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P10586 (PTPRF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 172. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Receptor-type tyrosine-protein phosphatase F

EC=3.1.3.48
Alternative name(s):
Leukocyte common antigen related
Short name=LAR
Gene names
Name:PTPRF
Synonyms:LAR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1907 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase). Ref.13

The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Ref.13

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Interacts with GRIP1 By similarity. Interacts with PPFIA1, PPFIA2 and PPFIA3. Interacts with INSR. Ref.8 Ref.9

Subcellular location

Membrane; Single-pass type I membrane protein.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Receptor class 2A subfamily.

Contains 8 fibronectin type-III domains.

Contains 3 Ig-like C2-type (immunoglobulin-like) domains.

Contains 2 tyrosine-protein phosphatase domains.

Sequence caution

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

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P10586-1)

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: P10586-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Potential
Chain30 – 19071878Receptor-type tyrosine-protein phosphatase F
PRO_0000025432

Regions

Topological domain30 – 12631234Extracellular Potential
Transmembrane1264 – 128421Helical; Potential
Topological domain1285 – 1907623Cytoplasmic Potential
Domain33 – 12391Ig-like C2-type 1
Domain135 – 22490Ig-like C2-type 2
Domain232 – 31483Ig-like C2-type 3
Domain321 – 41191Fibronectin type-III 1
Domain416 – 51095Fibronectin type-III 2
Domain514 – 60491Fibronectin type-III 3
Domain609 – 70698Fibronectin type-III 4
Domain711 – 819109Fibronectin type-III 5
Domain820 – 91495Fibronectin type-III 6
Domain918 – 101093Fibronectin type-III 7
Domain1014 – 109885Fibronectin type-III 8
Domain1352 – 1607256Tyrosine-protein phosphatase 1
Domain1639 – 1898260Tyrosine-protein phosphatase 2
Region68 – 7710Heparin-binding By similarity
Region1548 – 15547Substrate binding By similarity

Sites

Active site15481Phosphocysteine intermediate Probable
Active site18391Phosphocysteine intermediate By similarity
Binding site15161Substrate By similarity
Binding site15921Substrate By similarity

Amino acid modifications

Glycosylation1171N-linked (GlcNAc...) Potential
Glycosylation2501N-linked (GlcNAc...) Potential
Glycosylation2951N-linked (GlcNAc...) Potential
Glycosylation7211N-linked (GlcNAc...) Potential
Glycosylation9591N-linked (GlcNAc...); atypical Ref.11
Glycosylation9661N-linked (GlcNAc...) Ref.10 Ref.11
Disulfide bond54 ↔ 107 By similarity
Disulfide bond156 ↔ 207 By similarity
Disulfide bond253 ↔ 298 By similarity

Natural variations

Alternative sequence772 – 7809Missing in isoform 2.
VSP_036617
Natural variant4121A → V.
Corresponds to variant rs1065775 [ dbSNP | Ensembl ].
VAR_054766
Natural variant4501Y → C.
Corresponds to variant rs3748796 [ dbSNP | Ensembl ].
VAR_020299
Natural variant5621D → N.
Corresponds to variant rs3748800 [ dbSNP | Ensembl ].
VAR_020300

Experimental info

Mutagenesis15481C → S: Loss of activity. Ref.13
Sequence conflict6461Y → H in CAA68754. Ref.1
Sequence conflict14211I → T in AAH48768. Ref.5

Secondary structure

.......................................................................................................................................................................................... 1907
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 24, 2009. Version 2.
Checksum: 4A7C14A2090EA88F

FASTA1,907212,879
        10         20         30         40         50         60 
MAPEPAPGRT MVPLVPALVM LGLVAGAHGD SKPVFIKVPE DQTGLSGGVA SFVCQATGEP 

        70         80         90        100        110        120 
KPRITWMKKG KKVSSQRFEV IEFDDGAGSV LRIQPLRVQR DEAIYECTAT NSLGEINTSA 

       130        140        150        160        170        180 
KLSVLEEEQL PPGFPSIDMG PQLKVVEKAR TATMLCAAGG NPDPEISWFK DFLPVDPATS 

       190        200        210        220        230        240 
NGRIKQLRSG ALQIESSEES DQGKYECVAT NSAGTRYSAP ANLYVRVRRV APRFSIPPSS 

