Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P20851

- C4BPB_HUMAN

UniProt

P20851 - C4BPB_HUMAN

Protein

C4b-binding protein beta chain

Gene

C4BPB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Feb 1991)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. It also interacts with anticoagulant protein S and with serum amyloid P component. The beta chain binds protein S.

    GO - Molecular functioni

    1. protein binding Source: BHF-UCL

    GO - Biological processi

    1. blood coagulation Source: ProtInc
    2. complement activation, classical pathway Source: UniProtKB-KW
    3. innate immune response Source: Reactome
    4. negative regulation of complement activation, classical pathway Source: BHF-UCL
    5. positive regulation of protein catabolic process Source: BHF-UCL
    6. regulation of complement activation Source: Reactome
    7. 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 beta chain
    Gene namesi
    Name:C4BPB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1328. C4BPB.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25908.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Add
    BLAST
    Chaini18 – 252235C4b-binding protein beta chainPRO_0000005892Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi23 ↔ 63PROSITE-ProRule annotation
    Disulfide bondi49 ↔ 76PROSITE-ProRule annotation
    Glycosylationi64 – 641N-linked (GlcNAc...)2 Publications
    Glycosylationi71 – 711N-linked (GlcNAc...)1 Publication
    Disulfide bondi81 ↔ 121PROSITE-ProRule annotation
    Glycosylationi98 – 981N-linked (GlcNAc...)3 Publications
    Disulfide bondi107 ↔ 134PROSITE-ProRule annotation
    Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi139 ↔ 179PROSITE-ProRule annotation
    Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi165 ↔ 191PROSITE-ProRule annotation
    Disulfide bondi202 – 202Interchain (with alpha chain)PROSITE-ProRule annotation
    Disulfide bondi216 – 216Interchain (with alpha chain)PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP20851.
    PaxDbiP20851.
    PRIDEiP20851.

    Expressioni

    Gene expression databases

    ArrayExpressiP20851.
    BgeeiP20851.
    CleanExiHS_C4BPB.
    GenevestigatoriP20851.

    Organism-specific databases

    HPAiHPA051620.

    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.

    Protein-protein interaction databases

    BioGridi107186. 1 interaction.
    STRINGi9606.ENSP00000243611.

    Structurei

    3D structure databases

    ProteinModelPortaliP20851.
    SMRiP20851. Positions 40-213.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 7858Sushi 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini79 – 13658Sushi 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini137 – 19357Sushi 3PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 3 Sushi (CCP/SCR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Sushi

    Phylogenomic databases

    eggNOGiNOG260856.
    HOGENOMiHOG000032571.
    HOVERGENiHBG004922.
    InParanoidiP20851.
    KOiK04003.
    OMAiILKGSNW.
    OrthoDBiEOG7QRQVH.
    PhylomeDBiP20851.
    TreeFamiTF342864.

    Family and domain databases

    InterProiIPR000436. Sushi_SCR_CCP.
    [Graphical view]
    PfamiPF00084. Sushi. 3 hits.
    [Graphical view]
    SMARTiSM00032. CCP. 3 hits.
    [Graphical view]
    SUPFAMiSSF57535. SSF57535. 3 hits.
    PROSITEiPS50923. SUSHI. 3 hits.
    [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: P20851-1) [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

    MFFWCACCLM VAWRVSASDA EHCPELPPVD NSIFVAKEVE GQILGTYVCI    50
    KGYHLVGKKT LFCNASKEWD NTTTECRLGH CPDPVLVNGE FSSSGPVNVS 100
    DKITFMCNDH YILKGSNRSQ CLEDHTWAPP FPICKSRDCD PPGNPVHGYF 150
    EGNNFTLGST ISYYCEDRYY LVGVQEQQCV DGEWSSALPV CKLIQEAPKP 200
    ECEKALLAFQ ESKNLCEAME NFMQQLKESG MTMEELKYSL ELKKAELKAK 250
    LL 252
    Length:252
    Mass (Da):28,357
    Last modified:February 1, 1991 - v1
    Checksum:i0F6CC64067C5E2E7
    GO
    Isoform 2 (identifier: P20851-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         20-20: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:251
    Mass (Da):28,286
    Checksum:i2BA0722033999AF4
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti102 – 1021K → Q.1 Publication
    Corresponds to variant rs56258224 [ dbSNP | Ensembl ].
    VAR_038734
    Natural varianti198 – 1981P → S.
    Corresponds to variant rs1803226 [ dbSNP | Ensembl ].
    VAR_012039

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei20 – 201Missing in isoform 2. 1 PublicationVSP_022594

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11244 mRNA. Translation: AAA35615.1.
    L11245 mRNA. Translation: AAA35616.1.
    M29964 mRNA. Translation: AAB59520.1.
    EF613556 Genomic DNA. Translation: ABQ52216.1.
    AL445493 Genomic DNA. Translation: CAH70780.1.
    AL445493 Genomic DNA. Translation: CAH70781.1.
    CH471100 Genomic DNA. Translation: EAW93504.1.
    CH471100 Genomic DNA. Translation: EAW93506.1.
    BC005378 mRNA. Translation: AAH05378.1.
    CCDSiCCDS1476.1. [P20851-1]
    CCDS31005.1. [P20851-2]
    PIRiA47107. A34877.
    RefSeqiNP_000707.1. NM_000716.3. [P20851-1]
    NP_001017364.1. NM_001017364.1. [P20851-2]
    NP_001017365.1. NM_001017365.1. [P20851-1]
    NP_001017366.1. NM_001017366.1. [P20851-2]
    NP_001017367.1. NM_001017367.1. [P20851-1]
    XP_005273310.1. XM_005273253.2. [P20851-1]
    XP_005273311.1. XM_005273254.2. [P20851-1]
    UniGeneiHs.99886.

