P23467 (PTPRB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Receptor-type tyrosine-protein phosphatase beta
Short name=Protein-tyrosine phosphatase beta
Short name=R-PTP-beta
EC=3.1.3.48

Alternative name(s):
Vascular endothelial protein tyrosine phosphatase
Short name=VE-PTP

Gene names

Name:	PTPRB
Synonyms:	PTPB

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	1997 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	Plays an important role in blood vessel remodeling and angiogenesis. Not necessary for the initial formation of blood vessels, but is essential for their maintenance and remodeling. Can induce dephosphorylation of TEK/TIE2, CDH5/VE-cadherin and KDR/VEGFR-2. Regulates angiopoietin-TIE2 signaling in endothelial cells. Acts as a negative regulator of TIE2, and controls TIE2 driven endothelial cell proliferation, which in turn affects blood vessel remodeling during embryonic development and determines blood vessel size during perinatal growth. Essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells and this requires the presence of plakoglobin By similarity. Ref.7 Ref.8
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subunit structure	Monomer. Interacts with TEK. Interacts via fibronectin type-III 17 domain with CDH5 By similarity. Ref.9 Ref.10
Subcellular location	Membrane; Single-pass type I membrane protein Potential.
Induction	Up-regulated by hypoxia. Ref.7
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Receptor class 3 subfamily. Contains 17 fibronectin type-III domains. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Biological process	Angiogenesis
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Hydrolase Protein phosphatase
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	transmembrane receptor protein tyrosine phosphatase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ERBB2	P04626	2	EBI-1265766,EBI-641062
GHR	P10912	3	EBI-1265766,EBI-286316
TEK	Q02763	3	EBI-1265766,EBI-2257090

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P23467-1)

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: P23467-2)

The sequence of this isoform differs from the canonical sequence as follows:
     377-466: Missing.

Isoform 3 (identifier: P23467-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-18: MLSHGAGLALWITLSLLQ → MEAEFYMVIL...TQPFSSTTEE

