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P18564 (ITB6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Integrin beta-6
Gene names
Name:ITGB6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length788 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.13

Subunit structure

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. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

Belongs to the integrin beta chain family.

Contains 1 VWFA domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P18564-1)

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.
Isoform 2 (identifier: P18564-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 788767Integrin beta-6
PRO_0000016350

Regions

Topological domain22 – 709688Extracellular Potential
Transmembrane710 – 73021Helical; Potential
Topological domain731 – 78858Cytoplasmic Potential
Domain131 – 371241VWFA
Repeat456 – 50146I
Repeat502 – 54342II
Repeat544 – 58239III
Repeat583 – 61937IV
Region456 – 619164Cysteine-rich tandem repeats
Region731 – 75828Interaction with HAX1

Amino acid modifications

Glycosylation481N-linked (GlcNAc...) Potential
Glycosylation971N-linked (GlcNAc...) Potential
Glycosylation2601N-linked (GlcNAc...) Potential
Glycosylation3871N-linked (GlcNAc...) Potential
Glycosylation3961N-linked (GlcNAc...) Potential
Glycosylation4631N-linked (GlcNAc...) Potential
Glycosylation4711N-linked (GlcNAc...) Potential
Glycosylation5411N-linked (GlcNAc...) Potential
Glycosylation5751N-linked (GlcNAc...) Potential
Disulfide bond23 ↔ 454 By similarity
Disulfide bond31 ↔ 41 By similarity
Disulfide bond34 ↔ 70 By similarity
Disulfide bond44 ↔ 59 By similarity
Disulfide bond197 ↔ 204 By similarity
Disulfide bond252 ↔ 293 By similarity
Disulfide bond394 ↔ 406 By similarity
Disulfide bond426 ↔ 670 By similarity
Disulfide bond452 ↔ 456 By similarity
Disulfide bond467 ↔ 479 By similarity
Disulfide bond476 ↔ 511 By similarity
Disulfide bond481 ↔ 490 By similarity
Disulfide bond492 ↔ 502 By similarity
Disulfide bond517 ↔ 522 By similarity
Disulfide bond519 ↔ 552 By similarity
Disulfide bond524 ↔ 537 By similarity
Disulfide bond539 ↔ 544 By similarity
Disulfide bond558 ↔ 563 By similarity
Disulfide bond560 ↔ 591 By similarity
Disulfide bond565 ↔ 574 By similarity
Disulfide bond576 ↔ 583 By similarity
Disulfide bond597 ↔ 602 By similarity
Disulfide bond599 ↔ 645 By similarity
Disulfide bond604 ↔ 614 By similarity
Disulfide bond617 ↔ 620 By similarity
Disulfide bond624 ↔ 633 By similarity
Disulfide bond630 ↔ 702 By similarity
Disulfide bond649 ↔ 678 By similarity

Natural variations

Alternative sequence554 – 660107Missing in isoform 2.
VSP_055189
Natural variant4371P → T.
Corresponds to variant rs2305820 [ dbSNP | Ensembl ].
VAR_049636

Secondary structure

.................................................................................. 788
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 27, 2001. Version 2.
Checksum: EDB7D533EC4C8C4D

FASTA78885,936
        10         20         30         40         50         60 
MGIELLCLFF LFLGRNDHVQ GGCALGGAET CEDCLLIGPQ CAWCAQENFT HPSGVGERCD 

        70         80         90        100        110        120 
TPANLLAKGC QLNFIENPVS QVEILKNKPL SVGRQKNSSD IVQIAPQSLI LKLRPGGAQT 

       130        140        150        160        170        180 
LQVHVRQTED YPVDLYYLMD LSASMDDDLN TIKELGSRLS KEMSKLTSNF RLGFGSFVEK 

       190        200        210        220        230        240 
PVSPFVKTTP EEIANPCSSI PYFCLPTFGF KHILPLTNDA ERFNEIVKNQ KISANIDTPE 

       250        260        270        280        290        300 
GGFDAIMQAA VCKEKIGWRN DSLHLLVFVS DADSHFGMDS KLAGIVIPND GLCHLDSKNE 

       310        320        330        340        350        360 
YSMSTVLEYP TIGQLIDKLV QNNVLLIFAV TQEQVHLYEN YAKLIPGATV GLLQKDSGNI 

       370        380        390        400        410        420 
LQLIISAYEE LRSEVELEVL GDTEGLNLSF TAICNNGTLF QHQKKCSHMK VGDTASFSVT 

       430        440        450        460        470        480 
VNIPHCERRS RHIIIKPVGL GDALELLVSP ECNCDCQKEV EVNSSKCHHG NGSFQCGVCA 

       490        500        510        520        530        540 
CHPGHMGPRC ECGEDMLSTD SCKEAPDHPS CSGRGDCYCG QCICHLSPYG NIYGPYCQCD 

       550        560        570        580        590        600 
NFSCVRHKGL LCGGNGDCDC GECVCRSGWT GEYCNCTTST DSCVSEDGVL CSGRGDCVCG 

       610        620        630        640        650        660 
KCVCTNPGAS GPTCERCPTC GDPCNSKRSC IECHLSAAGQ AREECVDKCK LAGATISEEE 

       670        680        690        700        710        720 
DFSKDGSVSC SLQGENECLI TFLITTDNEG KTIIHSINEK DCPKPPNIPM IMLGVSLAIL 

       730        740        750        760        770        780 
LIGVVLLCIW KLLVSFHDRK EVAKFEAERS KAKWQTGTNP LYRGSTSTFK NVTYKHREKQ 


KVDLSTDC 

« Hide

Isoform 2 [UniParc].

Checksum: B761664C333068BB
Show »

FASTA68174,958

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2212.1.
PIRA37057.
RefSeqNP_000879.2. NM_000888.4.
NP_001269282.1. NM_001282353.1.
NP_001269284.1. NM_001282355.1.
NP_001269317.1. NM_001282388.1.
UniGeneHs.470399.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LH9model-A76-546[»]
ProteinModelPortalP18564.
SMRP18564. Positions 23-775.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109900. 5 interactions.
DIPDIP-59187N.
STRING9606.ENSP00000283249.

Chemistry

BindingDBP18564.
ChEMBLCHEMBL2111416.

PTM databases

PhosphoSiteP18564.

Polymorphism databases

DMDM13432176.

Proteomic databases

MaxQBP18564.
PaxDbP18564.
PeptideAtlasP18564.
PRIDEP18564.

Protocols and materials databases

DNASU3694.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000283249; ENSP00000283249; ENSG00000115221.
ENST00000409872; ENSP00000386367; ENSG00000115221.
ENST00000409967; ENSP00000386828; ENSG00000115221.
GeneID3694.
KEGGhsa:3694.
UCSCuc002ubh.2. human.

Organism-specific databases

CTD3694.
GeneCardsGC02M160920.
HGNCHGNC:6161. ITGB6.
HPAHPA023626.
MIM147558. gene.
neXtProtNX_P18564.
PharmGKBPA29960.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG145803.
HOGENOMHOG000252936.
HOVERGENHBG006190.
InParanoidP18564.
KOK06589.
OMAEYCNCTT.
OrthoDBEOG7T7GSB.
PhylomeDBP18564.
TreeFamTF105392.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
SignaLinkP18564.

Gene expression databases

ArrayExpressP18564.
BgeeP18564.
CleanExHS_ITGB6.
GenevestigatorP18564.

Family and domain databases

Gene3D1.20.5.630. 1 hit.
3.40.50.410. 1 hit.
InterProIPR013111. 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]
PANTHERPTHR10082. PTHR10082. 1 hit.
PTHR10082:SF11. PTHR10082:SF11. 1 hit.
PfamPF07974. EGF_2. 1 hit.
PF08725. Integrin_b_cyt. 1 hit.
PF07965. Integrin_B_tail. 1 hit.
PF00362. Integrin_beta. 1 hit.
[Graphical view]
PIRSFPIRSF002512. Integrin_B. 1 hit.
PRINTSPR01186. INTEGRINB.
SMARTSM00187. INB. 1 hit.
SM00423. PSI. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF103575. SSF103575. 1 hit.
SSF53300. SSF53300. 1 hit.
SSF69687. SSF69687. 1 hit.
PROSITEPS00022. EGF_1. 2 hits.
PS01186. EGF_2. 1 hit.
PS00243. INTEGRIN_BETA. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiIntegrin,_beta_6.
GenomeRNAi3694.
NextBio14479.
PROP18564.
SOURCESearch...

Entry information

Entry nameITB6_HUMAN
AccessionPrimary (citable) accession number: P18564
Secondary accession number(s): B2R9W5 expand/collapse secondary AC list , C9JA97, Q0VA95, Q16500, Q53RG5, Q53RR6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: April 27, 2001
Last modified: July 9, 2014
This is version 152 of the entry and version 2 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 2

Human chromosome 2: entries, gene names and cross-references to MIM