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P10586

- PTPRF_HUMAN

UniProt

P10586 - PTPRF_HUMAN

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
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    • History
      Entry version 177 (01 Oct 2014)
      Sequence version 2 (24 Mar 2009)
      Previous versions | rss
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    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

    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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1548 – 15481C → S: Loss of activity. 3 Publications

    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

    ArrayExpressiP10586.
    BgeeiP10586.
    CleanExiHS_PTPRF.
    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. 16 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 – 377
    Beta strandi42 – 454
    Beta strandi50 – 6011
    Beta strandi63 – 686
    Turni75 – 773
    Beta strandi78 – 836
    Helixi84 – 863
    Beta strandi88 – 936
    Helixi98 – 1014
    Beta strandi103 – 1119
    Beta strandi114 – 12512
    Helixi127 – 1293
    Beta strandi136 – 1394
    Beta strandi144 – 1474
    Beta strandi152 – 1543
    Beta strandi157 – 1593
    Beta strandi165 – 1706
    Helixi177 – 1793
    Beta strandi183 – 1864
    Beta strandi192 – 1943
    Helixi199 – 2013
    Beta strandi203 – 2119
    Beta strandi214 – 2174
    Beta strandi221 – 2266
    Beta strandi323 – 3319
    Beta strandi334 – 3407
    Beta strandi348 – 3569
    Beta strandi371 – 3788
    Beta strandi384 – 3929
    Beta strandi404 – 4074
    Beta strandi611 – 6199
    Beta strandi622 – 6287
    Helixi632 – 6343
    Beta strandi639 – 65214
    Beta strandi657 – 6637
    Beta strandi667 – 6715
    Beta strandi679 – 69012
    Beta strandi692 – 6954
    Beta strandi699 – 7024
    Beta strandi920 – 9234
    Beta strandi925 – 9273
    Beta strandi935 – 9373
    Beta strandi950 – 9578
    Beta strandi963 – 9719
    Beta strandi984 – 9874
    Helixi1334 – 134411
    Turni1347 – 13493
    Helixi1350 – 13589
    Helixi1368 – 13714
    Turni1373 – 13753
    Helixi1376 – 13783
    Turni1388 – 13903
    Turni1401 – 14044
    Beta strandi1407 – 14137
    Beta strandi1416 – 14238
    Turni1428 – 14303
    Helixi1431 – 144010
    Beta strandi1445 – 14484
    Beta strandi1452 – 14543
    Beta strandi1466 – 14727
    Beta strandi1475 – 148410
    Beta strandi1486 – 149712
    Beta strandi1503 – 15119
    Beta strandi1516 – 15183
    Helixi1524 – 153613
    Beta strandi1544 – 155310
    Helixi1554 – 157118
    Helixi1576 – 15849
    Helixi1594 – 161017
    Helixi1617 – 16193
    Helixi1620 – 16278
    Helixi1638 – 16447
    Turni1645 – 16473
    Turni1657 – 16604
    Helixi1662 – 16676
    Turni1677 – 16793
    Turni1690 – 16934
    Beta strandi1696 – 17005
    Beta strandi1703 – 17053
    Beta strandi1709 – 17124
    Helixi1717 – 17193
    Helixi1720 – 172910
    Beta strandi1734 – 17374
    Beta strandi1741 – 17433
    Beta strandi1746 – 17494
    Beta strandi1755 – 17573
    Beta strandi1759 – 17613
    Beta strandi1764 – 177310
    Beta strandi1775 – 178612
    Turni1787 – 17893
    Beta strandi1792 – 18009
    Beta strandi1805 – 18073
    Helixi1813 – 182816
    Beta strandi1835 – 184410
    Helixi1845 – 186218
    Beta strandi1863 – 18653
    Helixi1867 – 18748
    Turni1875 – 18773
    Helixi1885 – 190016

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1264 – 128421HelicalSequence AnalysisAdd
    BLAST

    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.
    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

