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P17927

- CR1_HUMAN

UniProt

P17927 - CR1_HUMAN

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Protein

Complement receptor type 1

Gene

CR1

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

Functioni

Mediates cellular binding of particles and immune complexes that have activated complement.

GO - Molecular functioni

  1. complement component C3b binding Source: UniProtKB
  2. complement component C3b receptor activity Source: UniProtKB
  3. complement component C4b binding Source: UniProtKB
  4. complement component C4b receptor activity Source: UniProtKB

GO - Biological processi

  1. complement activation, classical pathway Source: UniProtKB-KW
  2. complement receptor mediated signaling pathway Source: GOC
  3. innate immune response Source: Reactome
  4. negative regulation of complement activation, alternative pathway Source: UniProtKB
  5. negative regulation of complement activation, classical pathway Source: UniProtKB
  6. negative regulation of serine-type endopeptidase activity Source: UniProtKB
  7. positive regulation of serine-type endopeptidase activity Source: UniProtKB
  8. regulation of complement activation Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Blood group antigen, Receptor

Keywords - Biological processi

Complement pathway, Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiREACT_118707. Regulation of Complement cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Complement receptor type 1
Alternative name(s):
C3b/C4b receptor
CD_antigen: CD35
Gene namesi
Name:CR1
Synonyms:C3BR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:2334. CR1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini42 – 19711930ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1972 – 199625HelicalSequence AnalysisAdd
BLAST
Topological domaini1997 – 203943CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProtKB
  3. integral component of plasma membrane Source: UniProtKB
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

MIMi607486. phenotype.
611162. phenotype.
PharmGKBiPA26855.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4141Add
BLAST
Chaini42 – 20391998Complement receptor type 1PRO_0000006009Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei42 – 421Pyrrolidone carboxylic acidSequence Analysis
Disulfide bondi43 ↔ 86PROSITE-ProRule annotation
Glycosylationi56 – 561N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi73 ↔ 99PROSITE-ProRule annotation
Disulfide bondi104 ↔ 145PROSITE-ProRule annotation
Disulfide bondi131 ↔ 161PROSITE-ProRule annotation
Disulfide bondi166 ↔ 215PROSITE-ProRule annotation
Disulfide bondi195 ↔ 232PROSITE-ProRule annotation
Disulfide bondi238 ↔ 280PROSITE-ProRule annotation
Glycosylationi252 – 2521N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi266 ↔ 293PROSITE-ProRule annotation
Disulfide bondi297 ↔ 340PROSITE-ProRule annotation
Disulfide bondi326 ↔ 353PROSITE-ProRule annotation
Disulfide bondi358 ↔ 400PROSITE-ProRule annotation
Disulfide bondi386 ↔ 416PROSITE-ProRule annotation
Glycosylationi410 – 4101N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi421 ↔ 470PROSITE-ProRule annotation
Glycosylationi447 – 4471N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi450 ↔ 487PROSITE-ProRule annotation
Disulfide bondi493 ↔ 536PROSITE-ProRule annotation
Glycosylationi509 – 5091N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi523 ↔ 549PROSITE-ProRule annotation
Disulfide bondi554 ↔ 595PROSITE-ProRule annotation
Glycosylationi578 – 5781N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi581 ↔ 611PROSITE-ProRule annotation
Disulfide bondi616 ↔ 665PROSITE-ProRule annotation
Disulfide bondi645 ↔ 682PROSITE-ProRule annotation
Disulfide bondi688 ↔ 730PROSITE-ProRule annotation
Glycosylationi702 – 7021N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi716 ↔ 743PROSITE-ProRule annotation
Disulfide bondi747 ↔ 790PROSITE-ProRule annotation
Disulfide bondi776 ↔ 803PROSITE-ProRule annotation
Disulfide bondi808 ↔ 850PROSITE-ProRule annotation
Disulfide bondi836 ↔ 866PROSITE-ProRule annotation
Glycosylationi860 – 8601N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi871 ↔ 920PROSITE-ProRule annotation
Glycosylationi897 – 8971N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi900 ↔ 937PROSITE-ProRule annotation
Disulfide bondi943 ↔ 986PROSITE-ProRule annotation
Glycosylationi959 – 9591N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi973 ↔ 999PROSITE-ProRule annotation
Disulfide bondi1004 ↔ 1045
Glycosylationi1028 – 10281N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1031 ↔ 1061
Disulfide bondi1066 ↔ 1115
Disulfide bondi1095 ↔ 1132
Disulfide bondi1138 ↔ 1180PROSITE-ProRule annotation
Glycosylationi1152 – 11521N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1166 ↔ 1193PROSITE-ProRule annotation
Disulfide bondi1197 ↔ 1240PROSITE-ProRule annotation
Disulfide bondi1226 ↔ 1253PROSITE-ProRule annotation
Disulfide bondi1258 ↔ 1300PROSITE-ProRule annotation
Disulfide bondi1286 ↔ 1316PROSITE-ProRule annotation
Glycosylationi1310 – 13101N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1321 ↔ 1370PROSITE-ProRule annotation
Disulfide bondi1350 ↔ 1387PROSITE-ProRule annotation
Disulfide bondi1396 ↔ 1439PROSITE-ProRule annotation
Disulfide bondi1426 ↔ 1452PROSITE-ProRule annotation
Disulfide bondi1457 ↔ 1498PROSITE-ProRule annotation
Glycosylationi1481 – 14811N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1484 ↔ 1514PROSITE-ProRule annotation
Glycosylationi1504 – 15041N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1519 ↔ 1568PROSITE-ProRule annotation
Glycosylationi1534 – 15341N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1540 – 15401N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1548 ↔ 1585PROSITE-ProRule annotation
Disulfide bondi1591 ↔ 1633PROSITE-ProRule annotation
Glycosylationi1605 – 16051N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1619 ↔ 1646PROSITE-ProRule annotation
Disulfide bondi1650 ↔ 1693PROSITE-ProRule annotation
Disulfide bondi1679 ↔ 1706PROSITE-ProRule annotation
Disulfide bondi1711 ↔ 1753PROSITE-ProRule annotation
Disulfide bondi1739 ↔ 1769PROSITE-ProRule annotation
Glycosylationi1763 – 17631N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1774 ↔ 1823PROSITE-ProRule annotation
Disulfide bondi1803 ↔ 1840PROSITE-ProRule annotation
Disulfide bondi1848 ↔ 1891PROSITE-ProRule annotation
Disulfide bondi1877 ↔ 1904PROSITE-ProRule annotation
Glycosylationi1908 – 19081N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1909 ↔ 1952PROSITE-ProRule annotation
Disulfide bondi1938 ↔ 1965PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP17927.
PRIDEiP17927.

PTM databases

PhosphoSiteiP17927.

Expressioni

Tissue specificityi

Present on erythrocytes, leukocytes, glomerular podocytes, and splenic follicular dendritic cells.

Gene expression databases

BgeeiP17927.
CleanExiHS_CR1.
ExpressionAtlasiP17927. baseline and differential.
GenevestigatoriP17927.

Organism-specific databases

HPAiCAB002491.
CAB016271.
HPA042455.
HPA043579.
HPA049348.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi107769. 1 interaction.
IntActiP17927. 7 interactions.
MINTiMINT-1508305.
STRINGi9606.ENSP00000356016.

Structurei

Secondary structure

1
2039
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni57 – 593Combined sources
Beta strandi85 – 884Combined sources
Beta strandi91 – 933Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi115 – 1195Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi135 – 1395Combined sources
Beta strandi141 – 1477Combined sources
Beta strandi149 – 1568Combined sources
Beta strandi161 – 1633Combined sources
Beta strandi173 – 1753Combined sources
Beta strandi180 – 1834Combined sources
Beta strandi190 – 1923Combined sources
Beta strandi197 – 2015Combined sources
Beta strandi212 – 2154Combined sources
Beta strandi219 – 2235Combined sources
Beta strandi225 – 2284Combined sources
Beta strandi950 – 9545Combined sources
Beta strandi961 – 9666Combined sources
Beta strandi968 – 9736Combined sources
Beta strandi977 – 9793Combined sources
Beta strandi982 – 9865Combined sources
Beta strandi988 – 9903Combined sources
Beta strandi1014 – 10163Combined sources
Beta strandi1026 – 10305Combined sources
Beta strandi1033 – 10375Combined sources
Beta strandi1041 – 10477Combined sources
Beta strandi1049 – 10568Combined sources
Beta strandi1061 – 10633Combined sources
Beta strandi1090 – 10934Combined sources
Beta strandi1107 – 11093Combined sources
Beta strandi1112 – 11143Combined sources
Beta strandi1118 – 11225Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GKGNMR-A1002-1133[»]
1GKNNMR-A942-1065[»]
1GOPmodel-A942-1133[»]
1PPQNMR-A1002-1065[»]
2MCYNMR-A102-233[»]
2MCZNMR-A41-163[»]
2Q7ZX-ray-A42-1972[»]
ProteinModelPortaliP17927.
SMRiP17927. Positions 42-1961.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17927.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 10160Sushi 1PROSITE-ProRule annotationAdd
BLAST
Domaini102 – 16362Sushi 2PROSITE-ProRule annotationAdd
BLAST
Domaini164 – 23471Sushi 3PROSITE-ProRule annotationAdd
BLAST
Domaini236 – 29560Sushi 4PROSITE-ProRule annotationAdd
BLAST
Domaini295 – 35561Sushi 5PROSITE-ProRule annotationAdd
BLAST
Domaini356 – 41863Sushi 6PROSITE-ProRule annotationAdd
BLAST
Domaini419 – 48971Sushi 7PROSITE-ProRule annotationAdd
BLAST
Domaini491 – 55161Sushi 8PROSITE-ProRule annotationAdd
BLAST
Domaini552 – 61362Sushi 9PROSITE-ProRule annotationAdd
BLAST
Domaini614 – 68471Sushi 10PROSITE-ProRule annotationAdd
BLAST
Domaini686 – 74560Sushi 11PROSITE-ProRule annotationAdd
BLAST
Domaini745 – 80561Sushi 12PROSITE-ProRule annotationAdd
BLAST
Domaini806 – 86863Sushi 13PROSITE-ProRule annotationAdd
BLAST
Domaini869 – 93971Sushi 14PROSITE-ProRule annotationAdd
BLAST
Domaini941 – 100161Sushi 15PROSITE-ProRule annotationAdd
BLAST
Domaini1002 – 106362Sushi 16PROSITE-ProRule annotationAdd
BLAST
Domaini1064 – 113471Sushi 17PROSITE-ProRule annotationAdd
BLAST
Domaini1136 – 119560Sushi 18PROSITE-ProRule annotationAdd
BLAST
Domaini1195 – 125561Sushi 19PROSITE-ProRule annotationAdd
BLAST
Domaini1256 – 131863Sushi 20PROSITE-ProRule annotationAdd
BLAST
Domaini1319 – 138971Sushi 21PROSITE-ProRule annotationAdd
BLAST
Domaini1394 – 145461Sushi 22PROSITE-ProRule annotationAdd
BLAST
Domaini1455 – 151662Sushi 23PROSITE-ProRule annotationAdd
BLAST
Domaini1517 – 158771Sushi 24PROSITE-ProRule annotationAdd
BLAST
Domaini1589 – 164860Sushi 25PROSITE-ProRule annotationAdd
BLAST
Domaini1648 – 170861Sushi 26PROSITE-ProRule annotationAdd
BLAST
Domaini1709 – 177163Sushi 27PROSITE-ProRule annotationAdd
BLAST
Domaini1772 – 184271Sushi 28PROSITE-ProRule annotationAdd
BLAST
Domaini1846 – 190661Sushi 29PROSITE-ProRule annotationAdd
BLAST
Domaini1907 – 196761Sushi 30PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 30 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Sushi, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000139590.
HOVERGENiHBG005397.
InParanoidiP17927.
KOiK04011.
PhylomeDBiP17927.

Family and domain databases

InterProiIPR000436. Sushi_SCR_CCP.
[Graphical view]
PfamiPF00084. Sushi. 30 hits.
[Graphical view]
SMARTiSM00032. CCP. 30 hits.
[Graphical view]
SUPFAMiSSF57535. SSF57535. 30 hits.
PROSITEiPS50923. SUSHI. 30 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P17927-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGASSPRSPE PVGPPAPGLP FCCGGSLLAV VVLLALPVAW GQCNAPEWLP
60 70 80 90 100
FARPTNLTDE FEFPIGTYLN YECRPGYSGR PFSIICLKNS VWTGAKDRCR
110 120 130 140 150
RKSCRNPPDP VNGMVHVIKG IQFGSQIKYS CTKGYRLIGS SSATCIISGD
160 170 180 190 200
TVIWDNETPI CDRIPCGLPP TITNGDFIST NRENFHYGSV VTYRCNPGSG
210 220 230 240 250
GRKVFELVGE PSIYCTSNDD QVGIWSGPAP QCIIPNKCTP PNVENGILVS
260 270 280 290 300
DNRSLFSLNE VVEFRCQPGF VMKGPRRVKC QALNKWEPEL PSCSRVCQPP
310 320 330 340 350
PDVLHAERTQ RDKDNFSPGQ EVFYSCEPGY DLRGAASMRC TPQGDWSPAA
360 370 380 390 400
PTCEVKSCDD FMGQLLNGRV LFPVNLQLGA KVDFVCDEGF QLKGSSASYC
410 420 430 440 450
VLAGMESLWN SSVPVCEQIF CPSPPVIPNG RHTGKPLEVF PFGKTVNYTC
460 470 480 490 500
DPHPDRGTSF DLIGESTIRC TSDPQGNGVW SSPAPRCGIL GHCQAPDHFL
510 520 530 540 550
FAKLKTQTNA SDFPIGTSLK YECRPEYYGR PFSITCLDNL VWSSPKDVCK
560 570 580 590 600
RKSCKTPPDP VNGMVHVITD IQVGSRINYS CTTGHRLIGH SSAECILSGN
610 620 630 640 650
AAHWSTKPPI CQRIPCGLPP TIANGDFIST NRENFHYGSV VTYRCNPGSG
660 670 680 690 700
GRKVFELVGE PSIYCTSNDD QVGIWSGPAP QCIIPNKCTP PNVENGILVS
710 720 730 740 750
DNRSLFSLNE VVEFRCQPGF VMKGPRRVKC QALNKWEPEL PSCSRVCQPP
760 770 780 790 800
PDVLHAERTQ RDKDNFSPGQ EVFYSCEPGY DLRGAASMRC TPQGDWSPAA
810 820 830 840 850
PTCEVKSCDD FMGQLLNGRV LFPVNLQLGA KVDFVCDEGF QLKGSSASYC
860 870 880 890 900
VLAGMESLWN SSVPVCEQIF CPSPPVIPNG RHTGKPLEVF PFGKAVNYTC
910 920 930 940 950
DPHPDRGTSF DLIGESTIRC TSDPQGNGVW SSPAPRCGIL GHCQAPDHFL
960 970 980 990 1000
FAKLKTQTNA SDFPIGTSLK YECRPEYYGR PFSITCLDNL VWSSPKDVCK
1010 1020 1030 1040 1050
RKSCKTPPDP VNGMVHVITD IQVGSRINYS CTTGHRLIGH SSAECILSGN
1060 1070 1080 1090 1100
TAHWSTKPPI CQRIPCGLPP TIANGDFIST NRENFHYGSV VTYRCNLGSR
1110 1120 1130 1140 1150
GRKVFELVGE PSIYCTSNDD QVGIWSGPAP QCIIPNKCTP PNVENGILVS
1160 1170 1180 1190 1200
DNRSLFSLNE VVEFRCQPGF VMKGPRRVKC QALNKWEPEL PSCSRVCQPP
1210 1220 1230 1240 1250
PEILHGEHTP SHQDNFSPGQ EVFYSCEPGY DLRGAASLHC TPQGDWSPEA
1260 1270 1280 1290 1300
PRCAVKSCDD FLGQLPHGRV LFPLNLQLGA KVSFVCDEGF RLKGSSVSHC
1310 1320 1330 1340 1350
VLVGMRSLWN NSVPVCEHIF CPNPPAILNG RHTGTPSGDI PYGKEISYTC
1360 1370 1380 1390 1400
DPHPDRGMTF NLIGESTIRC TSDPHGNGVW SSPAPRCELS VRAGHCKTPE
1410 1420 1430 1440 1450
QFPFASPTIP INDFEFPVGT SLNYECRPGY FGKMFSISCL ENLVWSSVED
1460 1470 1480 1490 1500
NCRRKSCGPP PEPFNGMVHI NTDTQFGSTV NYSCNEGFRL IGSPSTTCLV
1510 1520 1530 1540 1550
SGNNVTWDKK APICEIISCE PPPTISNGDF YSNNRTSFHN GTVVTYQCHT
1560 1570 1580 1590 1600
GPDGEQLFEL VGERSIYCTS KDDQVGVWSS PPPRCISTNK CTAPEVENAI
1610 1620 1630 1640 1650
RVPGNRSFFS LTEIIRFRCQ PGFVMVGSHT VQCQTNGRWG PKLPHCSRVC
1660 1670 1680 1690 1700
QPPPEILHGE HTLSHQDNFS PGQEVFYSCE PSYDLRGAAS LHCTPQGDWS
1710 1720 1730 1740 1750
PEAPRCTVKS CDDFLGQLPH GRVLLPLNLQ LGAKVSFVCD EGFRLKGRSA
1760 1770 1780 1790 1800
SHCVLAGMKA LWNSSVPVCE QIFCPNPPAI LNGRHTGTPF GDIPYGKEIS
1810 1820 1830 1840 1850
YACDTHPDRG MTFNLIGESS IRCTSDPQGN GVWSSPAPRC ELSVPAACPH
1860 1870 1880 1890 1900
PPKIQNGHYI GGHVSLYLPG MTISYICDPG YLLVGKGFIF CTDQGIWSQL
1910 1920 1930 1940 1950
DHYCKEVNCS FPLFMNGISK ELEMKKVYHY GDYVTLKCED GYTLEGSPWS
1960 1970 1980 1990 2000
QCQADDRWDP PLAKCTSRTH DALIVGTLSG TIFFILLIIF LSWIILKHRK
2010 2020 2030
GNNAHENPKE VAIHLHSQGG SSVHPRTLQT NEENSRVLP
Length:2,039
Mass (Da):223,663
Last modified:March 2, 2010 - v3
Checksum:iFB01870F19D5E6DD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1731T → A in CAI16042. (PubMed:16710414)Curated
Sequence conflicti173 – 1731T → A in CAI16723. (PubMed:16710414)Curated
Sequence conflicti445 – 4451T → A in CAA68755. (PubMed:2972794)Curated
Sequence conflicti445 – 4451T → A in AAB60694. (PubMed:8245463)Curated
Sequence conflicti445 – 4451T → A in CAA32541. (PubMed:2971757)Curated
Sequence conflicti1876 – 18761I → T in CAA68755. (PubMed:2972794)Curated
Sequence conflicti1876 – 18761I → T in CAA28933. (PubMed:2951479)Curated

Polymorphismi

CR1 contains a system of antigens called the Knops blood group system. Polymorphisms within this system are involved in malarial rosetting, a process associated with cerebral malaria, the major cause of mortality in Plasmodium falciparum malaria. Common Knops system antigens include McCoy (McC) and Sl(a)/Vil (Kn4, or Swain-Langley; Vil or Villien). Sl(a-) phenotype is more common in persons of African descent and may protect against fatal malaria.
Other polymorphic forms of CR1 contain 23, 37 or 44 Sushi (CCP/SCR) domains instead of the 30 Sushi (CCP/SCR) domains. The most frequent alleles are the F allotype (shown here) and the S allotype (37 repeat Sushi domains). The gene frequencies of the F allotype and S allotype are 0.87 and 0.11 in Caucasians, 0.82 and 0.11 in African Americans, 0.89 and 0.11 in Mexicans.
Genetic variations in CR1 resulting in CR1 deficiency are involved in protection against severe malaria [MIMi:611162]. Parasitized red blood cells (RBCs) from children suffering from severe malaria often adhere to complement receptor 1 (CR1) on uninfected RBCs to form clumps of cells known as rosettes. CR1-deficient red blood cells show greatly reduced rosetting and CR1 deficiency occurs in healthy individuals from malaria-endemic regions.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1208 – 12081H → R.1 Publication
Corresponds to variant rs2274567 [ dbSNP | Ensembl ].
VAR_013819
Natural varianti1408 – 14081T → I.
VAR_013820
Natural varianti1408 – 14081T → M.
Corresponds to variant rs3737002 [ dbSNP | Ensembl ].
VAR_020263
Natural varianti1540 – 15401N → S.
Corresponds to variant rs17259045 [ dbSNP | Ensembl ].
VAR_055685
Natural varianti1590 – 15901K → E in MCC(b) antigen. 1 Publication
Corresponds to variant rs17047660 [ dbSNP | Ensembl ].
VAR_013821
Natural varianti1601 – 16011R → G in Sl(2)/Vil antigen and Sl(3) antigen. 2 Publications
Corresponds to variant rs17047661 [ dbSNP | Ensembl ].
VAR_013822
Natural varianti1610 – 16101S → T in Sl(3) antigen. 3 Publications
Corresponds to variant rs4844609 [ dbSNP | Ensembl ].
VAR_013823
Natural varianti1615 – 16151I → V.2 Publications
Corresponds to variant rs6691117 [ dbSNP | Ensembl ].
VAR_013824
Natural varianti1827 – 18271P → R.2 Publications
Corresponds to variant rs3811381 [ dbSNP | Ensembl ].
VAR_013825
Natural varianti1850 – 18501H → D.2 Publications
VAR_013826
Natural varianti1969 – 19691T → A.2 Publications
Corresponds to variant rs2296160 [ dbSNP | Ensembl ].
VAR_055686

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00816 mRNA. Translation: CAA68755.1.
L17418
, L17390, L17399, L17409, L17419, L17420, L17421, L17422, L17423, L17391, L17392, L17393, L17394, L17395, L17396, L17397, L17398, L17400, L17401, L17402, L17403, L17404, L17405, L17406, L17407, L17408, L17410, L17411, L17412, L17413, L17414, L17415, L17416, L17417 Genomic DNA. Translation: AAB60694.1.
L17418
, L17390, L17391, L17392, L17393, L17394, L17395, L17396, L17397, L17398, L17399, L17400, L17401, L17402, L17403, L17404, L17405, L17406, L17407, L17408, L17409, L17410, L17411, L17412, L17413, L17414, L17415, L17416, L17417, L17419, L17420, L17421, L17422, L17423, L17424, L17425, L17426, L17427, L17428, L17429, L17430 Genomic DNA. Translation: AAB60695.1.
AL137789, AL691452 Genomic DNA. Translation: CAI16042.1.
AL137789, AL691452 Genomic DNA. Translation: CAI16043.1.
AL691452, AL137789 Genomic DNA. Translation: CAI16723.1.
AL691452, AL137789 Genomic DNA. Translation: CAI16725.1.
X14362 mRNA. Translation: CAA32541.1.
X05309 mRNA. Translation: CAA28933.1.
M11569 mRNA. Translation: AAA52297.1.
M11617 mRNA. Translation: AAA52298.1.
M11618 mRNA. Translation: AAA52299.1.
CCDSiCCDS44309.1.
PIRiI73012.
RefSeqiNP_000564.2. NM_000573.3.
NP_000642.3. NM_000651.4.
UniGeneiHs.334019.

Genome annotation databases

EnsembliENST00000367051; ENSP00000356018; ENSG00000203710.
ENST00000367053; ENSP00000356020; ENSG00000203710.
ENST00000400960; ENSP00000383744; ENSG00000203710.
GeneIDi1378.
KEGGihsa:1378.
UCSCiuc001hfy.3. human.

Polymorphism databases

DMDMi290457678.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

dbRBC/BGMUT

Blood group antigen gene mutation database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00816 mRNA. Translation: CAA68755.1 .
L17418
, L17390 , L17399 , L17409 , L17419 , L17420 , L17421 , L17422 , L17423 , L17391 , L17392 , L17393 , L17394 , L17395 , L17396 , L17397 , L17398 , L17400 , L17401 , L17402 , L17403 , L17404 , L17405 , L17406 , L17407 , L17408 , L17410 , L17411 , L17412 , L17413 , L17414 , L17415 , L17416 , L17417 Genomic DNA. Translation: AAB60694.1 .
L17418
, L17390 , L17391 , L17392 , L17393 , L17394 , L17395 , L17396 , L17397 , L17398 , L17399 , L17400 , L17401 , L17402 , L17403 , L17404 , L17405 , L17406 , L17407 , L17408 , L17409 , L17410 , L17411 , L17412 , L17413 , L17414 , L17415 , L17416 , L17417 , L17419 , L17420 , L17421 , L17422 , L17423 , L17424 , L17425 , L17426 , L17427 , L17428 , L17429 , L17430 Genomic DNA. Translation: AAB60695.1 .
AL137789 , AL691452 Genomic DNA. Translation: CAI16042.1 .
AL137789 , AL691452 Genomic DNA. Translation: CAI16043.1 .
AL691452 , AL137789 Genomic DNA. Translation: CAI16723.1 .
AL691452 , AL137789 Genomic DNA. Translation: CAI16725.1 .
X14362 mRNA. Translation: CAA32541.1 .
X05309 mRNA. Translation: CAA28933.1 .
M11569 mRNA. Translation: AAA52297.1 .
M11617 mRNA. Translation: AAA52298.1 .
M11618 mRNA. Translation: AAA52299.1 .
CCDSi CCDS44309.1.
PIRi I73012.
RefSeqi NP_000564.2. NM_000573.3.
NP_000642.3. NM_000651.4.
UniGenei Hs.334019.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GKG NMR - A 1002-1133 [» ]
1GKN NMR - A 942-1065 [» ]
1GOP model - A 942-1133 [» ]
1PPQ NMR - A 1002-1065 [» ]
2MCY NMR - A 102-233 [» ]
2MCZ NMR - A 41-163 [» ]
2Q7Z X-ray - A 42-1972 [» ]
ProteinModelPortali P17927.
SMRi P17927. Positions 42-1961.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107769. 1 interaction.
IntActi P17927. 7 interactions.
MINTi MINT-1508305.
STRINGi 9606.ENSP00000356016.

PTM databases

PhosphoSitei P17927.

Polymorphism databases

DMDMi 290457678.

Proteomic databases

PaxDbi P17927.
PRIDEi P17927.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367051 ; ENSP00000356018 ; ENSG00000203710 .
ENST00000367053 ; ENSP00000356020 ; ENSG00000203710 .
ENST00000400960 ; ENSP00000383744 ; ENSG00000203710 .
GeneIDi 1378.
KEGGi hsa:1378.
UCSCi uc001hfy.3. human.

Organism-specific databases

CTDi 1378.
GeneCardsi GC01P207669.
HGNCi HGNC:2334. CR1.
HPAi CAB002491.
CAB016271.
HPA042455.
HPA043579.
HPA049348.
MIMi 120620. gene.
607486. phenotype.
611162. phenotype.
neXtProti NX_P17927.
PharmGKBi PA26855.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000139590.
HOVERGENi HBG005397.
InParanoidi P17927.
KOi K04011.
PhylomeDBi P17927.

Enzyme and pathway databases

Reactomei REACT_118707. Regulation of Complement cascade.

Miscellaneous databases

EvolutionaryTracei P17927.
GeneWikii Complement_receptor_1.
GenomeRNAii 1378.
NextBioi 5589.
PROi P17927.
SOURCEi Search...

Gene expression databases

Bgeei P17927.
CleanExi HS_CR1.
ExpressionAtlasi P17927. baseline and differential.
Genevestigatori P17927.

