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P10586

- PTPRF_HUMAN

UniProt

P10586 - PTPRF_HUMAN

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Protein

Receptor-type tyrosine-protein phosphatase F

Gene

PTPRF

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

Functioni

Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) and dephosphorylates EPHA2 regulating its activity.
The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1516 – 15161SubstrateBy similarity
Active sitei1548 – 15481Phosphocysteine intermediateCurated
Binding sitei1592 – 15921SubstrateBy similarity
Active sitei1839 – 18391Phosphocysteine intermediateBy similarity

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW
  2. protein tyrosine phosphatase activity Source: UniProtKB
  3. transmembrane receptor protein tyrosine phosphatase activity Source: ProtInc

GO - Biological processi

  1. cell adhesion Source: ProtInc
  2. cell migration Source: UniProtKB
  3. negative regulation of receptor binding Source: UniProtKB
  4. peptidyl-tyrosine dephosphorylation Source: UniProtKB
  5. transmembrane receptor protein tyrosine phosphatase signaling pathway Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase, Receptor

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

SignaLinkiP10586.

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-type tyrosine-protein phosphatase F (EC:3.1.3.48)
Alternative name(s):
Leukocyte common antigen related
Short name:
LAR
Gene namesi
Name:PTPRF
Synonyms:LAR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9670. PTPRF.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini30 – 12631234ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1264 – 128421HelicalSequence AnalysisAdd
BLAST
Topological domaini1285 – 1907623CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. integral component of plasma membrane Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1548 – 15481C → S: Loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA34015.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence AnalysisAdd
BLAST
Chaini30 – 19071878Receptor-type tyrosine-protein phosphatase FPRO_0000025432Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi54 ↔ 107PROSITE-ProRule annotation
Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi156 ↔ 207PROSITE-ProRule annotation
Glycosylationi250 – 2501N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi253 ↔ 298PROSITE-ProRule annotation
Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi721 – 7211N-linked (GlcNAc...)Sequence Analysis
Glycosylationi959 – 9591N-linked (GlcNAc...); atypical1 Publication
Glycosylationi966 – 9661N-linked (GlcNAc...)2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP10586.
PaxDbiP10586.
PRIDEiP10586.

PTM databases

PhosphoSiteiP10586.

Miscellaneous databases

PMAP-CutDBQ5T022.

Expressioni

Gene expression databases

BgeeiP10586.
CleanExiHS_PTPRF.
ExpressionAtlasiP10586. baseline and differential.
GenevestigatoriP10586.

Organism-specific databases

HPAiHPA012710.

Interactioni

Subunit structurei

Interacts with GRIP1 (By similarity). Interacts with PPFIA1, PPFIA2 and PPFIA3. Interacts with INSR.By similarity2 Publications

Protein-protein interaction databases

BioGridi111756. 20 interactions.
IntActiP10586. 6 interactions.
MINTiMINT-1189049.
STRINGi9606.ENSP00000353030.

