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O00241

- SIRB1_HUMAN

UniProt

O00241 - SIRB1_HUMAN

Protein

Signal-regulatory protein beta-1

Gene

SIRPB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 5 (02 Nov 2010)
      Previous versions | rss
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    Functioni

    Immunoglobulin-like cell surface receptor involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. Participates also in the recruitment of tyrosine kinase SYK.

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: ProtInc
    2. innate immune response Source: Reactome
    3. signal transduction Source: ProtInc

    Enzyme and pathway databases

    ReactomeiREACT_147694. DAP12 interactions.
    REACT_23916. Signal regulatory protein (SIRP) family interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Signal-regulatory protein beta-1
    Short name:
    SIRP-beta-1
    Alternative name(s):
    CD172 antigen-like family member B
    CD_antigen: CD172b
    Gene namesi
    Name:SIRPB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:15928. SIRPB1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. integral component of plasma membrane Source: ProtInc
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38051.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2929Sequence AnalysisAdd
    BLAST
    Chaini30 – 398369Signal-regulatory protein beta-1PRO_0000014956Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi54 ↔ 1201 PublicationPROSITE-ProRule annotation
    Disulfide bondi169 ↔ 227PROSITE-ProRule annotation
    Glycosylationi244 – 2441N-linked (GlcNAc...)2 Publications
    Glycosylationi269 – 2691N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi291 – 2911N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi320 – 320Interchain1 PublicationPROSITE-ProRule annotation

    Post-translational modificationi

    N-glycosylated.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiO00241.
    PRIDEiO00241.

    PTM databases

    PhosphoSiteiO00241.

    Expressioni

    Tissue specificityi

    Detected in monocytes and dendritic cells.1 Publication

    Gene expression databases

    ArrayExpressiO00241.
    BgeeiO00241.
    CleanExiHS_SIRPB1.
    GenevestigatoriO00241.

    Organism-specific databases

    HPAiHPA047463.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Interacts with TYROBP. This interaction results in the recruitment of SYK.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TYROBPO439144EBI-2615458,EBI-2214794

    Protein-protein interaction databases

    BioGridi115609. 3 interactions.
    IntActiO00241. 3 interactions.
    STRINGi9606.ENSP00000279477.

    Structurei

    Secondary structure

    1
    398
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi40 – 456
    Beta strandi50 – 523
    Beta strandi55 – 573
    Beta strandi65 – 695
    Beta strandi76 – 849
    Beta strandi89 – 913
    Beta strandi95 – 995
    Beta strandi105 – 1073
    Helixi112 – 1143
    Beta strandi116 – 1249
    Beta strandi127 – 1293
    Beta strandi131 – 1355
    Beta strandi139 – 1446

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D9CNMR-A32-154[»]
    2JJUX-ray1.19A/B30-148[»]
    ProteinModelPortaliO00241.
    SMRiO00241. Positions 30-347.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00241.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini30 – 371342ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini393 – 3986CytoplasmicSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei372 – 39221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 136107Ig-like V-typeAdd
    BLAST
    Domaini147 – 246100Ig-like C1-type 1Add
    BLAST
    Domaini253 – 34795Ig-like C1-type 2Add
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG291387.
    HOVERGENiHBG056632.
    InParanoidiO00241.
    KOiK06551.
    OrthoDBiEOG7CG6ZQ.
    PhylomeDBiO00241.
    TreeFamiTF341862.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    InterProiIPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003597. Ig_C1-set.
    IPR003599. Ig_sub.
    IPR013106. Ig_V-set.
    [Graphical view]
    PfamiPF07654. C1-set. 2 hits.
    PF07686. V-set. 1 hit.
    [Graphical view]
    SMARTiSM00409. IG. 1 hit.
    SM00407. IGc1. 2 hits.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 3 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O00241-1) [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

