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Q99467

- CD180_HUMAN

UniProt

Q99467 - CD180_HUMAN

Protein

CD180 antigen

Gene

CD180

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (18 May 2010)
      Previous versions | rss
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    Functioni

    May cooperate with MD-1 and TLR4 to mediate the innate immune response to bacterial lipopolysaccharide (LPS) in B-cells. Leads to NF-kappa-B activation. Also involved in the life/death decision of B-cells By similarity.By similarity

    GO - Biological processi

    1. B cell proliferation involved in immune response Source: Ensembl
    2. cellular response to lipopolysaccharide Source: Ensembl
    3. inflammatory response Source: UniProtKB-KW
    4. innate immune response Source: UniProtKB-KW
    5. positive regulation of lipopolysaccharide-mediated signaling pathway Source: MGI

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Immunity, Inflammatory response, Innate immunity

    Enzyme and pathway databases

    ReactomeiREACT_6894. Toll Like Receptor 4 (TLR4) Cascade.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CD180 antigen
    Alternative name(s):
    Lymphocyte antigen 64
    Radioprotective 105 kDa protein
    CD_antigen: CD180
    Gene namesi
    Name:CD180
    Synonyms:LY64, RP105
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:6726. CD180.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30490.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 23231 PublicationAdd
    BLAST
    Chaini24 – 661638CD180 antigenPRO_0000034741Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi34 – 341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi53 – 531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi70 – 701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi78 – 781N-linked (GlcNAc...)1 Publication
    Glycosylationi201 – 2011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi234 – 2341N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi244 – 2441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi394 – 3941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi402 – 4021N-linked (GlcNAc...)1 Publication
    Glycosylationi451 – 4511N-linked (GlcNAc...)1 Publication
    Glycosylationi573 – 5731N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ99467.
    PaxDbiQ99467.
    PRIDEiQ99467.

    PTM databases

    PhosphoSiteiQ99467.

    Expressioni

    Tissue specificityi

    Expressed mainly on mature peripherical B cells. Detected in spleen, lymph node and appendix. Not detected in pre-B and -T cells.

    Gene expression databases

    BgeeiQ99467.
    CleanExiHS_CD180.
    GenevestigatoriQ99467.

    Organism-specific databases

    HPAiHPA003740.

    Interactioni

    Subunit structurei

    M-shaped tetramer of two CD180-LY86 heterodimers.1 Publication

    Protein-protein interaction databases

    BioGridi110242. 2 interactions.
    DIPiDIP-59104N.
    STRINGi9606.ENSP00000256447.

    Structurei

    Secondary structure

    1
    661
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi29 – 324
    Turni33 – 353
    Beta strandi36 – 383
    Beta strandi57 – 593
    Beta strandi66 – 683
    Turni70 – 756
    Beta strandi80 – 834
    Turni94 – 996
    Beta strandi105 – 1073
    Turni118 – 1214
    Beta strandi129 – 1313
    Helixi140 – 1423
    Beta strandi153 – 1553
    Beta strandi177 – 1793
    Helixi190 – 1945
    Turni195 – 1984
    Beta strandi200 – 2056
    Turni216 – 2216
    Beta strandi223 – 2286
    Helixi235 – 2417
    Turni242 – 2443
    Beta strandi246 – 2516
    Turni265 – 2684
    Helixi269 – 2735
    Beta strandi274 – 2807
    Beta strandi286 – 2883
    Turni291 – 2944
    Helixi296 – 2994
    Beta strandi301 – 3044
    Beta strandi325 – 3273
    Helixi336 – 3394
    Helixi341 – 3433
    Beta strandi349 – 3513
    Turni365 – 3684
    Beta strandi374 – 3763
    Beta strandi384 – 3885
    Turni389 – 3913
    Beta strandi400 – 4023
    Beta strandi409 – 4113
    Turni413 – 4186
    Beta strandi424 – 4263
    Turni440 – 4434
    Beta strandi449 – 4513
    Turni462 – 4676
    Beta strandi473 – 4753
    Helixi482 – 4843
    Helixi491 – 4944
    Beta strandi500 – 5023
    Turni513 – 5186
    Beta strandi524 – 5263
    Helixi534 – 5407
    Beta strandi547 – 5493
    Helixi563 – 5675
    Beta strandi569 – 5735
    Helixi583 – 5853
    Helixi586 – 5949
    Beta strandi598 – 6003
    Beta strandi607 – 6137
    Turni618 – 6203