Structurei

Secondary structure

1
1907
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 377Combined sources
Beta strandi42 – 454Combined sources
Beta strandi50 – 6011Combined sources
Beta strandi63 – 686Combined sources
Turni75 – 773Combined sources
Beta strandi78 – 836Combined sources
Helixi84 – 863Combined sources
Beta strandi88 – 936Combined sources
Helixi98 – 1014Combined sources
Beta strandi103 – 1119Combined sources
Beta strandi114 – 12512Combined sources
Helixi127 – 1293Combined sources
Beta strandi136 – 1394Combined sources
Beta strandi144 – 1474Combined sources
Beta strandi152 – 1543Combined sources
Beta strandi157 – 1593Combined sources
Beta strandi165 – 1706Combined sources
Helixi177 – 1793Combined sources
Beta strandi183 – 1864Combined sources
Beta strandi192 – 1943Combined sources
Helixi199 – 2013Combined sources
Beta strandi203 – 2119Combined sources
Beta strandi214 – 2174Combined sources
Beta strandi221 – 2266Combined sources
Beta strandi323 – 3319Combined sources
Beta strandi334 – 3407Combined sources
Beta strandi348 – 3569Combined sources
Beta strandi371 – 3788Combined sources
Beta strandi384 – 3929Combined sources
Beta strandi404 – 4074Combined sources
Beta strandi611 – 6199Combined sources
Beta strandi622 – 6287Combined sources
Helixi632 – 6343Combined sources
Beta strandi639 – 65214Combined sources
Beta strandi657 – 6637Combined sources
Beta strandi667 – 6715Combined sources
Beta strandi679 – 69012Combined sources
Beta strandi692 – 6954Combined sources
Beta strandi699 – 7024Combined sources
Beta strandi920 – 9234Combined sources
Beta strandi925 – 9273Combined sources
Beta strandi935 – 9373Combined sources
Beta strandi950 – 9578Combined sources
Beta strandi963 – 9719Combined sources
Beta strandi984 – 9874Combined sources
Helixi1334 – 134411Combined sources
Turni1347 – 13493Combined sources
Helixi1350 – 13589Combined sources
Helixi1368 – 13714Combined sources
Turni1373 – 13753Combined sources
Helixi1376 – 13783Combined sources
Turni1388 – 13903Combined sources
Turni1401 – 14044Combined sources
Beta strandi1407 – 14137Combined sources
Beta strandi1416 – 14238Combined sources
Turni1428 – 14303Combined sources
Helixi1431 – 144010Combined sources
Beta strandi1445 – 14484Combined sources
Beta strandi1452 – 14543Combined sources
Beta strandi1466 – 14727Combined sources
Beta strandi1475 – 148410Combined sources
Beta strandi1486 – 149712Combined sources
Beta strandi1503 – 15119Combined sources
Beta strandi1516 – 15183Combined sources
Helixi1524 – 153613Combined sources
Beta strandi1544 – 155310Combined sources
Helixi1554 – 157118Combined sources
Helixi1576 – 15849Combined sources
Helixi1594 – 161017Combined sources
Helixi1617 – 16193Combined sources
Helixi1620 – 16278Combined sources
Helixi1638 – 16447Combined sources
Turni1645 – 16473Combined sources
Turni1657 – 16604Combined sources
Helixi1662 – 16676Combined sources
Turni1677 – 16793Combined sources
Turni1690 – 16934Combined sources
Beta strandi1696 – 17005Combined sources
Beta strandi1703 – 17053Combined sources
Beta strandi1709 – 17124Combined sources
Helixi1717 – 17193Combined sources
Helixi1720 – 172910Combined sources
Beta strandi1734 – 17374Combined sources
Beta strandi1741 – 17433Combined sources
Beta strandi1746 – 17494Combined sources
Beta strandi1755 – 17573Combined sources
Beta strandi1759 – 17613Combined sources
Beta strandi1764 – 177310Combined sources
Beta strandi1775 – 178612Combined sources
Turni1787 – 17893Combined sources
Beta strandi1792 – 18009Combined sources
Beta strandi1805 – 18073Combined sources
Helixi1813 – 182816Combined sources
Beta strandi1835 – 184410Combined sources
Helixi1845 – 186218Combined sources
Beta strandi1863 – 18653Combined sources
Helixi1867 – 18748Combined sources
Turni1875 – 18773Combined sources
Helixi1885 – 190016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1LARX-ray2.00A/B1333-1907[»]
2DJUNMR-A319-411[»]
2DN7NMR-A821-914[»]
2EDXNMR-A596-716[»]
2EDYNMR-A915-1010[»]
2YD5X-ray2.20A29-231[»]
2YD8X-ray2.05A29-231[»]
4N5UX-ray1.46A601-705[»]
ProteinModelPortaliP10586.
SMRiP10586. Positions 30-1010, 1334-1902.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10586.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini33 – 12391Ig-like C2-type 1Add
BLAST
Domaini135 – 22490Ig-like C2-type 2Add
BLAST
Domaini232 – 31483Ig-like C2-type 3Add
BLAST
Domaini321 – 41191Fibronectin type-III 1PROSITE-ProRule annotationAdd
BLAST
Domaini416 – 51095Fibronectin type-III 2PROSITE-ProRule annotationAdd
BLAST
Domaini514 – 60491Fibronectin type-III 3PROSITE-ProRule annotationAdd
BLAST
Domaini609 – 70698Fibronectin type-III 4PROSITE-ProRule annotationAdd
BLAST
Domaini711 – 819109Fibronectin type-III 5PROSITE-ProRule annotationAdd
BLAST
Domaini820 – 91495Fibronectin type-III 6PROSITE-ProRule annotationAdd
BLAST
Domaini918 – 101093Fibronectin type-III 7PROSITE-ProRule annotationAdd
BLAST
Domaini1014 – 109885Fibronectin type-III 8PROSITE-ProRule annotationAdd
BLAST
Domaini1352 – 1607256Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
BLAST
Domaini1639 – 1898260Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni68 – 7710Heparin-bindingBy similarity
Regioni1548 – 15547Substrate bindingBy similarity

