Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P23467

- PTPRB_HUMAN

UniProt

P23467 - PTPRB_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Receptor-type tyrosine-protein phosphatase beta

Gene

PTPRB

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

Functioni

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).By similarity

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1870 – 18701Substrate
Active sitei1904 – 19041Phosphocysteine intermediate1 PublicationPROSITE-ProRule annotation
Binding sitei1948 – 19481SubstrateBy similarity

GO - Molecular functioni

  1. transmembrane receptor protein tyrosine phosphatase activity Source: ProtInc

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. dephosphorylation Source: UniProtKB
  3. peptidyl-tyrosine dephosphorylation Source: GOC
  4. phosphate-containing compound metabolic process Source: ProtInc
  5. protein dephosphorylation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Angiogenesis

Enzyme and pathway databases

SignaLinkiP23467.

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-type tyrosine-protein phosphatase beta (EC:3.1.3.48)
Short name:
Protein-tyrosine phosphatase beta
Short name:
R-PTP-beta
Alternative name(s):
Vascular endothelial protein tyrosine phosphatase
Short name:
VE-PTP
Gene namesi
Name:PTPRB
Synonyms:PTPB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:9665. PTPRB.

Subcellular locationi

GO - Cellular componenti

  1. integral component of plasma membrane Source: ProtInc
  2. receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34010.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 19971975Receptor-type tyrosine-protein phosphatase betaPRO_0000025436Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi28 – 281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi53 – 531N-linked (GlcNAc...)Sequence Analysis
Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi172 – 1721N-linked (GlcNAc...)Sequence Analysis
Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi267 – 2671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi414 – 4141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi421 – 4211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi479 – 4791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi544 – 5441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi574 – 5741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi598 – 5981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi652 – 6521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi721 – 7211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi829 – 8291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1040 – 10401N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1096 – 10961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1163 – 11631N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1185 – 11851N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1212 – 12121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1274 – 12741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1367 – 13671N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1470 – 14701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1474 – 14741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1518 – 15181N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP23467.
PRIDEiP23467.

PTM databases

PhosphoSiteiP23467.

Expressioni

Inductioni

Up-regulated by hypoxia.1 Publication

Gene expression databases

BgeeiP23467.
CleanExiHS_PTPRB.
ExpressionAtlasiP23467. baseline and differential.
GenevestigatoriP23467.

Organism-specific databases

HPAiCAB004782.

Interactioni

Subunit structurei

Monomer. Interacts with TEK. Interacts via fibronectin type-III 17 domain with CDH5 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ERBB2P046262EBI-1265766,EBI-641062
GHRP109123EBI-1265766,EBI-286316
MAPK3P273612EBI-1265766,EBI-73995
METP085812EBI-1265766,EBI-1039152
TEKQ027633EBI-1265766,EBI-2257090

Protein-protein interaction databases

BioGridi111751. 6 interactions.
IntActiP23467. 27 interactions.
MINTiMINT-1349770.
STRINGi9606.ENSP00000334928.

Structurei

Secondary structure

1
1997
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi1685 – 16873
Helixi1688 – 170922
Turni1710 – 17167
Turni1720 – 17234
Helixi1728 – 17303
Helixi1740 – 17423
Beta strandi1743 – 17453
Helixi1753 – 17564
Beta strandi1757 – 17637
Beta strandi1766 – 17694
Beta strandi1771 – 17755
Turni1780 – 17823
Helixi1783 – 179210
Beta strandi1797 – 18004
Beta strandi1804 – 18063
Beta strandi1818 – 18214
Beta strandi1823 – 18253
Beta strandi1828 – 183710
Beta strandi1839 – 184911
Beta strandi1856 – 186510
Beta strandi1870 – 18723
Helixi1877 – 189317
Beta strandi1894 – 18963
Beta strandi1900 – 19034
Beta strandi1905 – 19084
Helixi1909 – 192618
Beta strandi1928 – 19303
Helixi1932 – 19409
Helixi1950 – 196516

