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P11717 (MPRI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 160. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cation-independent mannose-6-phosphate receptor

Short name=CI Man-6-P receptor
Short name=CI-MPR
Short name=M6PR
Alternative name(s):
300 kDa mannose 6-phosphate receptor
Short name=MPR 300
Insulin-like growth factor 2 receptor
Insulin-like growth factor II receptor
Short name=IGF-II receptor
M6P/IGF2 receptor
Short name=M6P/IGF2R
CD_antigen=CD222
Gene names
Name:IGF2R
Synonyms:MPRI
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2491 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7

Subunit structure

Binds HA-I and HA-II plasma membrane adapters By similarity. Interacts with DPP4; the interaction is direct. Binds GGA1, GGA2 and GGA3. Ref.7 Ref.8

Subcellular location

Lysosome membrane; Single-pass type I membrane protein. Note: Colocalized with DPP4 in internalized cytoplasmic vesicles adjacent to the cell surface. Ref.7

Domain

Contains 15 repeating units of approximately 147 AA harboring four disulfide bonds each. The most highly conserved region within the repeat consists of a stretch of 13 AA that contains cysteines at both ends.

Sequence similarities

Belongs to the MRL1/IGF2R family.

Contains 1 fibronectin type-II domain.

Ontologies

Keywords
   Biological processTransport
   Cellular componentLysosome
Membrane
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMAcetylation
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processinsulin-like growth factor receptor signaling pathway

Traceable author statement PubMed 10799489. Source: GOC

liver development

Inferred from electronic annotation. Source: Ensembl

organ regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

receptor-mediated endocytosis

Traceable author statement PubMed 10799489. Source: ProtInc

response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement PubMed 7753549. Source: ProtInc

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from direct assay Ref.7. Source: UniProtKB

clathrin coat

Inferred from electronic annotation. Source: Ensembl

endocytic vesicle

Inferred from direct assay Ref.7. Source: UniProtKB

endosome

Inferred from direct assay PubMed 15078902. Source: MGI

extracellular space

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

integral component of plasma membrane

Traceable author statement PubMed 10799489. Source: ProtInc

late endosome

Inferred from electronic annotation. Source: Ensembl

lysosomal membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear envelope lumen

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

trans-Golgi network transport vesicle

Inferred from direct assay PubMed 15078902. Source: MGI

   Molecular_functionG-protein coupled receptor activity

Inferred from electronic annotation. Source: Ensembl

glycoprotein binding

Inferred from direct assay Ref.7. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 22681933. Source: IntAct

insulin-like growth factor-activated receptor activity

Traceable author statement PubMed 10799489. Source: ProtInc

mannose binding

Inferred from electronic annotation. Source: Ensembl

phosphoprotein binding

Inferred from direct assay Ref.7. Source: UniProtKB

receptor activity

Traceable author statement PubMed 7753549. Source: ProtInc

retinoic acid binding

Inferred from electronic annotation. Source: Ensembl

transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4040
Chain41 – 24912451Cation-independent mannose-6-phosphate receptor
PRO_0000019229

Regions

Topological domain41 – 23042264Lumenal Potential
Transmembrane2305 – 232723Helical; Potential
Topological domain2328 – 2491164Cytoplasmic Potential
Repeat40 – 1891501
Repeat190 – 3441552
Repeat345 – 4891453
Repeat490 – 6431544
Repeat644 – 7831405
Repeat784 – 9501676
Repeat951 – 10991497
Repeat1100 – 12431448
Repeat1244 – 13841419
Repeat1385 – 153214810
Repeat1533 – 166613411
Repeat1667 – 182015412
Repeat1821 – 200818813
Domain1898 – 194447Fibronectin type-II
Repeat2009 – 213712914
Repeat2165 – 228912515

Amino acid modifications

Modified residue23521N6-acetyllysine Ref.21
Modified residue24091Phosphoserine Ref.10 Ref.15 Ref.20 Ref.22 Ref.24
Modified residue24791Phosphoserine Ref.10 Ref.20 Ref.22
Modified residue24841Phosphoserine Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.19 Ref.20 Ref.22 Ref.24
Glycosylation1121N-linked (GlcNAc...) Ref.9
Glycosylation4001N-linked (GlcNAc...) Potential
Glycosylation4351N-linked (GlcNAc...) Potential
Glycosylation5431N-linked (GlcNAc...) Potential
Glycosylation5811N-linked (GlcNAc...) Ref.9
Glycosylation6261N-linked (GlcNAc...) Ref.18
Glycosylation7471N-linked (GlcNAc...) Ref.9 Ref.18
Glycosylation8711N-linked (GlcNAc...) Potential
Glycosylation9511N-linked (GlcNAc...) Potential
Glycosylation9571N-linked (GlcNAc...) Potential
Glycosylation11641N-linked (GlcNAc...) Potential
Glycosylation12461N-linked (GlcNAc...) Ref.9
Glycosylation13121N-linked (GlcNAc...) Potential
Glycosylation16561N-linked (GlcNAc...) Potential
Glycosylation17571N-linked (GlcNAc...) Potential
Glycosylation18161N-linked (GlcNAc...) Potential
Glycosylation20851N-linked (GlcNAc...) Potential
Glycosylation21361N-linked (GlcNAc...) Potential
Disulfide bond49 ↔ 69 By similarity
Disulfide bond77 ↔ 84 By similarity
Disulfide bond117 ↔ 149 By similarity
Disulfide bond134 ↔ 161 By similarity
Disulfide bond174 ↔ 212 By similarity
Disulfide bond228 ↔ 235 By similarity
Disulfide bond275 ↔ 306 By similarity
Disulfide bond288 ↔ 318 By similarity
Disulfide bond328 ↔ 366 By similarity
Disulfide bond374 ↔ 382 By similarity
Disulfide bond420 ↔ 454 By similarity
Disulfide bond434 ↔ 466 By similarity
Disulfide bond627 ↔ 664 By similarity
Disulfide bond672 ↔ 679 By similarity
Disulfide bond731 ↔ 760 By similarity
Disulfide bond1516 ↔ 1553 Ref.25
Disulfide bond1559 ↔ 1566 Ref.25
Disulfide bond1598 ↔ 1634 Ref.25
Disulfide bond1614 ↔ 1646 Ref.25
Disulfide bond1652 ↔ 1695 Ref.25
Disulfide bond1706 ↔ 1713 Ref.25
Disulfide bond1750 ↔ 1783 Ref.25
Disulfide bond1766 ↔ 1795 Ref.25
Disulfide bond1804 ↔ 1839 Ref.25
Disulfide bond1850 ↔ 1856 Ref.25
Disulfide bond1893 ↔ 1975 Ref.25
Disulfide bond1903 ↔ 1927 Ref.25
Disulfide bond1917 ↔ 1942 Ref.25
Disulfide bond1957 ↔ 1987 Ref.25
Disulfide bond1994 ↔ 2029 Ref.25
Disulfide bond2039 ↔ 2046 Ref.25
Disulfide bond2082 ↔ 2113 Ref.25
Disulfide bond2096 ↔ 2125 Ref.25

Natural variations

Natural variant911R → H. Ref.5
Corresponds to variant rs8191704 [ dbSNP | Ensembl ].
VAR_021304
Natural variant2031P → L. Ref.5
Corresponds to variant rs8191746 [ dbSNP | Ensembl ].
VAR_020470
Natural variant2311G → D. Ref.5
Corresponds to variant rs8191753 [ dbSNP | Ensembl ].
VAR_021305
Natural variant2521L → V. Ref.5
Corresponds to variant rs8191754 [ dbSNP | Ensembl ].
VAR_020471
Natural variant2731D → G. Ref.5
Corresponds to variant rs8191758 [ dbSNP | Ensembl ].
VAR_021306
Natural variant5121K → Q. Ref.5
Corresponds to variant rs8191776 [ dbSNP | Ensembl ].
VAR_021307
Natural variant5291R → Q.
Corresponds to variant rs6413489 [ dbSNP | Ensembl ].
VAR_020472
Natural variant6041G → S. Ref.5
Corresponds to variant rs8191797 [ dbSNP | Ensembl ].
VAR_020473
Natural variant7241A → T. Ref.5
Corresponds to variant rs6413491 [ dbSNP | Ensembl ].
VAR_020474
Natural variant8171L → V. Ref.5
Corresponds to variant rs8191808 [ dbSNP | Ensembl ].
VAR_021308
Natural variant8561G → S. Ref.5
Corresponds to variant rs8191819 [ dbSNP | Ensembl ].
VAR_020475
Natural variant11071T → M. Ref.5
Corresponds to variant rs8191842 [ dbSNP | Ensembl ].
VAR_020476
Natural variant11241V → I. Ref.5
Corresponds to variant rs8191843 [ dbSNP | Ensembl ].
VAR_021309
Natural variant11841T → S. Ref.5
Corresponds to variant rs8191844 [ dbSNP | Ensembl ].
VAR_020477
Natural variant12541E → A.
Corresponds to variant rs2230043 [ dbSNP | Ensembl ].
VAR_050428
Natural variant13151G → E. Ref.5
Corresponds to variant rs8191859 [ dbSNP | Ensembl ].
VAR_021310
Natural variant13351R → H. Ref.5
Corresponds to variant rs8191860 [ dbSNP | Ensembl ].
VAR_021311
Natural variant13951T → S.
Corresponds to variant rs2230048 [ dbSNP | Ensembl ].
VAR_050429
Natural variant16191R → G. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs629849 [ dbSNP | Ensembl ].
VAR_021312
Natural variant16961Q → R.
Corresponds to variant rs11552587 [ dbSNP | Ensembl ].
VAR_050430
Natural variant18321R → H. Ref.5
Corresponds to variant rs8191904 [ dbSNP | Ensembl ].
VAR_021313
Natural variant18601G → D. Ref.5
Corresponds to variant rs8191905 [ dbSNP | Ensembl ].
VAR_021314
Natural variant19081I → M. Ref.5
Corresponds to variant rs8191908 [ dbSNP | Ensembl ].
VAR_021315
Natural variant20201N → S. Ref.5
Corresponds to variant rs1805075 [ dbSNP | Ensembl ].
VAR_014722
Natural variant24591A → V. Ref.5
Corresponds to variant rs8191955 [ dbSNP | Ensembl ].
VAR_021316

Experimental info

Sequence conflict2541L → V in AAA59866. Ref.2
Sequence conflict5101E → K in AAA59866. Ref.2
Sequence conflict6121H → R in CAA68395. Ref.1
Sequence conflict6121H → R in AAF16870. Ref.3
Sequence conflict8451V → A in AAA59866. Ref.2
Sequence conflict14891S → N in AAA59866. Ref.2
Sequence conflict17031G → A in CAA68395. Ref.1
Sequence conflict17031G → A in AAF16870. Ref.3
Sequence conflict20261I → M in AAA59866. Ref.2
Sequence conflict20751T → M in AAA59866. Ref.2
Sequence conflict21561K → N in AAA59866. Ref.2
Sequence conflict21601A → E in AAA59866. Ref.2
Sequence conflict21761Q → L in AAA59866. Ref.2
Sequence conflict23301E → K in AAA59866. Ref.2
Sequence conflict23351V → M in AAA59866. Ref.2
Sequence conflict23411T → S in AAA59866. Ref.2
Sequence conflict24101E → T in AAA59866. Ref.2

Secondary structure

.............................................................................................................................................. 2491
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P11717 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: 3841ADE559B48057

FASTA2,491274,375
        10         20         30         40         50         60 
MGAAAGRSPH LGPAPARRPQ RSLLLLQLLL LVAAPGSTQA QAAPFPELCS YTWEAVDTKN 

        70         80         90        100        110        120 
NVLYKINICG SVDIVQCGPS SAVCMHDLKT RTYHSVGDSV LRSATRSLLE FNTTVSCDQQ 

       130        140        150        160        170        180 
GTNHRVQSSI AFLCGKTLGT PEFVTATECV HYFEWRTTAA CKKDIFKANK EVPCYVFDEE 

       190        200        210        220        230        240 
LRKHDLNPLI KLSGAYLVDD SDPDTSLFIN VCRDIDTLRD PGSQLRACPP GTAACLVRGH 

       250        260        270        280        290        300 
QAFDVGQPRD GLKLVRKDRL VLSYVREEAG KLDFCDGHSP AVTITFVCPS ERREGTIPKL 

       310        320        330        340        350        360 
TAKSNCRYEI EWITEYACHR DYLESKTCSL SGEQQDVSID LTPLAQSGGS SYISDGKEYL 

       370        380        390        400        410        420 
FYLNVCGETE IQFCNKKQAA VCQVKKSDTS QVKAAGRYHN QTLRYSDGDL TLIYFGGDEC 

       430        440        450        460        470        480 
SSGFQRMSVI NFECNKTAGN DGKGTPVFTG EVDCTYFFTW DTEYACVKEK EDLLCGATDG 

       490        500        510        520        530        540 
KKRYDLSALV RHAEPEQNWE AVDGSQTETE KKHFFINICH RVLQEGKARG CPEDAAVCAV 

       550        560        570        580        590        600 
DKNGSKNLGK FISSPMKEKG NIQLSYSDGD DCGHGKKIKT NITLVCKPGD LESAPVLRTS 

       610        620        630        640        650        660 
GEGGCFYEFE WHTAAACVLS KTEGENCTVF DSQAGFSFDL SPLTKKNGAY KVETKKYDFY 

       670        680        690        700        710        720 
INVCGPVSVS PCQPDSGACQ VAKSDEKTWN LGLSNAKLSY YDGMIQLNYR GGTPYNNERH 

       730        740        750        760        770        780 
TPRATLITFL CDRDAGVGFP EYQEEDNSTY NFRWYTSYAC PEEPLECVVT DPSTLEQYDL 

       790        800        810        820        830        840 
SSLAKSEGGL GGNWYAMDNS GEHVTWRKYY INVCRPLNPV PGCNRYASAC QMKYEKDQGS 

       850        860        870        880        890        900 
FTEVVSISNL GMAKTGPVVE DSGSLLLEYV NGSACTTSDG RQTTYTTRIH LVCSRGRLNS 

       910        920        930        940        950        960 
HPIFSLNWEC VVSFLWNTEA ACPIQTTTDT DQACSIRDPN SGFVFNLNPL NSSQGYNVSG 

       970        980        990       1000       1010       1020 
IGKIFMFNVC GTMPVCGTIL GKPASGCEAE TQTEELKNWK PARPVGIEKS LQLSTEGFIT 

      1030       1040       1050       1060       1070       1080 
LTYKGPLSAK GTADAFIVRF VCNDDVYSGP LKFLHQDIDS GQGIRNTYFE FETALACVPS 

      1090       1100       1110       1120       1130       1140 
PVDCQVTDLA GNEYDLTGLS TVRKPWTAVD TSVDGRKRTF YLSVCNPLPY IPGCQGSAVG 

      1150       1160       1170       1180       1190       1200 
SCLVSEGNSW NLGVVQMSPQ AAANGSLSIM YVNGDKCGNQ RFSTRITFEC AQISGSPAFQ 

      1210       1220       1230       1240       1250       1260 
LQDGCEYVFI WRTVEACPVV RVEGDNCEVK DPRHGNLYDL KPLGLNDTIV SAGEYTYYFR 

      1270       1280       1290       1300       1310       1320 
VCGKLSSDVC PTSDKSKVVS SCQEKREPQG FHKVAGLLTQ KLTYENGLLK MNFTGGDTCH 

      1330       1340       1350       1360       1370       1380 
KVYQRSTAIF FYCDRGTQRP VFLKETSDCS YLFEWRTQYA CPPFDLTECS FKDGAGNSFD 

      1390       1400       1410       1420       1430       1440 
LSSLSRYSDN WEAITGTGDP EHYLINVCKS LAPQAGTEPC PPEAAACLLG GSKPVNLGRV 

      1450       1460       1470       1480       1490       1500 
RDGPQWRDGI IVLKYVDGDL CPDGIRKKST TIRFTCSESQ VNSRPMFISA VEDCEYTFAW 

      1510       1520       1530       1540       1550       1560 
PTATACPMKS NEHDDCQVTN PSTGHLFDLS SLSGRAGFTA AYSEKGLVYM SICGENENCP 

      1570       1580       1590       1600       1610       1620 
PGVGACFGQT RISVGKANKR LRYVDQVLQL VYKDGSPCPS KSGLSYKSVI SFVCRPEARP 

      1630       1640       1650       1660       1670       1680 
TNRPMLISLD KQTCTLFFSW HTPLACEQAT ECSVRNGSSI VDLSPLIHRT GGYEAYDESE 

      1690       1700       1710       1720       1730       1740 
DDASDTNPDF YINICQPLNP MHGVPCPAGA AVCKVPIDGP PIDIGRVAGP PILNPIANEI 

      1750       1760       1770       1780       1790       1800 
YLNFESSTPC LADKHFNYTS LIAFHCKRGV SMGTPKLLRT SECDFVFEWE TPVVCPDEVR 

      1810       1820       1830       1840       1850       1860 
MDGCTLTDEQ LLYSFNLSSL STSTFKVTRD SRTYSVGVCT FAVGPEQGGC KDGGVCLLSG 

      1870       1880       1890       1900       1910       1920 
TKGASFGRLQ SMKLDYRHQD EAVVLSYVNG DRCPPETDDG VPCVFPFIFN GKSYEECIIE 

      1930       1940       1950       1960       1970       1980 
SRAKLWCSTT ADYDRDHEWG FCRHSNSYRT SSIIFKCDED EDIGRPQVFS EVRGCDVTFE 

      1990       2000       2010       2020       2030       2040 
WKTKVVCPPK KLECKFVQKH KTYDLRLLSS LTGSWSLVHN GVSYYINLCQ KIYKGPLGCS 

      2050       2060       2070       2080       2090       2100 
ERASICRRTT TGDVQVLGLV HTQKLGVIGD KVVVTYSKGY PCGGNKTASS VIELTCTKTV 

      2110       2120       2130       2140       2150       2160 
GRPAFKRFDI DSCTYYFSWD SRAACAVKPQ EVQMVNGTIT NPINGKSFSL GDIYFKLFRA 

      2170       2180       2190       2200       2210       2220 
SGDMRTNGDN YLYEIQLSSI TSSRNPACSG ANICQVKPND QHFSRKVGTS DKTKYYLQDG 

      2230       2240       2250       2260       2270       2280 
DLDVVFASSS KCGKDKTKSV SSTIFFHCDP LVEDGIPEFS HETADCQYLF SWYTSAVCPL 

      2290       2300       2310       2320       2330       2340 
GVGFDSENPG DDGQMHKGLS ERSQAVGAVL SLLLVALTCC LLALLLYKKE RRETVISKLT 

      2350       2360       2370       2380       2390       2400 
TCCRRSSNVS YKYSKVNKEE ETDENETEWL MEEIQLPPPR QGKEGQENGH ITTKSVKALS 

      2410       2420       2430       2440       2450       2460 
SLHGDDQDSE DEVLTIPEVK VHSGRGAGAE SSHPVRNAQS NALQEREDDR VGLVRGEKAR 

      2470       2480       2490 
KGKSSSAQQK TVSSTKLVSF HDDSDEDLLH I 

« Hide

References

« Hide 'large scale' references
[1]"Insulin-like growth factor II receptor as a multifunctional binding protein."
Morgan D.O., Edman J.C., Standring D.N., Fried V.A., Smith M.C., Roth R.A., Rutter W.J.
Nature 329:301-307(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, VARIANT GLY-1619.
[2]"The human cation-independent mannose 6-phosphate receptor. Cloning and sequence of the full-length cDNA and expression of functional receptor in COS cells."
Oshima A., Nolan C.M., Kyle J.W., Grubb J.H., Sly W.S.
J. Biol. Chem. 263:2553-2562(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT GLY-1619.
[3]"The genomic structure of the gene encoding the human mannose 6 phosphate/insulin-like growth factor 2 receptor (M6P/IGF2R)."
Gemma A., Seike Y., Uematsu K., Seike M., Bennett W.P., Harris C.C., Kudoh S.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-1619.
[4]"Genomic structure of the human M6P/IGF2 receptor."
Killian J.K., Jirtle R.L.
Mamm. Genome 10:74-77(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]NIEHS SNPs program
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-91; LEU-203; ASP-231; VAL-252; GLY-273; GLN-512; SER-604; THR-724; VAL-817; SER-856; MET-1107; ILE-1124; SER-1184; GLU-1315; HIS-1335; GLY-1619; HIS-1832; ASP-1860; MET-1908; SER-2020 AND VAL-2459.
[6]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"Internalization of CD26 by mannose 6-phosphate/insulin-like growth factor II receptor contributes to T cell activation."
Ikushima H., Munakata Y., Ishii T., Iwata S., Terashima M., Tanaka H., Schlossman S.F., Morimoto C.
Proc. Natl. Acad. Sci. U.S.A. 97:8439-8444(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH DPP4, SUBCELLULAR LOCATION.
[8]"Sorting of mannose 6-phosphate receptors mediated by the GGAs."
Puertollano R., Aguilar R.C., Gorshkova I., Crouch R.J., Bonifacino J.S.
Science 292:1712-1716(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GGA1; GGA2 AND GGA3.
[9]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-112; ASN-581; ASN-747 AND ASN-1246.
[10]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409; SER-2479 AND SER-2484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Prostate cancer.
[12]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[14]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[17]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-626 AND ASN-747.
Tissue: Liver.
[19]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409; SER-2479 AND SER-2484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[21]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409; SER-2479 AND SER-2484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"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].
[24]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409 AND SER-2484, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"Structure and functional analysis of the IGF-II/IGF2R interaction."
Brown J., Delaine C., Zaccheo O.J., Siebold C., Gilbert R.J., van Boxel G., Denley A., Wallace J.C., Hassan A.B., Forbes B.E., Jones E.Y.
EMBO J. 27:265-276(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 1508-2128 ALONE AND IN COMPLEX WITH IGF2, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00285 mRNA. Translation: CAA68395.1.
J03528 mRNA. Translation: AAA59866.1.
AF109291 expand/collapse EMBL AC list , AF109244, AF109245, AF109246, AF109247, AF109248, AF109249, AF109250, AF109251, AF109252, AF109253, AF109254, AF109255, AF109256, AF109257, AF109258, AF109259, AF109260, AF109261, AF109262, AF109263, AF109264, AF109265, AF109266, AF109267, AF109268, AF109269, AF109270, AF109271, AF109272, AF109273, AF109274, AF109275, AF109276, AF109277, AF109278, AF109279, AF109280, AF109281, AF109282, AF109283, AF109284, AF109285, AF109286, AF109287, AF109288, AF109289, AF109290 Genomic DNA. Translation: AAF16870.1.
AF069333 Genomic DNA. Translation: AAL04402.1.
AY293855 Genomic DNA. Translation: AAP37954.1.
AL353625, AL035691 Genomic DNA. Translation: CAH72014.1.
AL035691, AL353625 Genomic DNA. Translation: CAI19940.1.
PIRA28372.
RefSeqNP_000867.2. NM_000876.2.
UniGeneHs.487062.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E6FX-ray1.75A/B1508-1650[»]
1GP0X-ray1.40A1508-1650[»]
1GP3X-ray1.95A1508-1650[»]
1GQBX-ray1.80A/B1508-1650[»]
1JPLX-ray2.40E/F/G/H2480-2491[»]
1JWGX-ray2.00C/D2479-2491[»]
1LF8X-ray2.30E/F/G/H2480-2491[»]
2CNJNMR-D1508-1650[»]
2L29NMR-A1508-1647[»]
2L2ANMR-A1508-1647[»]
2V5NX-ray3.20A1508-1799[»]
2V5OX-ray2.91A1508-2128[»]
2V5PX-ray4.10A/B1508-1992[»]
ProteinModelPortalP11717.
SMRP11717. Positions 41-467, 614-761, 1515-2128.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109703. 19 interactions.
DIPDIP-6027N.
IntActP11717. 13 interactions.
MINTMINT-5004044.
STRING9606.ENSP00000349437.

Chemistry

BindingDBP11717.
ChEMBLCHEMBL3240.

PTM databases

PhosphoSiteP11717.

Polymorphism databases

DMDM317373416.

Proteomic databases

PaxDbP11717.
PRIDEP11717.

Protocols and materials databases

DNASU3482.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356956; ENSP00000349437; ENSG00000197081.
GeneID3482.
KEGGhsa:3482.
UCSCuc003qta.3. human.

Organism-specific databases

CTD3482.
GeneCardsGC06P160390.
HGNCHGNC:5467. IGF2R.
HPACAB009661.
HPA011332.
MIM147280. gene.
neXtProtNX_P11717.
PharmGKBPA29701.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG260109.
HOGENOMHOG000113638.
HOVERGENHBG000334.
KOK06564.
OMANTEAACP.
OrthoDBEOG74BJRG.
PhylomeDBP11717.
TreeFamTF328963.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
SignaLinkP11717.

Gene expression databases

ArrayExpressP11717.
BgeeP11717.
CleanExHS_IGF2R.
GenevestigatorP11717.

Family and domain databases

Gene3D2.10.10.10. 1 hit.
2.70.130.10. 16 hits.
InterProIPR000479. CIMR.
IPR000562. FN_type2_col-bd.
IPR013806. Kringle-like.
IPR009011. Man6P_isomerase_rcpt-bd_dom.
[Graphical view]
PfamPF00878. CIMR. 15 hits.
PF00040. fn2. 1 hit.
[Graphical view]
SMARTSM00059. FN2. 1 hit.
[Graphical view]
SUPFAMSSF50911. SSF50911. 16 hits.
SSF57440. SSF57440. 1 hit.
PROSITEPS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIGF2R. human.
EvolutionaryTraceP11717.
GeneWikiInsulin-like_growth_factor_2_receptor.
GenomeRNAi3482.
NextBio13692.
PROP11717.
SOURCESearch...

Entry information

Entry nameMPRI_HUMAN
AccessionPrimary (citable) accession number: P11717
Secondary accession number(s): Q7Z7G9, Q96PT5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 160 of the entry and version 3 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 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries