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P17927

- CR1_HUMAN

UniProt

P17927 - CR1_HUMAN

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Protein
Complement receptor type 1
Gene
CR1, C3BR
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 – 19711930Extracellular Reviewed prediction
Add
BLAST
Transmembranei1972 – 199625Helical; Reviewed prediction
Add
BLAST
Topological domaini1997 – 203943Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  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.
Orphaneti536. Systemic lupus erythematosus.
PharmGKBiPA26855.

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

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

ArrayExpressiP17927.
BgeeiP17927.
CleanExiHS_CR1.
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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP17927.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal, Sushi, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000139590.
HOVERGENiHBG005397.
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

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MGASSPRSPE PVGPPAPGLP FCCGGSLLAV VVLLALPVAW GQCNAPEWLP     50
FARPTNLTDE FEFPIGTYLN YECRPGYSGR PFSIICLKNS VWTGAKDRCR 100
RKSCRNPPDP VNGMVHVIKG IQFGSQIKYS CTKGYRLIGS SSATCIISGD 150
TVIWDNETPI CDRIPCGLPP TITNGDFIST NRENFHYGSV VTYRCNPGSG 200
GRKVFELVGE PSIYCTSNDD QVGIWSGPAP QCIIPNKCTP PNVENGILVS 250
DNRSLFSLNE VVEFRCQPGF VMKGPRRVKC QALNKWEPEL PSCSRVCQPP 300
PDVLHAERTQ RDKDNFSPGQ EVFYSCEPGY DLRGAASMRC TPQGDWSPAA 350
PTCEVKSCDD FMGQLLNGRV LFPVNLQLGA KVDFVCDEGF QLKGSSASYC 400
VLAGMESLWN SSVPVCEQIF CPSPPVIPNG RHTGKPLEVF PFGKTVNYTC 450
DPHPDRGTSF DLIGESTIRC TSDPQGNGVW SSPAPRCGIL GHCQAPDHFL 500
FAKLKTQTNA SDFPIGTSLK YECRPEYYGR PFSITCLDNL VWSSPKDVCK 550
RKSCKTPPDP VNGMVHVITD IQVGSRINYS CTTGHRLIGH SSAECILSGN 600
AAHWSTKPPI CQRIPCGLPP TIANGDFIST NRENFHYGSV VTYRCNPGSG 650
GRKVFELVGE PSIYCTSNDD QVGIWSGPAP QCIIPNKCTP PNVENGILVS 700
DNRSLFSLNE VVEFRCQPGF VMKGPRRVKC QALNKWEPEL PSCSRVCQPP 750
PDVLHAERTQ RDKDNFSPGQ EVFYSCEPGY DLRGAASMRC TPQGDWSPAA 800
PTCEVKSCDD FMGQLLNGRV LFPVNLQLGA KVDFVCDEGF QLKGSSASYC 850
VLAGMESLWN SSVPVCEQIF CPSPPVIPNG RHTGKPLEVF PFGKAVNYTC 900
DPHPDRGTSF DLIGESTIRC TSDPQGNGVW SSPAPRCGIL GHCQAPDHFL 950
FAKLKTQTNA SDFPIGTSLK YECRPEYYGR PFSITCLDNL VWSSPKDVCK 1000
RKSCKTPPDP VNGMVHVITD IQVGSRINYS CTTGHRLIGH SSAECILSGN 1050
TAHWSTKPPI CQRIPCGLPP TIANGDFIST NRENFHYGSV VTYRCNLGSR 1100
GRKVFELVGE PSIYCTSNDD QVGIWSGPAP QCIIPNKCTP PNVENGILVS 1150
DNRSLFSLNE VVEFRCQPGF VMKGPRRVKC QALNKWEPEL PSCSRVCQPP 1200
PEILHGEHTP SHQDNFSPGQ EVFYSCEPGY DLRGAASLHC TPQGDWSPEA 1250
PRCAVKSCDD FLGQLPHGRV LFPLNLQLGA KVSFVCDEGF RLKGSSVSHC 1300
VLVGMRSLWN NSVPVCEHIF CPNPPAILNG RHTGTPSGDI PYGKEISYTC 1350
DPHPDRGMTF NLIGESTIRC TSDPHGNGVW SSPAPRCELS VRAGHCKTPE 1400
QFPFASPTIP INDFEFPVGT SLNYECRPGY FGKMFSISCL ENLVWSSVED 1450
NCRRKSCGPP PEPFNGMVHI NTDTQFGSTV NYSCNEGFRL IGSPSTTCLV 1500
SGNNVTWDKK APICEIISCE PPPTISNGDF YSNNRTSFHN GTVVTYQCHT 1550
GPDGEQLFEL VGERSIYCTS KDDQVGVWSS PPPRCISTNK CTAPEVENAI 1600
RVPGNRSFFS LTEIIRFRCQ PGFVMVGSHT VQCQTNGRWG PKLPHCSRVC 1650
QPPPEILHGE HTLSHQDNFS PGQEVFYSCE PSYDLRGAAS LHCTPQGDWS 1700
PEAPRCTVKS CDDFLGQLPH GRVLLPLNLQ LGAKVSFVCD EGFRLKGRSA 1750
SHCVLAGMKA LWNSSVPVCE QIFCPNPPAI LNGRHTGTPF GDIPYGKEIS 1800
YACDTHPDRG MTFNLIGESS IRCTSDPQGN GVWSSPAPRC ELSVPAACPH 1850
PPKIQNGHYI GGHVSLYLPG MTISYICDPG YLLVGKGFIF CTDQGIWSQL 1900
DHYCKEVNCS FPLFMNGISK ELEMKKVYHY GDYVTLKCED GYTLEGSPWS 1950
QCQADDRWDP PLAKCTSRTH DALIVGTLSG TIFFILLIIF LSWIILKHRK 2000
GNNAHENPKE VAIHLHSQGG SSVHPRTLQT NEENSRVLP 2039
Length:2,039
Mass (Da):223,663
Last modified:March 2, 2010 - v3
Checksum:iFB01870F19D5E6DD
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti173 – 1731T → A in CAI16042. 1 Publication
Sequence conflicti173 – 1731T → A in CAI16723. 1 Publication
Sequence conflicti445 – 4451T → A in CAA68755. 1 Publication
Sequence conflicti445 – 4451T → A in AAB60694. 1 Publication
Sequence conflicti445 – 4451T → A in CAA32541. 1 Publication
Sequence conflicti1876 – 18761I → T in CAA68755. 1 Publication
Sequence conflicti1876 – 18761I → T in CAA28933. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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.
Orphaneti 536. Systemic lupus erythematosus.
PharmGKBi PA26855.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000139590.
HOVERGENi HBG005397.
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

ArrayExpressi P17927.
Bgeei P17927.
CleanExi HS_CR1.
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: September 3, 2014
This is version 155 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

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