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P02745

- C1QA_HUMAN

UniProt

P02745 - C1QA_HUMAN

Protein

Complement C1q subcomponent subunit A

Gene

C1QA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 2 (01 Jul 1993)
      Previous versions | rss
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    Functioni

    C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca2+-dependent C1r2C1s2 proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes.

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. cell-cell signaling Source: ProtInc
    2. complement activation Source: Reactome
    3. complement activation, classical pathway Source: Reactome
    4. innate immune response Source: Reactome

    Keywords - Biological processi

    Complement pathway, Immunity, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_7956. Classical antibody-mediated complement activation.
    REACT_8024. Initial triggering of complement.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Complement C1q subcomponent subunit A
    Gene namesi
    Name:C1QA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1241. C1QA.

    Subcellular locationi

    GO - Cellular componenti

    1. collagen trimer Source: UniProtKB-KW
    2. complement component C1 complex Source: ProtInc
    3. extracellular region Source: Reactome
    4. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Complement component C1q deficiency (C1QD) [MIM:613652]: A disorder caused by impaired activation of the complement classical pathway. It generally leads to severe immune complex disease with features of systemic lupus erythematosus and glomerulonephritis.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi613652. phenotype.
    Orphaneti169147. Immunodeficiency due to an early component of complement deficiency.
    PharmGKBiPA25622.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 22221 PublicationAdd
    BLAST
    Chaini23 – 245223Complement C1q subcomponent subunit APRO_0000003517Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi26 – 26Interchain (with C-29 in B chain)
    Modified residuei33 – 3315-hydroxylysine; alternate1 Publication
    Glycosylationi33 – 331O-linked (Gal...); alternate
    Modified residuei39 – 3914-hydroxyproline1 Publication
    Modified residuei45 – 4514-hydroxyproline1 Publication
    Modified residuei48 – 4815-hydroxylysine; alternate1 Publication
    Glycosylationi48 – 481O-linked (Gal...); alternate
    Modified residuei54 – 5414-hydroxyproline1 Publication
    Modified residuei57 – 5714-hydroxyproline1 Publication
    Modified residuei67 – 6715-hydroxylysine; alternate1 Publication
    Glycosylationi67 – 671O-linked (Gal...); alternate
    Modified residuei73 – 7314-hydroxyproline1 Publication
    Modified residuei79 – 7914-hydroxyproline1 Publication
    Modified residuei85 – 8514-hydroxyproline1 Publication
    Modified residuei100 – 10015-hydroxylysine; alternate1 Publication
    Glycosylationi100 – 1001O-linked (Gal...); alternate
    Glycosylationi146 – 1461N-linked (GlcNAc...)2 Publications

    Post-translational modificationi

    O-linked glycans consist of Glc-Gal disaccharides bound to the oxygen atom of post-translationally added hydroxyl groups.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    PaxDbiP02745.
    PeptideAtlasiP02745.
    PRIDEiP02745.

    Expressioni

    Gene expression databases

    BgeeiP02745.
    CleanExiHS_C1QA.
    GenevestigatoriP02745.

    Organism-specific databases

    HPAiCAB009823.
    HPA002350.

    Interactioni

    Subunit structurei

    C1 is a calcium-dependent trimolecular complex of C1q, R and S in the molar ration of 1:2:2. C1q subcomponent is composed of nine subunits, six of which are disulfide-linked dimers of the A and B chains, and three of which are disulfide-linked dimers of the C chain.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    C1QBP027464EBI-1220209,EBI-2813376

    Protein-protein interaction databases

    BioGridi107173. 16 interactions.
    IntActiP02745. 15 interactions.
    MINTiMINT-1195525.
    STRINGi9606.ENSP00000363773.

    Structurei

    Secondary structure

    1
    245
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi116 – 1205
    Beta strandi128 – 1314
    Beta strandi135 – 1406
    Turni146 – 1483
    Beta strandi150 – 1523
    Beta strandi157 – 16913
    Beta strandi171 – 1799
    Beta strandi182 – 1843
    Beta strandi188 – 1914
    Beta strandi195 – 1973
    Beta strandi199 – 20911
    Beta strandi214 – 22411
    Beta strandi229 – 2324
    Beta strandi235 – 2439

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1PK6X-ray1.85A112-244[»]
    2JG8X-ray2.05A/D112-245[»]
    2JG9X-ray1.90A/D112-245[»]
    2WNUX-ray2.30A/D112-245[»]
    2WNVX-ray1.25A/D112-245[»]
    ProteinModelPortaliP02745.
    SMRiP02745. Positions 112-244.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02745.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 10979Collagen-likeAdd
    BLAST
    Domaini110 – 245136C1qPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 C1q domain.PROSITE-ProRule annotation
    Contains 1 collagen-like domain.Curated

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG126311.
    HOGENOMiHOG000085653.
    HOVERGENiHBG108220.
    KOiK03986.
    OMAiYYYFTFQ.
    OrthoDBiEOG70ZZPW.
    PhylomeDBiP02745.
    TreeFamiTF329591.

    Family and domain databases

    Gene3Di2.60.120.40. 1 hit.
    InterProiIPR001073. C1q.
    IPR008160. Collagen.
    IPR008983. Tumour_necrosis_fac-like_dom.
    [Graphical view]
    PfamiPF00386. C1q. 1 hit.
    PF01391. Collagen. 1 hit.
    [Graphical view]
    PRINTSiPR00007. COMPLEMNTC1Q.
    SMARTiSM00110. C1Q. 1 hit.
    [Graphical view]
    SUPFAMiSSF49842. SSF49842. 1 hit.
    PROSITEiPS50871. C1Q. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P02745-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEGPRGWLVL CVLAISLASM VTEDLCRAPD GKKGEAGRPG RRGRPGLKGE    50
    QGEPGAPGIR TGIQGLKGDQ GEPGPSGNPG KVGYPGPSGP LGARGIPGIK 100
    GTKGSPGNIK DQPRPAFSAI RRNPPMGGNV VIFDTVITNQ EEPYQNHSGR 150
    FVCTVPGYYY FTFQVLSQWE ICLSIVSSSR GQVRRSLGFC DTTNKGLFQV 200
    VSGGMVLQLQ QGDQVWVEKD PKKGHIYQGS EADSVFSGFL IFPSA 245
    Length:245
    Mass (Da):26,017
    Last modified:July 1, 1993 - v2
    Checksum:i8FF6B6AE02D49C4C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti97 – 971P → K AA sequence (PubMed:486087)Curated
    Sequence conflicti103 – 1031K → P AA sequence (PubMed:486087)Curated
    Sequence conflicti172 – 1721C → N AA sequence (PubMed:6981411)Curated
    Sequence conflicti178 – 1781S → W AA sequence (PubMed:6981411)Curated
    Sequence conflicti240 – 2434LIFP → ILPGF AA sequence (PubMed:6981411)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti23 – 231E → K.1 Publication
    Corresponds to variant rs17887074 [ dbSNP | Ensembl ].
    VAR_021090

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF135157 mRNA. Translation: AAD32626.1.
    AY789471 Genomic DNA. Translation: AAV40828.1.
    AL158086 Genomic DNA. Translation: CAI22892.1.
    AK311980 mRNA. Translation: BAG34919.1.
    AL158086 Genomic DNA. Translation: CAI22893.1.
    CH471134 Genomic DNA. Translation: EAW95014.1.
    BC030153 mRNA. Translation: AAH30153.1.
    BC071986 mRNA. Translation: AAH71986.1.
    CCDSiCCDS226.1.
    PIRiS14350. C1HUQA.
    RefSeqiNP_057075.1. NM_015991.2.
    UniGeneiHs.632379.

    Genome annotation databases

    EnsembliENST00000374642; ENSP00000363773; ENSG00000173372.
    ENST00000402322; ENSP00000385564; ENSG00000173372.
    GeneIDi712.
    KEGGihsa:712.
    UCSCiuc001bfy.3. human.

    Polymorphism databases

    DMDMi399138.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    C1QAbase

    C1QA mutation db

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF135157 mRNA. Translation: AAD32626.1 .
    AY789471 Genomic DNA. Translation: AAV40828.1 .
    AL158086 Genomic DNA. Translation: CAI22892.1 .
    AK311980 mRNA. Translation: BAG34919.1 .
    AL158086 Genomic DNA. Translation: CAI22893.1 .
    CH471134 Genomic DNA. Translation: EAW95014.1 .
    BC030153 mRNA. Translation: AAH30153.1 .
    BC071986 mRNA. Translation: AAH71986.1 .
    CCDSi CCDS226.1.
    PIRi S14350. C1HUQA.
    RefSeqi NP_057075.1. NM_015991.2.
    UniGenei Hs.632379.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PK6 X-ray 1.85 A 112-244 [» ]
    2JG8 X-ray 2.05 A/D 112-245 [» ]
    2JG9 X-ray 1.90 A/D 112-245 [» ]
    2WNU X-ray 2.30 A/D 112-245 [» ]
    2WNV X-ray 1.25 A/D 112-245 [» ]
    ProteinModelPortali P02745.
    SMRi P02745. Positions 112-244.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107173. 16 interactions.
    IntActi P02745. 15 interactions.
    MINTi MINT-1195525.
    STRINGi 9606.ENSP00000363773.

    Chemistry

    DrugBanki DB00054. Abciximab.
    DB00051. Adalimumab.
    DB00092. Alefacept.
    DB00087. Alemtuzumab.
    DB00074. Basiliximab.
    DB00112. Bevacizumab.
    DB00002. Cetuximab.
    DB00111. Daclizumab.
    DB00095. Efalizumab.
    DB00005. Etanercept.
    DB00056. Gemtuzumab ozogamicin.
    DB00078. Ibritumomab.
    DB00075. Muromonab.
    DB00108. Natalizumab.
    DB00110. Palivizumab.
    DB00073. Rituximab.
    DB00081. Tositumomab.
    DB00072. Trastuzumab.

    Polymorphism databases

    DMDMi 399138.

    Proteomic databases

    PaxDbi P02745.
    PeptideAtlasi P02745.
    PRIDEi P02745.

    Protocols and materials databases

    DNASUi 712.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000374642 ; ENSP00000363773 ; ENSG00000173372 .
    ENST00000402322 ; ENSP00000385564 ; ENSG00000173372 .
    GeneIDi 712.
    KEGGi hsa:712.
    UCSCi uc001bfy.3. human.

    Organism-specific databases

    CTDi 712.
    GeneCardsi GC01P022962.
    HGNCi HGNC:1241. C1QA.
    HPAi CAB009823.
    HPA002350.
    MIMi 120550. gene.
    613652. phenotype.
    neXtProti NX_P02745.
    Orphaneti 169147. Immunodeficiency due to an early component of complement deficiency.
    PharmGKBi PA25622.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG126311.
    HOGENOMi HOG000085653.
    HOVERGENi HBG108220.
    KOi K03986.
    OMAi YYYFTFQ.
    OrthoDBi EOG70ZZPW.
    PhylomeDBi P02745.
    TreeFami TF329591.

    Enzyme and pathway databases

    Reactomei REACT_7956. Classical antibody-mediated complement activation.
    REACT_8024. Initial triggering of complement.

    Miscellaneous databases

    ChiTaRSi C1QA. human.
    EvolutionaryTracei P02745.
    GeneWikii C1QA.
    GenomeRNAii 712.
    NextBioi 2894.
    PROi P02745.
    SOURCEi Search...

    Gene expression databases

    Bgeei P02745.
    CleanExi HS_C1QA.
    Genevestigatori P02745.

    Family and domain databases

    Gene3Di 2.60.120.40. 1 hit.
    InterProi IPR001073. C1q.
    IPR008160. Collagen.
    IPR008983. Tumour_necrosis_fac-like_dom.
    [Graphical view ]
    Pfami PF00386. C1q. 1 hit.
    PF01391. Collagen. 1 hit.
    [Graphical view ]
    PRINTSi PR00007. COMPLEMNTC1Q.
    SMARTi SM00110. C1Q. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49842. SSF49842. 1 hit.
    PROSITEi PS50871. C1Q. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization and organization of the genes encoding the A-, B- and C-chains of human complement subcomponent C1q. The complete derived amino acid sequence of human C1q."
      Sellar G.C., Blake D.J., Reid K.B.M.
      Biochem. J. 274:481-490(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Monocyte.
    2. Wan T., Zhang W., Cao X.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. SeattleSNPs variation discovery resource
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-23.
    4. "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: Spleen.
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Spleen.
    8. "Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement."
      Reid K.B.M.
      Biochem. J. 179:367-371(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-130, HYDROXYLATION AT LYS-33; PRO-39; PRO-45; LYS-48; PRO-54; PRO-57; LYS-67; PRO-73; PRO-79; PRO-85 AND LYS-100.
    9. "Completion of the amino acid sequences of the A and B chains of subcomponent C1q of the first component of human complement."
      Reid K.B.M., Gagnon J., Frampton J.
      Biochem. J. 203:559-569(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 131-245.
    10. "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-146.
      Tissue: Plasma.
    11. "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-146.
      Tissue: Liver.
    12. "The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties."
      Gaboriaud C., Juanhuix J., Gruez A., Lacroix M., Darnault C., Pignol D., Verger D., Fontecilla-Camps J.-C., Arlaud G.J.
      J. Biol. Chem. 278:46974-46982(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 112-244.
    13. "Molecular basis of hereditary C1q deficiency."
      Petry F.
      Immunobiology 199:286-294(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON C1Q DEFICIENCY.

    Entry informationi

    Entry nameiC1QA_HUMAN
    AccessioniPrimary (citable) accession number: P02745
    Secondary accession number(s): B2R4X2, Q5T963
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 1, 1993
    Last modified: October 1, 2014
    This is version 161 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

    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

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