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P02741 (CRP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C-reactive protein

Cleaved into the following chain:

  1. C-reactive protein(1-205)
Gene names
Name:CRP
Synonyms:PTX1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells.

Cofactor

Binds 2 calcium ions per subunit.

Subunit structure

Homopentamer. Pentaxin (or pentraxin) have a discoid arrangement of 5 non-covalently bound subunits.

Subcellular location

Secreted.

Tissue specificity

Found in plasma.

Induction

The concentration of CRP in plasma increases greatly during acute phase response to tissue injury, infection or other inflammatory stimuli. It is induced by IL1/interleukin-1 and IL6//interleukin-6.

Miscellaneous

This protein owes its name to its ability precipitate pneumococcal C-polysaccharide in the presence of calcium.

Sequence similarities

Belongs to the pentaxin family.

Contains 1 pentaxin domain.

Mass spectrometry

Molecular mass is 23028 Da from positions 19 - 224. Determined by MALDI. Ref.15

Molecular mass is 22930 Da from positions 19 - 223. Determined by MALDI. Ref.15

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FCGR2CP319952EBI-1395983,EBI-1396036

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P02741-1)

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.
Isoform 2 (identifier: P02741-2)

The sequence of this isoform differs from the canonical sequence as follows:
     67-199: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Ref.13
Chain19 – 224206C-reactive protein
PRO_0000023526
Chain19 – 223205C-reactive protein(1-205)
PRO_0000023527

Regions

Domain19 – 224206Pentaxin

Sites

Metal binding781Calcium 1
Metal binding791Calcium 1
Metal binding1561Calcium 1
Metal binding1561Calcium 2
Metal binding1571Calcium 1; via carbonyl oxygen
Metal binding1581Calcium 1
Metal binding1581Calcium 2
Metal binding1681Calcium 2

Amino acid modifications

Modified residue191Pyrrolidone carboxylic acid Ref.13
Disulfide bond54 ↔ 115 Ref.13

Natural variations

Alternative sequence67 – 199133Missing in isoform 2.
VSP_004656

Experimental info

Sequence conflict491K → G AA sequence Ref.14
Sequence conflict521T → G AA sequence Ref.14
Sequence conflict67 – 8216YSIFS…DNEIL → TVFSRMPPRDKTMRFF in CAA39671. Ref.4
Sequence conflict80 – 9819Missing AA sequence Ref.13
Sequence conflict1701L → V in AAA52074. Ref.12

Secondary structure

1 ...................................... 224
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 669228636A8544F6

FASTA22425,039
        10         20         30         40         50         60 
MEKLLCFLVL TSLSHAFGQT DMSRKAFVFP KESDTSYVSL KAPLTKPLKA FTVCLHFYTE 

        70         80         90        100        110        120 
LSSTRGYSIF SYATKRQDNE ILIFWSKDIG YSFTVGGSEI LFEVPEVTVA PVHICTSWES 

       130        140        150        160        170        180 
ASGIVEFWVD GKPRVRKSLK KGYTVGAEAS IILGQEQDSF GGNFEGSQSL VGDIGNVNMW 

       190        200        210        220 
DFVLSPDEIN TIYLGGPFSP NVLNWRALKY EVQGEVFTKP QLWP

« Hide

Isoform 2 [UniParc].

Checksum: A5E24599540DAA05
Show »

FASTA9110,415

References

« Hide 'large scale' references
[1]"Genomic DNA sequence for human C-reactive protein."
Lei K.-J., Liu T., Zon G., Soravia E., Liu T.-Y., Goldman N.D.
J. Biol. Chem. 260:13377-13383(1985) [PubMed: 2997165] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Characterization of genomic and complementary DNA sequence of human C-reactive protein, and comparison with the complementary DNA sequence of serum amyloid P component."
Woo P., Korenberg J.R., Whitehead A.S.
J. Biol. Chem. 260:13384-13388(1985) [PubMed: 3840479] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Extrahepetic transcription of human C-reactive protein."
Murphy T.M., Baum L., Beaman K.
Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]Tenchini M.L., Marchetti L., Bossi E., Malcovati M., Lorenzetti R.
Submitted (MAY-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[5]"Controlled gene expression using acute phase response elements."
Harraghy N.
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Urinary bladder.
[7]SeattleSNPs variation discovery resource
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"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. expand/collapse author list , 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: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Liver.
[11]"Biosynthesis and postsynthetic processing of human C-reactive protein."
Tucci A., Goldberger G., Whitehead A.S., Kay R.M., Woods D.E., Colten H.R.
J. Immunol. 131:2416-2419(1983) [PubMed: 6685157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-26.
[12]"Isolation of human C-reactive protein complementary DNA and localization of the gene to chromosome 1."
Whitehead A.S., Bruns G.A.P., Markham A.F., Colten H.R., Woods D.E.
Science 221:69-71(1983) [PubMed: 6857266] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 144-175.
[13]"Primary structure of human C-reactive protein."
Oliveira E.B., Gotschlich E.C., Liu T.-Y.
J. Biol. Chem. 254:489-502(1979) [PubMed: 762075] [Abstract]
Cited for: PROTEIN SEQUENCE OF 19-224.
[14]"Partial amino-acid sequences of human and rabbit C-reactive proteins: homology with immunoglobulins and histocompatibility antigens."
Osmand A.P., Gewurz H., Friedenson B.
Proc. Natl. Acad. Sci. U.S.A. 74:1214-1218(1977) [PubMed: 403526] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-55.
[15]"Selected expression profiling of full-length proteins and their variants in human plasma."
Kiernan U.A., Nedelkov D., Tubbs K.A., Niederkofler E.E., Nelson R.W.
Clin. Proteomics 1:7-16(2004)
Cited for: MASS SPECTROMETRY.
[16]"Comparative analyses of pentraxins: implications for protomer assembly and ligand binding."
Srinivasan N., White H.E., Emsley J., Wood S.P., Pepys M.B., Blundell T.L.
Structure 2:1017-1027(1994) [PubMed: 7881902] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[17]"Three dimensional structure of human C-reactive protein."
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.
Nat. Struct. Biol. 3:346-353(1996) [PubMed: 8599761] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[18]"The physiological structure of human C-reactive protein and its complex with phosphocholine."
Thompson D., Pepys M.B., Wood S.P.
Structure 7:169-177(1999) [PubMed: 10368284] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
+Additional computationally mapped references.

Web resources

Wikipedia

C-reactive protein entry

SeattleSNPs
Protein Spotlight

No more Christmas pudding? - Issue 30 of January 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M11880 Genomic DNA. Translation: AAB59526.1.
M11725 Genomic DNA. Translation: AAA52075.1.
X56692 mRNA. Translation: CAA40020.1.
X56214 mRNA. Translation: CAA39671.1.
AF442818 Genomic DNA. Translation: AAL48218.2.
AK289443 mRNA. Translation: BAF82132.1.
AF449713 Genomic DNA. Translation: AAL40835.1.
AL445528 Genomic DNA. Translation: CAH73654.1.
AL445528 Genomic DNA. Translation: CAH73656.1.
CH471121 Genomic DNA. Translation: EAW52778.1.
CH471121 Genomic DNA. Translation: EAW52779.1.
CH471121 Genomic DNA. Translation: EAW52780.1.
BC020766 mRNA. Translation: AAH20766.1.
BC125135 mRNA. Translation: AAI25136.1.
M35163 mRNA. Translation: AAA52076.1.
K00518 mRNA. Translation: AAA52074.1.
IPIIPI00022389.
IPI00218876.
PIRCJHU. A24515.
RefSeqNP_000558.2. NM_000567.2.
UniGeneHs.709456.
Hs.76452.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1B09X-ray2.50A/B/C/D/E19-224[»]
1CRVmodel-A/B/C/D/E19-224[»]
1GNHX-ray3.00A/B/C/D/E/F/G/H/I/J19-224[»]
1LJ7X-ray3.15A/B/C/D/E/F/G/H/I/J19-224[»]
3L2YX-ray2.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T19-224[»]
ProteinModelPortalP02741.
SMRP02741. Positions 19-224.
ModBaseSearch...

Protein-protein interaction databases

IntActP02741. 8 interactions.
MINTMINT-1206167.
STRINGP02741.

Polymorphism databases

DMDM117486.

2D gel databases

SWISS-2DPAGEP02741.
DOSAC-COBS-2DPAGEP02741.

Proteomic databases

PeptideAtlasP02741.
PRIDEP02741.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000255030; ENSP00000255030; ENSG00000132693.
GeneID1401.
KEGGhsa:1401.
UCSCuc001ftw.1. human.
uc001ftx.1. human.

Organism-specific databases

CTD1401.
GeneCardsGC01M159682.
H-InvDBHIX0028720.
HGNCHGNC:2367. CRP.
HPACAB005036.
HPA027367.
HPA027396.
MIM123260. gene.
neXtProtNX_P02741.
PharmGKBPA120.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG08533.
GeneTreeENSGT00550000074240.
HOGENOMHBG716040.
HOVERGENHBG005405.
InParanoidP02741.
OMACTSWESA.
OrthoDBEOG4R23VS.
PhylomeDBP02741.

Enzyme and pathway databases

Pathway_Interaction_DBil6_7pathway. IL6-mediated signaling events.

Gene expression databases

ArrayExpressP02741.
BgeeP02741.
CleanExHS_CRP.
GenevestigatorP02741.
GermOnlineENSG00000132693. Homo sapiens.

Family and domain databases

InterProIPR008985. ConA-like_lec_gl.
IPR013320. ConA-like_subgrp.
IPR001759. Pentaxin.
[Graphical view]
Gene3DG3DSA:2.60.120.200. ConA_like_subgrp. 1 hit.
PfamPF00354. Pentaxin. 1 hit.
[Graphical view]
PRINTSPR00895. PENTAXIN.
SMARTSM00159. PTX. 1 hit.
[Graphical view]
SUPFAMSSF49899. ConA_like_lec_gl. 1 hit.
PROSITEPS00289. PENTAXIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

DrugBankDB01076. Atorvastatin.
DB01393. Bezafibrate.
NextBio5737.
SOURCESearch...

Entry information

Entry nameCRP_HUMAN
AccessionPrimary (citable) accession number: P02741
Secondary accession number(s): A8K078 expand/collapse secondary AC list , D3DVD9, D3DVE0, Q08AK3, Q8WW75
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1988
Last modified: January 25, 2012
This is version 151 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents