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P0C0L4

- CO4A_HUMAN

UniProt

P0C0L4 - CO4A_HUMAN

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Protein

Complement C4-A

Gene

C4A

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

Functioni

Non-enzymatic component of 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.
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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1125 – 11251Responsible for effective binding to form amide bonds with immune aggregates or protein antigens

GO - Molecular functioni

  1. complement component C1q binding Source: BHF-UCL
  2. endopeptidase inhibitor activity Source: InterPro

GO - Biological processi

  1. complement activation Source: BHF-UCL
  2. complement activation, classical pathway Source: UniProtKB-KW
  3. inflammatory response Source: UniProtKB-KW
  4. innate immune response Source: Reactome
  5. positive regulation of apoptotic cell clearance Source: BHF-UCL
  6. 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.
SABIO-RKP0C0L4.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement C4-A
Alternative name(s):
Acidic complement C4
C3 and PZP-like alpha-2-macroglobulin domain-containing protein 2
Cleaved into the following 6 chains:
Gene namesi
Name:C4A
Synonyms:CO4, CPAMD2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6, UP000005640: Unplaced

Organism-specific databases

HGNCiHGNC:1323. C4A.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. extracellular region Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Complement component 4A deficiency (C4AD) [MIM:614380]: A rare defect of the complement classical pathway associated with the development of autoimmune disorders, mainly systemic lupus with or without associated glomerulonephritis.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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.2 Publications
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.

Keywords - Diseasei

Disease mutation, Systemic lupus erythematosus

Organism-specific databases

MIMi120790. phenotype.
152700. phenotype.
614374. phenotype.
614380. phenotype.
Orphaneti117. Behcet disease.
169147. Immunodeficiency due to an early component of complement deficiency.
536. Systemic lupus erythematosus.
PharmGKBiPA25903.
PA25904.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Add
BLAST
Chaini20 – 675656Complement C4 beta chainPRO_0000005966Add
BLAST
Propeptidei676 – 67941 PublicationPRO_0000005967
Chaini680 – 1446767Complement C4-A alpha chainPRO_0000005968Add
BLAST
Chaini680 – 75677C4a anaphylatoxinPRO_0000005969Add
BLAST
Chaini757 – 1446690C4b-APRO_0000005970Add
BLAST
Chaini957 – 1336380C4d-APRO_0000042698Add
BLAST
Propeptidei1447 – 14537PRO_0000005971
Chaini1454 – 1744291Complement C4 gamma chainPRO_0000005972Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi226 – 2261N-linked (GlcNAc...)3 Publications
Disulfide bondi702 ↔ 728By similarity
Disulfide bondi703 ↔ 735By similarity
Disulfide bondi716 ↔ 736By similarity
Glycosylationi862 – 8621N-linked (GlcNAc...)1 Publication
Cross-linki1010 ↔ 1013Isoglutamyl cysteine thioester (Cys-Gln)
Glycosylationi1244 – 12441O-linked (GalNAc...)1 Publication
Glycosylationi1328 – 13281N-linked (GlcNAc...) (complex)4 Publications
Glycosylationi1391 – 13911N-linked (GlcNAc...)3 Publications
Modified residuei1417 – 14171Sulfotyrosine1 Publication
Modified residuei1420 – 14201Sulfotyrosine1 Publication
Modified residuei1422 – 14221Sulfotyrosine1 Publication
Disulfide bondi1595 ↔ 1673By similarity
Disulfide bondi1618 ↔ 1742By 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.
N- and O-glycosylated. O-glycosylated with a core 1 or possibly core 8 glycan.8 Publications

Keywords - PTMi

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

Proteomic databases

PaxDbiP0C0L4.
PRIDEiP0C0L4.

PTM databases

PhosphoSiteiP0C0L4.

Miscellaneous databases

PMAP-CutDBB0QZR6.

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

BgeeiP0C0L4.
ExpressionAtlasiP0C0L4. baseline.
GenevestigatoriP0C0L4.

Organism-specific databases

HPAiCAB009811.
CAB032603.
HPA046356.
HPA048287.
HPA050103.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi107181. 8 interactions.
IntActiP0C0L4. 11 interactions.
STRINGi9606.ENSP00000364444.