    Genome annotation databases

    EnsembliENST00000243611; ENSP00000243611; ENSG00000123843. [P20851-1]
    ENST00000367076; ENSP00000356043; ENSG00000123843. [P20851-2]
    ENST00000367078; ENSP00000356045; ENSG00000123843. [P20851-1]
    ENST00000391923; ENSP00000375790; ENSG00000123843. [P20851-1]
    GeneIDi725.
    KEGGihsa:725.
    UCSCiuc001hfi.3. human. [P20851-2]
    uc001hfj.3. human. [P20851-1]

    Polymorphism databases

    DMDMi115213.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L11244 mRNA. Translation: AAA35615.1 .
    L11245 mRNA. Translation: AAA35616.1 .
    M29964 mRNA. Translation: AAB59520.1 .
    EF613556 Genomic DNA. Translation: ABQ52216.1 .
    AL445493 Genomic DNA. Translation: CAH70780.1 .
    AL445493 Genomic DNA. Translation: CAH70781.1 .
    CH471100 Genomic DNA. Translation: EAW93504.1 .
    CH471100 Genomic DNA. Translation: EAW93506.1 .
    BC005378 mRNA. Translation: AAH05378.1 .
    CCDSi CCDS1476.1. [P20851-1 ]
    CCDS31005.1. [P20851-2 ]
    PIRi A47107. A34877.
    RefSeqi NP_000707.1. NM_000716.3. [P20851-1 ]
    NP_001017364.1. NM_001017364.1. [P20851-2 ]
    NP_001017365.1. NM_001017365.1. [P20851-1 ]
    NP_001017366.1. NM_001017366.1. [P20851-2 ]
    NP_001017367.1. NM_001017367.1. [P20851-1 ]
    XP_005273310.1. XM_005273253.2. [P20851-1 ]
    XP_005273311.1. XM_005273254.2. [P20851-1 ]
    UniGenei Hs.99886.

    3D structure databases

    ProteinModelPortali P20851.
    SMRi P20851. Positions 40-213.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107186. 1 interaction.
    STRINGi 9606.ENSP00000243611.

    Polymorphism databases

    DMDMi 115213.

    Proteomic databases

    MaxQBi P20851.
    PaxDbi P20851.
    PRIDEi P20851.

    Protocols and materials databases

    DNASUi 725.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000243611 ; ENSP00000243611 ; ENSG00000123843 . [P20851-1 ]
    ENST00000367076 ; ENSP00000356043 ; ENSG00000123843 . [P20851-2 ]
    ENST00000367078 ; ENSP00000356045 ; ENSG00000123843 . [P20851-1 ]
    ENST00000391923 ; ENSP00000375790 ; ENSG00000123843 . [P20851-1 ]
    GeneIDi 725.
    KEGGi hsa:725.
    UCSCi uc001hfi.3. human. [P20851-2 ]
    uc001hfj.3. human. [P20851-1 ]

    Organism-specific databases

    CTDi 725.
    GeneCardsi GC01P207262.
    HGNCi HGNC:1328. C4BPB.
    HPAi HPA051620.
    MIMi 120831. gene.
    neXtProti NX_P20851.
    PharmGKBi PA25908.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG260856.
    HOGENOMi HOG000032571.
    HOVERGENi HBG004922.
    InParanoidi P20851.
    KOi K04003.
    OMAi ILKGSNW.
    OrthoDBi EOG7QRQVH.
    PhylomeDBi P20851.
    TreeFami TF342864.

    Enzyme and pathway databases

    Reactomei REACT_118707. Regulation of Complement cascade.

    Miscellaneous databases

    GenomeRNAii 725.
    NextBioi 2944.
    PROi P20851.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20851.
    Bgeei P20851.
    CleanExi HS_C4BPB.
    Genevestigatori P20851.

    Family and domain databases

    InterProi IPR000436. Sushi_SCR_CCP.
    [Graphical view ]
    Pfami PF00084. Sushi. 3 hits.
    [Graphical view ]
    SMARTi SM00032. CCP. 3 hits.
    [Graphical view ]
    SUPFAMi SSF57535. SSF57535. 3 hits.
    PROSITEi PS50923. SUSHI. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human C4b-binding protein beta-chain gene."
      Hillarp A., Pardo-Manuel F., Ruiz R., de Cordoba S., Dahlback B.
      J. Biol. Chem. 268:15017-15023(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning of cDNA coding for the beta chain of human complement component C4b-binding protein: sequence homology with the alpha chain."
      Hillarp A., Dahlback B.
      Proc. Natl. Acad. Sci. U.S.A. 87:1183-1187(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. SeattleSNPs variation discovery resource
      Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLN-102.
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 2).
      Tissue: Skeletal muscle.
    7. "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-64; ASN-71 AND ASN-98.
      Tissue: Plasma.
    8. "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-64 AND ASN-98.
      Tissue: Plasma.
    9. "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-98.
      Tissue: Liver.

    Entry informationi

    Entry nameiC4BPB_HUMAN
    AccessioniPrimary (citable) accession number: P20851
    Secondary accession number(s): A5JYP8
    , D3DT81, Q5VVR0, Q9BS25
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 1, 1991
    Last modified: October 1, 2014
    This is version 132 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

    Keywords - Technical termi

    Complete proteome, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3