# Integrin beta 1

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Mammalian protein found in Homo sapiens

ITGB1 Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4WK4, 3G9W, 3T9K, 3VI3, 3VI4, 4DX9, 4WJK, 4WK0, 4WK2 Identifiers Aliases ITGB1, CD29, FNRB, GPIIA, MDF2, MSK12, VLA-BETA, VLAB, integrin subunit beta 1 External IDs OMIM: 135630; MGI: 96610; HomoloGene: 22999; GeneCards: ITGB1; OMA:ITGB1 - orthologs Gene location (Human) Chr. Chromosome 10 (human)[1] Band 10p11.22 Start 32,900,319 bp[1] End 33,005,792 bp[1] Gene location (Mouse) Chr. Chromosome 8 (mouse)[2] Band 8|8 E2 Start 129,412,135 bp[2] End 129,459,681 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in visceral pleura seminal vesicula tail of epididymis parietal pleura stromal cell of endometrium tibia smooth muscle tissue superficial temporal artery Descending thoracic aorta palpebral conjunctiva Top expressed in Ileal epithelium stroma of bone marrow lactiferous gland left lung lobe cardiac muscle tissue of left ventricle umbilical cord atrium uterus calvaria extraocular muscle More reference expression data BioGPS More reference expression data Gene ontology Molecular function virus receptor activity metal ion binding integrin binding protein binding laminin binding cell adhesion molecule binding collagen binding involved in cell-matrix adhesion coreceptor activity protease binding fibronectin binding actin binding C-X3-C chemokine binding protein heterodimerization activity protein-containing complex binding cadherin binding signaling receptor activity Cellular component cytoplasm endosome membrane melanosome ruffle integrin alpha8-beta1 complex synapse ruffle membrane integrin complex perinuclear region of cytoplasm cell projection dendritic spine cell surface cleavage furrow integrin alpha7-beta1 complex extracellular exosome lamellipodium integral component of membrane recycling endosome integrin alpha1-beta1 complex intercalated disc filopodium neuromuscular junction receptor complex plasma membrane integrin alpha11-beta1 complex myelin sheath abaxonal region synaptic membrane integrin alpha10-beta1 complex cell junction integrin alpha2-beta1 complex sarcolemma external side of plasma membrane cytoplasmic vesicle integrin alpha3-beta1 complex membrane raft focal adhesion glial cell projection Schaffer collateral - CA1 synapse glutamatergic synapse integral component of synaptic membrane protein-containing complex Biological process leukocyte cell-cell adhesion cell migration involved in sprouting angiogenesis stress fiber assembly viral entry into host cell B cell differentiation neuron projection development transforming growth factor beta receptor signaling pathway regulation of collagen catabolic process negative regulation of cell differentiation cardiac muscle cell differentiation cellular response to low-density lipoprotein particle stimulus in utero embryonic development cell-substrate adhesion positive regulation of GTPase activity regulation of immune response viral process dendrite morphogenesis cell fate specification G1 phase heterotypic cell-cell adhesion extracellular matrix organization cell-cell adhesion mediated by integrin cellular defense response cell adhesion formation of radial glial scaffolds axon extension leukocyte tethering or rolling integrin-mediated signaling pathway cell-matrix adhesion sarcomere organization negative regulation of anoikis leukocyte migration homophilic cell adhesion via plasma membrane adhesion molecules visual learning calcium-independent cell-matrix adhesion cardiac muscle tissue development negative regulation of Rho protein signal transduction receptor internalization regulation of cell cycle positive regulation of cell population proliferation positive regulation of apoptotic process mesodermal cell differentiation cell migration germ cell migration cell adhesion mediated by integrin basement membrane organization positive regulation of protein localization to plasma membrane G1/S transition of mitotic cell cycle phagocytosis cytokine-mediated signaling pathway cell projection organization lamellipodium assembly positive regulation of angiogenesis modulation of chemical synaptic transmission positive regulation of protein kinase B signaling positive regulation of signaling receptor activity positive regulation of cell migration Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 3688 16412 Ensembl ENSG00000150093 ENSMUSG00000025809 UniProt P05556 P09055 RefSeq (mRNA) NM_002211 NM_033666 NM_033667 NM_033668 NM_033669 NM_133376 NM_010578 RefSeq (protein) NP_002202 NP_391988 NP_596867 NP_034708 Location (UCSC) Chr 10: 32.9 – 33.01 Mb Chr 8: 129.41 – 129.46 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**Integrin beta-1** (**ITGB1**), also known as **CD29**, is a [cell surface receptor](/source/Cell_surface_receptor) that in humans is encoded by the *ITGB1* [gene](/source/Gene).[5] This [integrin](/source/Integrin) associates with [integrin alpha 1](/source/Integrin_alpha_1) and [integrin alpha 2](/source/Integrin_alpha_2) to form integrin complexes which function as [collagen receptors](/source/Collagen_receptor). It also forms dimers with [integrin alpha 3](/source/CD49c) to form integrin receptors for [netrin 1](/source/NTN1) and [reelin](/source/Reelin). These and other integrin beta 1 complexes have been historically known as very late activation (VLA) antigens.

Integrin beta 1 is expressed as at least four different [isoforms](/source/Isoforms). In [cardiac muscle](/source/Cardiac_muscle) and [skeletal muscle](/source/Skeletal_muscle), the integrin beta-1D isoform is specifically expressed, and localizes to [costameres](/source/Costamere), where it aids in the lateral force transmission from the [Z-discs](/source/Sarcomere) to the [extracellular matrix](/source/Extracellular_matrix). Abnormal levels of integrin beta-1D have been found in [limb girdle muscular dystrophy](/source/Limb_girdle_muscular_dystrophy) and [polyneuropathy](/source/Polyneuropathy).

## Structure

Integrin beta-1 can exist as different [isoforms](/source/Isoform) via [alternative splicing](/source/Alternative_splicing). Six [alternatively spliced](/source/Alternative_splicing) variants have been found for this gene which encode five proteins with alternate [C-termini](/source/C-terminus).[6] Integrin receptors exist as heterodimers, and greater than 20 different integrin heterodimeric receptors have been described. All integrins, alpha and beta forms, have large extracellular and short intracellular domains.[7] The cytoplasmic domain of integrin beta-1 binds to the [actin](/source/Actin) [cytoskeleton](/source/Cytoskeleton).[8] Integrin beta-1 is the most abundant beta-integrin expressed and associates with at least 10 different integrin-alpha subunits.[7]

## Function

Integrin family members are membrane receptors involved in cell adhesion and recognition in a variety of processes including embryogenesis, [hemostasis](/source/Hemostasis), tissue repair, [immune response](/source/Immune_response) and [metastatic diffusion of tumor cells](/source/Collective%E2%80%93amoeboid_transition).[7] Integrins link the [actin](/source/Actin) [cytoskeleton](/source/Cytoskeleton) with the [extracellular matrix](/source/Extracellular_matrix) and they transmit signals bidirectionally between the [extracellular matrix](/source/Extracellular_matrix) and [cytoplasmic](/source/Cytoplasm) domains.[9][10] Beta-integrins are primarily responsible for targeting integrin dimers to the appropriate subcellular locations, which in adhesive cells is mainly [focal adhesions](/source/Focal_adhesion).[8][11] Integrin beta-1 mutants lose the ability to target to sites of [focal adhesions](/source/Focal_adhesion).[12][13]

Three novel isoforms of integrin beta-1 have been identified, termed beta-1B, beta-1C and beta-1D. Integrin beta-1B is transcribed when the proximal 26 [amino acids](/source/Amino_acid) of the [cytoplasmic](/source/Cytoplasm) domain in exon 6 are retained and then succeeded by a 12 [amino acid](/source/Amino_acid) stretch from an adjacent [intronic](/source/Intron) region.[14] The integrin beta-1B [isoform](/source/Isoform) appears to act as a dominant negative in that it inhibits cell adhesion.[15] A second integrin beta-1 [isoform](/source/Isoform), termed beta-1C, was described to have an additional 48 [amino acids](/source/Amino_acid) appended to the 26 [amino acids](/source/Amino_acid) in the [cytoplasmic](/source/Cytoplasm) domain;[16] the function of this isoform was an inhibitory one on [DNA synthesis](/source/DNA_synthesis) in the [G1 phase](/source/G1_phase) of the [cell cycle](/source/Cell_cycle).[17] The third [isoform](/source/Isoform), termed beta-1D, is a [striated muscle](/source/Striated_muscle)-specific isoform, which replaces the canonical beta-1A [isoform](/source/Isoform) in [cardiac](/source/Cardiac_muscle) and [skeletal muscle](/source/Skeletal_muscle) cells. This [isoform](/source/Isoform) is produced from splicing into a novel additional exon between exons 6 and 7. The [cytoplasmic](/source/Cytoplasm) domain of integrin beta-1D replaces the distal 21 [amino acids](/source/Amino_acid) (present in integrin beta-1A) with an alternative stretch of 24 [amino acids](/source/Amino_acid) (13 unique).[18][19]

Integrin beta-1D appears to be developmentally regulated during myofibrilogenesis,[19] appearing immediately following the fusion of [myoblasts](/source/Myoblast) in [C2C12](/source/C2C12) cell with rising levels throughout [myofibrillar](/source/Myofibril) differentiation.[20] Integrin beta-1D is specifically localized to [costameres](/source/Costamere) and [intercalated discs](/source/Intercalated_disc) of [cardiac muscle](/source/Cardiac_muscle) and [costameres](/source/Costamere), [myotendinous junctions](/source/Myotendinous_junction) and [neuromuscular junctions](/source/Neuromuscular_junction) of [skeletal muscle](/source/Skeletal_muscle), and it appears to function in general like other integrins, as the clustering of beta-1D integrins on the surface of [CHO cells](/source/Chinese_hamster_ovary_cell) resulted in [tyrosine](/source/Tyrosine) [phosphorylation](/source/Phosphorylation) of [pp125FAK](/source/PTK2) and induced [mitogen-activated protein kinase](/source/Mitogen-activated_protein_kinase) activation.[20]

## Clinical significance

In patients with [limb girdle muscular dystrophy](/source/Limb_girdle_muscular_dystrophy), type 2C, beta-1D integrin has been shown to be severely reduced in [skeletal muscle](/source/Skeletal_muscle) biopsies, coordinate with a reduction in [alpha 7B-integrin](/source/ITGA7) and [filamin 2](/source/FLNC).[21]

In patients with sensitive-motor [polyneuropathy](/source/Polyneuropathy), levels of [integrin alpha-7B](/source/ITGA7), integrin beta-1D and [agrin](/source/Agrin) were significantly reduced nearly to undetectable levels; and this corresponded with lower [mRNA](/source/MRNA) levels.[22]

## Interactions

CD29 has been shown to [interact](/source/Protein-protein_interaction) with

- [ACTN1](/source/ACTN1);[23][24]

- [CD46](/source/CD46),[25]

- [CD9](/source/CD9),[26][27]

- [FHL2](/source/FHL2),[28]

- [Filamin](/source/Filamin),[29][30]

- [FLNB](/source/FLNB),[29]

- [CD81](/source/CD81),[27][31]

- [GNB2L1](/source/GNB2L1),[32][33]

- [ITGB1BP1](/source/ITGB1BP1),[34][35]

- [LGALS8](/source/LGALS8),[36]

- [MAP4K4](/source/MAP4K4),[37]

- [NME1](/source/NME1),[38]

- [PKC alpha](/source/PKC_alpha),[32][39]

- [TLN1](/source/TLN1),[40][41]

- [TSPAN4](/source/TSPAN4),[42] and

- [YWHAB](/source/YWHAB).[43]

## References

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1. **[^](#cite_ref-pmid8630057_26-0)** Radford KJ, Thorne RF, Hersey P (May 1996). "CD63 associates with transmembrane 4 superfamily members, CD9 and CD81, and with beta 1 integrins in human melanoma". *Biochemical and Biophysical Research Communications*. **222** (1): 13–8. [Bibcode](/source/Bibcode_(identifier)):[1996BBRC..222...13R](https://ui.adsabs.harvard.edu/abs/1996BBRC..222...13R). [doi](/source/Doi_(identifier)):[10.1006/bbrc.1996.0690](https://doi.org/10.1006%2Fbbrc.1996.0690). [PMID](/source/PMID_(identifier)) [8630057](https://pubmed.ncbi.nlm.nih.gov/8630057).

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1. **[^](#cite_ref-pmid10229664_31-0)** Serru V, Le Naour F, Billard M, Azorsa DO, Lanza F, Boucheix C, Rubinstein E (May 1999). ["Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220227). *The Biochemical Journal*. **340** (Pt 1): 103–11. [doi](/source/Doi_(identifier)):[10.1042/0264-6021:3400103](https://doi.org/10.1042%2F0264-6021%3A3400103). [PMC](/source/PMC_(identifier)) [1220227](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1220227). [PMID](/source/PMID_(identifier)) [10229664](https://pubmed.ncbi.nlm.nih.gov/10229664).

1. ^ [***a***](#cite_ref-pmid12435334_32-0) [***b***](#cite_ref-pmid12435334_32-1) Lee HS, Millward-Sadler SJ, Wright MO, Nuki G, Al-Jamal R, Salter DM (Nov 2002). ["Activation of Integrin-RACK1/PKCalpha signalling in human articular chondrocyte mechanotransduction"](https://doi.org/10.1053%2Fjoca.2002.0842). *Osteoarthritis and Cartilage*. **10** (11): 890–7. [doi](/source/Doi_(identifier)):[10.1053/joca.2002.0842](https://doi.org/10.1053%2Fjoca.2002.0842). [PMID](/source/PMID_(identifier)) [12435334](https://pubmed.ncbi.nlm.nih.gov/12435334).

1. **[^](#cite_ref-pmid9442085_33-0)** Liliental J, Chang DD (Jan 1998). ["Rack1, a receptor for activated protein kinase C, interacts with integrin beta subunit"](https://doi.org/10.1074%2Fjbc.273.4.2379). *The Journal of Biological Chemistry*. **273** (4): 2379–83. [doi](/source/Doi_(identifier)):[10.1074/jbc.273.4.2379](https://doi.org/10.1074%2Fjbc.273.4.2379). [PMID](/source/PMID_(identifier)) [9442085](https://pubmed.ncbi.nlm.nih.gov/9442085).

1. **[^](#cite_ref-pmid9281591_34-0)** Chang DD, Wong C, Smith H, Liu J (Sep 1997). ["ICAP-1, a novel beta1 integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of beta1 integrin"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2136751). *The Journal of Cell Biology*. **138** (5): 1149–57. [doi](/source/Doi_(identifier)):[10.1083/jcb.138.5.1149](https://doi.org/10.1083%2Fjcb.138.5.1149). [PMC](/source/PMC_(identifier)) [2136751](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2136751). [PMID](/source/PMID_(identifier)) [9281591](https://pubmed.ncbi.nlm.nih.gov/9281591).

1. **[^](#cite_ref-pmid11741908_35-0)** Chang DD, Hoang BQ, Liu J, Springer TA (Mar 2002). ["Molecular basis for interaction between Icap1 alpha PTB domain and beta 1 integrin"](https://doi.org/10.1074%2Fjbc.M109031200). *The Journal of Biological Chemistry*. **277** (10): 8140–5. [doi](/source/Doi_(identifier)):[10.1074/jbc.M109031200](https://doi.org/10.1074%2Fjbc.M109031200). [PMID](/source/PMID_(identifier)) [11741908](https://pubmed.ncbi.nlm.nih.gov/11741908).

1. **[^](#cite_ref-pmid10852818_36-0)** Hadari YR, Arbel-Goren R, Levy Y, Amsterdam A, Alon R, Zakut R, Zick Y (Jul 2000). "Galectin-8 binding to integrins inhibits cell adhesion and induces apoptosis". *Journal of Cell Science*. **113** (13): 2385–97. [doi](/source/Doi_(identifier)):[10.1242/jcs.113.13.2385](https://doi.org/10.1242%2Fjcs.113.13.2385). [PMID](/source/PMID_(identifier)) [10852818](https://pubmed.ncbi.nlm.nih.gov/10852818).

1. **[^](#cite_ref-pmid11967148_37-0)** Poinat P, De Arcangelis A, Sookhareea S, Zhu X, Hedgecock EM, Labouesse M, Georges-Labouesse E (Apr 2002). ["A conserved interaction between beta1 integrin/PAT-3 and Nck-interacting kinase/MIG-15 that mediates commissural axon navigation in C. elegans"](https://doi.org/10.1016%2FS0960-9822%2802%2900764-9). *Current Biology*. **12** (8): 622–31. [Bibcode](/source/Bibcode_(identifier)):[2002CBio...12..622P](https://ui.adsabs.harvard.edu/abs/2002CBio...12..622P). [doi](/source/Doi_(identifier)):[10.1016/S0960-9822(02)00764-9](https://doi.org/10.1016%2FS0960-9822%2802%2900764-9). [PMID](/source/PMID_(identifier)) [11967148](https://pubmed.ncbi.nlm.nih.gov/11967148). [S2CID](/source/S2CID_(identifier)) [9977605](https://api.semanticscholar.org/CorpusID:9977605).

1. **[^](#cite_ref-pmid11919189_38-0)** Fournier HN, Dupé-Manet S, Bouvard D, Lacombe ML, Marie C, Block MR, Albiges-Rizo C (Jun 2002). ["Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha ) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement"](https://doi.org/10.1074%2Fjbc.M200200200). *The Journal of Biological Chemistry*. **277** (23): 20895–902. [doi](/source/Doi_(identifier)):[10.1074/jbc.M200200200](https://doi.org/10.1074%2Fjbc.M200200200). [PMID](/source/PMID_(identifier)) [11919189](https://pubmed.ncbi.nlm.nih.gov/11919189).

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1. **[^](#cite_ref-40)** Tapley P, Horwitz A, Buck C, Duggan K, Rohrschneider L (Mar 1989). "Integrins isolated from Rous sarcoma virus-transformed chicken embryo fibroblasts". *Oncogene*. **4** (3): 325–33. [PMID](/source/PMID_(identifier)) [2468126](https://pubmed.ncbi.nlm.nih.gov/2468126).

1. **[^](#cite_ref-41)** Horwitz A, Duggan K, Buck C, Beckerle MC, Burridge K (1986). ["Interaction of plasma membrane fibronectin receptor with talin--a transmembrane linkage"](https://cdr.lib.unc.edu/record/uuid:ccf789da-0198-42b3-99a9-8fe20c8109c7). *Nature*. **320** (6062): 531–3. [Bibcode](/source/Bibcode_(identifier)):[1986Natur.320..531H](https://ui.adsabs.harvard.edu/abs/1986Natur.320..531H). [doi](/source/Doi_(identifier)):[10.1038/320531a0](https://doi.org/10.1038%2F320531a0). [PMID](/source/PMID_(identifier)) [2938015](https://pubmed.ncbi.nlm.nih.gov/2938015). [S2CID](/source/S2CID_(identifier)) [4356748](https://api.semanticscholar.org/CorpusID:4356748).

1. **[^](#cite_ref-pmid9360996_42-0)** Tachibana I, Bodorova J, Berditchevski F, Zutter MM, Hemler ME (Nov 1997). ["NAG-2, a novel transmembrane-4 superfamily (TM4SF) protein that complexes with integrins and other TM4SF proteins"](https://doi.org/10.1074%2Fjbc.272.46.29181). *The Journal of Biological Chemistry*. **272** (46): 29181–9. [doi](/source/Doi_(identifier)):[10.1074/jbc.272.46.29181](https://doi.org/10.1074%2Fjbc.272.46.29181). [PMID](/source/PMID_(identifier)) [9360996](https://pubmed.ncbi.nlm.nih.gov/9360996).

1. **[^](#cite_ref-pmid11313964_43-0)** Han DC, Rodriguez LG, Guan JL (Jan 2001). "Identification of a novel interaction between integrin beta1 and 14-3-3beta". *Oncogene*. **20** (3): 346–57. [doi](/source/Doi_(identifier)):[10.1038/sj.onc.1204068](https://doi.org/10.1038%2Fsj.onc.1204068). [PMID](/source/PMID_(identifier)) [11313964](https://pubmed.ncbi.nlm.nih.gov/11313964). [S2CID](/source/S2CID_(identifier)) [7405925](https://api.semanticscholar.org/CorpusID:7405925).

## Further reading

- Evans JP (Jul 2001). "Fertilin beta and other ADAMs as integrin ligands: insights into cell adhesion and fertilization". *BioEssays*. **23** (7): 628–39. [doi](/source/Doi_(identifier)):[10.1002/bies.1088](https://doi.org/10.1002%2Fbies.1088). [PMID](/source/PMID_(identifier)) [11462216](https://pubmed.ncbi.nlm.nih.gov/11462216). [S2CID](/source/S2CID_(identifier)) [23712246](https://api.semanticscholar.org/CorpusID:23712246).

- Armulik A (Jan 2002). ["Splice variants of human beta 1 integrins: origin, biosynthesis and functions"](https://doi.org/10.2741%2Farmulik). *Frontiers in Bioscience*. **7** (1–3): d219-27. [doi](/source/Doi_(identifier)):[10.2741/armulik](https://doi.org/10.2741%2Farmulik). [PMID](/source/PMID_(identifier)) [11779688](https://pubmed.ncbi.nlm.nih.gov/11779688).

- Brakebusch C, Fässler R (Sep 2005). "beta 1 integrin function in vivo: adhesion, migration and more". *Cancer and Metastasis Reviews*. **24** (3): 403–11. [doi](/source/Doi_(identifier)):[10.1007/s10555-005-5132-5](https://doi.org/10.1007%2Fs10555-005-5132-5). [PMID](/source/PMID_(identifier)) [16258728](https://pubmed.ncbi.nlm.nih.gov/16258728). [S2CID](/source/S2CID_(identifier)) [24210890](https://api.semanticscholar.org/CorpusID:24210890).

## External links

- [CD29+Antigen](https://meshb.nlm.nih.gov/record/ui?name=CD29+Antigen) at the U.S. National Library of Medicine [Medical Subject Headings](/source/Medical_Subject_Headings) (MeSH)

- Human [*ITGB1*](https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&singleSearch=knownCanonical&position=ITGB1) genome location and [*ITGB1*](https://genome.ucsc.edu/cgi-bin/hgGene?db=hg38&hgg_type=knownGene&hgg_gene=ITGB1) gene details page in the [UCSC Genome Browser](/source/UCSC_Genome_Browser).

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation) 1–50 CD1 a-c 1A 1B 1D 1E CD2 CD3 γ δ ε CD4 CD5 CD6 CD7 CD8 a CD9 CD10 CD11 a b c d CD13 CD14 CD15 CD16 A B CD18 CD19 CD20 CD21 CD22 CD23 CD24 CD25 CD26 CD27 CD28 CD29 CD30 CD31 CD32 A B CD33 CD34 CD35 CD36 CD37 CD38 CD39 CD40 CD41 CD42 a b c d CD43 CD44 CD45 CD46 CD47 CD48 CD49 a b c d e f CD50 51–100 CD51 CD52 CD53 CD54 CD55 CD56 CD57 CD58 CD59 CD61 CD62 E L P CD63 CD64 A B C CD66 a b c d e f CD68 CD69 CD70 CD71 CD72 CD73 CD74 CD78 CD79 a b CD80 CD81 CD82 CD83 CD84 CD85 a d e h j k CD86 CD87 CD88 CD89 CD90 CD91 CD92 CD93 CD94 CD95 CD96 CD97 CD98 CD99 CD100 101–150 CD101 CD102 CD103 CD104 CD105 CD106 CD107 a b CD108 CD109 CD110 CD111 CD112 CD113 CD114 CD115 CD116 CD117 CD118 CD119 CD120 a b CD121 a b CD122 CD123 CD124 CD125 CD126 CD127 CD129 CD130 CD131 CD132 CD133 CD134 CD135 CD136 CD137 CD138 CD140b CD141 CD142 CD143 CD144 CD146 CD147 CD148 CD150 151–200 CD151 CD152 CD153 CD154 CD155 CD156 a b c CD157 CD158 (a d e i k) CD159 a c CD160 CD161 CD162 CD163 CD164 CD166 CD167 a b CD168 CD169 CD170 CD171 CD172 a b g CD174 CD177 CD178 CD179 a b CD180 CD181 CD182 CD183 CD184 CD185 CD186 CD191 CD192 CD193 CD194 CD195 CD196 CD197 CDw198 CDw199 CD200 201–250 CD201 CD202b CD204 CD205 CD206 CD207 CD208 CD209 CDw210 a b CD212 CD213a 1 2 CD217 CD218 (a b) CD220 CD221 CD222 CD223 CD224 CD225 CD226 CD227 CD228 CD229 CD230 CD233 CD234 CD235 a b CD236 CD238 CD239 CD240CE CD240D CD241 CD243 CD244 CD246 CD247 CD248 CD249 251–300 CD252 CD253 CD254 CD256 CD257 CD258 CD261 CD262 CD263 CD264 CD265 CD266 CD267 CD268 CD269 CD271 CD272 CD273 CD274 CD275 CD276 CD278 CD279 CD280 CD281 CD282 CD283 CD284 CD286 CD288 CD289 CD290 CD292 CDw293 CD294 CD295 CD297 CD298 CD299 301–350 CD300A CD301 CD302 CD303 CD304 CD305 CD306 CD307 CD309 CD312 CD314 CD315 CD316 CD317 CD318 CD320 CD321 CD322 CD324 CD325 CD326 CD327 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350 351–371 CD351 CD352 CD353 CD354 CD355 CD357 CD358 CD360 CD361 CD362 CD363 CD364 CD365 CD366 CD367 CD368 CD369 CD370 CD371 Category Commons

v t e Integrins Alpha A1 A2 A3 A4 A5 A6 A7 A8 A9 A10 A11 AD AE AL AM AV AX Beta B1 B2 B3 B4 B5 B6 B7 B8 Dimers Cytoadhesin receptor: Integrin alpha6beta4 Glycoprotein IIb/IIIa ITGA2B+ITGB3 Fibrinogen receptor: Macrophage-1 antigen CD11b+CD18 Fibronectin receptor: Integrin alpha2beta1 Integrin alpha4beta1 Integrin alpha5beta1 Leukocyte-adhesion receptor: LFA-1 CD11a+CD18 Macrophage-1 antigen CD11b+CD18 Integrin alphaXbeta2 CD11c+CD18 Very late antigen receptor: Integrin alpha1beta1 Integrin alpha2beta1 Integrin alpha3beta1 VLA-4 CD49d+CD29 Alpha-5 beta-1 Integrin alpha6beta1 Vitronectin receptor: Alpha-v beta-3 Alpha-v beta-5 see also cell surface receptor deficiencies

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Adapted from the Wikipedia article [Integrin beta 1](https://en.wikipedia.org/wiki/Integrin_beta_1) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/Integrin_beta_1?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.