Structurei

Secondary structure

1
1744
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi997 – 10015Combined sources
Helixi1011 – 103020Combined sources
Helixi1041 – 105717Combined sources
Helixi1076 – 108914Combined sources
Helixi1090 – 10923Combined sources
Helixi1097 – 110711Combined sources
Helixi1108 – 11103Combined sources
Helixi1126 – 11327Combined sources
Helixi1137 – 115317Combined sources
Turni1158 – 11614Combined sources
Helixi1162 – 118524Combined sources
Helixi1190 – 120213Combined sources
Helixi1207 – 121812Combined sources
Helixi1259 – 127517Combined sources
Helixi1280 – 129213Combined sources
Helixi1302 – 131918Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HZFX-ray2.30A957-1323[»]
4FXGX-ray3.75A/D20-675[»]
B/E680-1446[»]
C/F1454-1744[»]
4FXKX-ray3.60A20-675[»]
B680-1446[»]
C1454-1744[»]
ProteinModelPortaliP0C0L4.
SMRiP0C0L4. Positions 20-670, 681-1420, 1455-1744.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C0L4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini702 – 73635Anaphylatoxin-likePROSITE-ProRule annotationAdd
BLAST
Domaini1595 – 1742148NTRPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 anaphylatoxin-like domain.PROSITE-ProRule annotation
Contains 1 NTR domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2373.
GeneTreeiENSGT00760000118982.
HOVERGENiHBG107123.
InParanoidiP0C0L4.
KOiK03989.
OMAiTHQGGFQ.
PhylomeDBiP0C0L4.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P0C0L4-1) [UniParc]FASTAAdd to Basket

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

« Hide

        10         20         30         40         50
MRLLWGLIWA SSFFTLSLQK PRLLLFSPSV VHLGVPLSVG VQLQDVPRGQ
60 70 80 90 100
VVKGSVFLRN PSRNNVPCSP KVDFTLSSER DFALLSLQVP LKDAKSCGLH
110 120 130 140 150
QLLRGPEVQL VAHSPWLKDS LSRTTNIQGI NLLFSSRRGH LFLQTDQPIY
160 170 180 190 200
NPGQRVRYRV FALDQKMRPS TDTITVMVEN SHGLRVRKKE VYMPSSIFQD
210 220 230 240 250
DFVIPDISEP GTWKISARFS DGLESNSSTQ FEVKKYVLPN FEVKITPGKP
260 270 280 290 300
YILTVPGHLD EMQLDIQARY IYGKPVQGVA YVRFGLLDED GKKTFFRGLE
310 320 330 340 350
SQTKLVNGQS HISLSKAEFQ DALEKLNMGI TDLQGLRLYV AAAIIESPGG
360 370 380 390 400
EMEEAELTSW YFVSSPFSLD LSKTKRHLVP GAPFLLQALV REMSGSPASG
410 420 430 440 450
IPVKVSATVS SPGSVPEVQD IQQNTDGSGQ VSIPIIIPQT ISELQLSVSA
460 470 480 490 500
GSPHPAIARL TVAAPPSGGP GFLSIERPDS RPPRVGDTLN LNLRAVGSGA
510 520 530 540 550
TFSHYYYMIL SRGQIVFMNR EPKRTLTSVS VFVDHHLAPS FYFVAFYYHG
560 570 580 590 600
DHPVANSLRV DVQAGACEGK LELSVDGAKQ YRNGESVKLH LETDSLALVA
610 620 630 640 650
LGALDTALYA AGSKSHKPLN MGKVFEAMNS YDLGCGPGGG DSALQVFQAA
660 670 680 690 700
GLAFSDGDQW TLSRKRLSCP KEKTTRKKRN VNFQKAINEK LGQYASPTAK
710 720 730 740 750
RCCQDGVTRL PMMRSCEQRA ARVQQPDCRE PFLSCCQFAE SLRKKSRDKG
760 770 780 790 800
QAGLQRALEI LQEEDLIDED DIPVRSFFPE NWLWRVETVD RFQILTLWLP
810 820 830 840 850
DSLTTWEIHG LSLSKTKGLC VATPVQLRVF REFHLHLRLP MSVRRFEQLE
860 870 880 890 900
LRPVLYNYLD KNLTVSVHVS PVEGLCLAGG GGLAQQVLVP AGSARPVAFS
910 920 930 940 950
VVPTAAAAVS LKVVARGSFE FPVGDAVSKV LQIEKEGAIH REELVYELNP
960 970 980 990 1000
LDHRGRTLEI PGNSDPNMIP DGDFNSYVRV TASDPLDTLG SEGALSPGGV
1010 1020 1030 1040 1050
ASLLRLPRGC GEQTMIYLAP TLAASRYLDK TEQWSTLPPE TKDHAVDLIQ
1060 1070 1080 1090 1100
KGYMRIQQFR KADGSYAAWL SRDSSTWLTA FVLKVLSLAQ EQVGGSPEKL
1110 1120 1130 1140 1150
QETSNWLLSQ QQADGSFQDP CPVLDRSMQG GLVGNDETVA LTAFVTIALH
1160 1170 1180 1190 1200
HGLAVFQDEG AEPLKQRVEA SISKANSFLG EKASAGLLGA HAAAITAYAL
1210 1220 1230 1240 1250
TLTKAPVDLL GVAHNNLMAM AQETGDNLYW GSVTGSQSNA VSPTPAPRNP
1260 1270 1280 1290 1300
SDPMPQAPAL WIETTAYALL HLLLHEGKAE MADQASAWLT RQGSFQGGFR
1310 1320 1330 1340 1350
STQDTVIALD ALSAYWIASH TTEERGLNVT LSSTGRNGFK SHALQLNNRQ
1360 1370 1380 1390 1400
IRGLEEELQF SLGSKINVKV GGNSKGTLKV LRTYNVLDMK NTTCQDLQIE
1410 1420 1430 1440 1450
VTVKGHVEYT MEANEDYEDY EYDELPAKDD PDAPLQPVTP LQLFEGRRNR
1460 1470 1480 1490 1500
RRREAPKVVE EQESRVHYTV CIWRNGKVGL SGMAIADVTL LSGFHALRAD
1510 1520 1530 1540 1550
LEKLTSLSDR YVSHFETEGP HVLLYFDSVP TSRECVGFEA VQEVPVGLVQ
1560 1570 1580 1590 1600
PASATLYDYY NPERRCSVFY GAPSKSRLLA TLCSAEVCQC AEGKCPRQRR
1610 1620 1630 1640 1650
ALERGLQDED GYRMKFACYY PRVEYGFQVK VLREDSRAAF RLFETKITQV
1660 1670 1680 1690 1700
LHFTKDVKAA ANQMRNFLVR ASCRLRLEPG KEYLIMGLDG ATYDLEGHPQ
1710 1720 1730 1740
YLLDSNSWIE EMPSERLCRS TRQRAACAQL NDFLQEYGTQ GCQV
Length:1,744
Mass (Da):192,785
Last modified:April 3, 2013 - v2
Checksum:i9396A4CC4DA3602C
GO
Isoform 2 (identifier: P0C0L4-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1458-1503: Missing.

Note: No experimental confirmation available.

Show »
Length:1,698
Mass (Da):187,704
Checksum:i6169C0C84E28C512
GO

Sequence cautioni

The sequence AAB59537.1 differs from that shown. Reason: During cDNA synthesis, the 5' end has been inverted (PubMed:3838531).1 Publication
The sequence BAE06071.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti217 – 2171A → V in AAI71786. (PubMed:15489334)Curated
Sequence conflicti643 – 6431A → S in AAH63289. (PubMed:15489334)Curated
Sequence conflicti729 – 7291R → W in AAH63289. (PubMed:15489334)Curated
Sequence conflicti1013 – 10131Q → E AA sequence (PubMed:6978711)Curated
Sequence conflicti1013 – 10131Q → E AA sequence (PubMed:3696167)Curated
Sequence conflicti1013 – 10131Q → E AA sequence (PubMed:6950384)Curated
Sequence conflicti1109 – 11102SQ → IA AA sequence (PubMed:3696167)Curated
Sequence conflicti1182 – 11821K → I in AAH63289. (PubMed:15489334)Curated
Sequence conflicti1245 – 12451P → Q in AAH63289. (PubMed:15489334)Curated
Sequence conflicti1271 – 12711H → V AA sequence (PubMed:3696167)Curated
Sequence conflicti1271 – 12711H → V AA sequence (PubMed:6832377)Curated
Sequence conflicti1300 – 13001R → V AA sequence (PubMed:3696167)Curated
Sequence conflicti1300 – 13001R → V AA sequence (PubMed:6832377)Curated
Sequence conflicti1419 – 14213Missing in AAB59537. (PubMed:6546707)Curated
Sequence conflicti1635 – 16351D → G in AAH12372. (PubMed:15489334)Curated
Sequence conflicti1637 – 16371R → S in AAI44547. (PubMed:15489334)Curated
Sequence conflicti1637 – 16371R → S in AAI46850. (PubMed:15489334)Curated
Sequence conflicti1678 – 16781E → G in AAI71786. (PubMed:15489334)Curated
Sequence conflicti1704 – 17041D → E in AAH12372. (PubMed:15489334)Curated

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. 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 (PubMed:11367523). C4A6 allotype is deficient in hemolytic activity. Allotype C4A13 is infrequent.1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti141 – 1411L → V.
Corresponds to variant rs9296005 [ dbSNP | Ensembl ].
VAR_069154
Natural varianti347 – 3471S → Y in allotype C4A3a, allotype C4A6. 3 Publications
Corresponds to variant rs150969927 [ dbSNP | Ensembl ].
VAR_019778
Natural varianti418 – 4181V → A in allotype C4A4. 1 Publication
VAR_069155
Natural varianti477 – 4771R → W in allotype C4A6. 1 Publication
VAR_001987
Natural varianti549 – 5491H → P.1 Publication
Corresponds to variant rs2229405 [ dbSNP | Ensembl ].
VAR_069156
Natural varianti564 – 5641A → D.
Corresponds to variant rs35277227 [ dbSNP | Ensembl ].
VAR_069157
Natural varianti726 – 7261P → L in allotype C4A3a. 1 Publication
VAR_001988
Natural varianti727 – 7271D → N.1 Publication
VAR_019779
Natural varianti907 – 9071A → T.1 Publication
Corresponds to variant rs141302872 [ dbSNP | Ensembl ].
VAR_019780
Natural varianti1073 – 10731D → G in allotype C4A1, allotype C4A2. 3 Publications
Corresponds to variant rs147162052 [ dbSNP | Ensembl ].
VAR_069158
Natural varianti1176 – 11761N → S in allotype C4A1. 4 Publications
Corresponds to variant rs17874654 [ dbSNP | Ensembl ].
VAR_069159
Natural varianti1201 – 12011T → S in allotype C4A4. 1 Publication
VAR_001992
Natural varianti1207 – 12071V → A in allotype C4A1, allotype C4A13. 3 Publications
Corresponds to variant rs28357075 [ dbSNP | Ensembl ].
VAR_001993
Natural varianti1210 – 12101L → R in allotype C4A1, allotype C4A13. 3 Publications
Corresponds to variant rs28357076 [ dbSNP | Ensembl ].
VAR_001994
Natural varianti1286 – 12861S → A in allotype C4A1, allotype C4A3a, allotype C4A6. 6 Publications
Corresponds to variant rs201016130 [ dbSNP | Ensembl ].
VAR_001995

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1458 – 150346Missing in isoform 2. 1 PublicationVSP_046252Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02403 mRNA. Translation: AAB59537.1. Sequence problems.
M59815, M59816 Genomic DNA. Translation: AAA51855.1.
L26261 Genomic DNA. Translation: AAA20121.2.
AB209989 mRNA. Translation: BAE06071.1. Different initiation.
AL645922 Genomic DNA. No translation available.
AL844853 Genomic DNA. No translation available.
AL929593 Genomic DNA. No translation available.
CR936924 Genomic DNA. No translation available.
BC012372 mRNA. Translation: AAH12372.2.
BC063289 mRNA. Translation: AAH63289.1.
BC144546 mRNA. Translation: AAI44547.1.
BC146673 mRNA. Translation: AAI46674.1.
BC146849 mRNA. Translation: AAI46850.1.
BC151204 mRNA. Translation: AAI51205.1.
BC171786 mRNA. Translation: AAI71786.1.
M14824 Genomic DNA. Translation: AAA52292.1.
X77491 Genomic DNA. Translation: CAA54627.1.
AY379925 Genomic DNA. Translation: AAR89152.1.
AY379926 Genomic DNA. Translation: AAR89153.1.
AY379927 Genomic DNA. Translation: AAR89154.1.
AY379928 Genomic DNA. Translation: AAR89155.1.
AY379929 Genomic DNA. Translation: AAR89156.1.
AY379930 Genomic DNA. Translation: AAR89157.1.
AY379931 Genomic DNA. Translation: AAR89158.1.
AY379932 Genomic DNA. Translation: AAR89159.1.
AY379933 Genomic DNA. Translation: AAR89160.1.
AY379934 Genomic DNA. Translation: AAR89161.1.
AY379935 Genomic DNA. Translation: AAR89162.1.
AY379960 Genomic DNA. Translation: AAR89164.1.
AY379962 Genomic DNA. Translation: AAR89166.1.
AY379963 Genomic DNA. Translation: AAR89167.1.
AY379964 Genomic DNA. Translation: AAR89168.1.
AY379965 Genomic DNA. Translation: AAR89169.1.
AY379966 Genomic DNA. Translation: AAR89170.1.
U77886 Genomic DNA. Translation: AAK49810.1.
V00502 mRNA. Translation: CAA23760.1.
K00830 mRNA. Translation: AAA36229.1.
CCDSiCCDS47404.1. [P0C0L4-1]
CCDS59005.1. [P0C0L4-2]
PIRiB20807.
I56095. C4HU.
RefSeqiNP_001002029.3. NM_001002029.3.
NP_001239133.1. NM_001252204.1. [P0C0L4-2]
NP_009224.2. NM_007293.2. [P0C0L4-1]
UniGeneiHs.534847.
Hs.720022.

Genome annotation databases

EnsembliENST00000383325; ENSP00000372815; ENSG00000206340.
ENST00000421274; ENSP00000388662; ENSG00000227746.
ENST00000428956; ENSP00000396688; ENSG00000244731. [P0C0L4-1]
ENST00000498271; ENSP00000420212; ENSG00000244731. [P0C0L4-2]
GeneIDi720.
721.
KEGGihsa:720.
hsa:721.
UCSCiuc011doz.2. human.

Polymorphism databases

DMDMi476007827.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

dbRBC/BGMUT

Blood group antigen gene mutation database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02403 mRNA. Translation: AAB59537.1 . Sequence problems.
M59815 , M59816 Genomic DNA. Translation: AAA51855.1 .
L26261 Genomic DNA. Translation: AAA20121.2 .
AB209989 mRNA. Translation: BAE06071.1 . Different initiation.
AL645922 Genomic DNA. No translation available.
AL844853 Genomic DNA. No translation available.
AL929593 Genomic DNA. No translation available.
CR936924 Genomic DNA. No translation available.
BC012372 mRNA. Translation: AAH12372.2 .
BC063289 mRNA. Translation: AAH63289.1 .
BC144546 mRNA. Translation: AAI44547.1 .
BC146673 mRNA. Translation: AAI46674.1 .
BC146849 mRNA. Translation: AAI46850.1 .
BC151204 mRNA. Translation: AAI51205.1 .
BC171786 mRNA. Translation: AAI71786.1 .
M14824 Genomic DNA. Translation: AAA52292.1 .
X77491 Genomic DNA. Translation: CAA54627.1 .
AY379925 Genomic DNA. Translation: AAR89152.1 .
AY379926 Genomic DNA. Translation: AAR89153.1 .
AY379927 Genomic DNA. Translation: AAR89154.1 .
AY379928 Genomic DNA. Translation: AAR89155.1 .
AY379929 Genomic DNA. Translation: AAR89156.1 .
AY379930 Genomic DNA. Translation: AAR89157.1 .
AY379931 Genomic DNA. Translation: AAR89158.1 .
AY379932 Genomic DNA. Translation: AAR89159.1 .
AY379933 Genomic DNA. Translation: AAR89160.1 .
AY379934 Genomic DNA. Translation: AAR89161.1 .
AY379935 Genomic DNA. Translation: AAR89162.1 .
AY379960 Genomic DNA. Translation: AAR89164.1 .
AY379962 Genomic DNA. Translation: AAR89166.1 .
AY379963 Genomic DNA. Translation: AAR89167.1 .
AY379964 Genomic DNA. Translation: AAR89168.1 .
AY379965 Genomic DNA. Translation: AAR89169.1 .
AY379966 Genomic DNA. Translation: AAR89170.1 .
U77886 Genomic DNA. Translation: AAK49810.1 .
V00502 mRNA. Translation: CAA23760.1 .
K00830 mRNA. Translation: AAA36229.1 .
CCDSi CCDS47404.1. [P0C0L4-1 ]
CCDS59005.1. [P0C0L4-2 ]
PIRi B20807.
I56095. C4HU.
RefSeqi NP_001002029.3. NM_001002029.3.
NP_001239133.1. NM_001252204.1. [P0C0L4-2 ]
NP_009224.2. NM_007293.2. [P0C0L4-1 ]
UniGenei Hs.534847.
Hs.720022.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1HZF X-ray 2.30 A 957-1323 [» ]
4FXG X-ray 3.75 A/D 20-675 [» ]
B/E 680-1446 [» ]
C/F 1454-1744 [» ]
4FXK X-ray 3.60 A 20-675 [» ]
B 680-1446 [» ]
C 1454-1744 [» ]
ProteinModelPortali P0C0L4.
SMRi P0C0L4. Positions 20-670, 681-1420, 1455-1744.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107181. 8 interactions.
IntActi P0C0L4. 11 interactions.
STRINGi 9606.ENSP00000364444.

Chemistry

DrugBanki DB00028. Intravenous Immunoglobulin.

PTM databases

PhosphoSitei P0C0L4.

Polymorphism databases

DMDMi 476007827.

Proteomic databases

PaxDbi P0C0L4.
PRIDEi P0C0L4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000383325 ; ENSP00000372815 ; ENSG00000206340 .
ENST00000421274 ; ENSP00000388662 ; ENSG00000227746 .
ENST00000428956 ; ENSP00000396688 ; ENSG00000244731 . [P0C0L4-1 ]
ENST00000498271 ; ENSP00000420212 ; ENSG00000244731 . [P0C0L4-2 ]
GeneIDi 720.
721.
KEGGi hsa:720.
hsa:721.
UCSCi uc011doz.2. human.

Organism-specific databases

CTDi 720.
721.
GeneCardsi GC06P031993.
GC06Pm32059.
GC06Pn31940.
HGNCi HGNC:1323. C4A.
HPAi CAB009811.
CAB032603.
HPA046356.
HPA048287.
HPA050103.
MIMi 120790. phenotype.
120810. gene.
152700. phenotype.
614374. phenotype.
614380. phenotype.
neXtProti NX_P0C0L4.
Orphaneti 117. Behcet disease.
169147. Immunodeficiency due to an early component of complement deficiency.
536. Systemic lupus erythematosus.
PharmGKBi PA25903.
PA25904.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2373.
GeneTreei ENSGT00760000118982.
HOVERGENi HBG107123.
InParanoidi P0C0L4.
KOi K03989.
OMAi THQGGFQ.
PhylomeDBi P0C0L4.
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.
SABIO-RK P0C0L4.

Miscellaneous databases

EvolutionaryTracei P0C0L4.
GeneWikii C4A.
NextBioi 13630656.
PMAP-CutDB B0QZR6.
PROi P0C0L4.
SOURCEi Search...

Gene expression databases

Bgeei P0C0L4.
ExpressionAtlasi P0C0L4. baseline.
Genevestigatori P0C0L4.

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

« Hide 'large scale' publications
  1. "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] (ISOFORM 1), VARIANTS ALA-418 AND SER-1201.
    Tissue: Liver.
  2. "The complete exon-intron structure of a human complement component C4A gene. DNA sequences, polymorphism, and linkage to the 21-hydroxylase gene."
    Yu C.Y.
    J. Immunol. 146:1057-1066(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS TYR-347; LEU-726 AND ALA-1286.
  3. "Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
    Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS SER-1176 AND ALA-1286.
    Tissue: Brain.
  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; SER-1176 AND ALA-1286.
  5. "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] (ISOFORMS 1 AND 2), VARIANTS TYR-347; GLY-1073 AND ALA-1286.
    Tissue: Brain.
  6. "Polymorphism of human complement component C4."
    Belt K.T., Yu C.Y., Carroll M.C., Porter R.R.
    Immunogenetics 21:173-180(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22 AND 1056-1225.
  7. "Characterisation of the novel gene G11 lying adjacent to the complement C4A gene in the human major histocompatibility complex."
    Sargent C.A., Anderson M.J., Hsieh S.-L., Kendall E., Gomez-Escobar N., Campbell R.D.
    Hum. Mol. Genet. 3:481-488(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21, VARIANT ASN-727.
  8. "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] OF 448-570 AND 692-1225, VARIANTS TRP-477; PRO-549; THR-907; GLY-1073; SER-1176; ALA-1207 AND ARG-1210.
  9. "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.
  10. "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.
  11. "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.
  12. "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, VARIANTS GLY-1073; SER-1176; ALA-1207; ARG-1210 AND ALA-1286.
  13. "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.
  14. "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 C4A13).
  15. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1195-1294.
  16. "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, VARIANTS ALA-1207; ARG-1210 AND ALA-1286.
  17. "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.
  18. "Use of a cDNA clone for the fourth component of human complement (C4) for analysis of a genetic deficiency of C4 in guinea pig."
    Whitehead A.S., Goldberger G., Woods D.E., Markham A.F., Colten H.R.
    Proc. Natl. Acad. Sci. U.S.A. 80:5387-5391(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1448-1474.
  19. "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 ASP-1125 IN IMMUNOGLOBULIN-BINDING AND HEMOLYSIS.
  20. "Genetic basis of human complement C4A deficiency. Detection of a point mutation leading to nonexpression."
    Barba G., Rittner C., Schneider P.M.
    J. Clin. Invest. 91:1681-1686(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN C4AD.
  21. "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.
  22. "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.
  23. "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.
  24. "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.
  25. "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.
  26. "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.
  27. "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-862; ASN-1328 AND ASN-1391.
    Tissue: Plasma.
  28. "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.
  29. "Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry."
    Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.
    Proteomics 8:3833-3847(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-226 AND ASN-1328.
    Tissue: Milk.
  30. "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-226; ASN-1328 AND ASN-1391.
    Tissue: Liver.
  31. Cited for: GLYCOSYLATION AT ASN-1328.
  32. "Enrichment of glycopeptides for glycan structure and attachment site identification."
    Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
    Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS], STRUCTURE OF CARBOHYDRATES.
    Tissue: Cerebrospinal fluid.
  33. "LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
    Halim A., Ruetschi U., Larson G., Nilsson J.
    J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT THR-1244, IDENTIFICATION BY MASS SPECTROMETRY.
  34. "X-ray crystal structure of the C4d fragment of human complement component C4."
    van den Elsen J.M., Martin A., Wong V., Clemenza L., Rose D.R., Isenman D.E.
    J. Mol. Biol. 322:1103-1115(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 957-1323.
  35. "The coding sequence of the hemolytically inactive C4A6 allotype of human complement component C4 reveals that a single arginine to tryptophan substitution at beta-chain residue 458 is the likely cause of the defect."
    Anderson M.J., Milner C.M., Cotton G.H., Campbell R.D.
    J. Immunol. 148:2795-2802(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ALA-1286 (ALLOTYPE C4A6).

Entry informationi

Entry nameiCO4A_HUMAN
AccessioniPrimary (citable) accession number: P0C0L4
Secondary accession number(s): A6H8M8
, A6NHJ5, A7E2V2, B0QZR6, B0V2C8, B2RUT6, B7ZVZ6, P01028, P78445, Q13160, Q13906, Q14033, Q14835, Q4LE82, Q5JNX2, Q5JQM8, Q6P4R1, Q6U2E5, Q6U2E8, Q6U2F0, Q6U2F3, Q6U2F4, Q6U2F6, Q6U2F8, Q6U2G0, Q96EG2, Q96SA8, Q9NPK5, Q9UIP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 3, 2013
Last modified: November 26, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3