CD61

ITGB3
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	4O02, 1JV2, 1KUP, 1KUZ, 1L5G, 1M1X, 1M8O, 1MIZ, 1MK7, 1MK9, 1S4X, 1TYE, 1U8C, 2K9J, 2KNC, 2KV9, 2L1C, 2L91, 2LJD, 2LJE, 2LJF, 2MTP, 2Q6W, 2RMZ, 2RN0, 2VC2, 2VDK, 2VDL, 2VDM, 2VDN, 2VDP, 2VDQ, 2VDR, 3FCS, 3FCU, 3IJE, 3NID, 3NIF, 3NIG, 3T3M, 3T3P, 3ZDX, 3ZDY, 3ZDZ, 3ZE0, 3ZE1, 3ZE2, 4CAK, 4G1E, 4G1M, 4MMX, 4MMY, 4MMZ, 5HDB, 4Z7Q, 4Z7O, 4Z7N
Identifiers
Aliases	ITGB3, BDPLT16, BDPLT2, CD61, GP3A, GPIIIa, GT, integrin subunit beta 3
External IDs	OMIM: 173470 MGI: 96612 HomoloGene: 55444 GeneCards: ITGB3
Gene ontology
Molecular function	• vascular endothelial growth factor receptor 2 binding; • fibronectin binding; • virus receptor activity; • extracellular matrix binding; • protein disulfide isomerase activity; • protease binding; • platelet-derived growth factor receptor binding; • protein binding; • identical protein binding; • enzyme binding; • cell adhesion molecule binding; • receptor activity; • neuregulin binding; • coreceptor activity; • fibroblast growth factor binding; • insulin-like growth factor I binding; • C-X3-C chemokine binding;
Cellular component	• integral component of membrane; • cell projection; • alphav-beta3 integrin-vitronectin complex; • membrane; • focal adhesion; • melanosome; • receptor complex; • plasma membrane; • integral component of plasma membrane; • ruffle membrane; • cell surface; • cell junction; • integrin complex; • platelet alpha granule membrane; • integrin alphav-beta3 complex; • extracellular exosome; • lamellipodium membrane; • nucleus; • microvillus membrane; • filopodium membrane; • alphav-beta3 integrin-IGF-1-IGF1R complex;
Biological process	• negative regulation of lipoprotein metabolic process; • apolipoprotein A-I-mediated signaling pathway; • positive regulation of vascular endothelial growth factor receptor signaling pathway; • positive regulation of protein phosphorylation; • regulation of cell migration; • negative chemotaxis; • positive regulation of endothelial cell proliferation; • tube development; • negative regulation of low-density lipoprotein particle receptor biosynthetic process; • heterotypic cell-cell adhesion; • angiogenesis involved in wound healing; • wound healing; • platelet degranulation; • blood coagulation; • extracellular matrix organization; • smooth muscle cell migration; • positive regulation of endothelial cell migration; • cell growth; • cell-substrate adhesion; • vascular endothelial growth factor receptor signaling pathway; • cell adhesion; • positive regulation of peptidyl-tyrosine phosphorylation; • mesodermal cell differentiation; • cell-substrate junction assembly; • integrin-mediated signaling pathway; • negative regulation of lipid storage; • viral entry into host cell; • substrate adhesion-dependent cell spreading; • negative regulation of lipid transport; • cell-matrix adhesion; • viral process; • regulation of bone resorption; • platelet aggregation; • cell migration; • negative regulation of macrophage derived foam cell differentiation; • activation of protein kinase activity; • leukocyte migration; • cell adhesion mediated by integrin; • platelet activation;
	Sources:Amigo / QuickGO
RNA expression pattern
	; ; ; ;
	More reference expression data
Orthologs
	3690
	16416
	ENSG00000259207
	ENSMUSG00000020689
	P05106
	O54890
	NM_000212
	NM_016780
	NP_000203.2
	NP_058060.2
	Wikidata
View/Edit Human	View/Edit Mouse

Integrin beta-3 (β3) or CD61 is a protein that in humans is encoded by the ITGB3 gene.^[3] CD61 is a cluster of differentiation found on thrombocytes.^[4]

Structure and function[edit]

The ITGB3 protein product is the integrin beta chain beta 3. Integrins are integral cell-surface proteins composed of an alpha chain and a beta chain. A given chain may combine with multiple partners resulting in different integrins. Integrin beta 3 is found along with the alpha IIb chain in platelets. Integrins are known to participate in cell adhesion as well as cell-surface-mediated signaling.^[5]

Role in endometriosis[edit]

Defectively expressed β3 integrin subunit has been correlated with presence of endometriosis, and has been suggested as a putative marker of this condition.^[6]

Interactions[edit]

CD61 has been shown to interact with PTK2,^[7]^[8] ITGB3BP,^[9]^[10] TLN1^[11]^[12] and CIB1.^[13]

References[edit]

^ "Human PubMed Reference:".
^ "Mouse PubMed Reference:".
^ Sosnoski DM, Emanuel BS, Hawkins AL, van Tuinen P, Ledbetter DH, Nussbaum RL, Kaos FT, Schwartz E, Phillips D, Bennett JS, et al. (August 1988). "Chromosomal localization of the genes for the vitronectin and fibronectin receptors alpha subunits and for platelet glycoproteins IIb and IIIa". J Clin Invest. 81 (6): 1993–8. doi:10.1172/JCI113548. PMC 442653. PMID 2454952.
^ Heemskerk, J. W. M.; Mattheij, N. J. A.; Cosemans, J. M. E. M. (2013). "Platelet-based coagulation: different populations, different functions". Journal of Thrombosis and Haemostasis. 11 (1): 2–16. doi:10.1111/jth.12045. ISSN 1538-7933.
^ "Entrez Gene: ITGB3 integrin, beta 3 (platelet glycoprotein IIIa, antigen CD61)".
^ May, K. E.; Villar, J.; Kirtley, S.; Kennedy, S. H.; Becker, C. M. (2011). "Endometrial alterations in endometriosis: A systematic review of putative biomarkers". Human Reproduction Update. 17 (5): 637–653. doi:10.1093/humupd/dmr013. PMID 21672902.
^ Eliceiri, Brian P; Puente Xose S; Hood John D; Stupack Dwayne G; Schlaepfer David D; Huang Xiaozhu Z; Sheppard Dean; Cheresh David A (April 2002). "Src-mediated coupling of focal adhesion kinase to integrin alpha(v)beta5 in vascular endothelial growth factor signaling". J. Cell Biol. United States. 157 (1): 149–60. doi:10.1083/jcb.200109079. ISSN 0021-9525. PMC 2173263. PMID 11927607.
^ Chung, J; Gao A G; Frazier W A (June 1997). "Thrombspondin acts via integrin-associated protein to activate the platelet integrin alphaIIbbeta3". J. Biol. Chem. UNITED STATES. 272 (23): 14740–6. doi:10.1074/jbc.272.23.14740. ISSN 0021-9258. PMID 9169439.
^ Fujimoto, Tetsuro-Takahiro; Katsutani Shinya; Shimomura Takeshi; Fujimura Kingo (January 2002). "Novel alternatively spliced form of beta(3)-endonexin". Thromb. Res. United States. 105 (1): 63–70. doi:10.1016/S0049-3848(01)00405-4. ISSN 0049-3848. PMID 11864709.
^ Shattil, S J; O'Toole T; Eigenthaler M; Thon V; Williams M; Babior B M; Ginsberg M H (November 1995). "Beta 3-endonexin, a novel polypeptide that interacts specifically with the cytoplasmic tail of the integrin beta 3 subunit". J. Cell Biol. UNITED STATES. 131 (3): 807–16. doi:10.1083/jcb.131.3.807. ISSN 0021-9525. PMC 2120613. PMID 7593198.
^ Patil, S; Jedsadayanmata A; Wencel-Drake J D; Wang W; Knezevic I; Lam S C (October 1999). "Identification of a talin-binding site in the integrin beta(3) subunit distinct from the NPLY regulatory motif of post-ligand binding functions. The talin n-terminal head domain interacts with the membrane-proximal region of the beta(3) cytoplasmic tail". J. Biol. Chem. UNITED STATES. 274 (40): 28575–83. doi:10.1074/jbc.274.40.28575. ISSN 0021-9258. PMID 10497223.
^ Calderwood, David A; Yan Boxu; de Pereda Jose M; Alvarez Begoña García; Fujioka Yosuke; Liddington Robert C; Ginsberg Mark H (June 2002). "The phosphotyrosine binding-like domain of talin activates integrins". J. Biol. Chem. United States. 277 (24): 21749–58. doi:10.1074/jbc.M111996200. ISSN 0021-9258. PMID 11932255.
^ Naik, U P; Patel P M; Parise L V (February 1997). "Identification of a novel calcium-binding protein that interacts with the integrin alphaIIb cytoplasmic domain". J. Biol. Chem. UNITED STATES. 272 (8): 4651–4. doi:10.1074/jbc.272.8.4651. ISSN 0021-9258. PMID 9030514.

External links[edit]

CD61 Antigens at the US National Library of Medicine Medical Subject Headings (MeSH)
ITGB3 Info with links in the Cell Migration Gateway

This article on a gene on human chromosome 17 is a stub. You can help Wikipedia by expanding it.

[1] "Human PubMed Reference:".

[2] "Mouse PubMed Reference:".

