P18084 (ITB5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Integrin beta-5

Gene names

Name:

ITGB5

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	799 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Integrin alpha-V/beta-5 is a receptor for fibronectin. It recognizes the sequence R-G-D in its ligand.
Subunit structure	Heterodimer of an alpha and a beta subunit. Beta-5 associates with alpha-V. Interacts with MYO10. Interacts with DAB2. Ref.7
Subcellular location	Membrane; Single-pass type I membrane protein.
Sequence similarities	Belongs to the integrin beta chain family. Contains 1 PSI domain. Contains 1 VWFA domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Integrin Receptor
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Traceable author statement. Source: Reactome cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW extracellular matrix organization Traceable author statement. Source: Reactome integrin-mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: InterPro muscle contraction Traceable author statement. Source: Reactome
Cellular_component	cell leading edge Inferred from electronic annotation. Source: Compara focal adhesion Inferred from electronic annotation. Source: Compara integrin complex Inferred from electronic annotation. Source: InterPro phagocytic vesicle Traceable author statement. Source: Reactome plasma membrane Traceable author statement. Source: Reactome
Molecular_function	receptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ANGPTL4	Q9BY76	3	EBI-1223434,EBI-2968146
ITGAV	P06756	2	EBI-1223434,EBI-298282

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Chain	24 – 799	776	Integrin beta-5		PRO_0000016348
Regions
	Topological domain	24 – 719	696	Extracellular Potential
	Transmembrane	720 – 742	23	Helical; Potential
	Topological domain	743 – 799	57	Cytoplasmic Potential
	Domain	27 – 76	50	PSI
	Domain	136 – 378	243	VWFA
	Repeat	465 – 512	48	I
	Repeat	513 – 554	42	II
	Repeat	555 – 593	39	III
	Repeat	594 – 630	37	IV
	Region	465 – 630	166	Cysteine-rich tandem repeats
Amino acid modifications
	Glycosylation	347	1	N-linked (GlcNAc...) Potential
	Glycosylation	460	1	N-linked (GlcNAc...) Potential
	Glycosylation	477	1	N-linked (GlcNAc...) Potential
	Glycosylation	505	1	N-linked (GlcNAc...) Potential
	Glycosylation	552	1	N-linked (GlcNAc...) Potential
	Glycosylation	586	1	N-linked (GlcNAc...) Potential
	Glycosylation	654	1	N-linked (GlcNAc...) Potential
	Glycosylation	705	1	N-linked (GlcNAc...) Potential
	Disulfide bond	28 ↔ 463		By similarity
	Disulfide bond	36 ↔ 46		By similarity
	Disulfide bond	39 ↔ 75		By similarity
	Disulfide bond	49 ↔ 64		By similarity
	Disulfide bond	202 ↔ 211		By similarity
	Disulfide bond	259 ↔ 300		By similarity
	Disulfide bond	401 ↔ 413		By similarity
	Disulfide bond	433 ↔ 682		By similarity
	Disulfide bond	461 ↔ 465		By similarity
	Disulfide bond	476 ↔ 487		By similarity
	Disulfide bond	484 ↔ 522		By similarity
	Disulfide bond	489 ↔ 498		By similarity
	Disulfide bond	500 ↔ 513		By similarity
	Disulfide bond	528 ↔ 533		By similarity
	Disulfide bond	530 ↔ 563		By similarity
	Disulfide bond	535 ↔ 548		By similarity
	Disulfide bond	550 ↔ 555		By similarity
	Disulfide bond	569 ↔ 574		By similarity
	Disulfide bond	571 ↔ 602		By similarity
	Disulfide bond	576 ↔ 585		By similarity
	Disulfide bond	587 ↔ 594		By similarity
	Disulfide bond	608 ↔ 613		By similarity
	Disulfide bond	610 ↔ 657		By similarity
	Disulfide bond	615 ↔ 625		By similarity
	Disulfide bond	628 ↔ 631		By similarity
	Disulfide bond	635 ↔ 644		By similarity
	Disulfide bond	641 ↔ 714		By similarity
	Disulfide bond	661 ↔ 690		By similarity
Natural variations
	Natural variant	428	1	L → V. Corresponds to variant rs2291090 [ dbSNP | Ensembl ].		VAR_024290
	Natural variant	431	1	R → Q. Ref.4 Corresponds to variant rs2291089 [ dbSNP | Ensembl ].		VAR_049634
	Natural variant	477	1	N → S. Corresponds to variant rs2291087 [ dbSNP | Ensembl ].		VAR_049635
Experimental info
	Sequence conflict	193	1	T → A in AAA52707. Ref.2
	Sequence conflict	645	1	L → P in AAA59183. Ref.3
	Sequence conflict	790 – 792	3	Missing in AAA52707. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P18084 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: D7E4727CA310512B	FASTA	799	88,054
	10 20 30 40 50 60 MPRAPAPLYA CLLGLCALLP RLAGLNICTS GSATSCEECL LIHPKCAWCS KEDFGSPRSI 70 80 90 100 110 120 TSRCDLRANL VKNGCGGEIE SPASSFHVLR SLPLSSKGSG SAGWDVIQMT PQEIAVNLRP 130 140 150 160 170 180 GDKTTFQLQV RQVEDYPVDL YYLMDLSLSM KDDLDNIRSL GTKLAEEMRK LTSNFRLGFG 190 200 210 220 230 240 SFVDKDISPF SYTAPRYQTN PCIGYKLFPN CVPSFGFRHL LPLTDRVDSF NEEVRKQRVS 250 260 270 280 290 300 RNRDAPEGGF DAVLQAAVCK EKIGWRKDAL HLLVFTTDDV PHIALDGKLG GLVQPHDGQC 310 320 330 340 350 360 HLNEANEYTA SNQMDYPSLA LLGEKLAENN INLIFAVTKN HYMLYKNFTA LIPGTTVEIL 370 380 390 400 410 420 DGDSKNIIQL IINAYNSIRS KVELSVWDQP EDLNLFFTAT CQDGVSYPGQ RKCEGLKIGD 430 440 450 460 470 480 TASFEVSLEA RSCPSRHTEH VFALRPVGFR DSLEVGVTYN CTCGCSVGLE PNSARCNGSG 490 500 510 520 530 540 TYVCGLCECS PGYLGTRCEC QDGENQSVYQ NLCREAEGKP LCSGRGDCSC NQCSCFESEF 550 560 570 580 590 600 GKIYGPFCEC DNFSCARNKG VLCSGHGECH CGECKCHAGY IGDNCNCSTD ISTCRGRDGQ 610 620 630 640 650 660 ICSERGHCLC GQCQCTEPGA FGEMCEKCPT CPDACSTKRD CVECLLLHSG KPDNQTCHSL 670 680 690 700 710 720 CRDEVITWVD TIVKDDQEAV LCFYKTAKDC VMMFTYVELP SGKSNLTVLR EPECGNTPNA 730 740 750 760 770 780 MTILLAVVGS ILLVGLALLA IWKLLVTIHD RREFAKFQSE RSRARYEMAS NPLYRKPIST 790 HTVDFTFNKF NKSYNGTVD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, primary structure and properties of a novel human integrin beta subunit." Ramaswamy H., Hemler M.E. EMBO J. 9:1561-1568(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Thymic epithelium.
[2]	"Cloning of an integrin beta subunit exhibiting high homology with integrin beta 3 subunit." Suzuki S., Huang Z.S., Tanihara H. Proc. Natl. Acad. Sci. U.S.A. 87:5354-5358(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"cDNA sequence of the human integrin beta 5 subunit." McLean J.W., Vestal D.J., Cheresh D.A., Bodary S.C. J. Biol. Chem. 265:17126-17131(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"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], VARIANT GLN-431. Tissue: Brain.
[5]	SeattleSNPs variation discovery resource Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [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]. Tissue: Kidney.
[7]	"Myosin-X provides a motor-based link between integrins and the cytoskeleton." Zhang H., Berg J.S., Li Z., Wang Y., Lang P., Sousa A.D., Bhaskar A., Cheney R.E., Stromblad S. Nat. Cell Biol. 6:523-531(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MYO10.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X53002 mRNA. Translation: CAA37188.1. M35011 mRNA. Translation: AAA52707.1. J05633 mRNA. Translation: AAA59183.1. AK315429 mRNA. Translation: BAG37817.1. EU332848 Genomic DNA. Translation: ABY87537.1. BC006541 mRNA. Translation: AAH06541.1.
IPI	IPI00029741.
PIR	A38308.
RefSeq	NP_002204.2. NM_002213.3.
UniGene	Hs.536663.
3D structure databases
ProteinModelPortal	P18084.
ModBase	Search...
Protein-protein interaction databases
IntAct	P18084. 15 interactions.
MINT	MINT-258539.
STRING	9606.ENSP00000296181.
PTM databases
PhosphoSite	P18084.
Polymorphism databases
DMDM	124970.
Proteomic databases
PaxDb	P18084.
PRIDE	P18084.
Protocols and materials databases
DNASU	3693.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000296181; ENSP00000296181; ENSG00000082781.
GeneID	3693.
KEGG	hsa:3693.
UCSC	uc003eho.3. human.
Organism-specific databases
CTD	3693.
GeneCards	GC03M124498.
HGNC	HGNC:6160. ITGB5.
HPA	CAB022050. HPA001820.
MIM	147561. gene.
neXtProt	NX_P18084.
PharmGKB	PA29959.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG287997.
HOGENOM	HOG000252936.
HOVERGEN	HBG006190.
InParanoid	P18084.
KO	K06588.
OMA	QNLCREA.
OrthoDB	EOG45TCMH.
PhylomeDB	P18084.
Enzyme and pathway databases
Pathway_Interaction_DB	smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
Reactome	REACT_111102. Signal Transduction. REACT_118779. Extracellular matrix organization. REACT_17044. Muscle contraction. REACT_6900. Immune System.
SignaLink	P18084.
Gene expression databases
ArrayExpress	P18084.
Bgee	P18084.
CleanEx	HS_ITGB5.
Genevestigator	P18084.
GermOnline	ENSG00000082781. Homo sapiens.
Family and domain databases
Gene3D	1.20.5.630. 1 hit. 3.40.50.410. 1 hit.
InterPro	IPR000742. EG-like_dom. IPR027067. Integrin_beta-5. IPR015812. Integrin_bsu. IPR014836. Integrin_bsu_cyt_dom. IPR002369. Integrin_bsu_N. IPR012896. Integrin_bsu_tail. IPR003659. Plexin-like. IPR016201. Plexin-like_fold. IPR002035. VWF_A. [Graphical view]
PANTHER	PTHR10082. PTHR10082. 1 hit. PTHR10082:SF26. PTHR10082:SF26. 1 hit.
Pfam	PF08725. Integrin_b_cyt. 1 hit. PF07965. Integrin_B_tail. 1 hit. PF00362. Integrin_beta. 1 hit. [Graphical view]
PIRSF	PIRSF002512. Integrin_B. 1 hit.
PRINTS	PR01186. INTEGRINB.
SMART	SM00181. EGF. 1 hit. SM00187. INB. 1 hit. SM00423. PSI. 1 hit. SM00327. VWA. 1 hit. [Graphical view]
SUPFAM	SSF69687. Integrin_bsu_tail. 1 hit. SSF103575. Plexin-like_fold. 1 hit.
PROSITE	PS00022. EGF_1. 2 hits. Uncertain. PS01186. EGF_2. 2 hits. Uncertain. PS00243. INTEGRIN_BETA. 2 hits. PS50234. VWFA. False negative. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P18084.
ChEMBL	CHEMBL2600.
ChiTaRS	ITGB5. human.
GenomeRNAi	3693.
NextBio	14473.
SOURCE	Search...

Entry information

Entry name

ITB5_HUMAN

Accession

Primary (citable) accession number: P18084
Secondary accession number(s): B0LPF8, B2RD70

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	May 29, 2013
This is version 144 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.