Protein detail

ITB4

Integrin beta-4 (GP150) (CD antigen CD104)

Entry name
ITB4
UniProt ID
EVMP confidence score
0.50
Supporting publications (n)
4
Transmembrane count
1
Protein classification
Cancer-related genesCD markersDisease related genesHuman disease related genesPlasma proteinsPredicted intracellular proteinsPredicted membrane proteins
EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information13
Protein Names
Integrin beta-4 (GP150) (CD antigen CD104)
Protein Class (7)
Cancer-related genesCD markersDisease related genesHuman disease related genesPlasma proteinsPredicted intracellular proteinsPredicted membrane proteins
Protein Function (5)
  • Predicted intracellular proteins
  • CD markers
  • Cancer-related genes:Candidate cancer biomarkers
  • Human disease related genes:Congenital malformations:Congenital malformations of skin
  • Disease related genes
Transmembrane
711..733; Helical
Transmembrane Count
1
Entrez Gene Symbol
Gene Synonym
CD104
Gene Description
Integrin subunit beta 4
Chromosome
17
Position
75721328-75757818
Supporting publications (n)
4
EVMP confidence score
0.50
Fluorescence & Localization6
Tissue SpecificovaryBrain Regional Specificchoroid plexusCell SpecificAdipocytesSingle-Nuclei Brain Specificchoroid plexus epithelial cellSecretome LocationSecreted to extracellular matrixSecretome FunctionCell adhesion
Function & Pathway7
Protein Function (5)
  • Predicted intracellular proteins
  • CD markers
  • Cancer-related genes:Candidate cancer biomarkers
  • Human disease related genes:Congenital malformations:Congenital malformations of skin
  • Disease related genes
Mediation Categories (2)
Adhesion and uptake mediationReceptor-signaling mediation
Relations & Evidence88

Enzyme-Mediated Modification (13)

13 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
ITGB4FGFR1P11362Y1,564phosphorylationSparser_ProtMapperPhosphoSitePhosphoSite_ProtMapperProtMapperProtMapper:26918348
ITGB4EGFP01133Y1,469phosphorylationBEL-Large-Corpus_ProtMapperProtMapperProtMapper:17081983
ITGB4ANXA7P20073Y1,564phosphorylationRLIMS-P_ProtMapperREACH_ProtMapperSparser_ProtMapperProtMapperProtMapper:26918348
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Ligand-Receptor Signaling (59)

59 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
plasma_membraneplasma_membraneUniProt_locationNoNoNoYesNo
plasma_membraneplasma_membraneCellinkerNoNoNoYesNo
plasma_membraneplasma_membraneOmniPathNoNoNoYesNo
plasma_membrane_transmembraneplasma_membrane_transmembraneMembranomeNoNoNoYesNo
plasma_membrane_transmembraneplasma_membrane_transmembraneCSPANoNoNoYesNo
plasma_membrane_transmembraneplasma_membrane_transmembraneHPMRNoNoNoYesNo
plasma_membrane_transmembraneplasma_membrane_transmembraneOmniPathNoNoNoYesNo
cell_surfacecell_surfaceSurfaceomeNoNoNoYesNo
cell_surfacecell_surfaceconnectomeDB2020NoNoNoYesNo
cell_surfacecell_surfaceOmniPathNoNoNoYesNo
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Regulatory Interaction Network (13)

13 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
ITB4P16144PK3CAP42336YesYesNoWangCancerCellMapNetPathSIGNORCancerCellMap:11733063SIGNOR:9428518NetPath:11733063CancerCellMap:8143784CancerCellMap:7721947CancerCellMap:12867433
DOK1Q99704ITB4P16144YesNoYesSIGNORSIGNOR:19118207
ITBP1O14713ITB4P16144YesNoYesSIGNORSIGNOR:19118207
ITB4P16144PK3CDO00329YesYesNoWangNetPathCui2007SIGNORSIGNOR:9428518NetPath:11733063
ITB4P16144COMPLEX:P27986_P42336YesYesNoSIGNORSIGNOR:9428518
KAPCAP17612ITB4P16144YesYesYesWangphosphoELM_MIMPPhosphoSite_MIMPMIMPiPTMnetSIGNORProtMapperSIGNOR_ProtMapperPhosphoSite_ProtMapperSIGNOR:17615294ProtMapper:17615294
ITB4P16144PMP22Q01453YesYesNoSIGNORSIGNOR:16436605
KPCAP17252ITB4P16144YesYesYesSIGNORProtMapperPhosphoSite_KEAphosphoELM_KEAHPRDCancerCellMapWangPhosphoSite_ProtMapperphosphoELM_MIMPPhosphoSite_MIMPMIMPPhosphoSite_norefPhosphoPointiPTMnetKEAphosphoELMSIGNOR_ProtMapperPhosphoSiteAdhesomePhosphoSite:20870721PhosphoSite:22824799HPRD:12919677PhosphoSite:17615294HPRD:15121854KEA:15121854CancerCellMap:15121854phosphoELM:15121854Adhesome:15121854Adhesome:10592173SIGNOR:15121854HPRD:10477766ProtMapper:15121854Adhesome:10477766Adhesome:12919677PhosphoSite:19005215PhosphoSite:15121854CancerCellMap:12919677CancerCellMap:10477766
TLN1Q9Y490ITB4P16144YesYesNoWangSIGNORSIGNOR:19118207
ITB4P16144PK3CGP48736YesYesNoCancerCellMapNetPathSIGNORCancerCellMap:11733063SIGNOR:9428518NetPath:11733063CancerCellMap:8143784CancerCellMap:7721947CancerCellMap:12867433
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Protein Complex Composition (2)

2 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
ITGB4P161442PDBPDB:3fsoPDB:4wtwPDB:1qg3PDB:3fq4PDB:3f7qPDB:3h6a
ITGB4PLECP16144Q151493:2PDBPDB:4q58PDB:3f7p

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Protein Organic Solvent PrecipitationMass spectrometry132384937
Sequence, Structure & Domains15

Sequences

Length
1,822
Mass
202,167
Sequence
MAGPRPSPWARLLLAALISVSLSGTLANRCKKAPVKSCTECVRVDKDCAYCTDEMFRDRRCNTQAELLAAGCQRESIVVMESSFQITEETQIDTTLRRSQMSPQGLRVRLRPGEERHFELEVFEPLESPVDLYILMDFSNSMSDDLDNLKKMGQNLARVLSQLTSDYTIGFGKFVDKVSVPQTDMRPEKLKEPWPNSDPPFSFKNVISLTEDVDEFRNKLQGERISGNLDAPEGGFDAILQTAVCTRDIGWRPDSTHLLVFSTESAFHYEADGANVLAGIMSRNDERCHLDTTGTYTQYRTQDYPSVPTLVRLLAKHNIIPIFAVTNYSYSYYEKLHTYFPVSSLGVLQEDSSNIVELLEEAFNRIRSNLDIRALDSPRGLRTEVTSKMFQKTRTGSFHIRRGEVGIYQVQLRALEHVDGTHVCQLPEDQKGNIHLKPSFSDGLKMDAGIICDVCTCELQKEVRSARCSFNGDFVCGQCVCSEGWSGQTCNCSTGSLSDIQPCLREGEDKPCSGRGECQCGHCVCYGEGRYEGQFCEYDNFQCPRTSGFLCNDRGRCSMGQCVCEPGWTGPSCDCPLSNATCIDSNGGICNGRGHCECGRCHCHQQSLYTDTICEINYSAIHPGLCEDLRSCVQCQAWGTGEKKGRTCEECNFKVKMVDELKRAEEVVVRCSFRDEDDDCTYSYTMEGDGAPGPNSTVLVHKKKDCPPGSFWWLIPLLLLLLPLLALLLLLCWKYCACCKACLALLPCCNRGHMVGFKEDHYMLRENLMASDHLDTPMLRSGNLKGRDVVRWKVTNNMQRPGFATHAASINPTELVPYGLSLRLARLCTENLLKPDTRECAQLRQEVEENLNEVYRQISGVHKLQQTKFRQQPNAGKKQDHTIVDTVLMAPRSAKPALLKLTEKQVEQRAFHDLKVAPGYYTLTADQDARGMVEFQEGVELVDVRVPLFIRPEDDDEKQLLVEAIDVPAGTATLGRRLVNITIIKEQARDVVSFEQPEFSVSRGDQVARIPVIRRVLDGGKSQVSYRTQDGTAQGNRDYIPVEGELLFQPGEAWKELQVKLLELQEVDSLLRGRQVRRFHVQLSNPKFGAHLGQPHSTTIIIRDPDELDRSFTSQMLSSQPPPHGDLGAPQNPNAKAAGSRKIHFNWLPPSGKPMGYRVKYWIQGDSESEAHLLDSKVPSVELTNLYPYCDYEMKVCAYGAQGEGPYSSLVSCRTHQEVPSEPGRLAFNVVSSTVTQLSWAEPAETNGEITAYEVCYGLVNDDNRPIGPMKKVLVDNPKNRMLLIENLRESQPYRYTVKARNGAGWGPEREAIINLATQPKRPMSIPIIPDIPIVDAQSGEDYDSFLMYSDDVLRSPSGSQRPSVSDDTGCGWKFEPLLGEELDLRRVTWRLPPELIPRLSASSGRSSDAEAPHGPPDDGGAGGKGGSLPRSATPGPPGEHLVNGRMDFAFPGSTNSLHRMTTTSAAAYGTHLSPHVPHRVLSTSSTLTRDYNSLTRSEHSHSTTLPRDYSTLTSVSSHDSRLTAGVPDTPTRLVFSALGPTSLRVSWQEPRCERPLQGYSVEYQLLNGGELHRLNIPNPAQTSVVVEDLLPNHSYVFRVRAQSQEGWGREREGVITIESQVHPQSPLCPLPGSAFTLSTPSAPGPLVFTALSPDSLQLSWERPRRPNGDIVGYLVTCEMAQGGGPATAFRVDGDSPESRLTVPGLSENVPYKFKVQARTTEGFGPEREGIITIESQDGGPFPQLGSRAGLFQHPLQSEYSSITTTHTSATEPFLVDGLTLGAQHLEAGGSLTRHVTQEFVSRTLTTSGTLSTHMDQQFFQT
Alternative Products
Event=Alternative splicing; Named isoforms=5; Name=Beta-4C; IsoId=P16144-1; Sequence=Displayed; Name=Beta-4A; IsoId=P16144-2; Sequence=VSP_002749; Name=Beta-4B; IsoId=P16144-3; Sequence=VSP_002749, VSP_002750; Name=Beta-4D; IsoId=P16144-4; Sequence=VSP_002749, VSP_002751; Name=Beta-4E; IsoId=P16144-5; Sequence=VSP_002747, VSP_002748
Alternative Sequence
851..964; LNEVYRQISGVHKLQQTKFRQQPNAGKKQDHTIVDTVLMAPRSAKPALLKLTEKQVEQRAFHDLKVAPGYYTLTADQDARGMVEFQEGVELVDVRVPLFIRPEDDDEKQLLVEA -> VRTQELGLAGDVAERGLQADLRCTQAPADQVPAAAQCREKARPHHCGHSADGAPLGQAGPAEAYREAGGTEGLPRPQGGPRLLHPHCRPGRPGHGGVPGGRGAGGRTGAPLYPA (in isoform Beta-4E); 965..1822; Missing (in isoform Beta-4E); 1370..1439; Missing (in isoform Beta-4A, isoform Beta-4B and isoform Beta-4D); 1519; H -> HGLPPIWEHGRSRLPLSWALGSRSRAQMKGFPPSRGPRDSIILAGRPAAPSWGP (in isoform Beta-4B); 1678..1685; CEMAQGGG -> W (in isoform Beta-4D)

3D Structural Models

Turn
1035..1037; 1070..1073; 1567..1569; 1632..1635
Helix
1003..1005; 1168..1170; 1316..1318
Beta Strand
990..995; 997..1002; 1006..1016; 1022..1033; 1043..1048; 1054..1061; 1076..1087; 1096..1103; 1131..1137; 1139..1141; 1143..1148; 1156..1163; 1172..1183; 1191..1200; 1203..1207; 1211..1214; 1227..1230; 1232..1234; 1236..1239; 1252..1260; 1262..1264; 1266..1268; 1271..1275; 1282..1286; 1294..1302; 1310..1314; 1334..1336; 1344..1348; 1522..1524; 1532..1540; 1543..1549; 1558..1566; 1573..1577; 1584..1587; 1595..1604; 1612..1620; 1636..1639; 1648..1653; 1656..1662; 1671..1680; 1683..1685; 1688..1694; 1697..1703; 1712..1722; 1724..1732
3D Structure
NMR spectroscopy (1); X-ray crystallography (12)

Domain & Motif Annotations

Compositional Bias
1418..1427; Gly residues; 1503..1518; Polar residues
Domain (CC)
The VWFA domain (or beta I domain) contains three cation-binding sites: the ligand-associated metal ion-binding site (LIMBS or SyMBS), the metal ion-dependent adhesion site (MIDAS), and the adjacent MIDAS site (ADMIDAS). This domain is also part of the ligand-binding site.; DOMAIN: The fibronectin type-III-like domains bind BPAG1 and plectin and probably also recruit BP230.
Domain (FT)
29..73; PSI; 131..329; VWFA; 457..491; I-EGF 1; 492..537; I-EGF 2; 538..574; I-EGF 3; 575..615; I-EGF 4; 979..1084; Calx-beta; 1129..1218; Fibronectin type-III 1; 1222..1321; Fibronectin type-III 2; 1530..1625; Fibronectin type-III 3; 1643..1739; Fibronectin type-III 4
Region
194..199; Involved in NRG1- and IGF1-binding; 732..749; Palmitoylated on several cysteines; 1113..1140; Disordered; 1400..1444; Disordered; 1451..1752; Interaction with ARHGEF40; 1495..1525; Disordered
Protein Families
Integrin beta chain family
Sequence Similarities
Belongs to the integrin beta chain family.
Clinical Relevance2
Disease Involvement (3)
Cancer-related genesDisease variantEpidermolysis bullosa
Supporting Publications4
PMIDTitleAbstract
24505114Proteomics analysis of cancer exosomes using a novel modified aptamer-based array (SOMAscan™) platform.These included proteins of known association with cancer exosomes such as MFG-E8, integrins, and MET, and also those less widely reported as exosomally associated, such as ROR1 and ITIH4.
31588238Dual-platform affinity proteomics identifies links between the recurrence of ovarian carcinoma and proteins released into the tumor microenvironment.No abstract available
37922300Proteomic profiling of urinary extracellular vesicles differentiates breast cancer patients from healthy women.No abstract available
38731868The Deep Proteomics Approach Identified Extracellular Vesicular Proteins Correlated to Extracellular Matrix in Type One and Two Endometrial Cancer.No abstract available