CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003964
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cation-independent mannose-6-phosphate receptor 
Protein Synonyms/Alias
 CI Man-6-P receptor; CI-MPR; M6PR; 300 kDa mannose 6-phosphate receptor; MPR 300; Insulin-like growth factor 2 receptor; Insulin-like growth factor II receptor; IGF-II receptor; M6P/IGF2 receptor; M6P/IGF2R; CD222 
Gene Name
 IGF2R 
Gene Synonyms/Alias
 MPRI 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
89AVCMHDLKTRTYHSVubiquitination[1]
170KDIFKANKEVPCYVFubiquitination[1]
183VFDEELRKHDLNPLIubiquitination[1]
253GQPRDGLKLVRKDRLubiquitination[1]
481LCGATDGKKRYDLSAubiquitination[1]
482CGATDGKKRYDLSALubiquitination[1]
511GSQTETEKKHFFINIubiquitination[1]
512SQTETEKKHFFINICubiquitination[1]
546AVDKNGSKNLGKFISubiquitination[1]
557KFISSPMKEKGNIQLubiquitination[1]
687QVAKSDEKTWNLGLSubiquitination[1]
808GEHVTWRKYYINVCRubiquitination[1]
833YASACQMKYEKDQGSubiquitination[1]
1052DVYSGPLKFLHQDIDubiquitination[1]
1104TGLSTVRKPWTAVDTubiquitination[1]
1230EGDNCEVKDPRHGNLubiquitination[1]
1264YYFRVCGKLSSDVCPubiquitination[1]
1301VAGLLTQKLTYENGLubiquitination[1]
1776GVSMGTPKLLRTSECubiquitination[1]
1873FGRLQSMKLDYRHQDubiquitination[1]
2338RRETVISKLTTCCRRubiquitination[2]
2352RSSNVSYKYSKVNKEacetylation[3]
2352RSSNVSYKYSKVNKEubiquitination[1, 4, 5]
2383LPPPRQGKEGQENGHubiquitination[5]
2394ENGHITTKSVKALSSubiquitination[1, 2, 5]
2397HITTKSVKALSSLHGubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] 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]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional Description
 Transport of phosphorylated lysosomal enzymes from the Golgi complex and the cell surface to lysosomes. Lysosomal enzymes bearing phosphomannosyl residues bind specifically to mannose-6- phosphate receptors in the Golgi apparatus and the resulting receptor-ligand complex is transported to an acidic prelyosomal compartment where the low pH mediates the dissociation of the complex. This receptor also binds IGF2. Acts as a positive regulator of T-cell coactivation, by binding DPP4. 
Sequence Annotation
 REPEAT 40 189 1.
 REPEAT 190 344 2.
 REPEAT 345 489 3.
 REPEAT 490 643 4.
 REPEAT 644 783 5.
 REPEAT 784 950 6.
 REPEAT 951 1099 7.
 REPEAT 1100 1243 8.
 REPEAT 1244 1384 9.
 REPEAT 1385 1532 10.
 REPEAT 1533 1666 11.
 REPEAT 1667 1820 12.
 REPEAT 1821 2008 13.
 DOMAIN 1898 1944 Fibronectin type-II.
 REPEAT 2009 2137 14.
 REPEAT 2165 2289 15.
 MOD_RES 2352 2352 N6-acetyllysine.
 MOD_RES 2401 2401 Phosphoserine (By similarity).
 MOD_RES 2409 2409 Phosphoserine.
 MOD_RES 2479 2479 Phosphoserine.
 MOD_RES 2484 2484 Phosphoserine.
 CARBOHYD 112 112 N-linked (GlcNAc...).
 CARBOHYD 400 400 N-linked (GlcNAc...) (Potential).
 CARBOHYD 435 435 N-linked (GlcNAc...) (Potential).
 CARBOHYD 543 543 N-linked (GlcNAc...) (Potential).
 CARBOHYD 581 581 N-linked (GlcNAc...).
 CARBOHYD 626 626 N-linked (GlcNAc...).
 CARBOHYD 747 747 N-linked (GlcNAc...).
 CARBOHYD 871 871 N-linked (GlcNAc...) (Potential).
 CARBOHYD 951 951 N-linked (GlcNAc...) (Potential).
 CARBOHYD 957 957 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1164 1164 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1246 1246 N-linked (GlcNAc...).
 CARBOHYD 1312 1312 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1656 1656 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1757 1757 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1816 1816 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2085 2085 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2136 2136 N-linked (GlcNAc...) (Potential).
 DISULFID 49 69 By similarity.
 DISULFID 77 84 By similarity.
 DISULFID 117 149 By similarity.
 DISULFID 134 161 By similarity.
 DISULFID 174 212 By similarity.
 DISULFID 228 235 By similarity.
 DISULFID 275 306 By similarity.
 DISULFID 288 318 By similarity.
 DISULFID 328 366 By similarity.
 DISULFID 374 382 By similarity.
 DISULFID 420 454 By similarity.
 DISULFID 434 466 By similarity.
 DISULFID 627 664 By similarity.
 DISULFID 672 679 By similarity.
 DISULFID 731 760 By similarity.
 DISULFID 1516 1553
 DISULFID 1559 1566
 DISULFID 1598 1634
 DISULFID 1614 1646
 DISULFID 1652 1695
 DISULFID 1706 1713
 DISULFID 1750 1783
 DISULFID 1766 1795
 DISULFID 1804 1839
 DISULFID 1850 1856
 DISULFID 1893 1975
 DISULFID 1903 1927
 DISULFID 1917 1942
 DISULFID 1957 1987
 DISULFID 1994 2029
 DISULFID 2039 2046
 DISULFID 2082 2113
 DISULFID 2096 2125  
Keyword
 3D-structure; Acetylation; Complete proteome; Direct protein sequencing; Disulfide bond; Glycoprotein; Lysosome; Membrane; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2491 AA 
Protein Sequence
MGAAAGRSPH LGPAPARRPQ RSLLLLQLLL LVAAPGSTQA QAAPFPELCS YTWEAVDTKN 60
NVLYKINICG SVDIVQCGPS SAVCMHDLKT RTYHSVGDSV LRSATRSLLE FNTTVSCDQQ 120
GTNHRVQSSI AFLCGKTLGT PEFVTATECV HYFEWRTTAA CKKDIFKANK EVPCYVFDEE 180
LRKHDLNPLI KLSGAYLVDD SDPDTSLFIN VCRDIDTLRD PGSQLRACPP GTAACLVRGH 240
QAFDVGQPRD GLKLVRKDRL VLSYVREEAG KLDFCDGHSP AVTITFVCPS ERREGTIPKL 300
TAKSNCRYEI EWITEYACHR DYLESKTCSL SGEQQDVSID LTPLAQSGGS SYISDGKEYL 360
FYLNVCGETE IQFCNKKQAA VCQVKKSDTS QVKAAGRYHN QTLRYSDGDL TLIYFGGDEC 420
SSGFQRMSVI NFECNKTAGN DGKGTPVFTG EVDCTYFFTW DTEYACVKEK EDLLCGATDG 480
KKRYDLSALV RHAEPEQNWE AVDGSQTETE KKHFFINICH RVLQEGKARG CPEDAAVCAV 540
DKNGSKNLGK FISSPMKEKG NIQLSYSDGD DCGHGKKIKT NITLVCKPGD LESAPVLRTS 600
GEGGCFYEFE WHTAAACVLS KTEGENCTVF DSQAGFSFDL SPLTKKNGAY KVETKKYDFY 660
INVCGPVSVS PCQPDSGACQ VAKSDEKTWN LGLSNAKLSY YDGMIQLNYR GGTPYNNERH 720
TPRATLITFL CDRDAGVGFP EYQEEDNSTY NFRWYTSYAC PEEPLECVVT DPSTLEQYDL 780
SSLAKSEGGL GGNWYAMDNS GEHVTWRKYY INVCRPLNPV PGCNRYASAC QMKYEKDQGS 840
FTEVVSISNL GMAKTGPVVE DSGSLLLEYV NGSACTTSDG RQTTYTTRIH LVCSRGRLNS 900
HPIFSLNWEC VVSFLWNTEA ACPIQTTTDT DQACSIRDPN SGFVFNLNPL NSSQGYNVSG 960
IGKIFMFNVC GTMPVCGTIL GKPASGCEAE TQTEELKNWK PARPVGIEKS LQLSTEGFIT 1020
LTYKGPLSAK GTADAFIVRF VCNDDVYSGP LKFLHQDIDS GQGIRNTYFE FETALACVPS 1080
PVDCQVTDLA GNEYDLTGLS TVRKPWTAVD TSVDGRKRTF YLSVCNPLPY IPGCQGSAVG 1140
SCLVSEGNSW NLGVVQMSPQ AAANGSLSIM YVNGDKCGNQ RFSTRITFEC AQISGSPAFQ 1200
LQDGCEYVFI WRTVEACPVV RVEGDNCEVK DPRHGNLYDL KPLGLNDTIV SAGEYTYYFR 1260
VCGKLSSDVC PTSDKSKVVS SCQEKREPQG FHKVAGLLTQ KLTYENGLLK MNFTGGDTCH 1320
KVYQRSTAIF FYCDRGTQRP VFLKETSDCS YLFEWRTQYA CPPFDLTECS FKDGAGNSFD 1380
LSSLSRYSDN WEAITGTGDP EHYLINVCKS LAPQAGTEPC PPEAAACLLG GSKPVNLGRV 1440
RDGPQWRDGI IVLKYVDGDL CPDGIRKKST TIRFTCSESQ VNSRPMFISA VEDCEYTFAW 1500
PTATACPMKS NEHDDCQVTN PSTGHLFDLS SLSGRAGFTA AYSEKGLVYM SICGENENCP 1560
PGVGACFGQT RISVGKANKR LRYVDQVLQL VYKDGSPCPS KSGLSYKSVI SFVCRPEARP 1620
TNRPMLISLD KQTCTLFFSW HTPLACEQAT ECSVRNGSSI VDLSPLIHRT GGYEAYDESE 1680
DDASDTNPDF YINICQPLNP MHGVPCPAGA AVCKVPIDGP PIDIGRVAGP PILNPIANEI 1740
YLNFESSTPC LADKHFNYTS LIAFHCKRGV SMGTPKLLRT SECDFVFEWE TPVVCPDEVR 1800
MDGCTLTDEQ LLYSFNLSSL STSTFKVTRD SRTYSVGVCT FAVGPEQGGC KDGGVCLLSG 1860
TKGASFGRLQ SMKLDYRHQD EAVVLSYVNG DRCPPETDDG VPCVFPFIFN GKSYEECIIE 1920
SRAKLWCSTT ADYDRDHEWG FCRHSNSYRT SSIIFKCDED EDIGRPQVFS EVRGCDVTFE 1980
WKTKVVCPPK KLECKFVQKH KTYDLRLLSS LTGSWSLVHN GVSYYINLCQ KIYKGPLGCS 2040
ERASICRRTT TGDVQVLGLV HTQKLGVIGD KVVVTYSKGY PCGGNKTASS VIELTCTKTV 2100
GRPAFKRFDI DSCTYYFSWD SRAACAVKPQ EVQMVNGTIT NPINGKSFSL GDIYFKLFRA 2160
SGDMRTNGDN YLYEIQLSSI TSSRNPACSG ANICQVKPND QHFSRKVGTS DKTKYYLQDG 2220
DLDVVFASSS KCGKDKTKSV SSTIFFHCDP LVEDGIPEFS HETADCQYLF SWYTSAVCPL 2280
GVGFDSENPG DDGQMHKGLS ERSQAVGAVL SLLLVALTCC LLALLLYKKE RRETVISKLT 2340
TCCRRSSNVS YKYSKVNKEE ETDENETEWL MEEIQLPPPR QGKEGQENGH ITTKSVKALS 2400
SLHGDDQDSE DEVLTIPEVK VHSGRGAGAE SSHPVRNAQS NALQEREDDR VGLVRGEKAR 2460
KGKSSSAQQK TVSSTKLVSF HDDSDEDLLH I 2491 
Gene Ontology
 GO:0009986; C:cell surface; IDA:UniProtKB.
 GO:0030139; C:endocytic vesicle; IDA:UniProtKB.
 GO:0005768; C:endosome; IDA:MGI.
 GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
 GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
 GO:0005641; C:nuclear envelope lumen; IEA:Compara.
 GO:0030140; C:trans-Golgi network transport vesicle; IDA:MGI.
 GO:0001948; F:glycoprotein binding; IDA:UniProtKB.
 GO:0005010; F:insulin-like growth factor-activated receptor activity; TAS:ProtInc.
 GO:0005537; F:mannose binding; IEA:Compara.
 GO:0051219; F:phosphoprotein binding; IDA:UniProtKB.
 GO:0005215; F:transporter activity; IEA:InterPro.
 GO:0006898; P:receptor-mediated endocytosis; TAS:ProtInc. 
Interpro
 IPR000479; CIMR.
 IPR000562; FN_type2_col-bd.
 IPR013806; Kringle-like.
 IPR009011; Man6P_isomerase_rcpt-bd_dom. 
Pfam
 PF00878; CIMR
 PF00040; fn2 
SMART
 SM00059; FN2 
PROSITE
 PS00023; FN2_1
 PS51092; FN2_2 
PRINTS