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Q9UMF0

- ICAM5_HUMAN

UniProt

Q9UMF0 - ICAM5_HUMAN

Protein

Intercellular adhesion molecule 5

Gene

ICAM5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2).

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. phagocytosis Source: Ensembl
    2. single organismal cell-cell adhesion Source: InterPro

    Keywords - Biological processi

    Cell adhesion

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Intercellular adhesion molecule 5
    Short name:
    ICAM-5
    Alternative name(s):
    Telencephalin
    Gene namesi
    Name:ICAM5
    Synonyms:TLCN, TLN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:5348. ICAM5.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of plasma membrane Source: ProtInc
    2. plasma membrane Source: ProtInc

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29596.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Chaini32 – 924893Intercellular adhesion molecule 5PRO_0000014799Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi54 – 541N-linked (GlcNAc...) (high mannose)1 Publication
    Disulfide bondi55 ↔ 991 PublicationPROSITE-ProRule annotation
    Disulfide bondi59 ↔ 1031 PublicationPROSITE-ProRule annotation
    Glycosylationi74 – 741N-linked (GlcNAc...)1 Publication
    Glycosylationi137 – 1371N-linked (GlcNAc...)1 Publication
    Disulfide bondi142 ↔ 1981 PublicationPROSITE-ProRule annotation
    Modified residuei182 – 1821Phosphothreonine1 Publication
    Modified residuei184 – 1841Phosphothreonine1 Publication
    Glycosylationi195 – 1951N-linked (GlcNAc...)1 Publication
    Glycosylationi214 – 2141N-linked (GlcNAc...)1 Publication
    Disulfide bondi249 ↔ 302PROSITE-ProRule annotation
    Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi344 ↔ 383PROSITE-ProRule annotation
    Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi397 – 3971N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi415 ↔ 470PROSITE-ProRule annotation
    Disulfide bondi498 ↔ 552PROSITE-ProRule annotation
    Disulfide bondi580 ↔ 645PROSITE-ProRule annotation
    Glycosylationi583 – 5831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi646 – 6461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi673 ↔ 725PROSITE-ProRule annotation
    Glycosylationi764 – 7641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi769 ↔ 814PROSITE-ProRule annotation
    Glycosylationi795 – 7951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi796 – 7961N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Glycosylation at Asn-54 is critical for functional folding.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UMF0.
    PaxDbiQ9UMF0.
    PRIDEiQ9UMF0.

    PTM databases

    PhosphoSiteiQ9UMF0.

    Expressioni

    Tissue specificityi

    Expressed on neurons in the most rostral segment of the mammalian brain, the telencephalon.

    Gene expression databases

    ArrayExpressiQ9UMF0.
    BgeeiQ9UMF0.
    CleanExiHS_ICAM5.
    GenevestigatoriQ9UMF0.

    Organism-specific databases

    HPAiCAB025178.
    HPA008943.
    HPA009083.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACTN1P050943EBI-6398041,EBI-5847257From a different organism.

    Protein-protein interaction databases

    BioGridi112942. 3 interactions.
    IntActiQ9UMF0. 1 interaction.
    STRINGi9606.ENSP00000221980.

    Structurei

    Secondary structure

    1
    924
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi36 – 4611
    Beta strandi49 – 579
    Beta strandi63 – 686
    Beta strandi70 – 7910
    Beta strandi82 – 909
    Beta strandi92 – 954
    Beta strandi98 – 1036
    Beta strandi106 – 1116
    Beta strandi113 – 1186
    Beta strandi130 – 1334
    Beta strandi136 – 1449
    Helixi150 – 1523
    Beta strandi153 – 1597
    Beta strandi162 – 1687
    Beta strandi179 – 1868
    Helixi189 – 1913
    Beta strandi195 – 2039
    Helixi205 – 2073
    Beta strandi211 – 2155

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BN3X-ray2.10B32-227[»]
    ProteinModelPortaliQ9UMF0.
    SMRiQ9UMF0. Positions 32-823.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UMF0.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini32 – 835804ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini857 – 92468CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei836 – 85621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini48 – 13083Ig-like C2-type 1Add
    BLAST
    Domaini135 – 235101Ig-like C2-type 2Add
    BLAST
    Domaini242 – 32988Ig-like C2-type 3Add
    BLAST
    Domaini337 – 40266Ig-like C2-type 4Add
    BLAST
    Domaini408 – 48679Ig-like C2-type 5Add
    BLAST
    Domaini491 – 56878Ig-like C2-type 6Add
    BLAST
    Domaini573 – 66290Ig-like C2-type 7Add
    BLAST
    Domaini666 – 73974Ig-like C2-type 8Add
    BLAST
    Domaini746 – 83085Ig-like C2-type 9Add
    BLAST

    Sequence similaritiesi

    Belongs to the immunoglobulin superfamily. ICAM family.Curated

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG146347.
    HOGENOMiHOG000168514.
    HOVERGENiHBG052077.
    InParanoidiQ9UMF0.
    KOiK06769.
    OMAiVCNATNR.
    OrthoDBiEOG7MD4PS.
    PhylomeDBiQ9UMF0.
    TreeFamiTF333745.

    Family and domain databases

    Gene3Di2.60.40.10. 12 hits.
    InterProiIPR003988. ICAM.
    IPR013768. ICAM_N.
    IPR003987. ICAM_VCAM_N.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    [Graphical view]
    PfamiPF03921. ICAM_N. 1 hit.
    [Graphical view]
    PRINTSiPR01473. ICAM.
    PR01472. ICAMVCAM1.
    SMARTiSM00409. IG. 4 hits.
    SM00408. IGc2. 1 hit.
    [Graphical view]
    PROSITEiPS50835. IG_LIKE. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9UMF0-1 [UniParc]FASTAAdd to Basket

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    MPGPSPGLRR ALLGLWAALG LGLFGLSAVS QEPFWADLQP RVAFVERGGS    50
    LWLNCSTNCP RPERGGLETS LRRNGTQRGL RWLARQLVDI REPETQPVCF 100
    FRCARRTLQA RGLIRTFQRP DRVELMPLPP WQPVGENFTL SCRVPGAGPR 150
    ASLTLTLLRG AQELIRRSFA GEPPRARGAV LTATVLARRE DHGANFSCRA 200
    ELDLRPHGLG LFENSSAPRE LRTFSLSPDA PRLAAPRLLE VGSERPVSCT 250
    LDGLFPASEA RVYLALGDQN LSPDVTLEGD AFVATATATA SAEQEGARQL 300
    VCNVTLGGEN RETRENVTIY SFPAPLLTLS EPSVSEGQMV TVTCAAGAQA 350
    LVTLEGVPAA VPGQPAQLQL NATENDDRRS FFCDATLDVD GETLIKNRSA 400
    ELRVLYAPRL DDSDCPRSWT WPEGPEQTLR CEARGNPEPS VHCARSDGGA 450
    VLALGLLGPV TRALSGTYRC KAANDQGEAV KDVTLTVEYA PALDSVGCPE 500
    RITWLEGTEA SLSCVAHGVP PPDVICVRSG ELGAVIEGLL RVAREHAGTY 550
    RCEATNPRGS AAKNVAVTVE YGPRFEEPSC PSNWTWVEGS GRLFSCEVDG 600
    KPQPSVKCVG SGGATEGVLL PLAPPDPSPR APRIPRVLAP GIYVCNATNR 650
    HGSVAKTVVV SAESPPEMDE STCPSHQTWL EGAEASALAC AARGRPSPGV 700
    RCSREGIPWP EQQRVSREDA GTYHCVATNA HGTDSRTVTV GVEYRPVVAE 750
    LAASPPGGVR PGGNFTLTCR AEAWPPAQIS WRAPPGALNI GLSSNNSTLS 800
    VAGAMGSHGG EYECAATNAH GRHARRITVR VAGPWLWVAV GGAAGGAALL 850
    AAGAGLAFYV QSTACKKGEY NVQEAESSGE AVCLNGAGGG AGGAAGAEGG 900
    PEAAGGAAES PAEGEVFAIQ LTSA 924
    Length:924
    Mass (Da):97,116
    Last modified:May 18, 2010 - v3
    Checksum:i97D0A9467BD16D30
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti614 – 6141A → T in AAC50959. (PubMed:8995416)Curated
    Sequence conflicti786 – 7861G → R in AAC97931. (PubMed:9828136)Curated
    Sequence conflicti816 – 8161A → R in AAC50959. (PubMed:8995416)Curated
    Sequence conflicti816 – 8161A → R in AAC97931. (PubMed:9828136)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti140 – 1401L → V in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035515
    Natural varianti188 – 1881R → W in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035516
    Natural varianti301 – 3011V → I.1 Publication
    Corresponds to variant rs1056538 [ dbSNP | Ensembl ].
    VAR_056046
    Natural varianti348 – 3481A → T.1 Publication
    Corresponds to variant rs2228615 [ dbSNP | Ensembl ].
    VAR_056047
    Natural varianti488 – 4881E → Q in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035517

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U72671 mRNA. Translation: AAC50959.1.
    AF082802 Genomic DNA. Translation: AAC97931.1.
    AC011511 Genomic DNA. No translation available.
    CCDSiCCDS12233.1.
    RefSeqiNP_003250.3. NM_003259.3.
    UniGeneiHs.465862.