Sequence similaritiesi

Contains 8 fibronectin type-III domains.PROSITE-ProRule annotation
Contains 2 tyrosine-protein phosphatase domains.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00760000118900.
HOVERGENiHBG053758.
InParanoidiP10586.
KOiK05695.
OMAiVFTPTIE.
PhylomeDBiP10586.
TreeFamiTF312900.

Family and domain databases

Gene3Di2.60.40.10. 10 hits.
3.90.190.10. 2 hits.
InterProiIPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00041. fn3. 7 hits.
PF07679. I-set. 3 hits.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 8 hits.
SM00408. IGc2. 3 hits.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 5 hits.
SSF52799. SSF52799. 2 hits.
PROSITEiPS50853. FN3. 8 hits.
PS50835. IG_LIKE. 3 hits.
PS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 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: P10586-1) [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
MAPEPAPGRT MVPLVPALVM LGLVAGAHGD SKPVFIKVPE DQTGLSGGVA
60 70 80 90 100
SFVCQATGEP KPRITWMKKG KKVSSQRFEV IEFDDGAGSV LRIQPLRVQR
110 120 130 140 150
DEAIYECTAT NSLGEINTSA KLSVLEEEQL PPGFPSIDMG PQLKVVEKAR
160 170 180 190 200
TATMLCAAGG NPDPEISWFK DFLPVDPATS NGRIKQLRSG ALQIESSEES
210 220 230 240 250
DQGKYECVAT NSAGTRYSAP ANLYVRVRRV APRFSIPPSS QEVMPGGSVN
260 270 280 290 300
LTCVAVGAPM PYVKWMMGAE ELTKEDEMPV GRNVLELSNV VRSANYTCVA
310 320 330 340 350
ISSLGMIEAT AQVTVKALPK PPIDLVVTET TATSVTLTWD SGNSEPVTYY
360 370 380 390 400
GIQYRAAGTE GPFQEVDGVA TTRYSIGGLS PFSEYAFRVL AVNSIGRGPP
410 420 430 440 450
SEAVRARTGE QAPSSPPRRV QARMLSASTM LVQWEPPEEP NGLVRGYRVY
460 470 480 490 500
YTPDSRRPPN AWHKHNTDAG LLTTVGSLLP GITYSLRVLA FTAVGDGPPS
510 520 530 540 550
PTIQVKTQQG VPAQPADFQA EVESDTRIQL SWLLPPQERI IMYELVYWAA
560 570 580 590 600
EDEDQQHKVT FDPTSSYTLE DLKPDTLYRF QLAARSDMGV GVFTPTIEAR
610 620 630 640 650
TAQSTPSAPP QKVMCVSMGS TTVRVSWVPP PADSRNGVIT QYSVAYEAVD
660 670 680 690 700
GEDRGRHVVD GISREHSSWD LVGLEKWTEY RVWVRAHTDV GPGPESSPVL
710 720 730 740 750
VRTDEDVPSG PPRKVEVEPL NSTAVHVYWK LPVPSKQHGQ IRGYQVTYVR
760 770 780 790 800
LENGEPRGLP IIQDVMLAEA QWRPEESEDY ETTISGLTPE TTYSVTVAAY
810 820 830 840 850
TTKGDGARSK PKIVTTTGAV PGRPTMMIST TAMNTALLQW HPPKELPGEL
860 870 880 890 900
LGYRLQYCRA DEARPNTIDF GKDDQHFTVT GLHKGTTYIF RLAAKNRAGL
910 920 930 940 950
GEEFEKEIRT PEDLPSGFPQ NLHVTGLTTS TTELAWDPPV LAERNGRIIS
960 970 980 990 1000