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AHSX-ray2.10A/B1686-1971[»]
2H02X-ray2.30A/B1662-1973[»]
2H03X-ray1.65A1676-1970[»]
2H04X-ray2.30A1662-1973[»]
2HC1X-ray1.30A1676-1965[»]
2HC2X-ray1.40A1676-1965[»]
2I3RX-ray1.85A/B1662-1973[»]
2I3UX-ray1.85A1662-1973[»]
2I4EX-ray1.75A/B1662-1973[»]
2I4GX-ray1.65A1662-1973[»]
2I4HX-ray2.15A1662-1973[»]
2I5XX-ray1.70A/B1662-1973[»]
ProteinModelPortaliP23467.
SMRiP23467. Positions 1687-1967.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23467.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 16211599ExtracellularSequence AnalysisAdd
BLAST
Topological domaini1643 – 1997355CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei1622 – 164221HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 11189Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini112 – 20796Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini203 – 28886Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini291 – 37888Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini379 – 47193Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini467 – 55286Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST
Domaini556 – 64186Fibronectin type-III 7PROSITE-ProRule annotationAdd
BLAST
Domaini642 – 72988Fibronectin type-III 8PROSITE-ProRule annotationAdd
BLAST
Domaini730 – 829100Fibronectin type-III 9PROSITE-ProRule annotationAdd
BLAST
Domaini819 – 90688Fibronectin type-III 10PROSITE-ProRule annotationAdd
BLAST
Domaini909 – 100193Fibronectin type-III 11PROSITE-ProRule annotationAdd
BLAST
Domaini995 – 108389Fibronectin type-III 12PROSITE-ProRule annotationAdd
BLAST
Domaini1087 – 117589Fibronectin type-III 13PROSITE-ProRule annotationAdd
BLAST
Domaini1173 – 126088Fibronectin type-III 14PROSITE-ProRule annotationAdd
BLAST
Domaini1260 – 135697Fibronectin type-III 15PROSITE-ProRule annotationAdd
BLAST
Domaini1357 – 144892Fibronectin type-III 16PROSITE-ProRule annotationAdd
BLAST
Domaini1458 – 155497Fibronectin type-III 17PROSITE-ProRule annotationAdd
BLAST
Domaini1703 – 1963261Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1904 – 19107Substrate bindingBy similarity

Sequence similaritiesi

Contains 17 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00760000118836.
HOGENOMiHOG000060224.
HOVERGENiHBG053759.
InParanoidiP23467.
KOiK05694.
OMAiPEQQHPL.
OrthoDBiEOG7PCJFZ.
PhylomeDBiP23467.
TreeFamiTF351926.

Family and domain databases

Gene3Di2.60.40.10. 15 hits.
3.90.190.10. 1 hit.
InterProiIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00041. fn3. 15 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 17 hits.
SM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 17 hits.
SSF52799. SSF52799. 1 hit.
PROSITEiPS50853. FN3. 12 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P23467-1) [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
MLSHGAGLAL WITLSLLQTG LAEPERCNFT LAESKASSHS VSIQWRILGS
60 70 80 90 100
PCNFSLIYSS DTLGAALCPT FRIDNTTYGC NLQDLQAGTI YNFRIISLDE
110 120 130 140 150
ERTVVLQTDP LPPARFGVSK EKTTSTSLHV WWTPSSGKVT SYEVQLFDEN
160 170 180 190 200
NQKIQGVQIQ ESTSWNEYTF FNLTAGSKYN IAITAVSGGK RSFSVYTNGS
210 220 230 240 250
TVPSPVKDIG ISTKANSLLI SWSHGSGNVE RYRLMLMDKG ILVHGGVVDK
260 270 280 290 300
HATSYAFHGL TPGYLYNLTV MTEAAGLQNY RWKLVRTAPM EVSNLKVTND
310 320 330 340 350
GSLTSLKVKW QRPPGNVDSY NITLSHKGTI KESRVLAPWI TETHFKELVP
360 370 380 390 400
GRLYQVTVSC VSGELSAQKM AVGRTFPDKV ANLEANNNGR MRSLVVSWSP
410 420 430 440 450
PAGDWEQYRI LLFNDSVVLL NITVGKEETQ YVMDDTGLVP GRQYEVEVIV
460 470 480 490 500
ESGNLKNSER CQGRTVPLAV LQLRVKHANE TSLSIMWQTP VAEWEKYIIS
510 520 530 540 550
LADRDLLLIH KSLSKDAKEF TFTDLVPGRK YMATVTSISG DLKNSSSVKG
560 570 580 590 600
RTVPAQVTDL HVANQGMTSS LFTNWTQAQG DVEFYQVLLI HENVVIKNES
610 620 630 640 650
ISSETSRYSF HSLKSGSLYS VVVTTVSGGI SSRQVVVEGR TVPSSVSGVT
660 670 680 690 700
VNNSGRNDYL SVSWLLAPGD VDNYEVTLSH DGKVVQSLVI AKSVRECSFS
710 720 730 740 750
SLTPGRLYTV TITTRSGKYE NHSFSQERTV PDKVQGVSVS NSARSDYLRV
760 770 780 790 800
SWVHATGDFD HYEVTIKNKN NFIQTKSIPK SENECVFVQL VPGRLYSVTV
810 820 830 840 850
TTKSGQYEAN EQGNGRTIPE PVKDLTLRNR STEDLHVTWS GANGDVDQYE
860 870 880 890 900
IQLLFNDMKV FPPFHLVNTA TEYRFTSLTP GRQYKILVLT ISGDVQQSAF
910 920 930 940 950
IEGFTVPSAV KNIHISPNGA TDSLTVNWTP GGGDVDSYTV SAFRHSQKVD
960 970 980 990 1000
SQTIPKHVFE HTFHRLEAGE QYQIMIASVS GSLKNQINVV GRTVPASVQG
1010 1020 1030 1040 1050
VIADNAYSSY SLIVSWQKAA GVAERYDILL LTENGILLRN TSEPATTKQH
1060 1070 1080 1090 1100
KFEDLTPGKK YKIQILTVSG GLFSKEAQTE GRTVPAAVTD LRITENSTRH
1110 1120 1130 1140 1150
LSFRWTASEG ELSWYNIFLY NPDGNLQERA QVDPLVQSFS FQNLLQGRMY
1160 1170 1180 1190 1200
KMVIVTHSGE LSNESFIFGR TVPASVSHLR GSNRNTTDSL WFNWSPASGD
1210 1220 1230 1240 1250
FDFYELILYN PNGTKKENWK DKDLTEWRFQ GLVPGRKYVL WVVTHSGDLS
1260 1270 1280 1290 1300
NKVTAESRTA PSPPSLMSFA DIANTSLAIT WKGPPDWTDY NDFELQWLPR
1310 1320 1330 1340 1350
DALTVFNPYN NRKSEGRIVY GLRPGRSYQF NVKTVSGDSW KTYSKPIFGS
1360 1370 1380 1390 1400
VRTKPDKIQN LHCRPQNSTA IACSWIPPDS DFDGYSIECR KMDTQEVEFS
1410 1420 1430 1440 1450
RKLEKEKSLL NIMMLVPHKR YLVSIKVQSA GMTSEVVEDS TITMIDRPPP
1460 1470 1480 1490 1500
PPPHIRVNEK DVLISKSSIN FTVNCSWFSD TNGAVKYFTV VVREADGSDE
1510 1520 1530 1540 1550
LKPEQQHPLP SYLEYRHNAS IRVYQTNYFA SKCAENPNSN SKSFNIKLGA
1560 1570 1580 1590 1600
EMESLGGKCD PTQQKFCDGP LKPHTAYRIS IRAFTQLFDE DLKEFTKPLY
1610 1620 1630 1640 1650
SDTFFSLPIT TESEPLFGAI EGVSAGLFLI GMLVAVVALL ICRQKVSHGR
1660 1670 1680 1690 1700
ERPSARLSIR RDRPLSVHLN LGQKGNRKTS CPIKINQFEG HFMKLQADSN
1710 1720 1730 1740 1750
YLLSKEYEEL KDVGRNQSCD IALLPENRGK NRYNNILPYD ATRVKLSNVD
1760 1770 1780 1790 1800
DDPCSDYINA SYIPGNNFRR EYIVTQGPLP GTKDDFWKMV WEQNVHNIVM
1810 1820 1830 1840 1850
VTQCVEKGRV KCDHYWPADQ DSLYYGDLIL QMLSESVLPE WTIREFKICG
1860 1870 1880 1890 1900
EEQLDAHRLI RHFHYTVWPD HGVPETTQSL IQFVRTVRDY INRSPGAGPT
1910 1920 1930 1940 1950
VVHCSAGVGR TGTFIALDRI LQQLDSKDSV DIYGAVHDLR LHRVHMVQTE
1960 1970 1980 1990
CQYVYLHQCV RDVLRARKLR SEQENPLFPI YENVNPEYHR DPVYSRH
Length:1,997
Mass (Da):224,301
Last modified:January 11, 2011 - v3
Checksum:i76E67B4A6109AA0F
GO
Isoform 2 (identifier: P23467-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,907
Mass (Da):214,209
Checksum:iC8A61E610D7ECC31
GO
Isoform 3 (identifier: P23467-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:2,215
Mass (Da):249,143
Checksum:i605BB45BA4541F02
GO
Isoform 4 (identifier: P23467-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     997-1086: Missing.

Show »
Length:1,907
Mass (Da):214,505
Checksum:i237BC55F05D696E7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti261 – 2611T → S in CAA38066. (PubMed:2170109)Curated
Sequence conflicti666 – 6661L → V in CAA38066. (PubMed:2170109)Curated
Sequence conflicti926 – 9261V → A in BX648245. (PubMed:17974005)Curated
Sequence conflicti1559 – 15591C → R in CAA38066. (PubMed:2170109)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti94 – 941R → K.2 Publications
Corresponds to variant rs2252784 [ dbSNP | Ensembl ].
VAR_062251
Natural varianti127 – 1271S → G.1 Publication
Corresponds to variant rs2465811 [ dbSNP | Ensembl ].
VAR_062252
Natural varianti395 – 3951V → A.
Corresponds to variant rs36027530 [ dbSNP | Ensembl ].
VAR_057135
Natural varianti415 – 4151D → E.
Corresponds to variant rs2165627 [ dbSNP | Ensembl ].
VAR_057136
Natural varianti939 – 9391T → M.
Corresponds to variant rs2304821 [ dbSNP | Ensembl ].
VAR_057137
Natural varianti1032 – 10321T → I.
Corresponds to variant rs34902691 [ dbSNP | Ensembl ].
VAR_057138
Natural varianti1934 – 19341G → A.
Corresponds to variant rs17226367 [ dbSNP | Ensembl ].
VAR_057139

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1818MLSHG…LSLLQ → MEAEFYMVILTCLIFRNSEG FQIVHVQKQQCLFKNEKVVV GSCNRTIQNQQWMWTEDEKL LHVKSALCLAISNSSRGPSR SAILDRCSQAPRWTCYDQEG FLEVENASLFLQKQGSRVVV KKARKYLHSWMKIDVNKEGK LVNESLCLQKAGLGAEVSVR STRNTAPPQILTTFNAVPDG LVFLIRNTTEAFIRNAAENY SQNSSERQHPNLHMTGITDT SWVLSTTQPFSSTTEE in isoform 3. 1 PublicationVSP_040484Add
BLAST
Alternative sequencei377 – 46690Missing in isoform 2. 1 PublicationVSP_038521Add
BLAST
Alternative sequencei997 – 108690Missing in isoform 4. 1 PublicationVSP_053944Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
BC143356 mRNA. Translation: AAI43357.1.
BC143360 mRNA. Translation: AAI43361.1.
CCDSiCCDS44943.1. [P23467-3]
CCDS44944.1. [P23467-1]
CCDS55845.1. [P23467-2]
CCDS55846.1. [P23467-4]
PIRiS12050.
RefSeqiNP_001103224.1. NM_001109754.2. [P23467-3]
NP_001193900.1. NM_001206971.1. [P23467-2]
NP_001193901.1. NM_001206972.1. [P23467-4]
NP_002828.3. NM_002837.4. [P23467-1]
UniGeneiHs.434375.