    MAPEPAPGRT MVPLVPALVM LGLVAGAHGD SKPVFIKVPE DQTGLSGGVA     50
    SFVCQATGEP KPRITWMKKG KKVSSQRFEV IEFDDGAGSV LRIQPLRVQR 100
    DEAIYECTAT NSLGEINTSA KLSVLEEEQL PPGFPSIDMG PQLKVVEKAR 150
    TATMLCAAGG NPDPEISWFK DFLPVDPATS NGRIKQLRSG ALQIESSEES 200
    DQGKYECVAT NSAGTRYSAP ANLYVRVRRV APRFSIPPSS QEVMPGGSVN 250
    LTCVAVGAPM PYVKWMMGAE ELTKEDEMPV GRNVLELSNV VRSANYTCVA 300
    ISSLGMIEAT AQVTVKALPK PPIDLVVTET TATSVTLTWD SGNSEPVTYY 350
    GIQYRAAGTE GPFQEVDGVA TTRYSIGGLS PFSEYAFRVL AVNSIGRGPP 400
    SEAVRARTGE QAPSSPPRRV QARMLSASTM LVQWEPPEEP NGLVRGYRVY 450
    YTPDSRRPPN AWHKHNTDAG LLTTVGSLLP GITYSLRVLA FTAVGDGPPS 500
    PTIQVKTQQG VPAQPADFQA EVESDTRIQL SWLLPPQERI IMYELVYWAA 550
    EDEDQQHKVT FDPTSSYTLE DLKPDTLYRF QLAARSDMGV GVFTPTIEAR 600
    TAQSTPSAPP QKVMCVSMGS TTVRVSWVPP PADSRNGVIT QYSVAYEAVD 650
    GEDRGRHVVD GISREHSSWD LVGLEKWTEY RVWVRAHTDV GPGPESSPVL 700
    VRTDEDVPSG PPRKVEVEPL NSTAVHVYWK LPVPSKQHGQ IRGYQVTYVR 750
    LENGEPRGLP IIQDVMLAEA QWRPEESEDY ETTISGLTPE TTYSVTVAAY 800
    TTKGDGARSK PKIVTTTGAV PGRPTMMIST TAMNTALLQW HPPKELPGEL 850
    LGYRLQYCRA DEARPNTIDF GKDDQHFTVT GLHKGTTYIF RLAAKNRAGL 900
    GEEFEKEIRT PEDLPSGFPQ NLHVTGLTTS TTELAWDPPV LAERNGRIIS 950
    YTVVFRDINS QQELQNITTD TRFTLTGLKP DTTYDIKVRA WTSKGSGPLS 1000
    PSIQSRTMPV EQVFAKNFRV AAAMKTSVLL SWEVPDSYKS AVPFKILYNG 1050
    QSVEVDGHSM RKLIADLQPN TEYSFVLMNR GSSAGGLQHL VSIRTAPDLL 1100
    PHKPLPASAY IEDGRFDLSM PHVQDPSLVR WFYIVVVPID RVGGSMLTPR 1150
    WSTPEELELD ELLEAIEQGG EEQRRRRRQA ERLKPYVAAQ LDVLPETFTL 1200
    GDKKNYRGFY NRPLSPDLSY QCFVLASLKE PMDQKRYASS PYSDEIVVQV 1250
    TPAQQQEEPE MLWVTGPVLA VILIILIVIA ILLFKRKRTH SPSSKDEQSI 1300
    GLKDSLLAHS SDPVEMRRLN YQTPGMRDHP PIPITDLADN IERLKANDGL 1350
    KFSQEYESID PGQQFTWENS NLEVNKPKNR YANVIAYDHS RVILTSIDGV 1400
    PGSDYINANY IDGYRKQNAY IATQGPLPET MGDFWRMVWE QRTATVVMMT 1450
    RLEEKSRVKC DQYWPARGTE TCGLIQVTLL DTVELATYTV RTFALHKSGS 1500
    SEKRELRQFQ FMAWPDHGVP EYPTPILAFL RRVKACNPLD AGPMVVHCSA 1550
    GVGRTGCFIV IDAMLERMKH EKTVDIYGHV TCMRSQRNYM VQTEDQYVFI 1600
    HEALLEAATC GHTEVPARNL YAHIQKLGQV PPGESVTAME LEFKLLASSK 1650
    AHTSRFISAN LPCNKFKNRL VNIMPYELTR VCLQPIRGVE GSDYINASFL 1700
    DGYRQQKAYI ATQGPLAEST EDFWRMLWEH NSTIIVMLTK LREMGREKCH 1750
    QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTIRQFQF 1800
    TDWPEQGVPK TGEGFIDFIG QVHKTKEQFG QDGPITVHCS AGVGRTGVFI 1850
    TLSIVLERMR YEGVVDMFQT VKTLRTQRPA MVQTEDQYQL CYRAALEYLG 1900
    SFDHYAT 1907
    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.
    The sequence CAA68754.1 differs from that shown. Reason: Erroneous initiation.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 16 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.
    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

    ArrayExpressi P10586.
    Bgeei P10586.
    CleanExi HS_PTPRF.
    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

    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: October 1, 2014
    This is version 177 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

    Dasty 3