    MPVPASWPHL PSPFLLMTLL LGRLTGVAGE DELQVIQPEK SVSVAAGESA    50
    TLRCAMTSLI PVGPIMWFRG AGAGRELIYN QKEGHFPRVT TVSELTKRNN 100
    LDFSISISNI TPADAGTYYC VKFRKGSPDD VEFKSGAGTE LSVRAKPSAP 150
    VVSGPAVRAT PEHTVSFTCE SHGFSPRDIT LKWFKNGNEL SDFQTNVDPA 200
    GDSVSYSIHS TARVVLTRGD VHSQVICEIA HITLQGDPLR GTANLSEAIR 250
    VPPTLEVTQQ PMRAENQANV TCQVSNFYPR GLQLTWLENG NVSRTETAST 300
    LIENKDGTYN WMSWLLVNTC AHRDDVVLTC QVEHDGQQAV SKSYALEISA 350
    HQKEHGSDIT HEAALAPTAP LLVALLLGPK LLLVVGVSAI YICWKQKA 398
    Length:398
    Mass (Da):43,211
    Last modified:November 2, 2010 - v5
    Checksum:iC9C5E759514E212E
    GO
    Isoform 2 (identifier: O00241-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         145-361: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:181
    Mass (Da):19,394
    Checksum:i9EF21141C1DF3CBC
    GO
    Isoform 3 (identifier: Q5TFQ8-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform can be found in the external entry Q5TFQ8.
    Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
    Length:398
    Mass (Da):43,359
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti102 – 1021D → N in CAA71404. (PubMed:9062191)Curated
    Sequence conflicti106 – 1061S → R in BAG36297. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti23 – 231R → G.
    Corresponds to variant rs1535882 [ dbSNP | Ensembl ].
    VAR_028789
    Natural varianti53 – 531R → H.
    Corresponds to variant rs2746603 [ dbSNP | Ensembl ].
    VAR_028790
    Natural varianti229 – 2291I → M.2 Publications
    Corresponds to variant rs2253427 [ dbSNP | Ensembl ].
    VAR_028791
    Natural varianti363 – 3631A → P.3 Publications
    Corresponds to variant rs2243603 [ dbSNP | Ensembl ].
    VAR_028792

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei145 – 361217Missing in isoform 2. 1 PublicationVSP_007026Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10376 mRNA. Translation: CAA71404.1.
    AK313517 mRNA. Translation: BAG36297.1.
    AL049634, AL138804 Genomic DNA. Translation: CAI21864.1.
    AL049634, AL138804 Genomic DNA. Translation: CAI21865.1.
    BC025286 mRNA. Translation: AAH25286.1.
    BC075835 mRNA. Translation: AAH75835.1.
    CCDSiCCDS13019.1. [O00241-1]
    CCDS42850.1. [O00241-2]
    RefSeqiNP_001077379.1. NM_001083910.2. [O00241-2]
    NP_006056.2. NM_006065.3. [O00241-1]
    UniGeneiHs.664861.

    Genome annotation databases

    EnsembliENST00000381603; ENSP00000371016; ENSG00000101307. [O00241-2]
    ENST00000381605; ENSP00000371018; ENSG00000101307. [O00241-1]
    GeneIDi10326.
    KEGGihsa:10326.
    UCSCiuc002wfk.4. human. [O00241-2]
    uc010gai.3. human. [O00241-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y10376 mRNA. Translation: CAA71404.1 .
    AK313517 mRNA. Translation: BAG36297.1 .
    AL049634 , AL138804 Genomic DNA. Translation: CAI21864.1 .
    AL049634 , AL138804 Genomic DNA. Translation: CAI21865.1 .
    BC025286 mRNA. Translation: AAH25286.1 .
    BC075835 mRNA. Translation: AAH75835.1 .
    CCDSi CCDS13019.1. [O00241-1 ]
    CCDS42850.1. [O00241-2 ]
    RefSeqi NP_001077379.1. NM_001083910.2. [O00241-2 ]
    NP_006056.2. NM_006065.3. [O00241-1 ]
    UniGenei Hs.664861.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D9C NMR - A 32-154 [» ]
    2JJU X-ray 1.19 A/B 30-148 [» ]
    ProteinModelPortali O00241.
    SMRi O00241. Positions 30-347.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115609. 3 interactions.
    IntActi O00241. 3 interactions.
    STRINGi 9606.ENSP00000279477.

    PTM databases

    PhosphoSitei O00241.

    Proteomic databases

    PaxDbi O00241.
    PRIDEi O00241.

    Protocols and materials databases

    DNASUi 10326.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000381603 ; ENSP00000371016 ; ENSG00000101307 . [O00241-2 ]
    ENST00000381605 ; ENSP00000371018 ; ENSG00000101307 . [O00241-1 ]
    GeneIDi 10326.
    KEGGi hsa:10326.
    UCSCi uc002wfk.4. human. [O00241-2 ]
    uc010gai.3. human. [O00241-1 ]

    Organism-specific databases

    CTDi 10326.
    GeneCardsi GC20M001544.
    HGNCi HGNC:15928. SIRPB1.
    HPAi HPA047463.
    MIMi 603889. gene.
    neXtProti NX_O00241.
    PharmGKBi PA38051.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG291387.
    HOVERGENi HBG056632.
    InParanoidi O00241.
    KOi K06551.
    OrthoDBi EOG7CG6ZQ.
    PhylomeDBi O00241.
    TreeFami TF341862.

    Enzyme and pathway databases

    Reactomei REACT_147694. DAP12 interactions.
    REACT_23916. Signal regulatory protein (SIRP) family interactions.

    Miscellaneous databases

    EvolutionaryTracei O00241.
    GeneWikii SIRPB1.
    GenomeRNAii 10326.
    NextBioi 39145.
    PROi O00241.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00241.
    Bgeei O00241.
    CleanExi HS_SIRPB1.
    Genevestigatori O00241.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    InterProi IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003597. Ig_C1-set.
    IPR003599. Ig_sub.
    IPR013106. Ig_V-set.
    [Graphical view ]
    Pfami PF07654. C1-set. 2 hits.
    PF07686. V-set. 1 hit.
    [Graphical view ]
    SMARTi SM00409. IG. 1 hit.
    SM00407. IGc1. 2 hits.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A family of proteins that inhibit signalling through tyrosine kinase receptors."
      Kharitonenkov A., Chen Z., Sures I., Wang H., Schilling J., Ullrich A.
      Nature 386:181-186(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS MET-229 AND PRO-363.
      Tissue: Placenta.
    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] (ISOFORM 1), VARIANTS MET-229 AND PRO-363.
      Tissue: Neutrophil.
    3. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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), VARIANT PRO-363.
      Tissue: Skin.
    5. Cited for: INTERACTION WITH TYROBP AND SYK.
    6. "Signal-regulatory protein beta 1 is a DAP12-associated activating receptor expressed in myeloid cells."
      Dietrich J., Cella M., Seiffert M., Buehring H.-J., Colonna M.
      J. Immunol. 164:9-12(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TYROBP, GLYCOSYLATION, TISSUE SPECIFICITY.
    7. "SIRPbeta1 is expressed as a disulfide-linked homodimer in leukocytes and positively regulates neutrophil transepithelial migration."
      Liu Y., Soto I., Tong Q., Chin A., Buhring H.J., Wu T., Zen K., Parkos C.A.
      J. Biol. Chem. 280:36132-36140(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, INTERCHAIN DISULFIDE BOND.
    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-244.
      Tissue: Plasma.
    9. "Paired receptor specificity explained by structures of signal regulatory proteins alone and complexed with CD47."
      Hatherley D., Graham S.C., Turner J., Harlos K., Stuart D.I., Barclay A.N.
      Mol. Cell 31:266-277(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.19 ANGSTROMS) OF 30-148, DISULFIDE BOND.
    10. "Solution structure of the first Ig-like domain of signal-regulatory protein beta-1 (SIRP-beta-1)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (DEC-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 33-155.

    Entry informationi

    Entry nameiSIRB1_HUMAN
    AccessioniPrimary (citable) accession number: O00241
    Secondary accession number(s): A6NLM2
    , B2R8V0, Q5TFQ9, Q5TFR0, Q8TB12, Q9H1U5, Q9Y4V0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 138 of the entry and version 5 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, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 20
      Human chromosome 20: 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