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Protein

Integrin beta-6

Gene

ITGB6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Integrin alpha-V/beta-6 is a receptor for fibronectin and cytotactin. It recognizes the sequence R-G-D in its ligands. Internalisation of integrin alpha-V/beta-6 via clathrin-mediated endocytosis promotes carcinoma cell invasion.1 Publication

GO - Molecular functioni

  1. virus receptor activity Source: UniProtKB-KW

GO - Biological processi

  1. cell adhesion Source: ProtInc
  2. cell-matrix adhesion Source: InterPro
  3. extracellular matrix organization Source: Reactome
  4. inflammatory response Source: Ensembl
  5. integrin-mediated signaling pathway Source: UniProtKB-KW
  6. multicellular organismal development Source: InterPro
  7. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Host cell receptor for virus entry, Integrin, Receptor

Keywords - Biological processi

Cell adhesion, Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_13552. Integrin cell surface interactions.
REACT_150331. Molecules associated with elastic fibres.
REACT_150366. Elastic fibre formation.
REACT_163906. ECM proteoglycans.
SignaLinkiP18564.

Names & Taxonomyi

Protein namesi
Recommended name:
Integrin beta-6
Gene namesi
Name:ITGB6
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:6161. ITGB6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini22 – 709688ExtracellularSequence AnalysisAdd
BLAST
Transmembranei710 – 73021HelicalSequence AnalysisAdd
BLAST
Topological domaini731 – 78858CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. external side of plasma membrane Source: Ensembl
  2. extracellular vesicular exosome Source: UniProtKB
  3. integrin complex Source: ProtInc
  4. plasma membrane Source: Reactome
  5. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

Orphaneti100032. Hypocalcified amelogenesis imperfecta.
100031. Hypoplastic amelogenesis imperfecta.
PharmGKBiPA29960.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 788767Integrin beta-6PRO_0000016350Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi23 ↔ 454By similarity
Disulfide bondi31 ↔ 41By similarity
Disulfide bondi34 ↔ 70By similarity
Disulfide bondi44 ↔ 59By similarity
Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi97 – 971N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi197 ↔ 204By similarity
Disulfide bondi252 ↔ 293By similarity
Glycosylationi260 – 2601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi387 – 3871N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi394 ↔ 406By similarity
Glycosylationi396 – 3961N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi426 ↔ 670By similarity
Disulfide bondi452 ↔ 456By similarity
Glycosylationi463 – 4631N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi467 ↔ 479By similarity
Glycosylationi471 – 4711N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi476 ↔ 511By similarity
Disulfide bondi481 ↔ 490By similarity
Disulfide bondi492 ↔ 502By similarity
Disulfide bondi517 ↔ 522By similarity
Disulfide bondi519 ↔ 552By similarity
Disulfide bondi524 ↔ 537By similarity
Disulfide bondi539 ↔ 544By similarity
Glycosylationi541 – 5411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi558 ↔ 563By similarity
Disulfide bondi560 ↔ 591By similarity
Disulfide bondi565 ↔ 574By similarity
Glycosylationi575 – 5751N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi576 ↔ 583By similarity
Disulfide bondi597 ↔ 602By similarity
Disulfide bondi599 ↔ 645By similarity
Disulfide bondi604 ↔ 614By similarity
Disulfide bondi617 ↔ 620By similarity
Disulfide bondi624 ↔ 633By similarity
Disulfide bondi630 ↔ 702By similarity
Disulfide bondi649 ↔ 678By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP18564.
PaxDbiP18564.
PeptideAtlasiP18564.
PRIDEiP18564.

PTM databases

PhosphoSiteiP18564.

Expressioni

Gene expression databases

BgeeiP18564.
CleanExiHS_ITGB6.
ExpressionAtlasiP18564. baseline and differential.
GenevestigatoriP18564.

Organism-specific databases

HPAiHPA023626.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. Beta-6 associates with alpha-V. Interacts with FLNB. Interacts with HAX1. Alpha-V/beta-6 binds to foot-and-mouth disease virus (FMDV) VP1 protein, coxsackievirus A9, coxsackievirus B1 capsid proteins and acts as a receptor for these viruses.6 Publications

Protein-protein interaction databases

BioGridi109900. 5 interactions.
DIPiDIP-59187N.
STRINGi9606.ENSP00000283249.

Structurei

Secondary structure

1
788
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni24 – 263Combined sources
Helixi31 – 344Combined sources
Beta strandi42 – 443Combined sources
Helixi62 – 687Combined sources
Turni72 – 743Combined sources
Beta strandi81 – 866Combined sources
Helixi98 – 1003Combined sources
Beta strandi108 – 1136Combined sources
Beta strandi119 – 1268Combined sources
Beta strandi133 – 1408Combined sources
Helixi143 – 1453Combined sources
Helixi146 – 1516Combined sources
Helixi152 – 1543Combined sources
Helixi155 – 16612Combined sources
Beta strandi170 – 1778Combined sources
Turni183 – 1853Combined sources
Helixi190 – 1945Combined sources
Turni196 – 2016Combined sources
Beta strandi209 – 21810Combined sources
Helixi220 – 2289Combined sources
Beta strandi236 – 2416Combined sources
Helixi242 – 25110Combined sources
Helixi253 – 2564Combined sources
Beta strandi262 – 27211Combined sources
Helixi277 – 2837Combined sources
Beta strandi299 – 3013Combined sources
Turni302 – 3065Combined sources
Helixi312 – 32110Combined sources
Beta strandi324 – 3307Combined sources
Helixi332 – 34211Combined sources
Beta strandi349 – 3524Combined sources
Helixi360 – 37112Combined sources
Beta strandi375 – 3828Combined sources
Beta strandi387 – 3937Combined sources
Turni395 – 3973Combined sources
Beta strandi398 – 4014Combined sources
Beta strandi414 – 4229Combined sources
Beta strandi431 – 4377Combined sources
Beta strandi444 – 4507Combined sources
Helixi455 – 4573Combined sources
Beta strandi467 – 4759Combined sources
Beta strandi478 – 4814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LH9model-A76-546[»]
4UM8X-ray2.85B/D1-788[»]
4UM9X-ray2.50B/D1-788[»]
ProteinModelPortaliP18564.
SMRiP18564. Positions 23-775.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini131 – 371241VWFAAdd
BLAST
Repeati456 – 50146IAdd
BLAST
Repeati502 – 54342IIAdd
BLAST
Repeati544 – 58239IIIAdd
BLAST
Repeati583 – 61937IVAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni456 – 619164Cysteine-rich tandem repeatsAdd
BLAST
Regioni731 – 75828Interaction with HAX1Add
BLAST

Sequence similaritiesi

Belongs to the integrin beta chain family.Curated
Contains 1 VWFA domain.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG145803.
GeneTreeiENSGT00760000119064.
HOGENOMiHOG000252936.
HOVERGENiHBG006190.
InParanoidiP18564.
KOiK06589.
OMAiKRSCIEC.
OrthoDBiEOG7T7GSB.
PhylomeDBiP18564.
TreeFamiTF105392.

Family and domain databases

Gene3Di1.20.5.630. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR013111. EGF_extracell.
IPR015812. Integrin_bsu.
IPR015436. Integrin_bsu-6.
IPR014836. Integrin_bsu_cyt_dom.
IPR002369. Integrin_bsu_N.
IPR012896. Integrin_bsu_tail.
IPR016201. Plexin-like_fold.
IPR002035. VWF_A.
[Graphical view]
PANTHERiPTHR10082. PTHR10082. 1 hit.
PTHR10082:SF11. PTHR10082:SF11. 1 hit.
PfamiPF07974. EGF_2. 1 hit.
PF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 1 hit.
PF00362. Integrin_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF002512. Integrin_B. 1 hit.
PRINTSiPR01186. INTEGRINB.
SMARTiSM00187. INB. 1 hit.
SM00423. PSI. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF103575. SSF103575. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEiPS00022. EGF_1. 2 hits.
PS01186. EGF_2. 1 hit.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P18564-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGIELLCLFF LFLGRNDHVQ GGCALGGAET CEDCLLIGPQ CAWCAQENFT
60 70 80 90 100
HPSGVGERCD TPANLLAKGC QLNFIENPVS QVEILKNKPL SVGRQKNSSD
110 120 130 140 150
IVQIAPQSLI LKLRPGGAQT LQVHVRQTED YPVDLYYLMD LSASMDDDLN
160 170 180 190 200
TIKELGSRLS KEMSKLTSNF RLGFGSFVEK PVSPFVKTTP EEIANPCSSI
210 220 230 240 250
PYFCLPTFGF KHILPLTNDA ERFNEIVKNQ KISANIDTPE GGFDAIMQAA
260 270 280 290 300
VCKEKIGWRN DSLHLLVFVS DADSHFGMDS KLAGIVIPND GLCHLDSKNE
310 320 330 340 350
YSMSTVLEYP TIGQLIDKLV QNNVLLIFAV TQEQVHLYEN YAKLIPGATV
360 370 380 390 400
GLLQKDSGNI LQLIISAYEE LRSEVELEVL GDTEGLNLSF TAICNNGTLF
410 420 430 440 450
QHQKKCSHMK VGDTASFSVT VNIPHCERRS RHIIIKPVGL GDALELLVSP
460 470 480 490 500
ECNCDCQKEV EVNSSKCHHG NGSFQCGVCA CHPGHMGPRC ECGEDMLSTD
510 520 530 540 550
SCKEAPDHPS CSGRGDCYCG QCICHLSPYG NIYGPYCQCD NFSCVRHKGL
560 570 580 590 600
LCGGNGDCDC GECVCRSGWT GEYCNCTTST DSCVSEDGVL CSGRGDCVCG
610 620 630 640 650
KCVCTNPGAS GPTCERCPTC GDPCNSKRSC IECHLSAAGQ AREECVDKCK
660 670 680 690 700
LAGATISEEE DFSKDGSVSC SLQGENECLI TFLITTDNEG KTIIHSINEK
710 720 730 740 750
DCPKPPNIPM IMLGVSLAIL LIGVVLLCIW KLLVSFHDRK EVAKFEAERS
760 770 780
KAKWQTGTNP LYRGSTSTFK NVTYKHREKQ KVDLSTDC
Length:788
Mass (Da):85,936
Last modified:April 27, 2001 - v2
Checksum:iEDB7D533EC4C8C4D
GO
Isoform 2 (identifier: P18564-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     554-660: Missing.

Note: No experimental confirmation available. Gene prediction confirmed by EST data.

Show »
Length:681
Mass (Da):74,958
Checksum:iB761664C333068BB
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti437 – 4371P → T.
Corresponds to variant rs2305820 [ dbSNP | Ensembl ].
VAR_049636

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei554 – 660107Missing in isoform 2. CuratedVSP_055189Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35198 mRNA. Translation: AAA36122.2.
AC092153 Genomic DNA. Translation: AAX93093.1.
AK313944 mRNA. Translation: BAG36662.1.
AC080166 Genomic DNA. Translation: AAY24053.1.
CH471058 Genomic DNA. Translation: EAX11390.1.
BC121178 mRNA. Translation: AAI21179.1.
S49380 Genomic DNA. Translation: AAB23690.1.
CCDSiCCDS2212.1. [P18564-1]
CCDS63040.1. [P18564-2]
PIRiA37057.
RefSeqiNP_000879.2. NM_000888.4. [P18564-1]
NP_001269282.1. NM_001282353.1. [P18564-1]
NP_001269284.1. NM_001282355.1. [P18564-2]
NP_001269317.1. NM_001282388.1.
UniGeneiHs.470399.