YTVVFRDINS QQELQNITTD TRFTLTGLKP DTTYDIKVRA WTSKGSGPLS
1010 1020 1030 1040 1050
PSIQSRTMPV EQVFAKNFRV AAAMKTSVLL SWEVPDSYKS AVPFKILYNG
1060 1070 1080 1090 1100
QSVEVDGHSM RKLIADLQPN TEYSFVLMNR GSSAGGLQHL VSIRTAPDLL
1110 1120 1130 1140 1150
PHKPLPASAY IEDGRFDLSM PHVQDPSLVR WFYIVVVPID RVGGSMLTPR
1160 1170 1180 1190 1200
WSTPEELELD ELLEAIEQGG EEQRRRRRQA ERLKPYVAAQ LDVLPETFTL
1210 1220 1230 1240 1250
GDKKNYRGFY NRPLSPDLSY QCFVLASLKE PMDQKRYASS PYSDEIVVQV
1260 1270 1280 1290 1300
TPAQQQEEPE MLWVTGPVLA VILIILIVIA ILLFKRKRTH SPSSKDEQSI
1310 1320 1330 1340 1350
GLKDSLLAHS SDPVEMRRLN YQTPGMRDHP PIPITDLADN IERLKANDGL
1360 1370 1380 1390 1400
KFSQEYESID PGQQFTWENS NLEVNKPKNR YANVIAYDHS RVILTSIDGV
1410 1420 1430 1440 1450
PGSDYINANY IDGYRKQNAY IATQGPLPET MGDFWRMVWE QRTATVVMMT
1460 1470 1480 1490 1500
RLEEKSRVKC DQYWPARGTE TCGLIQVTLL DTVELATYTV RTFALHKSGS
1510 1520 1530 1540 1550
SEKRELRQFQ FMAWPDHGVP EYPTPILAFL RRVKACNPLD AGPMVVHCSA
1560 1570 1580 1590 1600
GVGRTGCFIV IDAMLERMKH EKTVDIYGHV TCMRSQRNYM VQTEDQYVFI
1610 1620 1630 1640 1650
HEALLEAATC GHTEVPARNL YAHIQKLGQV PPGESVTAME LEFKLLASSK
1660 1670 1680 1690 1700
AHTSRFISAN LPCNKFKNRL VNIMPYELTR VCLQPIRGVE GSDYINASFL
1710 1720 1730 1740 1750
DGYRQQKAYI ATQGPLAEST EDFWRMLWEH NSTIIVMLTK LREMGREKCH
1760 1770 1780 1790 1800
QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTIRQFQF
1810 1820 1830 1840 1850
TDWPEQGVPK TGEGFIDFIG QVHKTKEQFG QDGPITVHCS AGVGRTGVFI
1860 1870 1880 1890 1900
TLSIVLERMR YEGVVDMFQT VKTLRTQRPA MVQTEDQYQL CYRAALEYLG

SFDHYAT
Length:1,907
Mass (Da):212,879
Last modified:March 24, 2009 - v2
Checksum:i4A7C14A2090EA88F
GO
Isoform 2 (identifier: P10586-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     772-780: Missing.

Show »
Length:1,898
Mass (Da):211,687
Checksum:i5138123452E59A4E
GO

Sequence cautioni

The sequence BAD66835.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA68754.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti646 – 6461Y → H in CAA68754. (PubMed:2972792)Curated
Sequence conflicti1421 – 14211I → T in AAH48768. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti412 – 4121A → V.
Corresponds to variant rs1065775 [ dbSNP | Ensembl ].
VAR_054766
Natural varianti450 – 4501Y → C.
Corresponds to variant rs3748796 [ dbSNP | Ensembl ].
VAR_020299
Natural varianti562 – 5621D → N.
Corresponds to variant rs3748800 [ dbSNP | Ensembl ].
VAR_020300

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei772 – 7809Missing in isoform 2. 2 PublicationsVSP_036617

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00815 mRNA. Translation: CAA68754.1. Different initiation.
AB177857 mRNA. Translation: BAD66835.1. Different initiation.
AL583862, AC092815 Genomic DNA. Translation: CAI14894.1.
AL583862, AC092815 Genomic DNA. Translation: CAI14895.1.
CH471059 Genomic DNA. Translation: EAX07086.1.
CH471059 Genomic DNA. Translation: EAX07087.1.
CH471059 Genomic DNA. Translation: EAX07088.1.
CH471059 Genomic DNA. Translation: EAX07089.1.
BC048768 mRNA. Translation: AAH48768.1.
CCDSiCCDS489.2. [P10586-1]
CCDS490.2. [P10586-2]
PIRiS03841. TDHULK.
RefSeqiNP_002831.2. NM_002840.3. [P10586-1]
NP_569707.2. NM_130440.2. [P10586-2]
UniGeneiHs.272062.

Genome annotation databases

EnsembliENST00000359947; ENSP00000353030; ENSG00000142949. [P10586-1]
ENST00000438120; ENSP00000398822; ENSG00000142949. [P10586-2]
GeneIDi5792.
KEGGihsa:5792.
UCSCiuc001cjr.3. human. [P10586-1]
uc001cjs.3. human. [P10586-2]

Polymorphism databases

DMDMi226709091.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y00815 mRNA. Translation: CAA68754.1 . Different initiation.
AB177857 mRNA. Translation: BAD66835.1 . Different initiation.
AL583862 , AC092815 Genomic DNA. Translation: CAI14894.1 .
AL583862 , AC092815 Genomic DNA. Translation: CAI14895.1 .
CH471059 Genomic DNA. Translation: EAX07086.1 .
CH471059 Genomic DNA. Translation: EAX07087.1 .
CH471059 Genomic DNA. Translation: EAX07088.1 .
CH471059 Genomic DNA. Translation: EAX07089.1 .
BC048768 mRNA. Translation: AAH48768.1 .
CCDSi CCDS489.2. [P10586-1 ]
CCDS490.2. [P10586-2 ]
PIRi S03841. TDHULK.
RefSeqi NP_002831.2. NM_002840.3. [P10586-1 ]
NP_569707.2. NM_130440.2. [P10586-2 ]
UniGenei Hs.272062.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1LAR X-ray 2.00 A/B 1333-1907 [» ]
2DJU NMR - A 319-411 [» ]
2DN7 NMR - A 821-914 [» ]
2EDX NMR - A 596-716 [» ]
2EDY NMR - A 915-1010 [» ]
2YD5 X-ray 2.20 A 29-231 [» ]
2YD8 X-ray 2.05 A 29-231 [» ]
4N5U X-ray 1.46 A 601-705 [» ]
ProteinModelPortali P10586.
SMRi P10586. Positions 30-1010, 1334-1902.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111756. 20 interactions.
IntActi P10586. 6 interactions.
MINTi MINT-1189049.
STRINGi 9606.ENSP00000353030.

Chemistry

BindingDBi P10586.
ChEMBLi CHEMBL3521.

PTM databases

PhosphoSitei P10586.

Polymorphism databases

DMDMi 226709091.

Proteomic databases

MaxQBi P10586.
PaxDbi P10586.
PRIDEi P10586.

Protocols and materials databases

DNASUi 5792.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359947 ; ENSP00000353030 ; ENSG00000142949 . [P10586-1 ]
ENST00000438120 ; ENSP00000398822 ; ENSG00000142949 . [P10586-2 ]
GeneIDi 5792.
KEGGi hsa:5792.
UCSCi uc001cjr.3. human. [P10586-1 ]
uc001cjs.3. human. [P10586-2 ]

Organism-specific databases

CTDi 5792.
GeneCardsi GC01P043990.
HGNCi HGNC:9670. PTPRF.
HPAi HPA012710.
MIMi 179590. gene.
neXtProti NX_P10586.
PharmGKBi PA34015.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
GeneTreei ENSGT00760000118900.
HOVERGENi HBG053758.
InParanoidi P10586.
KOi K05695.
OMAi VFTPTIE.
PhylomeDBi P10586.
TreeFami TF312900.

Enzyme and pathway databases

SignaLinki P10586.

Miscellaneous databases

ChiTaRSi PTPRF. human.
EvolutionaryTracei P10586.
GeneWikii PTPRF.
GenomeRNAii 5792.
NextBioi 22550.
PMAP-CutDB Q5T022.
PROi P10586.
SOURCEi Search...

Gene expression databases

Bgeei P10586.
CleanExi HS_PTPRF.
ExpressionAtlasi P10586. baseline and differential.
Genevestigatori P10586.

Family and domain databases

Gene3Di 2.60.40.10. 10 hits.
3.90.190.10. 2 hits.
InterProi IPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
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. 7 hits.
PF07679. I-set. 3 hits.
PF00102. Y_phosphatase. 2 hits.
[Graphical view ]
PRINTSi PR00700. PRTYPHPHTASE.
SMARTi SM00060. FN3. 8 hits.
SM00408. IGc2. 3 hits.
SM00194. PTPc. 2 hits.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 5 hits.
SSF52799. SSF52799. 2 hits.
PROSITEi PS50853. FN3. 8 hits.
PS50835. IG_LIKE. 3 hits.
PS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A new member of the immunoglobulin superfamily that has a cytoplasmic region homologous to the leukocyte common antigen."
    Streuli M., Krueger N.X., Hall L.R., Schlossman S.F., Saito H.
    J. Exp. Med. 168:1523-1530(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Tonsil.
  2. "Alternative splice variants encoding unstable protein domains exist in the human brain."
    Homma K., Kikuno R.F., Nagase T., Ohara O., Nishikawa K.
    J. Mol. Biol. 343:1207-1220(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(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] (ISOFORM 2).
    Tissue: Retinoblastoma.
  6. "A family of receptor-linked protein tyrosine phosphatases in humans and Drosophila."
    Streuli M., Krueger N.X., Tsai A.Y.M., Saito H.
    Proc. Natl. Acad. Sci. U.S.A. 86:8698-8702(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  7. "Distinct functional roles of the two intracellular phosphatase like domains of the receptor-linked protein tyrosine phosphatases LCA and LAR."
    Streuli M., Krueger N.X., Thai T., Tang M., Saito H.
    EMBO J. 9:2399-2407(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  8. "Functional association between the insulin receptor and the transmembrane protein-tyrosine phosphatase LAR in intact cells."
    Ahmad F., Goldstein B.J.
    J. Biol. Chem. 272:448-457(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INSR.
  9. "Liprins, a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins."
    Serra-Pages C., Medley Q.G., Tang M., Hart A., Streuli M.
    J. Biol. Chem. 273:15611-15620(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPFIA1; PPFIA2 AND PPFIA3.
  10. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-966.
    Tissue: Plasma.
  11. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-959 AND ASN-966.
    Tissue: Leukemic T-cell.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Receptor protein tyrosine phosphatase-receptor tyrosine kinase substrate screen identifies EphA2 as a target for LAR in cell migration."
    Lee H., Bennett A.M.
    Mol. Cell. Biol. 33:1430-1441(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN EPHA2 DEPHOSPHORYLATION.
  14. "Crystal structure of the tandem phosphatase domains of RPTP LAR."
    Nam H.J., Poy F., Krueger N.X., Saito H., Frederick C.A.
    Cell 97:449-457(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1334-1897, FUNCTION, MUTAGENESIS OF CYS-1548.
  15. "Solution structures of FN3 domains of human receptor-type tyrosine-protein phosphatase F."
    RIKEN structural genomics initiative (RSGI)
    Submitted (AUG-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 319-415 AND 596-1010.

Entry informationi

Entry nameiPTPRF_HUMAN
AccessioniPrimary (citable) accession number: P10586
Secondary accession number(s): D3DPX6
, D3DPX7, Q5T021, Q5T022, Q5W9G2, Q86WS0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 24, 2009
Last modified: November 26, 2014
This is version 179 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 1
    Human chromosome 1: 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

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