Genome annotation databases

GeneIDi5787.
KEGGihsa:5787.
UCSCiuc001swb.4. human. [P23467-1]
uc001swc.4. human. [P23467-3]
uc010stp.2. human. [P23467-2]

Polymorphism databases

DMDMi317373518.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
BC143356 mRNA. Translation: AAI43357.1 .
BC143360 mRNA. Translation: AAI43361.1 .
CCDSi CCDS44943.1. [P23467-3 ]
CCDS44944.1. [P23467-1 ]
CCDS55845.1. [P23467-2 ]
CCDS55846.1. [P23467-4 ]
PIRi S12050.
RefSeqi NP_001103224.1. NM_001109754.2. [P23467-3 ]
NP_001193900.1. NM_001206971.1. [P23467-2 ]
NP_001193901.1. NM_001206972.1. [P23467-4 ]
NP_002828.3. NM_002837.4. [P23467-1 ]
UniGenei Hs.434375.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P23467.
SMRi P23467. Positions 1687-1967.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111751. 6 interactions.
IntActi P23467. 27 interactions.
MINTi MINT-1349770.
STRINGi 9606.ENSP00000334928.

Chemistry

ChEMBLi CHEMBL2706.

PTM databases

PhosphoSitei P23467.

Polymorphism databases

DMDMi 317373518.

Proteomic databases

PaxDbi P23467.
PRIDEi P23467.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 5787.
KEGGi hsa:5787.
UCSCi uc001swb.4. human. [P23467-1 ]
uc001swc.4. human. [P23467-3 ]
uc010stp.2. human. [P23467-2 ]

Organism-specific databases

CTDi 5787.
GeneCardsi GC12M070910.
H-InvDB HIX0017674.
HIX0037045.
HGNCi HGNC:9665. PTPRB.
HPAi CAB004782.
MIMi 176882. gene.
neXtProti NX_P23467.
PharmGKBi PA34010.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
GeneTreei ENSGT00760000118836.
HOGENOMi HOG000060224.
HOVERGENi HBG053759.
InParanoidi P23467.
KOi K05694.
OMAi PEQQHPL.
OrthoDBi EOG7PCJFZ.
PhylomeDBi P23467.
TreeFami TF351926.

Enzyme and pathway databases

SignaLinki P23467.

Miscellaneous databases

ChiTaRSi PTPRB. human.
EvolutionaryTracei P23467.
GeneWikii PTPRB.
GenomeRNAii 5787.
NextBioi 22514.
PROi P23467.
SOURCEi Search...

Gene expression databases

Bgeei P23467.
CleanExi HS_PTPRB.
ExpressionAtlasi P23467. baseline and differential.
Genevestigatori P23467.

Family and domain databases

Gene3Di 2.60.40.10. 15 hits.
3.90.190.10. 1 hit.
InterProi IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view ]
Pfami PF00041. fn3. 15 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view ]
PRINTSi PR00700. PRTYPHPHTASE.
SMARTi SM00060. FN3. 17 hits.
SM00194. PTPc. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 17 hits.
SSF52799. SSF52799. 1 hit.
PROSITEi PS50853. FN3. 12 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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; 2 AND 4), 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. 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. 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.

Entry informationi

Entry nameiPTPRB_HUMAN
AccessioniPrimary (citable) accession number: P23467
Secondary accession number(s): B7ZKS8
, B7ZKT0, C9JX87, F5H3G6, Q14D85, Q3MIV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 11, 2011
Last modified: October 29, 2014
This is version 149 of the entry and version 3 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 12
    Human chromosome 12: 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