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3B2DX-ray2.80A/B24-626[»]
    ProteinModelPortaliQ99467.
    SMRiQ99467. Positions 26-626.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 626603ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini651 – 66111CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei627 – 65024HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 5321LRRNTAdd
    BLAST
    Repeati54 – 7522LRR 1Add
    BLAST
    Repeati78 – 9922LRR 2Add
    BLAST
    Repeati102 – 12322LRR 3Add
    BLAST
    Repeati126 – 14722LRR 4Add
    BLAST
    Repeati150 – 17122LRR 5Add
    BLAST
    Repeati174 – 19522LRR 6Add
    BLAST
    Repeati201 – 22121LRR 7Add
    BLAST
    Repeati275 – 29622LRR 8Add
    BLAST
    Repeati299 – 32022LRR 9Add
    BLAST
    Repeati322 – 34322LRR 10Add
    BLAST
    Repeati346 – 36621LRR 11Add
    BLAST
    Repeati371 – 39121LRR 12Add
    BLAST
    Repeati397 – 41822LRR 13Add
    BLAST
    Repeati421 – 44222LRR 14Add
    BLAST
    Repeati446 – 46621LRR 15Add
    BLAST
    Repeati470 – 49324LRR 16Add
    BLAST
    Repeati497 – 51822LRR 17Add
    BLAST
    Repeati521 – 54424LRR 18Add
    BLAST
    Repeati546 – 56419LRR 19Add
    BLAST
    Domaini577 – 62751LRRCTAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Toll-like receptor family.Curated
    Contains 19 LRR (leucine-rich) repeats.Curated
    Contains 1 LRRCT domain.Curated
    Contains 1 LRRNT domain.Curated

    Keywords - Domaini

    Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG319009.
    HOGENOMiHOG000146395.
    HOVERGENiHBG050848.
    InParanoidiQ99467.
    KOiK06555.
    OMAiKGLCEMS.
    OrthoDBiEOG7ZKS9G.
    PhylomeDBiQ99467.
    TreeFamiTF351113.

    Family and domain databases

    InterProiIPR000483. Cys-rich_flank_reg_C.
    IPR001611. Leu-rich_rpt.
    [Graphical view]
    PfamiPF13855. LRR_8. 4 hits.
    [Graphical view]
    SMARTiSM00082. LRRCT. 1 hit.
    [Graphical view]
    PROSITEiPS51450. LRR. 12 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q99467-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAFDVSCFFW VVLFSAGCKV ITSWDQMCIE KEANKTYNCE NLGLSEIPDT    50
    LPNTTEFLEF SFNFLPTIHN RTFSRLMNLT FLDLTRCQIN WIHEDTFQSH 100
    HQLSTLVLTG NPLIFMAETS LNGPKSLKHL FLIQTGISNL EFIPVHNLEN 150
    LESLYLGSNH ISSIKFPKDF PARNLKVLDF QNNAIHYISR EDMRSLEQAI 200
    NLSLNFNGNN VKGIELGAFD STIFQSLNFG GTPNLSVIFN GLQNSTTQSL 250
    WLGTFEDIDD EDISSAMLKG LCEMSVESLN LQEHRFSDIS STTFQCFTQL 300
    QELDLTATHL KGLPSGMKGL NLLKKLVLSV NHFDQLCQIS AANFPSLTHL 350
    YIRGNVKKLH LGVGCLEKLG NLQTLDLSHN DIEASDCCSL QLKNLSHLQT 400
    LNLSHNEPLG LQSQAFKECP QLELLDLAFT RLHINAPQSP FQNLHFLQVL 450
    NLTYCFLDTS NQHLLAGLPV LRHLNLKGNH FQDGTITKTN LLQTVGSLEV 500
    LILSSCGLLS IDQQAFHSLG KMSHVDLSHN SLTCDSIDSL SHLKGIYLNL 550
    AANSINIISP RLLPILSQQS TINLSHNPLD CTCSNIHFLT WYKENLHKLE 600
    GSEETTCANP PSLRGVKLSD VKLSCGITAI GIFFLIVFLL LLAILLFFAV 650
    KYLLRWKYQH I 661
    Length:661
    Mass (Da):74,179
    Last modified:May 18, 2010 - v2
    Checksum:i93DE3178594B3383
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti223 – 2231I → V in BAA12019. (PubMed:8975706)Curated
    Sequence conflicti223 – 2231I → V in BAG35994. (PubMed:14702039)Curated
    Sequence conflicti223 – 2231I → V in EAW51318. 1 PublicationCurated
    Sequence conflicti223 – 2231I → V in AAI09070. (PubMed:15489334)Curated
    Sequence conflicti223 – 2231I → V in AAI09071. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti20 – 201V → L.
    Corresponds to variant rs5744463 [ dbSNP | Ensembl ].
    VAR_057298
    Natural varianti53 – 531N → K.
    Corresponds to variant rs16875312 [ dbSNP | Ensembl ].
    VAR_021978
    Natural varianti99 – 991S → R.
    Corresponds to variant rs2230520 [ dbSNP | Ensembl ].
    VAR_021979
    Natural varianti259 – 2591D → N.
    Corresponds to variant rs5744525 [ dbSNP | Ensembl ].
    VAR_057299
    Natural varianti356 – 3561V → M.
    Corresponds to variant rs56752081 [ dbSNP | Ensembl ].
    VAR_061859
    Natural varianti430 – 4301T → A.
    Corresponds to variant rs2230523 [ dbSNP | Ensembl ].
    VAR_057300
    Natural varianti648 – 6481F → L.
    Corresponds to variant rs2230524 [ dbSNP | Ensembl ].
    VAR_057301

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D83597 mRNA. Translation: BAA12019.1.
    AK313177 mRNA. Translation: BAG35994.1.
    AC026445 Genomic DNA. No translation available.
    CH471137 Genomic DNA. Translation: EAW51318.1.
    BC109069 mRNA. Translation: AAI09070.1.
    BC109070 mRNA. Translation: AAI09071.1.
    CCDSiCCDS3992.1.
    RefSeqiNP_005573.2. NM_005582.2.
    UniGeneiHs.87205.

    Genome annotation databases

    EnsembliENST00000256447; ENSP00000256447; ENSG00000134061.
    GeneIDi4064.
    KEGGihsa:4064.
    UCSCiuc003juy.2. human.

    Polymorphism databases

    DMDMi296434437.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D83597 mRNA. Translation: BAA12019.1 .
    AK313177 mRNA. Translation: BAG35994.1 .
    AC026445 Genomic DNA. No translation available.
    CH471137 Genomic DNA. Translation: EAW51318.1 .
    BC109069 mRNA. Translation: AAI09070.1 .
    BC109070 mRNA. Translation: AAI09071.1 .
    CCDSi CCDS3992.1.
    RefSeqi NP_005573.2. NM_005582.2.
    UniGenei Hs.87205.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3B2D X-ray 2.80 A/B 24-626 [» ]
    ProteinModelPortali Q99467.
    SMRi Q99467. Positions 26-626.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110242. 2 interactions.
    DIPi DIP-59104N.
    STRINGi 9606.ENSP00000256447.

    PTM databases

    PhosphoSitei Q99467.

    Polymorphism databases

    DMDMi 296434437.

    Proteomic databases

    MaxQBi Q99467.
    PaxDbi Q99467.
    PRIDEi Q99467.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000256447 ; ENSP00000256447 ; ENSG00000134061 .
    GeneIDi 4064.
    KEGGi hsa:4064.
    UCSCi uc003juy.2. human.

    Organism-specific databases

    CTDi 4064.
    GeneCardsi GC05M066514.
    H-InvDB HIX0032100.
    HGNCi HGNC:6726. CD180.
    HPAi HPA003740.
    MIMi 602226. gene.
    neXtProti NX_Q99467.
    PharmGKBi PA30490.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG319009.
    HOGENOMi HOG000146395.
    HOVERGENi HBG050848.
    InParanoidi Q99467.
    KOi K06555.
    OMAi KGLCEMS.
    OrthoDBi EOG7ZKS9G.
    PhylomeDBi Q99467.
    TreeFami TF351113.

    Enzyme and pathway databases

    Reactomei REACT_6894. Toll Like Receptor 4 (TLR4) Cascade.

    Miscellaneous databases

    ChiTaRSi CD180. human.
    GeneWikii CD180.
    GenomeRNAii 4064.
    NextBioi 15932.
    PROi Q99467.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q99467.
    CleanExi HS_CD180.
    Genevestigatori Q99467.

    Family and domain databases

    InterProi IPR000483. Cys-rich_flank_reg_C.
    IPR001611. Leu-rich_rpt.
    [Graphical view ]
    Pfami PF13855. LRR_8. 4 hits.
    [Graphical view ]
    SMARTi SM00082. LRRCT. 1 hit.
    [Graphical view ]
    PROSITEi PS51450. LRR. 12 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a human RP105 homologue and chromosomal localization of the mouse and human RP105 genes (Ly64 and LY64)."
      Miura Y., Miyake K., Yamashita Y., Shimazu R., Copeland N.G., Gilbert D.J., Jenkins N.A., Inazawa J., Abe T., Kimoto M.
      Genomics 38:299-304(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: B-cell lymphoma.
    2. "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.
    3. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
    6. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 24-38.
    7. "RP105 is associated with MD-1 and transmits an activation signal in human B cells."
      Miura Y., Shimazu R., Miyake K., Akashi S., Ogata H., Yamashita Y., Narisawa Y., Kimoto M.
      Blood 92:2815-2822(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LY86.
    8. "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-78.
      Tissue: Liver.
    9. "Crystal structures of mouse and human RP105/MD-1 complexes reveal unique dimer organization of the toll-like receptor family."
      Ohto U., Miyake K., Shimizu T.
      J. Mol. Biol. 413:815-825(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 24-626 IN COMPLEX WITH LY86, SUBUNIT, GLYCOSYLATION AT ASN-402 AND ASN-451.

    Entry informationi

    Entry nameiCD180_HUMAN
    AccessioniPrimary (citable) accession number: Q99467
    Secondary accession number(s): B2R7Z7, Q32MM5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 125 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 cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 5
      Human chromosome 5: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3