       250        260        270        280        290        300 
QEVMPGGSVN LTCVAVGAPM PYVKWMMGAE ELTKEDEMPV GRNVLELSNV VRSANYTCVA 

       310        320        330        340        350        360 
ISSLGMIEAT AQVTVKALPK PPIDLVVTET TATSVTLTWD SGNSEPVTYY GIQYRAAGTE 

       370        380        390        400        410        420 
GPFQEVDGVA TTRYSIGGLS PFSEYAFRVL AVNSIGRGPP SEAVRARTGE QAPSSPPRRV 

       430        440        450        460        470        480 
QARMLSASTM LVQWEPPEEP NGLVRGYRVY YTPDSRRPPN AWHKHNTDAG LLTTVGSLLP 

       490        500        510        520        530        540 
GITYSLRVLA FTAVGDGPPS PTIQVKTQQG VPAQPADFQA EVESDTRIQL SWLLPPQERI 

       550        560        570        580        590        600 
IMYELVYWAA EDEDQQHKVT FDPTSSYTLE DLKPDTLYRF QLAARSDMGV GVFTPTIEAR 

       610        620        630        640        650        660 
TAQSTPSAPP QKVMCVSMGS TTVRVSWVPP PADSRNGVIT QYSVAYEAVD GEDRGRHVVD 

       670        680        690        700        710        720 
GISREHSSWD LVGLEKWTEY RVWVRAHTDV GPGPESSPVL VRTDEDVPSG PPRKVEVEPL 

       730        740        750        760        770        780 
NSTAVHVYWK LPVPSKQHGQ IRGYQVTYVR LENGEPRGLP IIQDVMLAEA QWRPEESEDY 

       790        800        810        820        830        840 
ETTISGLTPE TTYSVTVAAY TTKGDGARSK PKIVTTTGAV PGRPTMMIST TAMNTALLQW 

       850        860        870        880        890        900 
HPPKELPGEL LGYRLQYCRA DEARPNTIDF GKDDQHFTVT GLHKGTTYIF RLAAKNRAGL 

       910        920        930        940        950        960 
GEEFEKEIRT PEDLPSGFPQ NLHVTGLTTS TTELAWDPPV LAERNGRIIS YTVVFRDINS 

       970        980        990       1000       1010       1020 
QQELQNITTD TRFTLTGLKP DTTYDIKVRA WTSKGSGPLS PSIQSRTMPV EQVFAKNFRV 

      1030       1040       1050       1060       1070       1080 
AAAMKTSVLL SWEVPDSYKS AVPFKILYNG QSVEVDGHSM RKLIADLQPN TEYSFVLMNR 

      1090       1100       1110       1120       1130       1140 
GSSAGGLQHL VSIRTAPDLL PHKPLPASAY IEDGRFDLSM PHVQDPSLVR WFYIVVVPID 

      1150       1160       1170       1180       1190       1200 
RVGGSMLTPR WSTPEELELD ELLEAIEQGG EEQRRRRRQA ERLKPYVAAQ LDVLPETFTL 

      1210       1220       1230       1240       1250       1260 
GDKKNYRGFY NRPLSPDLSY QCFVLASLKE PMDQKRYASS PYSDEIVVQV TPAQQQEEPE 

      1270       1280       1290       1300       1310       1320 
MLWVTGPVLA VILIILIVIA ILLFKRKRTH SPSSKDEQSI GLKDSLLAHS SDPVEMRRLN 

      1330       1340       1350       1360       1370       1380 
YQTPGMRDHP PIPITDLADN IERLKANDGL KFSQEYESID PGQQFTWENS NLEVNKPKNR 

      1390       1400       1410       1420       1430       1440 
YANVIAYDHS RVILTSIDGV PGSDYINANY IDGYRKQNAY IATQGPLPET MGDFWRMVWE 

      1450       1460       1470       1480       1490       1500 
QRTATVVMMT RLEEKSRVKC DQYWPARGTE TCGLIQVTLL DTVELATYTV RTFALHKSGS 

      1510       1520       1530       1540       1550       1560 
SEKRELRQFQ FMAWPDHGVP EYPTPILAFL RRVKACNPLD AGPMVVHCSA GVGRTGCFIV 

      1570       1580       1590       1600       1610       1620 
IDAMLERMKH EKTVDIYGHV TCMRSQRNYM VQTEDQYVFI HEALLEAATC GHTEVPARNL 

