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Q9UMF0 (ICAM5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Intercellular adhesion molecule 5

Short name=ICAM-5
Alternative name(s):
Telencephalin
Gene names
Name:ICAM5
Synonyms:TLCN, TLN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length924 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subcellular location

Membrane; Single-pass type I membrane protein.

Tissue specificity

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

Post-translational modification

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

Sequence similarities

Belongs to the immunoglobulin superfamily. ICAM family.

Contains 9 Ig-like C2-type (immunoglobulin-like) domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ACTN1P050943EBI-6398041,EBI-5847257From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 924893Intercellular adhesion molecule 5
PRO_0000014799

Regions

Topological domain32 – 835804Extracellular Potential
Transmembrane836 – 85621Helical; Potential
Topological domain857 – 92468Cytoplasmic Potential
Domain48 – 13083Ig-like C2-type 1
Domain135 – 235101Ig-like C2-type 2
Domain242 – 32988Ig-like C2-type 3
Domain337 – 40266Ig-like C2-type 4
Domain408 – 48679Ig-like C2-type 5
Domain491 – 56878Ig-like C2-type 6
Domain573 – 66290Ig-like C2-type 7
Domain666 – 73974Ig-like C2-type 8
Domain746 – 83085Ig-like C2-type 9

Amino acid modifications

Modified residue1821Phosphothreonine Ref.4
Modified residue1841Phosphothreonine Ref.4
Glycosylation541N-linked (GlcNAc...) (high mannose) Probable
Glycosylation741N-linked (GlcNAc...) Ref.5
Glycosylation1371N-linked (GlcNAc...) Ref.5
Glycosylation1951N-linked (GlcNAc...) Ref.5
Glycosylation2141N-linked (GlcNAc...) Ref.5
Glycosylation3031N-linked (GlcNAc...) Potential
Glycosylation3161N-linked (GlcNAc...) Potential
Glycosylation3711N-linked (GlcNAc...) Potential
Glycosylation3971N-linked (GlcNAc...) Potential
Glycosylation5831N-linked (GlcNAc...) Potential
Glycosylation6461N-linked (GlcNAc...) Potential
Glycosylation7641N-linked (GlcNAc...) Potential
Glycosylation7951N-linked (GlcNAc...) Potential
Glycosylation7961N-linked (GlcNAc...) Potential
Disulfide bond55 ↔ 99 Ref.5
Disulfide bond59 ↔ 103 Ref.5
Disulfide bond142 ↔ 198 Ref.5
Disulfide bond249 ↔ 302 By similarity
Disulfide bond344 ↔ 383 By similarity
Disulfide bond415 ↔ 470 By similarity
Disulfide bond498 ↔ 552 By similarity
Disulfide bond580 ↔ 645 By similarity
Disulfide bond673 ↔ 725 By similarity
Disulfide bond769 ↔ 814 By similarity

Natural variations

Natural variant1401L → V in a breast cancer sample; somatic mutation. Ref.6
VAR_035515
Natural variant1881R → W in a breast cancer sample; somatic mutation. Ref.6
VAR_035516
Natural variant3011V → I. Ref.1
Corresponds to variant rs1056538 [ dbSNP | Ensembl ].
VAR_056046
Natural variant3481A → T. Ref.1
Corresponds to variant rs2228615 [ dbSNP | Ensembl ].
VAR_056047
Natural variant4881E → Q in a breast cancer sample; somatic mutation. Ref.6
VAR_035517

Experimental info

Sequence conflict6141A → T in AAC50959. Ref.1
Sequence conflict7861G → R in AAC97931. Ref.2
Sequence conflict8161A → R in AAC50959. Ref.1
Sequence conflict8161A → R in AAC97931. Ref.2

Secondary structure

...................................... 924
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UMF0 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: 97D0A9467BD16D30

FASTA92497,116
        10         20         30         40         50         60 
MPGPSPGLRR ALLGLWAALG LGLFGLSAVS QEPFWADLQP RVAFVERGGS LWLNCSTNCP 

        70         80         90        100        110        120 
RPERGGLETS LRRNGTQRGL RWLARQLVDI REPETQPVCF FRCARRTLQA RGLIRTFQRP 

       130        140        150        160        170        180 
DRVELMPLPP WQPVGENFTL SCRVPGAGPR ASLTLTLLRG AQELIRRSFA GEPPRARGAV 

       190        200        210        220        230        240 
LTATVLARRE DHGANFSCRA ELDLRPHGLG LFENSSAPRE LRTFSLSPDA PRLAAPRLLE 