Family and domain databases

InterProi IPR000436. Sushi_SCR_CCP.
[Graphical view ]
Pfami PF00084. Sushi. 30 hits.
[Graphical view ]
SMARTi SM00032. CCP. 30 hits.
[Graphical view ]
SUPFAMi SSF57535. SSF57535. 30 hits.
PROSITEi PS50923. SUSHI. 30 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of distinct C3b and C4b recognition sites in the human C3b/C4b receptor (CR1, CD35) by deletion mutagenesis."
    Klickstein L.B., Bartow T.J., Miletic V., Rabson L.D., Smith J.A., Fearon D.T.
    J. Exp. Med. 168:1699-1717(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE S AND ALLELE F).
  2. "Structure of the gene for the F allele of complement receptor type 1 and sequence of the coding region unique to the S allele."
    Vik D.P., Wong W.W.
    J. Immunol. 151:6214-6224(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE S AND ALLELE F), VARIANTS VAL-1615; ARG-1827; ASP-1850 AND ALA-1969.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-1610.
  4. "Structure of the human CR1 gene. Molecular basis of the structural and quantitative polymorphisms and identification of a new CR1-like allele."
    Wong W.W., Cahill J.M., Rosen M.D., Kennedy C.A., Bonaccio E.T., Morris M.J., Wilson J.G., Klickstein L.B., Fearon D.T.
    J. Exp. Med. 169:847-863(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 1-41.
  5. "Identification of an alternative polyadenylation site in the human C3b/C4b receptor (complement receptor type 1) transcriptional unit and prediction of a secreted form of complement receptor type 1."
    Hourcade D., Miesner D.R., Atkinson J.P., Holers V.M.
    J. Exp. Med. 168:1255-1270(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-584.
  6. "Human C3b/C4b receptor (CR1). Demonstration of long homologous repeating domains that are composed of the short consensus repeats characteristics of C3/C4 binding proteins."
    Klickstein L.B., Wong W.W., Smith J.A., Weis J.H., Wilson J.G., Fearon D.T.
    J. Exp. Med. 165:1095-1112(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 503-2039, VARIANT ALA-1969.
  7. "Identification of a partial cDNA clone for the human receptor for complement fragments C3b/C4b."
    Wong W.W., Klickstein L.B., Smith J.A., Weis J.H., Fearon D.T.
    Proc. Natl. Acad. Sci. U.S.A. 82:7711-7715(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 761-783; 831-845 AND 1179-1195.
  8. "Structural polymorphisms of complement receptor 1 (CR1) in systemic lupus erythematosus (SLE) patients and normal controls of three ethnic groups."
    Moulds J.M., Reveille J.D., Arnett F.C.
    Clin. Exp. Immunol. 105:302-305(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: POLYMORPHISM.
  9. "A human complement receptor 1 polymorphism that reduces Plasmodium falciparum rosetting confers protection against severe malaria."
    Cockburn I.A., Mackinnon M.J., O'Donnell A., Allen S.J., Moulds J.M., Baisor M., Bockarie M., Reeder J.C., Rowe J.A.
    Proc. Natl. Acad. Sci. U.S.A. 101:272-277(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: POLYMORPHISM, INVOLVEMENT IN PROTECTION AGAINST MALARIA.
  10. "Molecular identification of Knops blood group polymorphisms found in long homologous region D of complement receptor 1."
    Moulds J.M., Zimmerman P.A., Doumbo O.K., Kassambara L., Sagara I., Diallo D.A., Atkinson J.P., Krych-Goldberg M., Hauhart R.E., Hourcade D.E., McNamara D.T., Birmingham D.J., Rowe J.A., Moulds J.J., Miller L.H.
    Blood 97:2879-2885(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ARG-1208; GLU-1590; GLY-1601; THR-1610; VAL-1615; ARG-1827 AND ASP-1850.
  11. Cited for: VARIANTS SL(2)/VIL GLY-1601 AND SL(3) THR-1610.
  12. "Structure of the C3b binding site of CR1 (CD35), the immune adherence receptor."
    Smith B.O., Mallin R.L., Krych-Goldberg M., Wang X., Hauhart R.E., Bromek K., Uhrin D., Atkinson J.P., Barlow P.N.
    Cell 108:769-780(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 942-1133.

Entry informationi

Entry nameiCR1_HUMAN
AccessioniPrimary (citable) accession number: P17927
Secondary accession number(s): Q16744
, Q16745, Q5SR43, Q5SR45, Q9UQV2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: March 2, 2010
Last modified: November 26, 2014
This is version 158 of the entry and version 3 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, Reference proteome

Documents

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

External Data

Dasty 3