      1630       1640       1650       1660       1670       1680 
YAHIQKLGQV PPGESVTAME LEFKLLASSK AHTSRFISAN LPCNKFKNRL VNIMPYELTR 

      1690       1700       1710       1720       1730       1740 
VCLQPIRGVE GSDYINASFL DGYRQQKAYI ATQGPLAEST EDFWRMLWEH NSTIIVMLTK 

      1750       1760       1770       1780       1790       1800 
LREMGREKCH QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTIRQFQF 

      1810       1820       1830       1840       1850       1860 
TDWPEQGVPK TGEGFIDFIG QVHKTKEQFG QDGPITVHCS AGVGRTGVFI TLSIVLERMR 

      1870       1880       1890       1900 
YEGVVDMFQT VKTLRTQRPA MVQTEDQYQL CYRAALEYLG SFDHYAT 

« Hide

Isoform 2 [UniParc].

Checksum: 5138123452E59A4E
Show »

FASTA1,898211,687

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]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. expand/collapse author list , 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 (SEP-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] (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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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.
[14]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRTDHULK. S03841.
RefSeqNP_002831.2. NM_002840.3.
NP_569707.2. NM_130440.2.
UniGeneHs.272062.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LARX-ray2.00A/B1334-1897[»]
2DJUNMR-A319-411[»]
2DN7NMR-A821-914[»]
2EDXNMR-A596-716[»]
2EDYNMR-A915-1010[»]
2YD5X-ray2.20A29-231[»]
2YD8X-ray2.05A29-231[»]
4N5UX-ray1.46A601-705[»]
ProteinModelPortalP10586.
SMRP10586. Positions 30-1010, 1334-1902.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111756. 15 interactions.
IntActP10586. 6 interactions.
MINTMINT-1189049.
STRING9606.ENSP00000353030.

Chemistry

BindingDBP10586.
ChEMBLCHEMBL3521.

PTM databases

PhosphoSiteP10586.

Polymorphism databases

DMDM226709091.

Proteomic databases

PaxDbP10586.
PRIDEP10586.

Protocols and materials databases

DNASU5792.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359947; ENSP00000353030; ENSG00000142949. [P10586-1]
ENST00000372413; ENSP00000361490; ENSG00000142949. [P10586-2]
ENST00000372414; ENSP00000361491; ENSG00000142949. [P10586-1]
ENST00000438120; ENSP00000398822; ENSG00000142949. [P10586-2]
GeneID5792.
KEGGhsa:5792.
UCSCuc001cjr.3. human. [P10586-1]
uc001cjs.3. human. [P10586-2]

Organism-specific databases

CTD5792.
GeneCardsGC01P043990.
HGNCHGNC:9670. PTPRF.
HPAHPA012710.
MIM179590. gene.
neXtProtNX_P10586.
PharmGKBPA34015.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOVERGENHBG053758.
InParanoidP10586.
KOK05695.
OMAVFTPTIE.
PhylomeDBP10586.
TreeFamTF312900.

Enzyme and pathway databases

SignaLinkP10586.

Gene expression databases

ArrayExpressP10586.
BgeeP10586.
CleanExHS_PTPRF.
GenevestigatorP10586.

Family and domain databases

Gene3D2.60.40.10. 10 hits.
InterProIPR003961. Fibronectin_type3.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00041. fn3. 7 hits.
PF07679. I-set. 3 hits.
PF00102. Y_phosphatase. 2 hits.
[Graphical view]
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00060. FN3. 8 hits.
SM00408. IGc2. 3 hits.
SM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMSSF49265. SSF49265. 5 hits.
PROSITEPS50853. 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]
ProtoNetSearch...

Other

ChiTaRSPTPRF. human.
EvolutionaryTraceP10586.
GeneWikiPTPRF.
GenomeRNAi5792.
NextBio22550.
PMAP-CutDBQ5T022.
PROP10586.
SOURCESearch...

Entry information

Entry namePTPRF_HUMAN
AccessionPrimary (citable) accession number: P10586
Secondary accession number(s): D3DPX6 expand/collapse secondary AC list , D3DPX7, Q5T021, Q5T022, Q5W9G2, Q86WS0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 24, 2009
Last modified: April 16, 2014
This is version 172 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM