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Q9UMF0

- ICAM5_HUMAN

UniProt

Q9UMF0 - ICAM5_HUMAN

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Protein
Intercellular adhesion molecule 5
Gene
ICAM5, TLCN, TLN
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini32 – 835804Extracellular Reviewed prediction
Add
BLAST
Transmembranei836 – 85621Helical; Reviewed prediction
Add
BLAST
Topological domaini857 – 92468Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of plasma membrane Source: ProtInc
  2. plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29596.

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

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

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.

Miscellaneous databases

EvolutionaryTraceiQ9UMF0.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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

« Hide

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti614 – 6141A → T in AAC50959. 1 Publication
Sequence conflicti786 – 7861G → R in AAC97931. 1 Publication
Sequence conflicti816 – 8161A → R in AAC50959. 1 Publication
Sequence conflicti816 – 8161A → R in AAC97931. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 127 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

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