    Genome annotation databases

    EnsembliENST00000221980; ENSP00000221980; ENSG00000105376.
    GeneIDi7087.
    KEGGihsa:7087.
    UCSCiuc002mnu.4. human.

    Polymorphism databases

    DMDMi296439327.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U72671 mRNA. Translation: AAC50959.1 .
    AF082802 Genomic DNA. Translation: AAC97931.1 .
    AC011511 Genomic DNA. No translation available.
    CCDSi CCDS12233.1.
    RefSeqi NP_003250.3. NM_003259.3.
    UniGenei Hs.465862.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BN3 X-ray 2.10 B 32-227 [» ]
    ProteinModelPortali Q9UMF0.
    SMRi Q9UMF0. Positions 32-823.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112942. 3 interactions.
    IntActi Q9UMF0. 1 interaction.
    STRINGi 9606.ENSP00000221980.

    PTM databases

    PhosphoSitei Q9UMF0.

    Polymorphism databases

    DMDMi 296439327.

    Proteomic databases

    MaxQBi Q9UMF0.
    PaxDbi Q9UMF0.
    PRIDEi Q9UMF0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000221980 ; ENSP00000221980 ; ENSG00000105376 .
    GeneIDi 7087.
    KEGGi hsa:7087.
    UCSCi uc002mnu.4. human.

    Organism-specific databases

    CTDi 7087.
    GeneCardsi GC19P010400.
    H-InvDB HIX0014740.
    HGNCi HGNC:5348. ICAM5.
    HPAi CAB025178.
    HPA008943.
    HPA009083.
    MIMi 601852. gene.
    neXtProti NX_Q9UMF0.
    PharmGKBi PA29596.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG146347.
    HOGENOMi HOG000168514.
    HOVERGENi HBG052077.
    InParanoidi Q9UMF0.
    KOi K06769.
    OMAi VCNATNR.
    OrthoDBi EOG7MD4PS.
    PhylomeDBi Q9UMF0.
    TreeFami TF333745.

    Miscellaneous databases

    EvolutionaryTracei Q9UMF0.
    GeneWikii ICAM5.
    GenomeRNAii 7087.
    NextBioi 27719.
    PROi Q9UMF0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UMF0.
    Bgeei Q9UMF0.
    CleanExi HS_ICAM5.
    Genevestigatori Q9UMF0.

    Family and domain databases

    Gene3Di 2.60.40.10. 12 hits.
    InterProi IPR003988. ICAM.
    IPR013768. ICAM_N.
    IPR003987. ICAM_VCAM_N.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR003598. Ig_sub2.
    [Graphical view ]
    Pfami PF03921. ICAM_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01473. ICAM.
    PR01472. ICAMVCAM1.
    SMARTi SM00409. IG. 4 hits.
    SM00408. IGc2. 1 hit.
    [Graphical view ]
    PROSITEi PS50835. IG_LIKE. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning and chromosomal localization of the human telencephalin and its distinctive interaction with lymphocyte function-associated antigen-1."
      Mizuno T., Yoshihara Y., Inazawa J., Kagamiyama H., Mori K.
      J. Biol. Chem. 272:1156-1163(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ILE-301 AND THR-348.
      Tissue: Brain.
    2. "Mapping of the ICAM-5 (telencephalin) gene, a neuronal member of the ICAM family, to a location between ICAM-1 and ICAM-3 on human chromosome 19p13.2."
      Kilgannon P., Turner T., Meyer J., Wisdom W., Gallatin W.M.
      Genomics 54:328-330(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-182 AND THR-184, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    5. "An unusual allosteric mobility of the C-terminal helix of a high-affinity alphaL integrin I domain variant bound to ICAM-5."
      Zhang H., Casasnovas J.M., Jin M., Liu J.H., Gahmberg C.G., Springer T.A., Wang J.H.
      Mol. Cell 31:432-437(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 32-227 IN COMPLEX WITH ITGAL, GLYCOSYLATION AT ASN-54; ASN-74; ASN-137; ASN-195 AND ASN-214, DISULFIDE BONDS.
    6. Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-140; TRP-188 AND GLN-488.

    Entry informationi

    Entry nameiICAM5_HUMAN
    AccessioniPrimary (citable) accession number: Q9UMF0
    Secondary accession number(s): Q9Y6F3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 128 of the entry and version 3 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 chromosome 19
      Human chromosome 19: 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