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P02741

- CRP_HUMAN

UniProt

P02741 - CRP_HUMAN

Protein

C-reactive protein

Gene

CRP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 178 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    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
    6. protein binding Source: UniProtKB

    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

    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

    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

    ArrayExpressiP02741.
    BgeeiP02741.
    CleanExiHS_CRP.
    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.
    HOGENOMiHOG000247043.
    HOVERGENiHBG005405.
    InParanoidiP02741.
    KOiK16143.
    OMAiWRALKYE.
    OrthoDBiEOG71RXMB.
    PhylomeDBiP02741.
    TreeFamiTF330208.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    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

    MEKLLCFLVL TSLSHAFGQT DMSRKAFVFP KESDTSYVSL KAPLTKPLKA    50
    FTVCLHFYTE LSSTRGYSIF SYATKRQDNE ILIFWSKDIG YSFTVGGSEI 100
    LFEVPEVTVA PVHICTSWES ASGIVEFWVD GKPRVRKSLK KGYTVGAEAS 150
    IILGQEQDSF GGNFEGSQSL VGDIGNVNMW DFVLSPDEIN TIYLGGPFSP 200
    NVLNWRALKY EVQGEVFTKP QLWP 224
    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 DB01076. Atorvastatin.
    DB01393. Bezafibrate.

    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.
    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

    ArrayExpressi P02741.
    Bgeei P02741.
    CleanExi HS_CRP.
    Genevestigatori P02741.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    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

    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 1, 2014
    This is version 178 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