CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024612
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Receptor-type tyrosine-protein phosphatase S 
Protein Synonyms/Alias
 R-PTP-S; PTPNU-3; Receptor-type tyrosine-protein phosphatase sigma; R-PTP-sigma 
Gene Name
 Ptprs 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
1297KDSEPRTKCLLNNADubiquitination[1]
1376HSNLEANKPKNRYANubiquitination[1]
1644TGMELEFKRLASSKAubiquitination[1]
1810WPEQGAPKSGEGFIDubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Interacts with LAR-interacting protein LIP.1 (By similarity). 
Sequence Annotation
 DOMAIN 33 123 Ig-like C2-type 1.
 DOMAIN 135 224 Ig-like C2-type 2.
 DOMAIN 232 314 Ig-like C2-type 3.
 DOMAIN 319 407 Fibronectin type-III 1.
 DOMAIN 413 507 Fibronectin type-III 2.
 DOMAIN 512 600 Fibronectin type-III 3.
 DOMAIN 605 702 Fibronectin type-III 4.
 DOMAIN 707 806 Fibronectin type-III 5.
 DOMAIN 814 899 Fibronectin type-III 6.
 DOMAIN 904 1007 Fibronectin type-III 7.
 DOMAIN 1009 1092 Fibronectin type-III 8.
 DOMAIN 1352 1607 Tyrosine-protein phosphatase 1.
 DOMAIN 1639 1898 Tyrosine-protein phosphatase 2.
 REGION 1548 1554 Substrate binding (By similarity).
 ACT_SITE 1548 1548 Phosphocysteine intermediate (By
 ACT_SITE 1839 1839 Phosphocysteine intermediate (By
 BINDING 1516 1516 Substrate (By similarity).
 BINDING 1592 1592 Substrate (By similarity).
 CARBOHYD 250 250 N-linked (GlcNAc...) (Potential).
 CARBOHYD 295 295 N-linked (GlcNAc...) (Potential).
 CARBOHYD 720 720 N-linked (GlcNAc...) (Potential).
 CARBOHYD 916 916 N-linked (GlcNAc...) (Potential).
 DISULFID 54 107 By similarity.
 DISULFID 156 207 By similarity.
 DISULFID 253 298 By similarity.  
Keyword
 3D-structure; Alternative splicing; Cell adhesion; Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Immunoglobulin domain; Membrane; Protein phosphatase; Receptor; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1907 AA 
Protein Sequence
MAPTWSPSVV SVVGPVGLFL VLLARGCLAE EPPRFIREPK DQIGVSGGVA SFVCQATGDP 60
KPRVTWNKKG KKVNSQRFET IDFDESSGAV LRIQPLRTPR DENVYECVAQ NSVGEITIHA 120
KLTVLREDQL PPGFPNIDMG PQLKVVERTR TATMLCAASG NPDPEITWFK DFLPVDPSAS 180
NGRIKQLRSG ALQIESSEET DQGKYECVAT NSAGVRYSSP ANLYVRVRRV APRFSILPMS 240
HEIMPGGNVN ITCVAVGSPM PYVKWMQGAE DLTPEDDMPV GRNVLELTDV KDSANYTCVA 300
MSSLGVIEAV AQITVKSLPK APGTPVVTEN TATSITVTWD SGNPDPVSYY VIEYKSKSQD 360
GPYQIKEDIT TTRYSIGGLS PNSEYEIWVS AVNSIGQGPP SESVVTRTGE QAPASAPRNV 420
QARMLSATTM IVQWEEPVEP NGLIRGYRVY YTMEPEHPVG NWQKHNVDDS LLTTVGSLLE 480
DETYTVRVLA FTSVGDGPLS DPIQVKTQQG VPGQPMNLRA EAKSETSIGL SWSAPRQESV 540
IKYELLFREG DRGREVGRTF DPTTAFVVED LKPNTEYAFR LAARSPQGLG AFTAVVRQRT 600
LQAKPSAPPQ DVKCTSLRST AILVSWRPPP PETHNGALVG YSVRYRPLGS EDPDPKEVNN 660
IPPTTTQILL EALEKWTEYR VTAVAYTEVG PGPESSPVVV RTDEDVPSAP PRKVEAEALN 720
ATAIRVLWRS PTPGRQHGQI RGYQVHYVRM EGAEARGPPR IKDIMLADAQ EMVITNLQPE 780
TAYSITVAAY TMKGDGARSK PKVVVTKGAV LGRPTLSVQQ TPEGSLLARW EPPADAAEDP 840
VLGYRLQFGR EDAAPATLEL AAWERRFAAP AHKGATYVFR LAARGRAGLG EEAAAALSIP 900
EDAPRGFPQI LGAAGNVSAG SVLLRWLPPV PAERNGAIIK YTVSVREAGA PGPATETELA 960
AAAQPGAETA LTLRGLRPET AYELRVRAHT RRGPGPFSPP LRYRLARDPV SPKNFKVKMI 1020
MKTSVLLSWE FPDNYNSPTP YKIQYNGLTL DVDGRTTKKL ITHLKPHTFY NFVLTNRGSS 1080
LGGLQQTVTA RTAFNMLSGK PSVAPKPDND GFIVVYLPDG QSPVTVQNYF IVMVPLRKSR 1140
GGQFPVLLGS PEDMDLEELI QDISRLQRRS LRHSRQLEVP RPYIAARFSI LPAVFHPGNQ 1200
KQYGGFDNRG LEPGHRYVLF VLAVLQKNEP TFAASPFSDP FQLDNPDPQP IVDGEEGLIW 1260
VIGPVLAVVF IICIVIAILL YKNKPDSKRK DSEPRTKCLL NNADLAPHHP KDPVEMRRIN 1320
FQTPGMLSHP PIPITDMAEH MERLKANDSL KLSQEYESID PGQQFTWEHS NLEANKPKNR 1380
YANVIAYDHS RVILQPLEGI MGSDYINANY VDGYRRQNAY IATQGPLPET FGDFWRMVWE 1440
QRSATVVMMT RLEEKSRIKC DQYWPNRGTE TYGFIQVTLL DTMELATFCV RTFSLHKNGS 1500
SEKREVRHFQ FTAWPDHGVP EYPTPFLAFL RRVKTCNPPD AGPIVVHCSA GVGRTGCFIV 1560
IDAMLERIKT EKTVDVYGHV TLMRSQRNYM VQTEDQYGFI HEALLEAVGC GNTEVPARSL 1620
YTYIQKLAQV EPGEHVTGME LEFKRLASSK AHTSRFITAS LPCNKFKNRL VNILPYESSR 1680
VCLQPIRGVE GSDYINASFI DGYRQQKAYI ATQGPLAETT EDFWRALWEN NSTIVVMLTK 1740
LREMGREKCH QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTVRQFQF 1800
TDWPEQGAPK SGEGFIDFIG QVHKTKEQFG QDGPISVHCS AGVGRTGVFI TLSIVLERMR 1860
YEGVVDIFQT VKVLRTQRPA MVQTEDEYQF CFQAALEYLG SFDHYAT 1907 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0004725; F:protein tyrosine phosphatase activity; IEA:EC.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO:0021549; P:cerebellum development; IMP:MGI.
 GO:0021987; P:cerebral cortex development; IMP:MGI.
 GO:0022038; P:corpus callosum development; IMP:MGI.
 GO:0021766; P:hippocampus development; IMP:MGI.
 GO:0035335; P:peptidyl-tyrosine dephosphorylation; IEA:GOC.
 GO:0021510; P:spinal cord development; IMP:MGI. 
Interpro
 IPR003961; 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. 
Pfam
 PF00041; fn3
 PF07679; I-set
 PF00102; Y_phosphatase 
SMART
 SM00060; FN3
 SM00408; IGc2
 SM00194; PTPc 
PROSITE
 PS50853; FN3
 PS50835; IG_LIKE
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2
 PS50055; TYR_PHOSPHATASE_PTP 
PRINTS
 PR00700; PRTYPHPHTASE.