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P04003

- C4BPA_HUMAN

UniProt

P04003 - C4BPA_HUMAN

Protein

C4b-binding protein alpha chain

Gene

C4BPA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 2 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Controls the classical pathway of complement activation. It binds as a cofactor to C3b/C4b inactivator (C3bINA), which then hydrolyzes the complement fragment C4b. It also accelerates the degradation of the C4bC2a complex (C3 convertase) by dissociating the complement fragment C2a. Alpha chain binds C4b. It interacts also with anticoagulant protein S and with serum amyloid P component.

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. complement activation, classical pathway Source: UniProtKB-KW
    2. innate immune response Source: Reactome
    3. negative regulation of complement activation, classical pathway Source: BHF-UCL
    4. positive regulation of protein catabolic process Source: BHF-UCL
    5. regulation of complement activation Source: Reactome
    6. regulation of opsonization Source: BHF-UCL

    Keywords - Biological processi

    Complement pathway, Immunity, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_118707. Regulation of Complement cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    C4b-binding protein alpha chain
    Short name:
    C4bp
    Alternative name(s):
    Proline-rich protein
    Short name:
    PRP
    Gene namesi
    Name:C4BPA
    Synonyms:C4BP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1325. C4BPA.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. extracellular region Source: UniProtKB
    3. extracellular space Source: BHF-UCL
    4. other organism cell Source: BHF-UCL
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25905.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 48481 PublicationAdd
    BLAST
    Chaini49 – 597549C4b-binding protein alpha chainPRO_0000005888Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi50 ↔ 961 PublicationPROSITE-ProRule annotation
    Disulfide bondi81 ↔ 1081 PublicationPROSITE-ProRule annotation
    Disulfide bondi113 ↔ 1541 PublicationPROSITE-ProRule annotation
    Disulfide bondi140 ↔ 1701 PublicationPROSITE-ProRule annotation
    Disulfide bondi175 ↔ 217PROSITE-ProRule annotation
    Disulfide bondi203 ↔ 234PROSITE-ProRule annotation
    Glycosylationi221 – 2211N-linked (GlcNAc...)3 Publications
    Disulfide bondi239 ↔ 281PROSITE-ProRule annotation
    Disulfide bondi267 ↔ 294PROSITE-ProRule annotation
    Disulfide bondi299 ↔ 348PROSITE-ProRule annotation
    Disulfide bondi332 ↔ 360PROSITE-ProRule annotation
    Disulfide bondi365 ↔ 409PROSITE-ProRule annotation
    Disulfide bondi399 ↔ 422PROSITE-ProRule annotation
    Disulfide bondi426 ↔ 468PROSITE-ProRule annotation
    Disulfide bondi454 ↔ 480PROSITE-ProRule annotation
    Disulfide bondi484 ↔ 525PROSITE-ProRule annotation
    Glycosylationi506 – 5061N-linked (GlcNAc...)4 Publications
    Disulfide bondi511 ↔ 538PROSITE-ProRule annotation
    Glycosylationi528 – 5281N-linked (GlcNAc...)2 Publications
    Disulfide bondi546 – 546Interchain (with beta chain)PROSITE-ProRule annotation
    Disulfide bondi558 – 558Interchain (with beta chain)PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP04003.
    PaxDbiP04003.
    PeptideAtlasiP04003.
    PRIDEiP04003.

    PTM databases

    PhosphoSiteiP04003.

    Expressioni

    Tissue specificityi

    Chylomicrons in the plasma.

    Gene expression databases

    ArrayExpressiP04003.
    BgeeiP04003.
    CleanExiHS_C4BPA.
    GenevestigatoriP04003.

    Organism-specific databases

    HPAiHPA000926.
    HPA001578.

    Interactioni

    Subunit structurei

    Disulfide-linked complex of alpha and beta chains of 3 possible sorts: a 570 kDa complex of 7 alpha chains and 1 beta chain, a 530 kDa homoheptamer of alpha chains or a 500 kDa complex of 6 alpha chains and 1 beta chain. The central body of the alpha chain homopolymer supports tentacles, each with the binding site for C4b at the end.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    arp4P130505EBI-978348,EBI-978341From a different organism.

    Protein-protein interaction databases

    BioGridi107183. 8 interactions.
    IntActiP04003. 6 interactions.
    STRINGi9606.ENSP00000356037.

    Structurei

    Secondary structure

    1
    597
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi85 – 873
    Beta strandi98 – 1036
    Beta strandi108 – 1103
    Beta strandi131 – 1333
    Beta strandi158 – 1603
    Helixi547 – 5559
    Beta strandi558 – 5614
    Helixi562 – 58928
    Helixi591 – 5966

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2A55NMR-A49-172[»]
    4B0FX-ray2.80A/B/C/D/E/F/G540-597[»]
    ProteinModelPortaliP04003.
    SMRiP04003. Positions 49-597.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04003.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini49 – 11062Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini111 – 17262Sushi 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini173 – 23664Sushi 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini237 – 29660Sushi 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini297 – 36266Sushi 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini363 – 42462Sushi 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini425 – 48258Sushi 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini483 – 54058Sushi 8PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 8 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Sushi

    Phylogenomic databases

    eggNOGiNOG150577.
    HOGENOMiHOG000015324.
    HOVERGENiHBG004657.
    InParanoidiP04003.
    KOiK04002.
    OMAiVENETIG.
    OrthoDBiEOG725DH2.
    PhylomeDBiP04003.
    TreeFamiTF334137.

    Family and domain databases

    InterProiIPR000436. Sushi_SCR_CCP.
    [Graphical view]
    PfamiPF00084. Sushi. 8 hits.
    [Graphical view]
    SMARTiSM00032. CCP. 8 hits.
    [Graphical view]
    SUPFAMiSSF57535. SSF57535. 8 hits.
    PROSITEiPS50923. SUSHI. 8 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P04003-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHPPKTPSGA LHRKRKMAAW PFSRLWKVSD PILFQMTLIA ALLPAVLGNC    50
    GPPPTLSFAA PMDITLTETR FKTGTTLKYT CLPGYVRSHS TQTLTCNSDG 100
    EWVYNTFCIY KRCRHPGELR NGQVEIKTDL SFGSQIEFSC SEGFFLIGST 150
    TSRCEVQDRG VGWSHPLPQC EIVKCKPPPD IRNGRHSGEE NFYAYGFSVT 200
    YSCDPRFSLL GHASISCTVE NETIGVWRPS PPTCEKITCR KPDVSHGEMV 250
    SGFGPIYNYK DTIVFKCQKG FVLRGSSVIH CDADSKWNPS PPACEPNSCI 300
    NLPDIPHASW ETYPRPTKED VYVVGTVLRY RCHPGYKPTT DEPTTVICQK 350
    NLRWTPYQGC EALCCPEPKL NNGEITQHRK SRPANHCVYF YGDEISFSCH 400
    ETSRFSAICQ GDGTWSPRTP SCGDICNFPP KIAHGHYKQS SSYSFFKEEI 450
    IYECDKGYIL VGQAKLSCSY SHWSAPAPQC KALCRKPELV NGRLSVDKDQ 500
    YVEPENVTIQ CDSGYGVVGP QSITCSGNRT WYPEVPKCEW ETPEGCEQVL 550
    TGKRLMQCLP NPEDVKMALE VYKLSLEIEQ LELQRDSARQ STLDKEL 597
    Length:597
    Mass (Da):67,033
    Last modified:October 1, 1993 - v2
    Checksum:i67E03F2EA85A16DD
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti4 – 41P → Q.
    Corresponds to variant rs55867570 [ dbSNP | Ensembl ].
    VAR_061123
    Natural varianti60 – 601A → V.
    Corresponds to variant rs17020956 [ dbSNP | Ensembl ].
    VAR_048815
    Natural varianti240 – 2401R → H.
    Corresponds to variant rs45574833 [ dbSNP | Ensembl ].
    VAR_061124
    Natural varianti300 – 3001I → T.
    Corresponds to variant rs4844573 [ dbSNP | Ensembl ].
    VAR_024420
    Natural varianti357 – 3571Y → H.
    VAR_001978
    Natural varianti473 – 4731W → L.
    Corresponds to variant rs1801341 [ dbSNP | Ensembl ].
    VAR_012038

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31452 mRNA. Translation: AAA36507.1.
    M62486
    , M62475, M62476, M62477, M62478, M62479, M62480, M62481, M62482, M62484, M62485 Genomic DNA. Translation: AAA36506.1.
    AK313164 mRNA. Translation: BAG35982.1.
    CH471100 Genomic DNA. Translation: EAW93502.1.
    CH471100 Genomic DNA. Translation: EAW93503.1.
    BC022312 mRNA. Translation: AAH22312.1.
    X07853 mRNA. Translation: CAA30701.1.
    X04284 Genomic DNA. Translation: CAB51244.1.
    X04296 Genomic DNA. Translation: CAA27839.1.
    X02865 mRNA. Translation: CAA26617.1.
    CCDSiCCDS1477.1.
    PIRiA33568. NBHUC4.
    RefSeqiNP_000706.1. NM_000715.3.
    XP_005273308.1. XM_005273251.1.
    XP_005273309.1. XM_005273252.2.
    UniGeneiHs.1012.

    Genome annotation databases

    EnsembliENST00000367070; ENSP00000356037; ENSG00000123838.
    GeneIDi722.
    KEGGihsa:722.
    UCSCiuc001hfo.3. human.

    Polymorphism databases

    DMDMi416733.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31452 mRNA. Translation: AAA36507.1 .
    M62486
    , M62475 , M62476 , M62477 , M62478 , M62479 , M62480 , M62481 , M62482 , M62484 , M62485 Genomic DNA. Translation: AAA36506.1 .
    AK313164 mRNA. Translation: BAG35982.1 .
    CH471100 Genomic DNA. Translation: EAW93502.1 .
    CH471100 Genomic DNA. Translation: EAW93503.1 .
    BC022312 mRNA. Translation: AAH22312.1 .
    X07853 mRNA. Translation: CAA30701.1 .
    X04284 Genomic DNA. Translation: CAB51244.1 .
    X04296 Genomic DNA. Translation: CAA27839.1 .
    X02865 mRNA. Translation: CAA26617.1 .
    CCDSi CCDS1477.1.
    PIRi A33568. NBHUC4.
    RefSeqi NP_000706.1. NM_000715.3.
    XP_005273308.1. XM_005273251.1.
    XP_005273309.1. XM_005273252.2.
    UniGenei Hs.1012.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2A55 NMR - A 49-172 [» ]
    4B0F X-ray 2.80 A/B/C/D/E/F/G 540-597 [» ]
    ProteinModelPortali P04003.
    SMRi P04003. Positions 49-597.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107183. 8 interactions.
    IntActi P04003. 6 interactions.
    STRINGi 9606.ENSP00000356037.

    PTM databases

    PhosphoSitei P04003.

    Polymorphism databases

    DMDMi 416733.

    Proteomic databases

    MaxQBi P04003.
    PaxDbi P04003.
    PeptideAtlasi P04003.
    PRIDEi P04003.

    Protocols and materials databases

    DNASUi 722.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000367070 ; ENSP00000356037 ; ENSG00000123838 .
    GeneIDi 722.
    KEGGi hsa:722.
    UCSCi uc001hfo.3. human.

    Organism-specific databases

    CTDi 722.
    GeneCardsi GC01P207277.
    HGNCi HGNC:1325. C4BPA.
    HPAi HPA000926.
    HPA001578.
    MIMi 120830. gene.
    neXtProti NX_P04003.
    PharmGKBi PA25905.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG150577.
    HOGENOMi HOG000015324.
    HOVERGENi HBG004657.
    InParanoidi P04003.
    KOi K04002.
    OMAi VENETIG.
    OrthoDBi EOG725DH2.
    PhylomeDBi P04003.
    TreeFami TF334137.

    Enzyme and pathway databases

    Reactomei REACT_118707. Regulation of Complement cascade.

    Miscellaneous databases

    EvolutionaryTracei P04003.
    GenomeRNAii 722.
    NextBioi 2938.
    PROi P04003.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P04003.
    Bgeei P04003.
    CleanExi HS_C4BPA.
    Genevestigatori P04003.

    Family and domain databases

    InterProi IPR000436. Sushi_SCR_CCP.
    [Graphical view ]
    Pfami PF00084. Sushi. 8 hits.
    [Graphical view ]
    SMARTi SM00032. CCP. 8 hits.
    [Graphical view ]
    SUPFAMi SSF57535. SSF57535. 8 hits.
    PROSITEi PS50923. SUSHI. 8 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the cDNA coding for proline-rich protein (PRP): identity of PRP as C4b-binding protein."
      Matsuguchi T., Okamura S., Aso T., Sata T., Niho Y.
      Biochem. Biophys. Res. Commun. 165:138-144(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    2. "Genomic organization of the alpha chain of the human C4b-binding protein gene."
      Aso T., Okamura S., Matsuguchi T., Sakamoto N., Sata T., Niho Y.
      Biochem. Biophys. Res. Commun. 174:222-227(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    3. "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].
      Tissue: Lung.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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].
      Tissue: Lung.
    6. "Derivation of the sequence of the signal peptide in human C4b-binding protein and interspecies cross-hybridisation of the C4bp cDNA sequence."
      Lintin S.J., Lewin A.R., Reid K.B.M.
      FEBS Lett. 232:328-332(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-81.
    7. "Studies on the structure of the human C4b-binding protein gene."
      Lintin S.J., Reid K.B.M.
      FEBS Lett. 204:77-81(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 203-288.
    8. "Molecular cloning and characterization of the cDNA coding for C4b-binding protein, a regulatory protein of the classical pathway of the human complement system."
      Chung L.P., Bentley D.R., Reid K.B.M.
      Biochem. J. 230:133-141(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 80-597.
    9. "Amino acid sequence studies of human C4b-binding protein: N-terminal sequence analysis and alignment of the fragments produced by limited proteolysis with chymotrypsin and the peptides produced by cyanogen bromide treatment."
      Chung L.P., Gagnon J., Reid K.B.M.
      Mol. Immunol. 22:427-435(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 49-88.
    10. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
      Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
      Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-506 AND ASN-528.
      Tissue: Plasma.
    11. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221 AND ASN-506.
      Tissue: Plasma.
    12. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-221 AND ASN-506.
      Tissue: Liver.
    13. "Visualization of human C4b-binding protein and its complexes with vitamin K-dependent protein S and complement protein C4b."
      Dahlback B., Smith C.A., Mueller-Eberhard H.J.
      Proc. Natl. Acad. Sci. U.S.A. 80:3461-3465(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY ELECTRON MICROSCOPY, LIGAND-BINDING.
    14. "Human C4b-binding protein, structural basis for interaction with streptococcal M protein, a major bacterial virulence factor."
      Jenkins H.T., Mark L., Ball G., Persson J., Lindahl G., Uhrin D., Blom A.M., Barlow P.N.
      J. Biol. Chem. 281:3690-3697(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 49-172, DISULFIDE BONDS.

    Entry informationi

    Entry nameiC4BPA_HUMAN
    AccessioniPrimary (citable) accession number: P04003
    Secondary accession number(s): Q5VVQ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 23, 1986
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 148 of the entry and version 2 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

    Caution

    It is uncertain whether Met-1 or Met-17 is the initiator.Curated

    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. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3