
    Sayer D., Puschendorf M., Wetherall J.
    Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-907 AND ASP-1073.
  4. "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], VARIANTS TYR-347 AND ALA-907.
  5. "Complete primary structure of human C4a anaphylatoxin."
    Moon K.E., Gorski J.P., Hugli T.E.
    J. Biol. Chem. 256:8685-8692(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 680-756.
  6. "Importance of the alpha 3-fragment of complement C4 for the binding with C4b-binding protein."
    Hessing M., van 't Veer C., Hackeng T.M., Bouma B.N., Iwanaga S.
    FEBS Lett. 271:131-136(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 757-771 AND 980-990.
  7. "The structural basis of the multiple forms of human complement component C4."
    Belt K.T., Carroll M.C., Porter R.R.
    Cell 36:907-914(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 956-1336, VARIANT ASP-1073.
    Tissue: Liver.
  8. "Amino acid sequence around the thiol and reactive acyl groups of human complement component C4."
    Campbell R.D., Gagnon J., Porter R.R.
    Biochem. J. 199:359-370(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 957-1044.
  9. "The chemical structure of the C4d fragment of the human complement component C4."
    Chakravarti D.N., Campbell R.D., Porter R.R.
    Mol. Immunol. 24:1187-1197(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 957-1336.
  10. "Sequence determination of the thiolester site of the fourth component of human complement."
    Harrison R.A., Thomas M.L., Tack B.F.
    Proc. Natl. Acad. Sci. U.S.A. 78:7388-7392(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 990-1037.
  11. "C4d DNA sequences of two infrequent human allotypes (C4A13 and C4B12) and the presence of signal sequences enhancing recombination."
    Martinez-Quiles N., Paz-Artal E., Moreno-Pelayo M.A., Longas J., Ferre-Lopez S., Rosal M., Arnaiz-Villena A.
    J. Immunol. 161:3438-3443(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1055-1225 (ALLOTYPE C4B12).
  12. "C4d DNA sequence of complement C4B93 and recombination mechanisms for its generation."
    Lopez-Goyanes A., Moreno M.A., Ferre S., Paz-Artal E.
    Tissue Antigens 63:260-262(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1055-1225, VARIANTS ASN-1176; VAL-1207 AND LEU-1210.
  13. "Amino acid sequence of a polymorphic segment from fragment C4d of human complement component C4."
    Chakravarti D.N., Campbell R.D., Gagnon J.
    FEBS Lett. 154:387-390(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1199-1304.
  14. "Identification of the site of sulfation of the fourth component of human complement."
    Hortin G., Sims H., Strauss A.W.
    J. Biol. Chem. 261:1786-1793(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1405-1431, SULFATION AT TYR-1417; TYR-1420 AND TYR-1422.
  15. "Complete C4B deficiency in black Americans with systemic lupus erythematosus."
    Wilson W.A., Perez M.C.
    J. Rheumatol. 15:1855-1858(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN C4BD AND SLE.
  16. "Substitution of a single amino acid (aspartic acid for histidine) converts the functional activity of human complement C4B to C4A."
    Carroll M.C., Fathallah D.M., Bergamaschini L., Alicot E.M., Isenman D.E.
    Proc. Natl. Acad. Sci. U.S.A. 87:6868-6872(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INVOLVEMENT OF HIS-1125 IN IMMUNOGLOBULIN-BINDING AND HEMOLYSIS, MUTAGENESIS OF LEU-1120; SER-1121; ILE-1124 AND HIS-1125.
  17. "The reaction mechanism of the internal thioester in the human complement component C4."
    Dodds A.W., Ren X.D., Willis A.C., Law S.K.
    Nature 379:177-179(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "Deficiency of human complement protein C4 due to identical frameshift mutations in the C4A and C4B genes."
    Lokki M.L., Circolo A., Ahokas P., Rupert K.L., Yu C.Y., Colten H.R.
    J. Immunol. 162:3687-3693(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN SLE.
  19. "Genetic, structural and functional diversities of human complement components C4A and C4B and their mouse homologues, Slp and C4."
    Blanchong C.A., Chung E.K., Rupert K.L., Yang Y., Yang Z., Zhou B., Moulds J.M., Yu C.Y.
    Int. Immunopharmacol. 1:365-392(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, DESCRIPTION OF ALLOTYPES, TISSUE SPECIFICITY.
  20. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
    Zhang H., Li X.-J., Martin D.B., Aebersold R.
    Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-226.
  21. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
    Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
    Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1391.
    Tissue: Plasma.
  22. "Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
    Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
    J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1328.
    Tissue: Saliva.
  23. "Structural basis of the polymorphism of human complement components C4A and C4B: gene size, reactivity and antigenicity."
    Yu C.Y., Belt K.T., Giles C.M., Campbell R.D., Porter R.R.
    EMBO J. 5:2873-2881(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURAL BASIS OF POLYMORPHISM.
  24. "Gene copy-number variation and associated polymorphisms of complement component C4 in human systemic lupus erythematosus (SLE): low copy number is a risk factor for and high copy number is a protective factor against SLE susceptibility in European Americans."
    Yang Y., Chung E.K., Wu Y.L., Savelli S.L., Nagaraja H.N., Zhou B., Hebert M., Jones K.N., Shu Y., Kitzmiller K., Blanchong C.A., McBride K.L., Higgins G.C., Rennebohm R.M., Rice R.R., Hackshaw K.V., Roubey R.A., Grossman J.M.
    , Tsao B.P., Birmingham D.J., Rovin B.H., Hebert L.A., Yu C.Y.
    Am. J. Hum. Genet. 80:1037-1054(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN SLE.

Entry informationi

Entry nameiCO4B_HUMAN
AccessioniPrimary (citable) accession number: P0C0L5
Secondary accession number(s): A2BHY4
, P01028, P78445, Q13160, Q13906, Q14033, Q14835, Q6U2E9, Q6U2G1, Q6U2I5, Q6U2L1, Q6U2L7, Q6U2L9, Q6U2M5, Q6VCV8, Q96SA7, Q9NPK5, Q9UIP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 3, 2013
Last modified: September 3, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Blood group antigen proteins
    Nomenclature of blood group antigens and list of entries
  2. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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