[pmid2454952-3] Sosnoski DM, Emanuel BS, Hawkins AL, van Tuinen P, Ledbetter DH, Nussbaum RL, Kaos FT, Schwartz E, Phillips D, Bennett JS, et al. (August 1988). "Chromosomal localization of the genes for the vitronectin and fibronectin receptors alpha subunits and for platelet glycoproteins IIb and IIIa". J Clin Invest. 81 (6): 1993–8. doi:10.1172/JCI113548. PMC 442653. PMID 2454952.

[HeemskerkMattheij2013-4] Heemskerk, J. W. M.; Mattheij, N. J. A.; Cosemans, J. M. E. M. (2013). "Platelet-based coagulation: different populations, different functions". Journal of Thrombosis and Haemostasis. 11 (1): 2–16. doi:10.1111/jth.12045. ISSN 1538-7933.

[5] "Entrez Gene: ITGB3 integrin, beta 3 (platelet glycoprotein IIIa, antigen CD61)".

[6] May, K. E.; Villar, J.; Kirtley, S.; Kennedy, S. H.; Becker, C. M. (2011). "Endometrial alterations in endometriosis: A systematic review of putative biomarkers". Human Reproduction Update. 17 (5): 637–653. doi:10.1093/humupd/dmr013. PMID 21672902.

[pmid11927607-7] Eliceiri, Brian P; Puente Xose S; Hood John D; Stupack Dwayne G; Schlaepfer David D; Huang Xiaozhu Z; Sheppard Dean; Cheresh David A (April 2002). "Src-mediated coupling of focal adhesion kinase to integrin alpha(v)beta5 in vascular endothelial growth factor signaling". J. Cell Biol. United States. 157 (1): 149–60. doi:10.1083/jcb.200109079. ISSN 0021-9525. PMC 2173263. PMID 11927607.

[pmid9169439-8] Chung, J; Gao A G; Frazier W A (June 1997). "Thrombspondin acts via integrin-associated protein to activate the platelet integrin alphaIIbbeta3". J. Biol. Chem. UNITED STATES. 272 (23): 14740–6. doi:10.1074/jbc.272.23.14740. ISSN 0021-9258. PMID 9169439.

[pmid11864709-9] Fujimoto, Tetsuro-Takahiro; Katsutani Shinya; Shimomura Takeshi; Fujimura Kingo (January 2002). "Novel alternatively spliced form of beta(3)-endonexin". Thromb. Res. United States. 105 (1): 63–70. doi:10.1016/S0049-3848(01)00405-4. ISSN 0049-3848. PMID 11864709.

[pmid7593198-10] Shattil, S J; O'Toole T; Eigenthaler M; Thon V; Williams M; Babior B M; Ginsberg M H (November 1995). "Beta 3-endonexin, a novel polypeptide that interacts specifically with the cytoplasmic tail of the integrin beta 3 subunit". J. Cell Biol. UNITED STATES. 131 (3): 807–16. doi:10.1083/jcb.131.3.807. ISSN 0021-9525. PMC 2120613. PMID 7593198.

[pmid10497223-11] Patil, S; Jedsadayanmata A; Wencel-Drake J D; Wang W; Knezevic I; Lam S C (October 1999). "Identification of a talin-binding site in the integrin beta(3) subunit distinct from the NPLY regulatory motif of post-ligand binding functions. The talin n-terminal head domain interacts with the membrane-proximal region of the beta(3) cytoplasmic tail". J. Biol. Chem. UNITED STATES. 274 (40): 28575–83. doi:10.1074/jbc.274.40.28575. ISSN 0021-9258. PMID 10497223.

[pmid11932255-12] Calderwood, David A; Yan Boxu; de Pereda Jose M; Alvarez Begoña García; Fujioka Yosuke; Liddington Robert C; Ginsberg Mark H (June 2002). "The phosphotyrosine binding-like domain of talin activates integrins". J. Biol. Chem. United States. 277 (24): 21749–58. doi:10.1074/jbc.M111996200. ISSN 0021-9258. PMID 11932255.

[pmid9030514-13] Naik, U P; Patel P M; Parise L V (February 1997). "Identification of a novel calcium-binding protein that interacts with the integrin alphaIIb cytoplasmic domain". J. Biol. Chem. UNITED STATES. 272 (8): 4651–4. doi:10.1074/jbc.272.8.4651. ISSN 0021-9258. PMID 9030514.

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[13]

v t e Proteins: clusters of differentiation (see also list of human clusters of differentiation)

1-50	CD1 a-c 1A 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 CD328 CD329 CD331 CD332 CD333 CD334 CD335 CD336 CD337 CD338 CD339 CD340 CD344 CD349 CD350

CD61

Contents

Structure and function[edit]

Role in endometriosis[edit]

Interactions[edit]

See also[edit]

References[edit]

Further reading[edit]

External links[edit]

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