Genome annotation databases

EnsembliENST00000283249; ENSP00000283249; ENSG00000115221. [P18564-1]
ENST00000409872; ENSP00000386367; ENSG00000115221. [P18564-1]
ENST00000409967; ENSP00000386828; ENSG00000115221. [P18564-2]
GeneIDi3694.
KEGGihsa:3694.
UCSCiuc002ubh.2. human. [P18564-1]

Polymorphism databases

DMDMi13432176.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35198 mRNA. Translation: AAA36122.2.
AC092153 Genomic DNA. Translation: AAX93093.1.
AK313944 mRNA. Translation: BAG36662.1.
AC080166 Genomic DNA. Translation: AAY24053.1.
CH471058 Genomic DNA. Translation: EAX11390.1.
BC121178 mRNA. Translation: AAI21179.1.
S49380 Genomic DNA. Translation: AAB23690.1.
CCDSiCCDS2212.1. [P18564-1]
CCDS63040.1. [P18564-2]
PIRiA37057.
RefSeqiNP_000879.2. NM_000888.4. [P18564-1]
NP_001269282.1. NM_001282353.1. [P18564-1]
NP_001269284.1. NM_001282355.1. [P18564-2]
NP_001269317.1. NM_001282388.1.
UniGeneiHs.470399.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LH9model-A76-546[»]
4UM8X-ray2.85B/D1-788[»]
4UM9X-ray2.50B/D1-788[»]
ProteinModelPortaliP18564.
SMRiP18564. Positions 23-775.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109900. 5 interactions.
DIPiDIP-59187N.
STRINGi9606.ENSP00000283249.

Chemistry

BindingDBiP18564.
ChEMBLiCHEMBL2111416.

PTM databases

PhosphoSiteiP18564.

Polymorphism databases

DMDMi13432176.

Proteomic databases

MaxQBiP18564.
PaxDbiP18564.
PeptideAtlasiP18564.
PRIDEiP18564.

Protocols and materials databases

DNASUi3694.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000283249; ENSP00000283249; ENSG00000115221. [P18564-1]
ENST00000409872; ENSP00000386367; ENSG00000115221. [P18564-1]
ENST00000409967; ENSP00000386828; ENSG00000115221. [P18564-2]
GeneIDi3694.
KEGGihsa:3694.
UCSCiuc002ubh.2. human. [P18564-1]

Organism-specific databases

CTDi3694.
GeneCardsiGC02M160920.
HGNCiHGNC:6161. ITGB6.
HPAiHPA023626.
MIMi147558. gene.
neXtProtiNX_P18564.
Orphaneti100032. Hypocalcified amelogenesis imperfecta.
100031. Hypoplastic amelogenesis imperfecta.
PharmGKBiPA29960.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG145803.
GeneTreeiENSGT00760000119064.
HOGENOMiHOG000252936.
HOVERGENiHBG006190.
InParanoidiP18564.
KOiK06589.
OMAiKRSCIEC.
OrthoDBiEOG7T7GSB.
PhylomeDBiP18564.
TreeFamiTF105392.

Enzyme and pathway databases

ReactomeiREACT_13552. Integrin cell surface interactions.
REACT_150331. Molecules associated with elastic fibres.
REACT_150366. Elastic fibre formation.
REACT_163906. ECM proteoglycans.
SignaLinkiP18564.

Miscellaneous databases

GeneWikiiIntegrin,_beta_6.
GenomeRNAii3694.
NextBioi14479.
PROiP18564.
SOURCEiSearch...

Gene expression databases

BgeeiP18564.
CleanExiHS_ITGB6.
ExpressionAtlasiP18564. baseline and differential.
GenevestigatoriP18564.

Family and domain databases

Gene3Di1.20.5.630. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR013111. EGF_extracell.
IPR015812. Integrin_bsu.
IPR015436. Integrin_bsu-6.
IPR014836. Integrin_bsu_cyt_dom.
IPR002369. Integrin_bsu_N.
IPR012896. Integrin_bsu_tail.
IPR016201. Plexin-like_fold.
IPR002035. VWF_A.
[Graphical view]
PANTHERiPTHR10082. PTHR10082. 1 hit.
PTHR10082:SF11. PTHR10082:SF11. 1 hit.
PfamiPF07974. EGF_2. 1 hit.
PF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 1 hit.
PF00362. Integrin_beta. 1 hit.
[Graphical view]
PIRSFiPIRSF002512. Integrin_B. 1 hit.
PRINTSiPR01186. INTEGRINB.
SMARTiSM00187. INB. 1 hit.
SM00423. PSI. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF103575. SSF103575. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEiPS00022. EGF_1. 2 hits.
PS01186. EGF_2. 1 hit.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete amino acid sequence of a novel integrin beta subunit (beta 6) identified in epithelial cells using the polymerase chain reaction."
    Sheppard D., Rozzo C., Starr L., Quaranta V., Erle D.J., Pytela R.
    J. Biol. Chem. 265:11502-11507(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Pancreas.
  2. Askins J.
    Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 18-24; 158; 642 AND 719.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Placenta.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  7. "The gene organization of the human beta 7 subunit, the common beta subunit of the leukocyte integrins HML-1 and LPAM-1."
    Jiang W.-M., Jenkins D., Yuan Q., Leung E., Choo K.H., Watson J.D., Krissansen G.W.
    Int. Immunol. 4:1031-1040(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 116-197.
  8. "Integrin alpha v beta 6 enhances coxsackievirus B1 lytic infection of human colon cancer cells."
    Agrez M.V., Shafren D.R., Gu X., Cox K., Sheppard D., Barry R.D.
    Virology 239:71-77(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COXSACKIEVIRUS B1 CAPSID PROTEINS.
  9. "The epithelial integrin alphavbeta6 is a receptor for foot-and-mouth disease virus."
    Jackson T., Sheppard D., Denyer M., Blakemore W., King A.M.
    J. Virol. 74:4949-4956(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FMDV VP1.
  10. "Different splice variants of filamin-B affect myogenesis, subcellular distribution, and determine binding to integrin (beta) subunits."
    van Der Flier A., Kuikman I., Kramer D., Geerts D., Kreft M., Takafuta T., Shapiro S.S., Sonnenberg A.
    J. Cell Biol. 156:361-376(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FLNB.
    Tissue: Keratinocyte and Skeletal muscle.
  11. "Integrin alpha v beta 6 is an RGD-dependent receptor for coxsackievirus A9."
    Williams C.H., Kajander T., Hyypia T., Jackson T., Sheppard D., Stanway G.
    J. Virol. 78:6967-6973(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COXSACKIEVIRUS A9 CAPSID PROTEINS.
  12. "Specificity of the VP1 GH loop of Foot-and-Mouth Disease virus for alphav integrins."
    Burman A., Clark S., Abrescia N.G., Fry E.E., Stuart D.I., Jackson T.
    J. Virol. 80:9798-9810(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FMDV VP1.
  13. "HS1-associated protein X-1 regulates carcinoma cell migration and invasion via clathrin-mediated endocytosis of integrin alphavbeta6."
    Ramsay A.G., Keppler M.D., Jazayeri M., Thomas G.J., Parsons M., Violette S., Weinreb P., Hart I.R., Marshall J.F.
    Cancer Res. 67:5275-5284(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HAX1, FUNCTION.

Entry informationi

Entry nameiITB6_HUMAN
AccessioniPrimary (citable) accession number: P18564
Secondary accession number(s): B2R9W5
, C9JA97, Q0VA95, Q16500, Q53RG5, Q53RR6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: April 27, 2001
Last modified: February 4, 2015
This is version 158 of the entry and version 2 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 2
    Human chromosome 2: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.