CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005726
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Receptor-type tyrosine-protein phosphatase mu 
Protein Synonyms/Alias
 Protein-tyrosine phosphatase mu; R-PTP-mu 
Gene Name
 Ptprm 
Gene Synonyms/Alias
 Kiaa4044 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
1373KLIRQVDKWQEEYNGubiquitination[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
 Involved in cell-cell adhesion through homophilic interactions. May play a key role in signal transduction and growth control. 
Sequence Annotation
 DOMAIN 22 184 MAM.
 DOMAIN 186 277 Ig-like C2-type.
 DOMAIN 281 371 Fibronectin type-III 1.
 DOMAIN 379 477 Fibronectin type-III 2.
 DOMAIN 482 581 Fibronectin type-III 3.
 DOMAIN 589 671 Fibronectin type-III 4.
 DOMAIN 900 1154 Tyrosine-protein phosphatase 1.
 DOMAIN 1186 1448 Tyrosine-protein phosphatase 2.
 REGION 1095 1101 Substrate binding (By similarity).
 ACT_SITE 1095 1095 Phosphocysteine intermediate (By
 ACT_SITE 1389 1389 Phosphocysteine intermediate (By
 BINDING 1063 1063 Substrate (By similarity).
 BINDING 1139 1139 Substrate (By similarity).
 MOD_RES 821 821 Phosphoserine (By similarity).
 CARBOHYD 72 72 N-linked (GlcNAc...) (Potential).
 CARBOHYD 92 92 N-linked (GlcNAc...) (Potential).
 CARBOHYD 131 131 N-linked (GlcNAc...) (Potential).
 CARBOHYD 249 249 N-linked (GlcNAc...) (Potential).
 CARBOHYD 406 406 N-linked (GlcNAc...) (Potential).
 CARBOHYD 414 414 N-linked (GlcNAc...) (Potential).
 CARBOHYD 454 454 N-linked (GlcNAc...) (Potential).
 CARBOHYD 534 534 N-linked (GlcNAc...) (Potential).
 CARBOHYD 544 544 N-linked (GlcNAc...) (Potential).
 CARBOHYD 598 598 N-linked (GlcNAc...) (Potential).
 CARBOHYD 651 651 N-linked (GlcNAc...) (Potential).
 CARBOHYD 681 681 N-linked (GlcNAc...) (Potential).
 DISULFID 27 36 By similarity.
 DISULFID 96 182 By similarity.
 DISULFID 206 260 By similarity.  
Keyword
 Cell adhesion; Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Immunoglobulin domain; Membrane; Phosphoprotein; Protein phosphatase; Receptor; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1452 AA 
Protein Sequence
MRTLGTCLVT LAGLLLTAAG ETFSGGCLFD EPYSTCGYSQ ADEDDFNWEQ VNTLTKPTSD 60
PWMPSGSFML VNTSGKPEGQ RAHLLLPQLK ENDTHCIDFH YFVSSKSNAA PGLLNVYVKV 120
NNGPLGNPIW NISGDPTRTW HRAELAISTF WPNFYQVIFE VVTSGHQGYL AIDEVKVLGH 180
PCTRTPHFLR IQNVEVNAGQ FATFQCSAIG RTVAGDRLWL QGIDVRDAPL KEIKVTSSRR 240
FIASFNVVNT TKRDAGKYRC MICTEGGVGI SNYAELVVKE PPVPIAPPQL ASVGATYLWI 300
QLNANSINGD GPIVAREVEY CTASGSWNDR QPVDSTSYKI GHLDPDTEYE ISVLLTRPGE 360
GGTGSPGPAL RTRTKCADPM RGPRKLEVVE VKSRQITIRW EPFGYNVTRC HSYNLTVHYG 420
YQVGGQEQVR EEVSWDTDNS HPQHTITNLS PYTNVSVKLI LMNPEGRKES QELTVQTDED 480
LPGAVPTESI QGSAFEEKIF LQWREPTQTY GVITLYEITY KAVSSFDPEI DLSNQSGRVS 540
KLGNETHFLF FGLYPGTTYS FTIRASTAKG FGPPATNQFT TKISAPSMPA YEFETPLNQT 600
DNTVTVMLKP AQSRGAPVSV YQIVVEEERP RRTKKTTEIL KCYPVPIHFQ NASILNSQYY 660
FAAEFPADSL QAAQPFTIGD NKTYNGYWNT PLLPHKSYRI YYQAASRANG ETKIDCVRVA 720
TKGAVTPKPV PEPEKQTDHT VKIAGVIAGI LLFVIIFLGV VLVMKKRKLA KKRKETMSST 780
RQEMTVMVNS MDKSYAEQGT NCDEAFSFMG THNLNGRSVS SPSSFTMKTN TLSTSVPNSY 840
YPDETHTMAS DTSSLAQPHT YKKREAADVP YQTGQLHPAI RVADLLQHIT QMKCAEGYGF 900
KEEYESFFEG QSAPWDSAKK DENRMKNRYG NIIAYDHSRV RLQMLEGDNN SDYINGNYID 960
GYHRPNHYIA TQGPMQETIY DFWRMVWHEN TASIIMVTNL VEVGRVKCCK YWPDDTEIYK 1020
DIKVTLIDTE LLAEYVIRTF AVEKRGIHEI REIRQFHFTG WPDHGVPYHA TGLLGFVRQV 1080
KSKSPPNAGP LVVHCSAGAG RTGCFIVIDI MLDMAEREGV VDIYNCVREL RSRRVNMVQT 1140
EEQYVFIHDA ILEACLCGDT SIPASQVRSL YYDMNKLDPQ TNSSQIKEEF RTLNMVTPTL 1200
RVEDCSIALL PRNHEKNRCM DILPPDRCLP FLITIDGESS NYINAALMDS YKQPSAFIVT 1260
QHPLPNTVKD FWRLVLDYHC TSVVMLNDVD PAQLCPQYWP ENGVHRHGPI QVEFVSADLE 1320
EDIISRIFRI YNASRPQDGH RMVQQFQFLG WPMYRDTPVS KRSFLKLIRQ VDKWQEEYNG 1380
GEGRTVVHCL NGGGRSGTFC AISIVCEMLR HQRTVDVFHA VKTLRNNKPN MVDLLDQYKF 1440
CYEVALEYLN SG 1452 
Gene Ontology
 GO:0005913; C:cell-cell adherens junction; ISS:UniProtKB.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0030027; C:lamellipodium; ISS:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
 GO:0045296; F:cadherin binding; ISS:UniProtKB.
 GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; ISS:UniProtKB.
 GO:0007156; P:homophilic cell adhesion; ISS:UniProtKB.
 GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
 GO:0010596; P:negative regulation of endothelial cell migration; ISS:UniProtKB.
 GO:0001937; P:negative regulation of endothelial cell proliferation; ISS:UniProtKB.
 GO:0045909; P:positive regulation of vasodilation; IMP:MGI.
 GO:0042493; P:response to drug; ISS:UniProtKB.
 GO:0010842; P:retina layer formation; ISS:UniProtKB.
 GO:0031290; P:retinal ganglion cell axon guidance; ISS:UniProtKB. 
Interpro
 IPR008985; ConA-like_lec_gl_sf.
 IPR003961; Fibronectin_type3.
 IPR007110; Ig-like_dom.
 IPR013783; Ig-like_fold.
 IPR003599; Ig_sub.
 IPR013151; Immunoglobulin.
 IPR000998; MAM_dom.
 IPR000387; Tyr/Dual-sp_Pase.
 IPR016130; Tyr_Pase_AS.
 IPR000242; Tyr_Pase_rcpt/non-rcpt. 
Pfam
 PF00041; fn3
 PF00047; ig
 PF00629; MAM
 PF00102; Y_phosphatase 
SMART
 SM00060; FN3
 SM00409; IG
 SM00137; MAM
 SM00194; PTPc 
PROSITE
 PS50853; FN3
 PS50835; IG_LIKE
 PS00740; MAM_1
 PS50060; MAM_2
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2
 PS50055; TYR_PHOSPHATASE_PTP 
PRINTS
 PR00020; MAMDOMAIN.
 PR00700; PRTYPHPHTASE.