CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-039493
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Receptor-type tyrosine-protein phosphatase F 
Protein Synonyms/Alias
  
Gene Name
 PTPRF 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
643RTHSPSSKDEQSIGLubiquitination[1, 2]
651DEQSIGLKDSLLAHSubiquitination[1, 2, 3, 4, 5]
735NSNLEVNKPKNRYANubiquitination[1]
1169WPEQGVPKTGEGFIDubiquitination[1, 2, 5]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Hydrolase; Protein phosphatase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1266 AA 
Protein Sequence
MYELVYWAAE DEDQQHKVTF DPTSSYTLED LKPDTLYRFQ LAARSDMGVG VFTPTIEART 60
AQSMPSGPPR KVEVEPLNST AVHVYWKLPV PSKQHGQIRG YQVTYVRLEN GEPRGLPIIQ 120
DVMLAEAQET TISGLTPETT YSVTVAAYTT KGDGARSKPK IVTTTGAVPG RPTMMISTTA 180
MNTALLQWHP PKELPGELLG YRLQYCRADE ARPNTIDFGK DDQHFTVTGL HKGTTYIFRL 240
AAKNRAGLGE EFEKEIRTPE DLPSGFPQNL HVTGLTTSTT ELAWDPPVLA ERNGRIISYT 300
VVFRDINSQQ ELQNITTDTR FTLTGLKPDT TYDIKVRAWT SKGSGPLSPS IQSRTMPVEQ 360
VFAKNFRVAA AMKTSVLLSW EVPDSYKSAV PFKILYNGQS VEVDGHSMRK LIADLQPNTE 420
YSFVLMNRGS SAGGLQHLVS IRTAPDLLPH KPLPASAYIE DGRFDLSMPH VQDPSLVRWF 480
YIVVVPIDRV GGSMLTPRWS TPEELELDEL LEAIEQGGEE QRRRRRQAER LKPYVAAQLD 540
VLPETFTLGD KKNYRGFYNR PLSPDLSYQC FVLASLKEPM DQKRYASSPY SDEIVVQVTP 600
AQQQEEPEML WVTGPVLAVI LIILIVIAIL LFKRKRTHSP SSKDEQSIGL KDSLLAHSSD 660
PVEMRRLNYQ TPGSSVPSCP NTSSMRDHPP IPITDLADNI ERLKANDGLK FSQEYESIDP 720
GQQFTWENSN LEVNKPKNRY ANVIAYDHSR VILTSIDGVP GSDYINANYI DGYRKQNAYI 780
ATQGPLPETM GDFWRMVWEQ RTATVVMMTR LEEKSRVKCD QYWPARGTET CGLIQVTLLD 840
TVELATYTVR TFALHKSGSS EKRELRQFQF MAWPDHGVPE YPTPILAFLR RVKACNPLDA 900
GPMVVHCSAG VGRTGCFIVI DAMLERMKHE KTVDIYGHVT CMRSQRNYMV QTEDQYVFIH 960
EALLEAATCG HTEVPARNLY AHIQKLGQVP PGESVTAMEL EFKLLASSKA HTSRFISANL 1020
PCNKFKNRLV NIMPYELTRV CLQPIRGVEG SDYINASFLD GYRQQKAYIA TQGPLAESTE 1080
DFWRMLWEHN STIIVMLTKL REMGREKCHQ YWPAERSARY QYFVVDPMAE YNMPQYILRE 1140
FKVTDARDGQ SRTIRQFQFT DWPEQGVPKT GEGFIDFIGQ VHKTKEQFGQ DGPITVHCSA 1200
GVGRTGVFIT LSIVLERMRY EGVVDMFQTV KTLRTQRPAM VQTEDQYQLC YRAALEYLGS 1260
FDHYAT 1266 
Gene Ontology
 GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
 GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC. 
Interpro
 IPR003961; Fibronectin_type3.
 IPR013783; Ig-like_fold.
 IPR000387; Tyr/Dual-sp_Pase.
 IPR016130; Tyr_Pase_AS.
 IPR000242; Tyr_Pase_rcpt/non-rcpt. 
Pfam
 PF00041; fn3
 PF00102; Y_phosphatase 
SMART
 SM00060; FN3
 SM00194; PTPc 
PROSITE
 PS50853; FN3
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2
 PS50055; TYR_PHOSPHATASE_PTP 
PRINTS
 PR00700; PRTYPHPHTASE.