Reviewed, UniProtKB/Swiss-Prot P11717 (MPRI_HUMAN)

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):
    Insulin-like growth factor 2 receptor
    Insulin-like growth factor II receptor
      Short name=IGF-II receptor
    M6P/IGF2 receptor
      Short name=M6P/IGF2R
    300 kDa mannose 6-phosphate receptor
    MPR 300
    CD_antigen=CD222

Gene names

Name:	IGF2R
Synonyms:	MPRI

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.
Subunit structure	Binds GGA1, GGA2 and GGA3.
Subcellular location	Lysosome membrane; Single-pass type I membrane protein.
Domain	Contains 15 repeating units of approximately 147 AA. 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
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	receptor-mediated endocytosis Traceable author statement. Source: ProtInc signal transduction Traceable author statement. Source: ProtInc
Cellular component	endosome Inferred from direct assay. Source: MGI integral to plasma membrane Traceable author statement. Source: ProtInc lysosomal membrane Inferred from electronic annotation. Source: UniProtKB-SubCell trans-Golgi network transport vesicle Inferred from direct assay. Source: MGI
Molecular function	insulin-like growth factor receptor activity Traceable author statement. Source: ProtInc 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

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

2401

1

Phosphoserine By similarity

Modified residue

2409

1

Phosphoserine Ref.9 Ref.14 Ref.15

Modified residue

2479

1

Phosphoserine Ref.9 Ref.15

Modified residue

2484

1

Phosphoserine Ref.9 Ref.14 Ref.15 Ref.10 Ref.11 Ref.12 Ref.13 Ref.16

Glycosylation

112

1

N-linked (GlcNAc...) Ref.8

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.8

Glycosylation

626

1

N-linked (GlcNAc...)

Glycosylation

747

1

N-linked (GlcNAc...) Ref.8

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.8

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

1903 ↔ 1927

By similarity

Disulfide bond

1917 ↔ 1942

By similarity

Natural variations

Natural variant

91

1

R → H: dbSNP rs8191704. Ref.5

VAR_021304

Natural variant

203

1

P → L: dbSNP rs8191746. Ref.5

VAR_020470

Natural variant

231

1

G → D: dbSNP rs8191753. Ref.5

VAR_021305

Natural variant

252

1

L → V: dbSNP rs8191754. Ref.5

VAR_020471

Natural variant

273

1

D → G: dbSNP rs8191758. Ref.5

VAR_021306

Natural variant

512

1

K → Q: dbSNP rs8191776. Ref.5

VAR_021307

Natural variant

529

1

R → Q: dbSNP rs6413489.

VAR_020472

Natural variant

604

1

G → S: dbSNP rs8191797. Ref.5

VAR_020473

Natural variant

724

1

A → T: dbSNP rs6413491. Ref.5

VAR_020474

Natural variant

817

1

L → V: dbSNP rs8191808. Ref.5

VAR_021308

Natural variant

856

1

G → S: dbSNP rs8191819. Ref.5

VAR_020475

Natural variant

1107

1

T → M: dbSNP rs8191842. Ref.5

VAR_020476

Natural variant

1124

1

V → I: dbSNP rs8191843. Ref.5

VAR_021309

Natural variant

1184

1

T → S: dbSNP rs8191844. Ref.5

VAR_020477

Natural variant

1254

1

E → A: dbSNP rs2230043.

VAR_050428

Natural variant

1315

1

G → E: dbSNP rs8191859. Ref.5

VAR_021310

Natural variant

1335

1

R → H: dbSNP rs8191860. Ref.5

VAR_021311

Natural variant

1395

1

T → S: dbSNP rs2230048.

VAR_050429

Natural variant

1619

1

G → R: dbSNP rs629849. Ref.5 Ref.4 Ref.6

VAR_021312

Natural variant

1696

1

Q → R: dbSNP rs11552587.

VAR_050430

Natural variant

1832

1

R → H: dbSNP rs8191904. Ref.5

VAR_021313

Natural variant

1860

1

G → D: dbSNP rs8191905. Ref.5

VAR_021314

Natural variant

1908

1

I → M: dbSNP rs8191908. Ref.5

VAR_021315

Natural variant

2020

1

N → S: dbSNP rs1805075. Ref.5

VAR_014722

Natural variant

2459

1

A → V: dbSNP rs8191955. Ref.5

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 Ref.1

Sequence conflict

612

1

H → R 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 Ref.1

Sequence conflict

1703

1

G → A 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...

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

1563 – 1567

5

Turn

1568 – 1570

3

Beta strand

1582 – 1584

3

Beta strand

1587 – 1592

6

Beta strand

1599 – 1601

3

Beta strand

1607 – 1614

8

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

1689 – 1692

4

Beta strand

1694 – 1696

3

Beta strand

1711 – 1715

5

Beta strand

1717 – 1719

3

Beta strand

1732 – 1734

3

Turn

1735 – 1738

4

Beta strand

1739 – 1749

11

Beta strand

1756 – 1765

10

Beta strand

1776 – 1780

5

Beta strand

1782 – 1790

9

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)
	P11717-1 [UniParc]. Last modified March 1, 2005. Version 2. Checksum: A94DCE4E42F466CC	FASTA	2,491	274,276
	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 SFVCRPEAGP 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: 2957598] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[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: 2963003] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
[4]	"Genomic structure of the human M6P/IGF2 receptor." Killian J.K., Jirtle R.L. Mamm. Genome 10:74-77(1999) [PubMed: 9892739] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-1619.
[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; ARG-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: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-1619.
[7]	"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: 11387475] [Abstract] Cited for: INTERACTION WITH GGA1; GGA2 AND GGA3.
[8]	"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: 12754519] [Abstract] Cited for: GLYCOSYLATION AT ASN-112; ASN-581; ASN-747 AND ASN-1246.
[9]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409; SER-2479 AND SER-2484, MASS SPECTROMETRY. Tissue: Epithelium.
[10]	"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: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, MASS SPECTROMETRY.
[11]	"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction." Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R. Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed: 17693683] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, MASS SPECTROMETRY.
[12]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, MASS SPECTROMETRY.
[13]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, MASS SPECTROMETRY.
[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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409 AND SER-2484, MASS SPECTROMETRY.
[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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2409; SER-2479 AND SER-2484, MASS SPECTROMETRY.
[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: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2484, MASS SPECTROMETRY. Tissue: Liver.
[17]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: 19159218] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-626 AND ASN-747, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

UniGene

Hs.487062

3D structure databases

PDBPDBe

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	[»]
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	[»]

SMR

P11717. Positions 41-467.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:6027N.

IntAct

P11717. 1 interaction.

PTM databases

PhosphoSite

P11717.

Proteomic databases

PRIDE

P11717.

Genome annotation databases

Ensembl

ENSG00000197081. Homo sapiens. [Contig view]

GeneID

3482.

KEGG

hsa:3482.

Organism-specific databases

GeneCards

GC06P160360.

HGNC

HGNC:5467. IGF2R.

HPA

CAB009661.
HPA011332.

MIM

147280. gene.

PharmGKB

PA29701.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P11717.

HOVERGEN

P11717.

Gene expression databases

ArrayExpress

P11717.

Bgee

P11717.

CleanEx

HS_IGF2R.

GermOnline

ENSG00000197081. Homo sapiens.

Family and domain databases

InterPro

IPR000479. CIMR.
IPR000562. FN_type2_col_bd.
[Graphical view]

Pfam

PF00878. CIMR. 14 hits.
PF00040. fn2. 1 hit.
[Graphical view]

PRINTS

PR00013. FNTYPEII.

ProDom

PD000995. FN_Type_II. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00059. FN2. 1 hit.
[Graphical view]

PROSITE

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

ProtoNet

Search...

Other Resources

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:	March 1, 2005
Last modified:	May 26, 2009
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)