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P02741

- CRP_HUMAN

UniProt

P02741 - CRP_HUMAN

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Protein

C-reactive protein

Gene

CRP

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

Functioni

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.

Cofactori

Binds 2 calcium ions per subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi78 – 781Calcium 1
Metal bindingi79 – 791Calcium 1
Metal bindingi156 – 1561Calcium 1
Metal bindingi156 – 1561Calcium 2
Metal bindingi157 – 1571Calcium 1; via carbonyl oxygen
Metal bindingi158 – 1581Calcium 1
Metal bindingi158 – 1581Calcium 2
Metal bindingi168 – 1681Calcium 2

GO - Molecular functioni

  1. calcium ion binding Source: BHF-UCL
  2. cholesterol binding Source: Ensembl
  3. choline binding Source: BHF-UCL
  4. complement component C1q binding Source: BHF-UCL
  5. low-density lipoprotein particle binding Source: BHF-UCL

GO - Biological processi

  1. acute-phase response Source: BHF-UCL
  2. aging Source: Ensembl
  3. cellular response to calcium ion Source: Ensembl
  4. complement activation, classical pathway Source: Ensembl
  5. defense response to Gram-positive bacterium Source: BHF-UCL
  6. inflammatory response Source: ProtInc
  7. negative regulation of lipid storage Source: BHF-UCL
  8. negative regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  9. opsonization Source: BHF-UCL
  10. positive regulation of dendrite development Source: Ensembl
  11. protein polymerization Source: Ensembl
  12. regulation of interleukin-8 secretion Source: UniProtKB
  13. response to ethanol Source: Ensembl
  14. response to hypoxia Source: Ensembl
  15. response to lead ion Source: Ensembl
  16. wound healing Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Acute phase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_7956. Classical antibody-mediated complement activation.

Names & Taxonomyi

Protein namesi
Recommended name:
C-reactive protein
Cleaved into the following chain:
Gene namesi
Name:CRP
Synonyms:PTX1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:2367. CRP.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. extracellular space Source: BHF-UCL
  3. extracellular vesicular exosome Source: UniProt
  4. filopodium Source: Ensembl
  5. growth cone Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA120.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18181 PublicationAdd
BLAST
Chaini19 – 224206C-reactive proteinPRO_0000023526Add
BLAST
Chaini19 – 223205C-reactive protein(1-205)PRO_0000023527Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Pyrrolidone carboxylic acid1 Publication
Disulfide bondi54 ↔ 1151 Publication

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

PaxDbiP02741.
PeptideAtlasiP02741.
PRIDEiP02741.

2D gel databases

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

PTM databases

PhosphoSiteiP02741.

Expressioni

Tissue specificityi

Found in plasma.

Inductioni

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.

Gene expression databases

BgeeiP02741.
CleanExiHS_CRP.
ExpressionAtlasiP02741. baseline and differential.
GenevestigatoriP02741.

Organism-specific databases

HPAiCAB005036.
HPA027367.
HPA027396.

Interactioni

Subunit structurei

Homopentamer. Pentaxin (or pentraxin) have a discoid arrangement of 5 non-covalently bound subunits. Interacts with FCN1; may regulate monocyte activation by FCN1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FCGR2CP319952EBI-1395983,EBI-1396036

Protein-protein interaction databases

BioGridi107791. 13 interactions.
DIPiDIP-39125N.
IntActiP02741. 9 interactions.
MINTiMINT-1206167.
STRINGi9606.ENSP00000255030.

Structurei

Secondary structure

1
224
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi25 – 295
Beta strandi37 – 404
Beta strandi48 – 6013
Helixi61 – 633
Beta strandi67 – 748
Beta strandi77 – 8610
Turni87 – 893
Beta strandi90 – 956
Beta strandi98 – 1036
Beta strandi112 – 1198
Turni120 – 1223
Beta strandi124 – 1296
Beta strandi132 – 1387
Beta strandi150 – 1556
Helixi166 – 1683
Beta strandi172 – 18211
Helixi186 – 1949
Beta strandi201 – 2033
Helixi205 – 2073
Beta strandi210 – 2156
Beta strandi217 – 2204

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
3PVNX-ray1.98A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T19-224[»]
3PVOX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T19-224[»]
ProteinModelPortaliP02741.
SMRiP02741. Positions 19-224.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02741.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 224206PentaxinAdd
BLAST

Sequence similaritiesi

Belongs to the pentaxin family.Curated
Contains 1 pentaxin domain.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG113288.
GeneTreeiENSGT00760000119128.
HOGENOMiHOG000247043.
HOVERGENiHBG005405.
InParanoidiP02741.
KOiK16143.
OMAiWRALKYE.
OrthoDBiEOG71RXMB.
PhylomeDBiP02741.
TreeFamiTF330208.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001759. Pentaxin.
[Graphical view]
PfamiPF00354. Pentaxin. 1 hit.
[Graphical view]
PRINTSiPR00895. PENTAXIN.
SMARTiSM00159. PTX. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00289. PENTAXIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P02741-1) [UniParc]FASTAAdd to Basket

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

« Hide

        10         20         30         40         50
MEKLLCFLVL TSLSHAFGQT DMSRKAFVFP KESDTSYVSL KAPLTKPLKA
60 70 80 90 100
FTVCLHFYTE LSSTRGYSIF SYATKRQDNE ILIFWSKDIG YSFTVGGSEI
110 120 130 140 150
LFEVPEVTVA PVHICTSWES ASGIVEFWVD GKPRVRKSLK KGYTVGAEAS
160 170 180 190 200
IILGQEQDSF GGNFEGSQSL VGDIGNVNMW DFVLSPDEIN TIYLGGPFSP
210 220
NVLNWRALKY EVQGEVFTKP QLWP
Length:224
Mass (Da):25,039
Last modified:January 1, 1988 - v1
Checksum:i669228636A8544F6
GO
Isoform 2 (identifier: P02741-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     67-199: Missing.

Note: No experimental confirmation available.

Show »
Length:91
Mass (Da):10,415
Checksum:iA5E24599540DAA05
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti49 – 491K → G AA sequence (PubMed:403526)Curated
Sequence conflicti52 – 521T → G AA sequence (PubMed:403526)Curated
Sequence conflicti67 – 8216YSIFS…DNEIL → TVFSRMPPRDKTMRFF in CAA39671. 1 PublicationCuratedAdd
BLAST
Sequence conflicti80 – 9819Missing AA sequence (PubMed:762075)CuratedAdd
BLAST
Sequence conflicti170 – 1701L → V in AAA52074. (PubMed:6857266)Curated

Mass spectrometryi

Molecular mass is 23028 Da from positions 19 - 224. Determined by MALDI. 1 Publication
Molecular mass is 22930 Da from positions 19 - 223. Determined by MALDI. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei67 – 199133Missing in isoform 2. 1 PublicationVSP_004656Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS30911.1. [P02741-1]
PIRiA24515. CJHU.
RefSeqiNP_000558.2. NM_000567.2. [P02741-1]
UniGeneiHs.709456.
Hs.76452.

Genome annotation databases

EnsembliENST00000255030; ENSP00000255030; ENSG00000132693. [P02741-1]
ENST00000368112; ENSP00000357093; ENSG00000132693. [P02741-2]
GeneIDi1401.
KEGGihsa:1401.
UCSCiuc001ftw.3. human. [P02741-1]
uc001ftx.1. human. [P02741-2]

Polymorphism databases

DMDMi117486.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Wikipedia

C-reactive protein entry

SeattleSNPs
Protein Spotlight

No more Christmas pudding? - Issue 30 of January 2003

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS30911.1. [P02741-1 ]
PIRi A24515. CJHU.
RefSeqi NP_000558.2. NM_000567.2. [P02741-1 ]
UniGenei Hs.709456.
Hs.76452.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B09 X-ray 2.50 A/B/C/D/E 19-224 [» ]
1CRV model - A/B/C/D/E 19-224 [» ]
1GNH X-ray 3.00 A/B/C/D/E/F/G/H/I/J 19-224 [» ]
1LJ7 X-ray 3.15 A/B/C/D/E/F/G/H/I/J 19-224 [» ]
3L2Y X-ray 2.70 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T 19-224 [» ]
3PVN X-ray 1.98 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T 19-224 [» ]
3PVO X-ray 3.00 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T 19-224 [» ]
ProteinModelPortali P02741.
SMRi P02741. Positions 19-224.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107791. 13 interactions.
DIPi DIP-39125N.
IntActi P02741. 9 interactions.
MINTi MINT-1206167.
STRINGi 9606.ENSP00000255030.

Chemistry

DrugBanki DB05278. inhaled insulin.

PTM databases

PhosphoSitei P02741.

Polymorphism databases

DMDMi 117486.

2D gel databases

DOSAC-COBS-2DPAGE P02741.
SWISS-2DPAGE P02741.

Proteomic databases

PaxDbi P02741.
PeptideAtlasi P02741.
PRIDEi P02741.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000255030 ; ENSP00000255030 ; ENSG00000132693 . [P02741-1 ]
ENST00000368112 ; ENSP00000357093 ; ENSG00000132693 . [P02741-2 ]
GeneIDi 1401.
KEGGi hsa:1401.
UCSCi uc001ftw.3. human. [P02741-1 ]
uc001ftx.1. human. [P02741-2 ]

Organism-specific databases

CTDi 1401.
GeneCardsi GC01M159682.
H-InvDB HIX0028720.
HGNCi HGNC:2367. CRP.
HPAi CAB005036.
HPA027367.
HPA027396.
MIMi 123260. gene.
neXtProti NX_P02741.
PharmGKBi PA120.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG113288.
GeneTreei ENSGT00760000119128.
HOGENOMi HOG000247043.
HOVERGENi HBG005405.
InParanoidi P02741.
KOi K16143.
OMAi WRALKYE.
OrthoDBi EOG71RXMB.
PhylomeDBi P02741.
TreeFami TF330208.

Enzyme and pathway databases

Reactomei REACT_7956. Classical antibody-mediated complement activation.

Miscellaneous databases

ChiTaRSi CRP. human.
EvolutionaryTracei P02741.
GeneWikii C-reactive_protein.
GenomeRNAii 1401.
NextBioi 5737.
PROi P02741.
SOURCEi Search...

Gene expression databases

Bgeei P02741.
CleanExi HS_CRP.
ExpressionAtlasi P02741. baseline and differential.
Genevestigatori P02741.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR013320. ConA-like_dom.
IPR001759. Pentaxin.
[Graphical view ]
Pfami PF00354. Pentaxin. 1 hit.
[Graphical view ]
PRINTSi PR00895. PENTAXIN.
SMARTi SM00159. PTX. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS00289. PENTAXIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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.
    , 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] [Europe PMC] [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.
    , 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].
  9. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-224, PYROGLUTAMATE FORMATION AT GLN-19.
  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] [Europe PMC] [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. "Secreted M-ficolin anchors onto monocyte transmembrane G protein-coupled receptor 43 and cross talks with plasma C-reactive protein to mediate immune signaling and regulate host defense."
    Zhang J., Yang L., Ang Z., Yoong S.L., Tran T.T., Anand G.S., Tan N.S., Ho B., Ding J.L.
    J. Immunol. 185:6899-6910(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FCN1.
  17. "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] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  18. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
  19. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

Entry informationi

Entry nameiCRP_HUMAN
AccessioniPrimary (citable) accession number: P02741
Secondary accession number(s): A8K078
, D3DVD9, D3DVE0, Q08AK3, Q8WW75
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 1, 1988
Last modified: October 29, 2014
This is version 179 of the entry and version 1 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

Miscellaneous

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

Keywords - Technical termi

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

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3