       250        260        270        280        290        300 
VGSERPVSCT LDGLFPASEA RVYLALGDQN LSPDVTLEGD AFVATATATA SAEQEGARQL 

       310        320        330        340        350        360 
VCNVTLGGEN RETRENVTIY SFPAPLLTLS EPSVSEGQMV TVTCAAGAQA LVTLEGVPAA 

       370        380        390        400        410        420 
VPGQPAQLQL NATENDDRRS FFCDATLDVD GETLIKNRSA ELRVLYAPRL DDSDCPRSWT 

       430        440        450        460        470        480 
WPEGPEQTLR CEARGNPEPS VHCARSDGGA VLALGLLGPV TRALSGTYRC KAANDQGEAV 

       490        500        510        520        530        540 
KDVTLTVEYA PALDSVGCPE RITWLEGTEA SLSCVAHGVP PPDVICVRSG ELGAVIEGLL 

       550        560        570        580        590        600 
RVAREHAGTY RCEATNPRGS AAKNVAVTVE YGPRFEEPSC PSNWTWVEGS GRLFSCEVDG 

       610        620        630        640        650        660 
KPQPSVKCVG SGGATEGVLL PLAPPDPSPR APRIPRVLAP GIYVCNATNR HGSVAKTVVV 

       670        680        690        700        710        720 
SAESPPEMDE STCPSHQTWL EGAEASALAC AARGRPSPGV RCSREGIPWP EQQRVSREDA 

       730        740        750        760        770        780 
GTYHCVATNA HGTDSRTVTV GVEYRPVVAE LAASPPGGVR PGGNFTLTCR AEAWPPAQIS 

       790        800        810        820        830        840 
WRAPPGALNI GLSSNNSTLS VAGAMGSHGG EYECAATNAH GRHARRITVR VAGPWLWVAV 

       850        860        870        880        890        900 
GGAAGGAALL AAGAGLAFYV QSTACKKGEY NVQEAESSGE AVCLNGAGGG AGGAAGAEGG 

       910        920 
PEAAGGAAES PAEGEVFAIQ LTSA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-140; TRP-188 AND GLN-488.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U72671 mRNA. Translation: AAC50959.1.
AF082802 Genomic DNA. Translation: AAC97931.1.
AC011511 Genomic DNA. No translation available.
RefSeqNP_003250.3. NM_003259.3.
UniGeneHs.465862.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BN3X-ray2.10B32-227[»]
ProteinModelPortalQ9UMF0.
SMRQ9UMF0. Positions 32-821.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112942. 3 interactions.
IntActQ9UMF0. 1 interaction.
STRING9606.ENSP00000221980.

PTM databases

PhosphoSiteQ9UMF0.

Polymorphism databases

DMDM296439327.

Proteomic databases

PaxDbQ9UMF0.
PRIDEQ9UMF0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000221980; ENSP00000221980; ENSG00000105376.
GeneID7087.
KEGGhsa:7087.
UCSCuc002mnu.4. human.

Organism-specific databases

CTD7087.
GeneCardsGC19P010400.
H-InvDBHIX0014740.
HGNCHGNC:5348. ICAM5.
HPACAB025178.
HPA008943.
HPA009083.
MIM601852. gene.
neXtProtNX_Q9UMF0.
PharmGKBPA29596.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG146347.
HOGENOMHOG000168514.
HOVERGENHBG052077.
InParanoidQ9UMF0.
KOK06769.
OMAPSVSCVR.
OrthoDBEOG7MD4PS.
PhylomeDBQ9UMF0.
TreeFamTF333745.

Gene expression databases

ArrayExpressQ9UMF0.
BgeeQ9UMF0.
CleanExHS_ICAM5.
GenevestigatorQ9UMF0.

Family and domain databases

Gene3D2.60.40.10. 12 hits.
InterProIPR003988. ICAM.
IPR013768. ICAM_N.
IPR003987. ICAM_VCAM_N.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
[Graphical view]
PfamPF03921. ICAM_N. 1 hit.
[Graphical view]
PRINTSPR01473. ICAM.
PR01472. ICAMVCAM1.
SMARTSM00409. IG. 4 hits.
SM00408. IGc2. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9UMF0.
GeneWikiICAM5.
GenomeRNAi7087.
NextBio27719.
PROQ9UMF0.
SOURCESearch...

Entry information

Entry nameICAM5_HUMAN
AccessionPrimary (citable) accession number: Q9UMF0
Secondary accession number(s): Q9Y6F3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM