P11717 (MPRI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2491 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Transport
Cellular component	Lysosome Membrane
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Acetylation Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	receptor-mediated endocytosis Traceable author statement PubMed 10799489. Source: ProtInc
Cellular_component	cell surface Inferred from direct assay Ref.7. Source: UniProtKB endocytic vesicle Inferred from direct assay Ref.7. Source: UniProtKB endosome Inferred from direct assay PubMed 15078902. Source: MGI integral to plasma membrane Traceable author statement PubMed 10799489. Source: ProtInc lysosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear envelope lumen Inferred from electronic annotation. Source: Compara trans-Golgi network transport vesicle Inferred from direct assay PubMed 15078902. Source: MGI
Molecular_function	glycoprotein binding Inferred from direct assay Ref.7. Source: UniProtKB insulin-like growth factor-activated receptor activity Traceable author statement PubMed 10799489. Source: ProtInc mannose binding Inferred from electronic annotation. Source: Compara phosphoprotein binding Inferred from direct assay Ref.7. Source: UniProtKB transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 40

40

Chain

41 – 2491

2451

Cation-independent mannose-6-phosphate receptor

PRO_0000019229

Regions

Topological domain

41 – 2304

2264

Lumenal Potential

Transmembrane

2305 – 2327

23

Helical; Potential

Topological domain

2328 – 2491

164

Cytoplasmic Potential

Repeat

40 – 189

150

1

Repeat

190 – 344

155

2

Repeat

345 – 489

145

3

Repeat

490 – 643

154

4

Repeat

644 – 783

140

5

Repeat

784 – 950

167

6

Repeat

951 – 1099

149

7

Repeat

1100 – 1243

144

8

Repeat

1244 – 1384

141

9

Repeat

1385 – 1532

148

10

Repeat

1533 – 1666

134

11

Repeat

1667 – 1820

154

12

Repeat

1821 – 2008

188

13

Domain

1898 – 1944

47

Fibronectin type-II

Repeat

2009 – 2137

129

14

Repeat

2165 – 2289

125

15

Amino acid modifications

Modified residue

2352

1

N6-acetyllysine Ref.20

Modified residue

2401

1

Phosphoserine By similarity

Modified residue

2409

1

Phosphoserine Ref.10 Ref.15 Ref.19 Ref.21 Ref.23

Modified residue

2479

1

Phosphoserine Ref.10 Ref.19 Ref.21

Modified residue

2484

1

Phosphoserine Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.18 Ref.19 Ref.21 Ref.23

Glycosylation

112

1

N-linked (GlcNAc...) Ref.9

Glycosylation

400

1

N-linked (GlcNAc...) Potential

Glycosylation

435

1

N-linked (GlcNAc...) Potential

Glycosylation

543

1

N-linked (GlcNAc...) Potential

Glycosylation

581

1

N-linked (GlcNAc...) Ref.9

Glycosylation

626

1

N-linked (GlcNAc...) Ref.17

Glycosylation

747

1

N-linked (GlcNAc...) Ref.9 Ref.17

Glycosylation

871

1

N-linked (GlcNAc...) Potential

Glycosylation

951

1

N-linked (GlcNAc...) Potential

Glycosylation

957

1

N-linked (GlcNAc...) Potential

Glycosylation

1164

1

N-linked (GlcNAc...) Potential

Glycosylation

1246

1

N-linked (GlcNAc...) Ref.9

Glycosylation

1312

1

N-linked (GlcNAc...) Potential

Glycosylation

1656

1

N-linked (GlcNAc...) Potential

Glycosylation

1757

1

N-linked (GlcNAc...) Potential

Glycosylation

1816

1

N-linked (GlcNAc...) Potential

Glycosylation

2085

1

N-linked (GlcNAc...) Potential

Glycosylation

2136

1

N-linked (GlcNAc...) Potential

Disulfide bond

49 ↔ 69

By similarity

Disulfide bond

77 ↔ 84

By similarity

Disulfide bond

117 ↔ 149

By similarity

Disulfide bond

134 ↔ 161

By similarity

Disulfide bond

174 ↔ 212

By similarity

Disulfide bond

228 ↔ 235

By similarity

Disulfide bond

275 ↔ 306

By similarity

Disulfide bond

288 ↔ 318

By similarity

Disulfide bond

328 ↔ 366

By similarity

Disulfide bond

374 ↔ 382

By similarity

Disulfide bond

420 ↔ 454

By similarity

Disulfide bond

434 ↔ 466

By similarity

Disulfide bond

627 ↔ 664

By similarity

Disulfide bond

672 ↔ 679

By similarity

Disulfide bond

731 ↔ 760

By similarity

Disulfide bond

1516 ↔ 1553

Ref.24

Disulfide bond

1559 ↔ 1566

Ref.24

Disulfide bond

1598 ↔ 1634

Ref.24

Disulfide bond

1614 ↔ 1646

Ref.24

Disulfide bond

1652 ↔ 1695

Ref.24

Disulfide bond

1706 ↔ 1713

Ref.24

Disulfide bond

1750 ↔ 1783

Ref.24

Disulfide bond

1766 ↔ 1795

Ref.24

Disulfide bond

1804 ↔ 1839

Ref.24

Disulfide bond

1850 ↔ 1856

Ref.24

Disulfide bond

1893 ↔ 1975

Ref.24

Disulfide bond

1903 ↔ 1927

Ref.24

Disulfide bond

1917 ↔ 1942

Ref.24

Disulfide bond

1957 ↔ 1987

Ref.24

Disulfide bond

1994 ↔ 2029

Ref.24

Disulfide bond

2039 ↔ 2046

Ref.24

Disulfide bond

2082 ↔ 2113

Ref.24

Disulfide bond

2096 ↔ 2125

Ref.24

Natural variations

Natural variant

91

1

R → H. Ref.5
Corresponds to variant rs8191704 [ dbSNP | Ensembl ].

VAR_021304

Natural variant

203

1

P → L. Ref.5
Corresponds to variant rs8191746 [ dbSNP | Ensembl ].

VAR_020470

Natural variant

231

1

G → D. Ref.5
Corresponds to variant rs8191753 [ dbSNP | Ensembl ].

VAR_021305

Natural variant

252

1

L → V. Ref.5
Corresponds to variant rs8191754 [ dbSNP | Ensembl ].

VAR_020471

Natural variant

273

1

D → G. Ref.5
Corresponds to variant rs8191758 [ dbSNP | Ensembl ].

VAR_021306

Natural variant

512

1

K → Q. Ref.5
Corresponds to variant rs8191776 [ dbSNP | Ensembl ].

VAR_021307

Natural variant

529

1

R → Q.
Corresponds to variant rs6413489 [ dbSNP | Ensembl ].

VAR_020472

Natural variant

604

1

G → S. Ref.5
Corresponds to variant rs8191797 [ dbSNP | Ensembl ].

VAR_020473

Natural variant

724

1

A → T. Ref.5
Corresponds to variant rs6413491 [ dbSNP | Ensembl ].

VAR_020474

Natural variant

817

1

L → V. Ref.5
Corresponds to variant rs8191808 [ dbSNP | Ensembl ].

VAR_021308

Natural variant

856

1

G → S. Ref.5
Corresponds to variant rs8191819 [ dbSNP | Ensembl ].

VAR_020475

Natural variant

1107

1

T → M. Ref.5
Corresponds to variant rs8191842 [ dbSNP | Ensembl ].

VAR_020476

Natural variant

1124

1

V → I. Ref.5
Corresponds to variant rs8191843 [ dbSNP | Ensembl ].

VAR_021309

Natural variant

1184

1

T → S. Ref.5
Corresponds to variant rs8191844 [ dbSNP | Ensembl ].

VAR_020477

Natural variant

1254

1

E → A.
Corresponds to variant rs2230043 [ dbSNP | Ensembl ].

VAR_050428

Natural variant

1315

1

G → E. Ref.5
Corresponds to variant rs8191859 [ dbSNP | Ensembl ].

VAR_021310

Natural variant

1335

1

R → H. Ref.5
Corresponds to variant rs8191860 [ dbSNP | Ensembl ].

VAR_021311

Natural variant

1395

1

T → S.
Corresponds to variant rs2230048 [ dbSNP | Ensembl ].

VAR_050429

Natural variant

1619

1

R → G. Ref.1 Ref.2 Ref.3 Ref.5
Corresponds to variant rs629849 [ dbSNP | Ensembl ].

VAR_021312

Natural variant

1696

1

Q → R.
Corresponds to variant rs11552587 [ dbSNP | Ensembl ].

VAR_050430

Natural variant

1832

1

R → H. Ref.5
Corresponds to variant rs8191904 [ dbSNP | Ensembl ].

VAR_021313

Natural variant

1860

1

G → D. Ref.5
Corresponds to variant rs8191905 [ dbSNP | Ensembl ].

VAR_021314

Natural variant

1908

1

I → M. Ref.5
Corresponds to variant rs8191908 [ dbSNP | Ensembl ].

VAR_021315

Natural variant

2020

1

N → S. Ref.5
Corresponds to variant rs1805075 [ dbSNP | Ensembl ].

VAR_014722

Natural variant

2459

1

A → V. Ref.5
Corresponds to variant rs8191955 [ dbSNP | Ensembl ].

VAR_021316

Experimental info

Sequence conflict

254

1

L → V in AAA59866. Ref.2

Sequence conflict

510

1

E → K in AAA59866. Ref.2

Sequence conflict

612

1

H → R in CAA68395. Ref.1

Sequence conflict

612

1

H → R in AAF16870. Ref.3

Sequence conflict

845

1

V → A in AAA59866. Ref.2

Sequence conflict

1489

1

S → N in AAA59866. Ref.2

Sequence conflict

1703

1

G → A in CAA68395. Ref.1

Sequence conflict

1703

1

G → A in AAF16870. Ref.3

Sequence conflict

2026

1

I → M in AAA59866. Ref.2

Sequence conflict

2075

1

T → M in AAA59866. Ref.2

Sequence conflict

2156

1

K → N in AAA59866. Ref.2

Sequence conflict

2160

1

A → E in AAA59866. Ref.2

Sequence conflict

2176

1

Q → L in AAA59866. Ref.2

Sequence conflict

2330

1

E → K in AAA59866. Ref.2

Sequence conflict

2335

1

V → M in AAA59866. Ref.2

Sequence conflict

2341

1

T → S in AAA59866. Ref.2

Sequence conflict

2410

1

E → T in AAA59866. Ref.2

Secondary structure

1

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2491

Helix Strand Turn

Details...

Turn

1514 – 1516

3

Beta strand

1517 – 1519

3

Turn

1521 – 1523

3

Beta strand

1526 – 1528

3

Helix

1530 – 1532

3

Beta strand

1533 – 1536

4

Beta strand

1538 – 1542

5

Turn

1543 – 1545

3

Beta strand

1546 – 1550

5

Beta strand

1552 – 1554

3

Beta strand

1558 – 1560

3

Beta strand

1563 – 1567

5

Turn

1568 – 1570

3

Beta strand

1573 – 1576

4

Beta strand

1582 – 1584

3

Beta strand

1587 – 1592

6

Beta strand

1596 – 1598

3

Beta strand

1599 – 1601

3

Beta strand

1607 – 1614

8

Beta strand

1616 – 1618

3

Beta strand

1625 – 1630

6

Turn

1631 – 1634

4

Beta strand

1635 – 1642

8

Helix

1643 – 1645

3

Beta strand

1653 – 1656

4

Beta strand

1659 – 1662

4

Helix

1664 – 1666

3

Beta strand

1669 – 1671

3

Beta strand

1673 – 1675

3

Beta strand

1690 – 1692

3

Beta strand

1694 – 1696

3

Beta strand

1711 – 1714

4

Beta strand

1717 – 1719

3

Beta strand

1722 – 1727

6

Beta strand

1732 – 1734

3

Beta strand

1735 – 1737

3

Beta strand

1743 – 1745

3

Beta strand

1759 – 1766

8

Beta strand

1775 – 1777

3

Turn

1781 – 1783

3

Beta strand

1784 – 1791

8

Helix

1792 – 1794

3

Turn

1801 – 1804

4

Beta strand

1805 – 1807

3

Turn

1809 – 1811

3

Beta strand

1814 – 1816

3

Helix

1818 – 1821

4

Beta strand

1825 – 1829

5

Beta strand

1832 – 1836

5

Beta strand

1838 – 1840

3

Turn

1845 – 1847

3

Beta strand

1850 – 1858

9

Beta strand

1863 – 1876

14

Turn

1878 – 1880

3

Beta strand

1883 – 1888

6

Beta strand

1905 – 1909

5

Beta strand

1912 – 1916

5

Beta strand

1920 – 1924

5

Beta strand

1926 – 1932

7

Helix

1933 – 1936

4

Beta strand

1939 – 1943

5

Beta strand

1950 – 1957

8

Beta strand

1967 – 1972

6

Turn

1973 – 1975

3

Beta strand

1976 – 1984

9

Beta strand

1995 – 2000

6

Beta strand

2002 – 2004

3

Helix

2005 – 2007

3

Beta strand

2011 – 2013

3

Beta strand

2015 – 2019

5

Beta strand

2022 – 2026

5

Beta strand

2043 – 2048

6

Beta strand

2054 – 2059

6

Helix

2060 – 2062

3

Beta strand

2064 – 2068

5

Beta strand

2071 – 2076

6

Beta strand

2089 – 2096

8

Beta strand

2098 – 2109

12

Turn

2110 – 2113

4

Beta strand

2114 – 2121

8

Helix

2122 – 2124

3

Sequences

	Sequence		Length	Mass (Da)
	P11717 [UniParc]. Last modified January 11, 2011. Version 3. Checksum: 3841ADE559B48057	FASTA	2,491	274,375
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Liver.
[17]	"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, MASS SPECTROMETRY. Tissue: Liver.
[18]	"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, MASS SPECTROMETRY.
[19]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[20]	"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, MASS SPECTROMETRY.
[21]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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].
[23]	"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, MASS SPECTROMETRY.
[24]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y00285 mRNA. Translation: CAA68395.1.
J03528 mRNA. Translation: AAA59866.1.
AF109291 , 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.

IPI

IPI00289819.

PIR

A28372.

RefSeq

NP_000867.2. NM_000876.2.

UniGene

Hs.487062.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E6F	X-ray	1.75	A/B	1508-1650	[»]
1GP0	X-ray	1.40	A	1508-1650	[»]
1GP3	X-ray	1.95	A	1508-1650	[»]
1GQB	X-ray	1.80	A/B	1508-1650	[»]
1JWG	X-ray	2.00	C/D	2479-2491	[»]
1LF8	X-ray	2.30	E/F/G/H	2480-2491	[»]
2CNJ	NMR	-	D	1508-1650	[»]
2L29	NMR	-	A	1508-1647	[»]
2L2A	NMR	-	A	1508-1647	[»]
2V5N	X-ray	3.20	A	1508-1799	[»]
2V5O	X-ray	2.91	A	1508-2128	[»]
2V5P	X-ray	4.10	A/B	1508-1992	[»]

ProteinModelPortal

P11717.

SMR

P11717. Positions 41-467, 614-761, 1515-2128.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6027N.

IntAct

P11717. 7 interactions.

MINT

MINT-5004044.

STRING

9606.ENSP00000349437.

PTM databases

PhosphoSite

P11717.

Polymorphism databases

DMDM

60416403.

Proteomic databases

PaxDb

P11717.

PRIDE

P11717.

Protocols and materials databases

DNASU

3482.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000356956; ENSP00000349437; ENSG00000197081.

GeneID

3482.

KEGG

hsa:3482.

UCSC

uc003qta.3. human.

Organism-specific databases

CTD

3482.

GeneCards

GC06P160390.

HGNC

HGNC:5467. IGF2R.

HPA

CAB009661.
HPA011332.

MIM

147280. gene.

neXtProt

NX_P11717.

PharmGKB

PA29701.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG260109.

HOGENOM

HOG000113638.

HOVERGEN

HBG000334.

KO

K06564.

OMA

NTEAACP.

OrthoDB

EOG4G1MFG.

PhylomeDB

P11717.

Enzyme and pathway databases

Reactome

REACT_11123. Membrane Trafficking.

SignaLink

P11717.

Gene expression databases

ArrayExpress

P11717.

Bgee

P11717.

CleanEx

HS_IGF2R.

Genevestigator

P11717.

GermOnline

ENSG00000197081. Homo sapiens.

Family and domain databases

Gene3D

2.10.10.10. 1 hit.

InterPro

IPR000479. CIMR.
IPR000562. FN_type2_col-bd.
IPR013806. Kringle-like.
IPR009011. Man6P_isomerase_rcpt-bd_dom.
[Graphical view]

Pfam

PF00878. CIMR. 15 hits.
PF00040. fn2. 1 hit.
[Graphical view]

SMART

SM00059. FN2. 1 hit.
[Graphical view]

SUPFAM

SSF57440. Kringle-like. 1 hit.
SSF50911. Man6php_recept. 15 hits.

PROSITE

PS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P11717.

ChEMBL

CHEMBL3240.

ChiTaRS

IGF2R. human.

EvolutionaryTrace

P11717.

GenomeRNAi

3482.

NextBio

13692.

SOURCE

Search...

Entry information

Entry name

MPRI_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 152 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.