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Potential

Chain

23 – 1997

1975

Receptor-type tyrosine-protein phosphatase beta

PRO_0000025436

Regions

Topological domain

23 – 1621

1599

Extracellular Potential

Transmembrane

1622 – 1642

21

Helical; Potential

Topological domain

1643 – 1997

355

Cytoplasmic Potential

Domain

23 – 108

86

Fibronectin type-III 1

Domain

110 – 201

92

Fibronectin type-III 2

Domain

203 – 288

86

Fibronectin type-III 3

Domain

289 – 375

87

Fibronectin type-III 4

Domain

377 – 465

89

Fibronectin type-III 5

Domain

467 – 552

86

Fibronectin type-III 6

Domain

554 – 641

88

Fibronectin type-III 7

Domain

643 – 730

88

Fibronectin type-III 8

Domain

731 – 817

87

Fibronectin type-III 9

Domain

819 – 906

88

Fibronectin type-III 10

Domain

907 – 993

87

Fibronectin type-III 11

Domain

995 – 1083

89

Fibronectin type-III 12

Domain

1085 – 1172

88

Fibronectin type-III 13

Domain

1173 – 1260

88

Fibronectin type-III 14

Domain

1261 – 1353

93

Fibronectin type-III 15

Domain

1355 – 1443

89

Fibronectin type-III 16

Domain

1448 – 1550

103

Fibronectin type-III 17

Domain

1703 – 1963

261

Tyrosine-protein phosphatase

Region

1904 – 1910

7

Substrate binding By similarity

Sites

Active site

1904

1

Phosphocysteine intermediate Ref.10

Binding site

1870

1

Substrate

Binding site

1948

1

Substrate By similarity

Amino acid modifications

Glycosylation

28

1

N-linked (GlcNAc...) Potential

Glycosylation

53

1

N-linked (GlcNAc...) Potential

Glycosylation

75

1

N-linked (GlcNAc...) Potential

Glycosylation

172

1

N-linked (GlcNAc...) Potential

Glycosylation

198

1

N-linked (GlcNAc...) Potential

Glycosylation

267

1

N-linked (GlcNAc...) Potential

Glycosylation

321

1

N-linked (GlcNAc...) Potential

Glycosylation

414

1

N-linked (GlcNAc...) Potential

Glycosylation

421

1

N-linked (GlcNAc...) Potential

Glycosylation

479

1

N-linked (GlcNAc...) Potential

Glycosylation

544

1

N-linked (GlcNAc...) Potential

Glycosylation

574

1

N-linked (GlcNAc...) Potential

Glycosylation

598

1

N-linked (GlcNAc...) Potential

Glycosylation

652

1

N-linked (GlcNAc...) Potential

Glycosylation

721

1

N-linked (GlcNAc...) Potential

Glycosylation

829

1

N-linked (GlcNAc...) Potential

Glycosylation

1040

1

N-linked (GlcNAc...) Potential

Glycosylation

1096

1

N-linked (GlcNAc...) Potential

Glycosylation

1163

1

N-linked (GlcNAc...) Potential

Glycosylation

1185

1

N-linked (GlcNAc...) Potential

Glycosylation

1212

1

N-linked (GlcNAc...) Potential

Glycosylation

1274

1

N-linked (GlcNAc...) Potential

Glycosylation

1367

1

N-linked (GlcNAc...) Potential

Glycosylation

1470

1

N-linked (GlcNAc...) Potential

Glycosylation

1474

1

N-linked (GlcNAc...) Potential

Glycosylation

1518

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

1 – 18

18

MLSHG…LSLLQ → MEAEFYMVILTCLIFRNSEG FQIVHVQKQQCLFKNEKVVV GSCNRTIQNQQWMWTEDEKL LHVKSALCLAISNSSRGPSR SAILDRCSQAPRWTCYDQEG FLEVENASLFLQKQGSRVVV KKARKYLHSWMKIDVNKEGK LVNESLCLQKAGLGAEVSVR STRNTAPPQILTTFNAVPDG LVFLIRNTTEAFIRNAAENY SQNSSERQHPNLHMTGITDT SWVLSTTQPFSSTTEE in isoform 3.

VSP_040484

Alternative sequence

377 – 466

90

Missing in isoform 2.

VSP_038521

Natural variant

94

1

R → K. Ref.1 Ref.5
Corresponds to variant rs2252784 [ dbSNP | Ensembl ].

VAR_062251

Natural variant

127

1

S → G. Ref.1
Corresponds to variant rs2465811 [ dbSNP | Ensembl ].

VAR_062252

Natural variant

395

1

V → A.
Corresponds to variant rs36027530 [ dbSNP | Ensembl ].

VAR_057135

Natural variant

415

1

D → E.
Corresponds to variant rs2165627 [ dbSNP | Ensembl ].

VAR_057136

Natural variant

939

1

T → M.
Corresponds to variant rs2304821 [ dbSNP | Ensembl ].

VAR_057137

Natural variant

1032

1

T → I.
Corresponds to variant rs34902691 [ dbSNP | Ensembl ].

VAR_057138

Natural variant

1934

1

G → A.
Corresponds to variant rs17226367 [ dbSNP | Ensembl ].

VAR_057139

Experimental info

Sequence conflict

261

1

T → S in CAA38066. Ref.1

Sequence conflict

666

1

L → V in CAA38066. Ref.1

Sequence conflict

926

1

V → A in BX648245. Ref.2

Sequence conflict

1559

1

C → R in CAA38066. Ref.1

Secondary structure

1

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1997

Helix Strand Turn

Details...

Helix

1685 – 1687

3

Helix

1688 – 1709

22

Turn

1710 – 1716

7

Turn

1720 – 1723

4

Helix

1728 – 1730

3

Helix

1740 – 1742

3

Beta strand

1743 – 1745

3

Helix

1753 – 1756

4

Beta strand

1757 – 1763

7

Beta strand

1766 – 1769

4

Beta strand

1771 – 1775

5

Turn

1780 – 1782

3

Helix

1783 – 1792

10

Beta strand

1797 – 1800

4

Beta strand

1804 – 1806

3

Beta strand

1818 – 1821

4

Beta strand

1823 – 1825

3

Beta strand

1828 – 1837

10

Beta strand

1839 – 1849

11

Beta strand

1856 – 1865

10

Beta strand

1870 – 1872

3

Helix

1877 – 1893

17

Beta strand

1894 – 1896

3

Beta strand

1900 – 1903

4

Beta strand

1905 – 1908

4

Helix

1909 – 1926

18

Beta strand

1928 – 1930

3

Helix

1932 – 1940

9

Helix

1950 – 1965

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 11, 2011. Version 3. Checksum: 76E67B4A6109AA0F	FASTA	1,997	224,301
	10 20 30 40 50 60 MLSHGAGLAL WITLSLLQTG LAEPERCNFT LAESKASSHS VSIQWRILGS PCNFSLIYSS 70 80 90 100 110 120 DTLGAALCPT FRIDNTTYGC NLQDLQAGTI YNFRIISLDE ERTVVLQTDP LPPARFGVSK 130 140 150 160 170 180 EKTTSTSLHV WWTPSSGKVT SYEVQLFDEN NQKIQGVQIQ ESTSWNEYTF FNLTAGSKYN 190 200 210 220 230 240 IAITAVSGGK RSFSVYTNGS TVPSPVKDIG ISTKANSLLI SWSHGSGNVE RYRLMLMDKG 250 260 270 280 290 300 ILVHGGVVDK HATSYAFHGL TPGYLYNLTV MTEAAGLQNY RWKLVRTAPM EVSNLKVTND 310 320 330 340 350 360 GSLTSLKVKW QRPPGNVDSY NITLSHKGTI KESRVLAPWI TETHFKELVP GRLYQVTVSC 370 380 390 400 410 420 VSGELSAQKM AVGRTFPDKV ANLEANNNGR MRSLVVSWSP PAGDWEQYRI LLFNDSVVLL 430 440 450 460 470 480 NITVGKEETQ YVMDDTGLVP GRQYEVEVIV ESGNLKNSER CQGRTVPLAV LQLRVKHANE 490 500 510 520 530 540 TSLSIMWQTP VAEWEKYIIS LADRDLLLIH KSLSKDAKEF TFTDLVPGRK YMATVTSISG 550 560 570 580 590 600 DLKNSSSVKG RTVPAQVTDL HVANQGMTSS LFTNWTQAQG DVEFYQVLLI HENVVIKNES 610 620 630 640 650 660 ISSETSRYSF HSLKSGSLYS VVVTTVSGGI SSRQVVVEGR TVPSSVSGVT VNNSGRNDYL 670 680 690 700 710 720 SVSWLLAPGD VDNYEVTLSH DGKVVQSLVI AKSVRECSFS SLTPGRLYTV TITTRSGKYE 730 740 750 760 770 780 NHSFSQERTV PDKVQGVSVS NSARSDYLRV SWVHATGDFD HYEVTIKNKN NFIQTKSIPK 790 800 810 820 830 840 SENECVFVQL VPGRLYSVTV TTKSGQYEAN EQGNGRTIPE PVKDLTLRNR STEDLHVTWS 850 860 870 880 890 900 GANGDVDQYE IQLLFNDMKV FPPFHLVNTA TEYRFTSLTP GRQYKILVLT ISGDVQQSAF 910 920 930 940 950 960 IEGFTVPSAV KNIHISPNGA TDSLTVNWTP GGGDVDSYTV SAFRHSQKVD SQTIPKHVFE 970 980 990 1000 1010 1020 HTFHRLEAGE QYQIMIASVS GSLKNQINVV GRTVPASVQG VIADNAYSSY SLIVSWQKAA 1030 1040 1050 1060 1070 1080 GVAERYDILL LTENGILLRN TSEPATTKQH KFEDLTPGKK YKIQILTVSG GLFSKEAQTE 1090 1100 1110 1120 1130 1140 GRTVPAAVTD LRITENSTRH LSFRWTASEG ELSWYNIFLY NPDGNLQERA QVDPLVQSFS 1150 1160 1170 1180 1190 1200 FQNLLQGRMY KMVIVTHSGE LSNESFIFGR TVPASVSHLR GSNRNTTDSL WFNWSPASGD 1210 1220 1230 1240 1250 1260 FDFYELILYN PNGTKKENWK DKDLTEWRFQ GLVPGRKYVL WVVTHSGDLS NKVTAESRTA 1270 1280 1290 1300 1310 1320 PSPPSLMSFA DIANTSLAIT WKGPPDWTDY NDFELQWLPR DALTVFNPYN NRKSEGRIVY 1330 1340 1350 1360 1370 1380 GLRPGRSYQF NVKTVSGDSW KTYSKPIFGS VRTKPDKIQN LHCRPQNSTA IACSWIPPDS 1390 1400 1410 1420 1430 1440 DFDGYSIECR KMDTQEVEFS RKLEKEKSLL NIMMLVPHKR YLVSIKVQSA GMTSEVVEDS 1450 1460 1470 1480 1490 1500 TITMIDRPPP PPPHIRVNEK DVLISKSSIN FTVNCSWFSD TNGAVKYFTV VVREADGSDE 1510 1520 1530 1540 1550 1560 LKPEQQHPLP SYLEYRHNAS IRVYQTNYFA SKCAENPNSN SKSFNIKLGA EMESLGGKCD 1570 1580 1590 1600 1610 1620 PTQQKFCDGP LKPHTAYRIS IRAFTQLFDE DLKEFTKPLY SDTFFSLPIT TESEPLFGAI 1630 1640 1650 1660 1670 1680 EGVSAGLFLI GMLVAVVALL ICRQKVSHGR ERPSARLSIR RDRPLSVHLN LGQKGNRKTS 1690 1700 1710 1720 1730 1740 CPIKINQFEG HFMKLQADSN YLLSKEYEEL KDVGRNQSCD IALLPENRGK NRYNNILPYD 1750 1760 1770 1780 1790 1800 ATRVKLSNVD DDPCSDYINA SYIPGNNFRR EYIVTQGPLP GTKDDFWKMV WEQNVHNIVM 1810 1820 1830 1840 1850 1860 VTQCVEKGRV KCDHYWPADQ DSLYYGDLIL QMLSESVLPE WTIREFKICG EEQLDAHRLI 1870 1880 1890 1900 1910 1920 RHFHYTVWPD HGVPETTQSL IQFVRTVRDY INRSPGAGPT VVHCSAGVGR TGTFIALDRI 1930 1940 1950 1960 1970 1980 LQQLDSKDSV DIYGAVHDLR LHRVHMVQTE CQYVYLHQCV RDVLRARKLR SEQENPLFPI 1990 YENVNPEYHR DPVYSRH
	Isoform 2 [UniParc]. Checksum: C8A61E610D7ECC31	FASTA	1,907	214,209
	10 20 30 40 50 60 MLSHGAGLAL WITLSLLQTG LAEPERCNFT LAESKASSHS VSIQWRILGS PCNFSLIYSS 70 80 90 100 110 120 DTLGAALCPT FRIDNTTYGC NLQDLQAGTI YNFRIISLDE ERTVVLQTDP LPPARFGVSK 130 140 150 160 170 180 EKTTSTSLHV WWTPSSGKVT SYEVQLFDEN NQKIQGVQIQ ESTSWNEYTF FNLTAGSKYN 190 200 210 220 230 240 IAITAVSGGK RSFSVYTNGS TVPSPVKDIG ISTKANSLLI SWSHGSGNVE RYRLMLMDKG 250 260 270 280 290 300 ILVHGGVVDK HATSYAFHGL TPGYLYNLTV MTEAAGLQNY RWKLVRTAPM EVSNLKVTND 310 320 330 340 350 360 GSLTSLKVKW QRPPGNVDSY NITLSHKGTI KESRVLAPWI TETHFKELVP GRLYQVTVSC 370 380 390 400 410 420 VSGELSAQKM AVGRTFPLAV LQLRVKHANE TSLSIMWQTP VAEWEKYIIS LADRDLLLIH 430 440 450 460 470 480 KSLSKDAKEF TFTDLVPGRK YMATVTSISG DLKNSSSVKG RTVPAQVTDL HVANQGMTSS 490 500 510 520 530 540 LFTNWTQAQG DVEFYQVLLI HENVVIKNES ISSETSRYSF HSLKSGSLYS VVVTTVSGGI 550 560 570 580 590 600 SSRQVVVEGR TVPSSVSGVT VNNSGRNDYL SVSWLLAPGD VDNYEVTLSH DGKVVQSLVI 610 620 630 640 650 660 AKSVRECSFS SLTPGRLYTV TITTRSGKYE NHSFSQERTV PDKVQGVSVS NSARSDYLRV 670 680 690 700 710 720 SWVHATGDFD HYEVTIKNKN NFIQTKSIPK SENECVFVQL VPGRLYSVTV TTKSGQYEAN 730 740 750 760 770 780 EQGNGRTIPE PVKDLTLRNR STEDLHVTWS GANGDVDQYE IQLLFNDMKV FPPFHLVNTA 790 800 810 820 830 840 TEYRFTSLTP GRQYKILVLT ISGDVQQSAF IEGFTVPSAV KNIHISPNGA TDSLTVNWTP 850 860 870 880 890 900 GGGDVDSYTV SAFRHSQKVD SQTIPKHVFE HTFHRLEAGE QYQIMIASVS GSLKNQINVV 910 920 930 940 950 960 GRTVPASVQG VIADNAYSSY SLIVSWQKAA GVAERYDILL LTENGILLRN TSEPATTKQH 970 980 990 1000 1010 1020 KFEDLTPGKK YKIQILTVSG GLFSKEAQTE GRTVPAAVTD LRITENSTRH LSFRWTASEG 1030 1040 1050 1060 1070 1080 ELSWYNIFLY NPDGNLQERA QVDPLVQSFS FQNLLQGRMY KMVIVTHSGE LSNESFIFGR 1090 1100 1110 1120 1130 1140 TVPASVSHLR GSNRNTTDSL WFNWSPASGD FDFYELILYN PNGTKKENWK DKDLTEWRFQ 1150 1160 1170 1180 1190 1200 GLVPGRKYVL WVVTHSGDLS NKVTAESRTA PSPPSLMSFA DIANTSLAIT WKGPPDWTDY 1210 1220 1230 1240 1250 1260 NDFELQWLPR DALTVFNPYN NRKSEGRIVY GLRPGRSYQF NVKTVSGDSW KTYSKPIFGS 1270 1280 1290 1300 1310 1320 VRTKPDKIQN LHCRPQNSTA IACSWIPPDS DFDGYSIECR KMDTQEVEFS RKLEKEKSLL 1330 1340 1350 1360 1370 1380 NIMMLVPHKR YLVSIKVQSA GMTSEVVEDS TITMIDRPPP PPPHIRVNEK DVLISKSSIN 1390 1400 1410 1420 1430 1440 FTVNCSWFSD TNGAVKYFTV VVREADGSDE LKPEQQHPLP SYLEYRHNAS IRVYQTNYFA 1450 1460 1470 1480 1490 1500 SKCAENPNSN SKSFNIKLGA EMESLGGKCD PTQQKFCDGP LKPHTAYRIS IRAFTQLFDE 1510 1520 1530 1540 1550 1560 DLKEFTKPLY SDTFFSLPIT TESEPLFGAI EGVSAGLFLI GMLVAVVALL ICRQKVSHGR 1570 1580 1590 1600 1610 1620 ERPSARLSIR RDRPLSVHLN LGQKGNRKTS CPIKINQFEG HFMKLQADSN YLLSKEYEEL 1630 1640 1650 1660 1670 1680 KDVGRNQSCD IALLPENRGK NRYNNILPYD ATRVKLSNVD DDPCSDYINA SYIPGNNFRR 1690 1700 1710 1720 1730 1740 EYIVTQGPLP GTKDDFWKMV WEQNVHNIVM VTQCVEKGRV KCDHYWPADQ DSLYYGDLIL 1750 1760 1770 1780 1790 1800 QMLSESVLPE WTIREFKICG EEQLDAHRLI RHFHYTVWPD HGVPETTQSL IQFVRTVRDY 1810 1820 1830 1840 1850 1860 INRSPGAGPT VVHCSAGVGR TGTFIALDRI LQQLDSKDSV DIYGAVHDLR LHRVHMVQTE 1870 1880 1890 1900 CQYVYLHQCV RDVLRARKLR SEQENPLFPI YENVNPEYHR DPVYSRH
	Isoform 3 [UniParc]. Checksum: 605BB45BA4541F02	FASTA	2,215	249,143
	10 20 30 40 50 60 MEAEFYMVIL TCLIFRNSEG FQIVHVQKQQ CLFKNEKVVV GSCNRTIQNQ QWMWTEDEKL 70 80 90 100 110 120 LHVKSALCLA ISNSSRGPSR SAILDRCSQA PRWTCYDQEG FLEVENASLF LQKQGSRVVV 130 140 150 160 170 180 KKARKYLHSW MKIDVNKEGK LVNESLCLQK AGLGAEVSVR STRNTAPPQI LTTFNAVPDG 190 200 210 220 230 240 LVFLIRNTTE AFIRNAAENY SQNSSERQHP NLHMTGITDT SWVLSTTQPF SSTTEETGLA 250 260 270 280 290 300 EPERCNFTLA ESKASSHSVS IQWRILGSPC NFSLIYSSDT LGAALCPTFR IDNTTYGCNL 310 320 330 340 350 360 QDLQAGTIYN FRIISLDEER TVVLQTDPLP PARFGVSKEK TTSTSLHVWW TPSSGKVTSY 370 380 390 400 410 420 EVQLFDENNQ KIQGVQIQES TSWNEYTFFN LTAGSKYNIA ITAVSGGKRS FSVYTNGSTV 430 440 450 460 470 480 PSPVKDIGIS TKANSLLISW SHGSGNVERY RLMLMDKGIL VHGGVVDKHA TSYAFHGLTP 490 500 510 520 530 540 GYLYNLTVMT EAAGLQNYRW KLVRTAPMEV SNLKVTNDGS LTSLKVKWQR PPGNVDSYNI 550 560 570 580 590 600 TLSHKGTIKE SRVLAPWITE THFKELVPGR LYQVTVSCVS GELSAQKMAV GRTFPDKVAN 610 620 630 640 650 660 LEANNNGRMR SLVVSWSPPA GDWEQYRILL FNDSVVLLNI TVGKEETQYV MDDTGLVPGR 670 680 690 700 710 720 QYEVEVIVES GNLKNSERCQ GRTVPLAVLQ LRVKHANETS LSIMWQTPVA EWEKYIISLA 730 740 750 760 770 780 DRDLLLIHKS LSKDAKEFTF TDLVPGRKYM ATVTSISGDL KNSSSVKGRT VPAQVTDLHV 790 800 810 820 830 840 ANQGMTSSLF TNWTQAQGDV EFYQVLLIHE NVVIKNESIS SETSRYSFHS LKSGSLYSVV 850 860 870 880 890 900 VTTVSGGISS RQVVVEGRTV PSSVSGVTVN NSGRNDYLSV SWLLAPGDVD NYEVTLSHDG 910 920 930 940 950 960 KVVQSLVIAK SVRECSFSSL TPGRLYTVTI TTRSGKYENH SFSQERTVPD KVQGVSVSNS 970 980 990 1000 1010 1020 ARSDYLRVSW VHATGDFDHY EVTIKNKNNF IQTKSIPKSE NECVFVQLVP GRLYSVTVTT 1030 1040 1050 1060 1070 1080 KSGQYEANEQ GNGRTIPEPV KDLTLRNRST EDLHVTWSGA NGDVDQYEIQ LLFNDMKVFP 1090 1100 1110 1120 1130 1140 PFHLVNTATE YRFTSLTPGR QYKILVLTIS GDVQQSAFIE GFTVPSAVKN IHISPNGATD 1150 1160 1170 1180 1190 1200 SLTVNWTPGG GDVDSYTVSA FRHSQKVDSQ TIPKHVFEHT FHRLEAGEQY QIMIASVSGS 1210 1220 1230 1240 1250 1260 LKNQINVVGR TVPASVQGVI ADNAYSSYSL IVSWQKAAGV AERYDILLLT ENGILLRNTS 1270 1280 1290 1300 1310 1320 EPATTKQHKF EDLTPGKKYK IQILTVSGGL FSKEAQTEGR TVPAAVTDLR ITENSTRHLS 1330 1340 1350 1360 1370 1380 FRWTASEGEL SWYNIFLYNP DGNLQERAQV DPLVQSFSFQ NLLQGRMYKM VIVTHSGELS 1390 1400 1410 1420 1430 1440 NESFIFGRTV PASVSHLRGS NRNTTDSLWF NWSPASGDFD FYELILYNPN GTKKENWKDK 1450 1460 1470 1480 1490 1500 DLTEWRFQGL VPGRKYVLWV VTHSGDLSNK VTAESRTAPS PPSLMSFADI ANTSLAITWK 1510 1520 1530 1540 1550 1560 GPPDWTDYND FELQWLPRDA LTVFNPYNNR KSEGRIVYGL RPGRSYQFNV KTVSGDSWKT 1570 1580 1590 1600 1610 1620 YSKPIFGSVR TKPDKIQNLH CRPQNSTAIA CSWIPPDSDF DGYSIECRKM DTQEVEFSRK 1630 1640 1650 1660 1670 1680 LEKEKSLLNI MMLVPHKRYL VSIKVQSAGM TSEVVEDSTI TMIDRPPPPP PHIRVNEKDV 1690 1700 1710 1720 1730 1740 LISKSSINFT VNCSWFSDTN GAVKYFTVVV READGSDELK PEQQHPLPSY LEYRHNASIR 1750 1760 1770 1780 1790 1800 VYQTNYFASK CAENPNSNSK SFNIKLGAEM ESLGGKCDPT QQKFCDGPLK PHTAYRISIR 1810 1820 1830 1840 1850 1860 AFTQLFDEDL KEFTKPLYSD TFFSLPITTE SEPLFGAIEG VSAGLFLIGM LVAVVALLIC 1870 1880 1890 1900 1910 1920 RQKVSHGRER PSARLSIRRD RPLSVHLNLG QKGNRKTSCP IKINQFEGHF MKLQADSNYL 1930 1940 1950 1960 1970 1980 LSKEYEELKD VGRNQSCDIA LLPENRGKNR YNNILPYDAT RVKLSNVDDD PCSDYINASY 1990 2000 2010 2020 2030 2040 IPGNNFRREY IVTQGPLPGT KDDFWKMVWE QNVHNIVMVT QCVEKGRVKC DHYWPADQDS 2050 2060 2070 2080 2090 2100 LYYGDLILQM LSESVLPEWT IREFKICGEE QLDAHRLIRH FHYTVWPDHG VPETTQSLIQ 2110 2120 2130 2140 2150 2160 FVRTVRDYIN RSPGAGPTVV HCSAGVGRTG TFIALDRILQ QLDSKDSVDI YGAVHDLRLH 2170 2180 2190 2200 2210 RVHMVQTECQ YVYLHQCVRD VLRARKLRSE QENPLFPIYE NVNPEYHRDP VYSRH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural diversity and evolution of human receptor-like protein tyrosine phosphatases." Krueger N.X., Streuli M., Saito H. EMBO J. 9:3241-3252(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS LYS-94 AND GLY-127. Tissue: Placenta.
[2]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Fetal kidney.
[3]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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. , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORMS 1 AND 2), VARIANT LYS-94. Tissue: Colon.
[6]	"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[7]	"Tyrosine phosphatase beta regulates angiopoietin-Tie2 signaling in human endothelial cells." Yacyshyn O.K., Lai P.F.H., Forse K., Teichert-Kuliszewska K., Jurasz P., Stewart D.J. Angiogenesis 12:25-33(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION.
[8]	"Transcriptional profiling reveals a critical role for tyrosine phosphatase VE-PTP in regulation of VEGFR2 activity and endothelial cell morphogenesis." Mellberg S., Dimberg A., Bahram F., Hayashi M., Rennel E., Ameur A., Westholm J.O., Larsson E., Lindahl P., Cross M.J., Claesson-Welsh L. FASEB J. 23:1490-1502(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"VE-PTP controls blood vessel development by balancing Tie-2 activity." Winderlich M., Keller L., Cagna G., Broermann A., Kamenyeva O., Kiefer F., Deutsch U., Nottebaum A.F., Vestweber D. J. Cell Biol. 185:657-671(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TEK.
[10]	"Engineering the catalytic domain of human protein tyrosine phosphatase beta for structure-based drug discovery." Evdokimov A.G., Pokross M., Walter R., Mekel M., Cox B., Li C., Bechard R., Genbauffe F., Andrews R., Diven C., Howard B., Rastogi V., Gray J., Maier M., Peters K.G. Acta Crystallogr. D 62:1435-1445(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 1676-1965 IN COMPLEX WITH INHIBITOR SULFAMIC ACID, SUBUNIT, ACTIVE SITE.
[11]	"Design and synthesis of potent, non-peptidic inhibitors of HPTPbeta." Amarasinghe K.K.D., Evdokimov A.G., Xu K., Clark C.M., Maier M.B., Srivastava A., Colson A.-O., Gerwe G.S., Stake G.E., Howard B.W., Pokross M.E., Gray J.L., Peters K.G. Bioorg. Med. Chem. Lett. 16:4252-4256(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1662-1973 IN COMPLEX WITH INHIBITOR SULFAMIC ACID.
[12]	"Large-scale structural analysis of the classical human protein tyrosine phosphatome." Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P., Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S. Cell 136:352-363(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1686-1971.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X54131 mRNA. Translation: CAA38066.1.
BX648245 mRNA. No translation available.
AC025569 Genomic DNA. No translation available.
AC083809 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW97254.1.
BC101679 mRNA. Translation: AAI01680.1.
BC113463 mRNA. Translation: AAI13464.1.
BC143360 mRNA. Translation: AAI43361.1.

IPI

IPI00745991.
IPI00943305.
IPI00954453.

PIR

S12050.

RefSeq

NP_001103224.1. NM_001109754.2.
NP_001193900.1. NM_001206971.1.
NP_001193901.1. NM_001206972.1.
NP_002828.3. NM_002837.4.

UniGene

Hs.434375.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AHS	X-ray	2.10	A/B	1686-1971	[»]
2H02	X-ray	2.30	A/B	1662-1973	[»]
2H03	X-ray	1.65	A	1676-1970	[»]
2H04	X-ray	2.30	A	1662-1973	[»]
2HC1	X-ray	1.30	A	1676-1965	[»]
2HC2	X-ray	1.40	A	1676-1965	[»]
2I3R	X-ray	1.85	A/B	1662-1973	[»]
2I3U	X-ray	1.85	A	1662-1973	[»]
2I4E	X-ray	1.75	A/B	1662-1973	[»]
2I4G	X-ray	1.65	A	1662-1973	[»]
2I4H	X-ray	2.15	A	1662-1973	[»]
2I5X	X-ray	1.70	A/B	1662-1973	[»]

ProteinModelPortal

P23467.

SMR

P23467. Positions 1687-1967.

ModBase

Search...

Protein-protein interaction databases

IntAct

P23467. 24 interactions.

MINT

MINT-1349770.

STRING

9606.ENSP00000334928.

PTM databases

PhosphoSite

P23467.

Polymorphism databases

DMDM

281185481.

Proteomic databases

PaxDb

P23467.

PRIDE

P23467.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261266; ENSP00000261266; ENSG00000127329.
ENST00000334414; ENSP00000334928; ENSG00000127329.
ENST00000550857; ENSP00000447302; ENSG00000127329.

GeneID

5787.

KEGG

hsa:5787.

UCSC

uc001swb.4. human.
uc001swc.4. human.
uc010stp.2. human.

Organism-specific databases

CTD

5787.

GeneCards

GC12M070910.

H-InvDB

HIX0017674.
HIX0037045.

HGNC

HGNC:9665. PTPRB.

HPA

CAB004782.

MIM

176882. gene.

neXtProt

NX_P23467.

PharmGKB

PA34010.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5599.

HOGENOM

HOG000060224.

HOVERGEN

HBG053759.

InParanoid

P23467.

KO

K05694.

OMA

FTVNCSW.

Gene expression databases

ArrayExpress

P23467.

Bgee

P23467.

CleanEx

HS_PTPRB.

Genevestigator

P23467.

GermOnline

ENSG00000127329. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 15 hits.

InterPro

IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]

Pfam

PF00041. fn3. 15 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]

PRINTS

PR00700. PRTYPHPHTASE.

SMART

SM00060. FN3. 17 hits.
SM00194. PTPc. 1 hit.
[Graphical view]

SUPFAM

SSF49265. FN_III-like. 16 hits.

PROSITE

PS50853. FN3. 17 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL2706.

ChiTaRS

PTPRB. human.

EvolutionaryTrace

P23467.

GenomeRNAi

5787.

NextBio

22514.

SOURCE

Search...

Entry information

Entry name

PTPRB_HUMAN

Accession

Primary (citable) accession number: P23467
Secondary accession number(s): B7ZKT0 , C9JX87, Q14D85, Q3MIV7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	January 11, 2011
Last modified:	April 3, 2013
This is version 134 of the entry and version 3 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.