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UniProtKB/Swiss-Prot entry P02741


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CRP_HUMAN
Primary accession number P02741
Secondary accession numbers A8K078 Q08AK3 Q8WW75
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 1, 1988 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 126)
Name and origin of the protein
Protein name C-reactive protein [Precursor]
Synonyms None
Contains C-reactive protein(1-205)
Gene name
Name: CRP
Synonyms: PTX1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2997165 [NCBI, ExPASy, EBI, Israel, Japan]
Lei K.-J., Liu T., Zon G., Soravia E., Liu T.-Y., Goldman N.D.;
"Genomic DNA sequence for human C-reactive protein.";
J. Biol. Chem. 260:13377-13383(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3840479 [NCBI, ExPASy, EBI, Israel, Japan]
Woo P., Korenberg J.R., Whitehead A.S.;
"Characterization of genomic and complementary DNA sequence of human C-reactive protein, and comparison with the complementary DNA sequence of serum amyloid P component.";
J. Biol. Chem. 260:13384-13388(1985).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Murphy T.M., Baum L., Beaman K.;
"Extrahepetic transcription of human C-reactive protein.";
Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Tenchini M.L., Marchetti L., Bossi E., Malcovati M., Lorenzetti R.;
Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Harraghy N.;
"Controlled gene expression using acute phase response elements.";
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Urinary bladder;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Liver;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-26.
PubMed=6685157 [NCBI, ExPASy, EBI, Israel, Japan]
Tucci A., Goldberger G., Whitehead A.S., Kay R.M., Woods D.E., Colten H.R.;
"Biosynthesis and postsynthetic processing of human C-reactive protein.";
J. Immunol. 131:2416-2419(1983).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 144-175.
DOI=10.1126/science.6857266; PubMed=6857266 [NCBI, ExPASy, EBI, Israel, Japan]
Whitehead A.S., Bruns G.A.P., Markham A.F., Colten H.R., Woods D.E.;
"Isolation of human C-reactive protein complementary DNA and localization of the gene to chromosome 1.";
Science 221:69-71(1983).
[12]
PROTEIN SEQUENCE OF 19-224.
PubMed=762075 [NCBI, ExPASy, EBI, Israel, Japan]
Oliveira E.B., Gotschlich E.C., Liu T.-Y.;
"Primary structure of human C-reactive protein.";
J. Biol. Chem. 254:489-502(1979).
[13]
PROTEIN SEQUENCE OF 22-55.
DOI=10.1073/pnas.74.3.1214; PubMed=403526 [NCBI, ExPASy, EBI, Israel, Japan]
Osmand A.P., Gewurz H., Friedenson B.;
"Partial amino-acid sequences of human and rabbit C-reactive proteins: homology with immunoglobulins and histocompatibility antigens.";
Proc. Natl. Acad. Sci. U.S.A. 74:1214-1218(1977).
[14]
MASS SPECTROMETRY.
Kiernan U.A., Nedelkov D., Tubbs K.A., Niederkofler E.E., Nelson R.W.;
"Selected expression profiling of full-length proteins and their variants in human plasma.";
Clin. Proteomics 1:7-16(2004).
[15]
3D-STRUCTURE MODELING.
DOI=10.1016/S0969-2126(94)00105-7; PubMed=7881902 [NCBI, ExPASy, EBI, Israel, Japan]
Srinivasan N., White H.E., Emsley J., Wood S.P., Pepys M.B., Blundell T.L.;
"Comparative analyses of pentraxins: implications for protomer assembly and ligand binding.";
Structure 2:1017-1027(1994).
[16]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
DOI=10.1038/nsb0496-346; PubMed=8599761 [NCBI, ExPASy, EBI, Israel, Japan]
Shrive A.K., Cheetham G.M.T., Holden D., Myles D.A.A., Turnell W.G., Volanakis J.E., Pepys M.B., Bloomer A.C., Greenhough T.J.;
"Three dimensional structure of human C-reactive protein.";
Nat. Struct. Biol. 3:346-353(1996).
[17]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
DOI=10.1016/S0969-2126(99)80023-9; PubMed=10368284 [NCBI, ExPASy, EBI, Israel, Japan]
Thompson D., Pepys M.B., Wood S.P.;
"The physiological structure of human C-reactive protein and its complex with phosphocholine.";
Structure 7:169-177(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M11880; AAB59526.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M11725; AAA52075.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X56692; CAA40020.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X56214; CAA39671.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF442818; AAL48218.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK289443; BAF82132.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF449713; AAL40835.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL445528; CAH73654.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL445528; CAH73656.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC020766; AAH20766.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC125135; AAI25136.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M35163; AAA52076.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
K00518; AAA52074.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00022389; -.
IPI00218876; -.
PIR A24515; CJHU.
RefSeq NP_000558.2; -.
UniGene Hs.709456
3D structure databases
PDB
1B09; X-ray; 2.50 A; A/B/C/D/E=19-224.[ExPASy / RCSB / EBI]
1CRV; Model; -; A/B/C/D/E=19-224.[ExPASy / RCSB / EBI]
1GNH; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J=19-224.[ExPASy / RCSB / EBI]
1LJ7; X-ray; 3.15 A; A/B/C/D/E/F/G/H/I/J=19-224.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1B09; -.
1CRV; -.
1GNH; -.
1LJ7; -.
ModBase P02741.
Protein-protein interaction databases
IntAct P02741; 3.
Enzyme and pathway databases
Pathway_Interaction_DB il6_7pathway; IL6-mediated signaling events.
2D gel databases
SWISS-2DPAGE P02741; -.
DOSAC-COBS-2DPAGE P02741; -.
Organism-specific databases
GeneCards GC01M157948; -.
H-InvDB HIX0028720; -.
HGNC HGNC:2367; CRP.
GenAtlas CRP.
HPA CAB005036; -.
MIM 123260; gene. [NCBI / EBI]
PharmGKB PA120; -.
Gene expression databases
ArrayExpress P02741; -.
Bgee P02741; -.
CleanEx HS_CRP; -.
GermOnline ENSG00000132693; Homo sapiens.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (non-traceable author statement from UniProtKB).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0033265; Molecular function: choline binding (traceable author statement from UniProtKB).
GO:0051637; Molecular function: Gram-positive bacterial cell surface binding (traceable author statement from UniProtKB).
GO:0030169; Molecular function: low-density lipoprotein binding (inferred from direct assay from UniProtKB).
GO:0006953; Biological process: acute-phase response (traceable author statement from UniProtKB).
GO:0010745; Biological process: negative regulation of foam cell differentiation (inferred from direct assay from UniProtKB).
GO:0010888; Biological process: negative regulation of lipid storage (inferred from direct assay from UniProtKB).
GO:0008228; Biological process: opsonization (traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR013320; ConA-like_subgrp.
IPR001759; Pentaxin.
Graphical view of domain structure.
Gene3D G3DSA:2.60.120.200; ConA_like_subgrp; 1.
Pfam PF00354; Pentaxin; 1.
Pfam graphical view of domain structure.
PRINTS PR00895; PENTAXIN.
ProDom PD002153; Pentaxin; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00159; PTX; 1.
SMART graphical view of domain structure.
PROSITE PS00289; PENTAXIN; 1.
Proteomic databases
PeptideAtlas P02741; -.
PRIDE P02741; -.
Genome annotation databases
Ensembl ENSG00000132693; Homo sapiens. [Contig view]
GeneID 1401; -.
KEGG hsa:1401; -.
Phylogenomic databases
HOGENOM P02741; -.
HOVERGEN P02741; -.
OMA P02741; VAPVHIC.
Other
DrugBank DB01076; Atorvastatin.
DB01393; Bezafibrate.
NextBio 5737; -.
SOURCE CRP; Homo sapiens.
ProtoNet P02741.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acute phase; Alternative splicing; Calcium; Direct protein sequencing; Disulfide bond; Metal-binding; Pyrrolidone carboxylic acid; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    18  18      
CHAIN   19   224  206     C-reactive protein. PRO_0000023526
CHAIN   19   223  205     C-reactive protein(1-205). PRO_0000023527
DOMAIN   19   224  206     Pentaxin. 
METAL   78    78        Calcium 1. 
METAL   79    79        Calcium 1. 
METAL   156   156        Calcium 1. 
METAL   156   156        Calcium 2. 
METAL   157   157        Calcium 1; via carbonyl oxygen. 
METAL   158   158        Calcium 1. 
METAL   158   158        Calcium 2. 
METAL   168   168        Calcium 2. 
MOD_RES   19    19        Pyrrolidone carboxylic acid. 
DISULFID   54   115         
VAR_SEQ   67   199        Missing (in isoform 2). VSP_004656
CONFLICT   49    49        K -> G (in Ref. 13; AA sequence). 
CONFLICT   52    52        T -> G (in Ref. 13; AA sequence). 
CONFLICT   67    82        YSIFSYATKRQDNEIL -> TVFSRMPPRDKTMRFF (in Ref. 4; CAA39671). 
CONFLICT   80    98        Missing (in Ref. 12; AA sequence). 
CONFLICT   170   170        L -> V (in Ref. 11; AAA52074). 
STRAND   25    29  5      
STRAND   37    40  4      
STRAND   48    58  11      
HELIX   61    63  3      
STRAND   67    73  7      
STRAND   80    86  7      
TURN   87    89  3      
STRAND   90    95  6      
STRAND   98   103  6      
STRAND   112   119  8      
TURN   120   122  3      
STRAND   124   129  6      
STRAND   150   155  6      
HELIX   166   168  3      
STRAND   172   182  11      
HELIX   186   194  9      
STRAND   201   203  3      
HELIX   205   207  3      
STRAND   210   215  6      
STRAND   217   220  4      
Sequence information