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P11717

- MPRI_HUMAN

UniProt

P11717 - MPRI_HUMAN

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Protein

Cation-independent mannose-6-phosphate receptor

Gene

IGF2R

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 DPP4.1 Publication

GO - Molecular functioni

  1. glycoprotein binding Source: UniProtKB
  2. G-protein coupled receptor activity Source: Ensembl
  3. identical protein binding Source: IntAct
  4. insulin-like growth factor-activated receptor activity Source: ProtInc
  5. mannose binding Source: Ensembl
  6. phosphoprotein binding Source: UniProtKB
  7. receptor activity Source: ProtInc
  8. retinoic acid binding Source: Ensembl
  9. transporter activity Source: InterPro

GO - Biological processi

  1. insulin-like growth factor receptor signaling pathway Source: GOC
  2. liver development Source: Ensembl
  3. organ regeneration Source: Ensembl
  4. positive regulation of apoptotic process Source: Ensembl
  5. post-embryonic development Source: Ensembl
  6. receptor-mediated endocytosis Source: ProtInc
  7. response to retinoic acid Source: Ensembl
  8. signal transduction Source: ProtInc
  9. spermatogenesis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transport

Enzyme and pathway databases

ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.
SignaLinkiP11717.

Names & Taxonomyi

Protein namesi
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 namesi
Name:IGF2R
Synonyms:MPRI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:5467. IGF2R.

Subcellular locationi

Lysosome membrane 1 Publication; Single-pass type I membrane protein 1 Publication
Note: Colocalized with DPP4 in internalized cytoplasmic vesicles adjacent to the cell surface.

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. clathrin coat Source: Ensembl
  3. endocytic vesicle Source: UniProtKB
  4. endosome Source: MGI
  5. extracellular space Source: Ensembl
  6. extracellular vesicular exosome Source: UniProtKB
  7. focal adhesion Source: UniProtKB
  8. integral component of plasma membrane Source: ProtInc
  9. late endosome Source: MGI
  10. lysosome Source: UniProtKB-KW
  11. membrane Source: UniProtKB
  12. nuclear envelope lumen Source: Ensembl
  13. perinuclear region of cytoplasm Source: Ensembl
  14. trans-Golgi network transport vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29701.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4040Add
BLAST
Chaini41 – 24912451Cation-independent mannose-6-phosphate receptorPRO_0000019229Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 69PROSITE-ProRule annotation
Disulfide bondi77 ↔ 84PROSITE-ProRule annotation
Glycosylationi112 – 1121N-linked (GlcNAc...)1 Publication
Disulfide bondi117 ↔ 149PROSITE-ProRule annotation
Disulfide bondi134 ↔ 161PROSITE-ProRule annotation
Disulfide bondi174 ↔ 212PROSITE-ProRule annotation
Disulfide bondi228 ↔ 235PROSITE-ProRule annotation
Disulfide bondi275 ↔ 306PROSITE-ProRule annotation
Disulfide bondi288 ↔ 318PROSITE-ProRule annotation
Disulfide bondi328 ↔ 366PROSITE-ProRule annotation
Disulfide bondi374 ↔ 382PROSITE-ProRule annotation
Glycosylationi400 – 4001N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi420 ↔ 454PROSITE-ProRule annotation
Disulfide bondi434 ↔ 466PROSITE-ProRule annotation
Glycosylationi435 – 4351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi543 – 5431N-linked (GlcNAc...)Sequence Analysis
Glycosylationi581 – 5811N-linked (GlcNAc...)1 Publication
Glycosylationi626 – 6261N-linked (GlcNAc...)1 Publication
Disulfide bondi627 ↔ 664PROSITE-ProRule annotation
Disulfide bondi672 ↔ 679PROSITE-ProRule annotation
Disulfide bondi731 ↔ 760PROSITE-ProRule annotation
Glycosylationi747 – 7471N-linked (GlcNAc...)2 Publications
Glycosylationi871 – 8711N-linked (GlcNAc...)Sequence Analysis
Glycosylationi951 – 9511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi957 – 9571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1164 – 11641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1246 – 12461N-linked (GlcNAc...)1 Publication
Glycosylationi1312 – 13121N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1516 ↔ 15531 PublicationPROSITE-ProRule annotation
Disulfide bondi1559 ↔ 15661 PublicationPROSITE-ProRule annotation
Disulfide bondi1598 ↔ 16341 PublicationPROSITE-ProRule annotation
Disulfide bondi1614 ↔ 16461 PublicationPROSITE-ProRule annotation
Disulfide bondi1652 ↔ 16951 PublicationPROSITE-ProRule annotation
Glycosylationi1656 – 16561N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1706 ↔ 17131 PublicationPROSITE-ProRule annotation
Disulfide bondi1750 ↔ 17831 PublicationPROSITE-ProRule annotation
Glycosylationi1757 – 17571N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1766 ↔ 17951 PublicationPROSITE-ProRule annotation
Disulfide bondi1804 ↔ 18391 PublicationPROSITE-ProRule annotation
Glycosylationi1816 – 18161N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1850 ↔ 18561 PublicationPROSITE-ProRule annotation
Disulfide bondi1893 ↔ 19751 PublicationPROSITE-ProRule annotation
Disulfide bondi1903 ↔ 19271 PublicationPROSITE-ProRule annotation
Disulfide bondi1917 ↔ 19421 PublicationPROSITE-ProRule annotation
Disulfide bondi1957 ↔ 19871 PublicationPROSITE-ProRule annotation
Disulfide bondi1994 ↔ 20291 PublicationPROSITE-ProRule annotation
Disulfide bondi2039 ↔ 20461 PublicationPROSITE-ProRule annotation
Disulfide bondi2082 ↔ 21131 PublicationPROSITE-ProRule annotation
Glycosylationi2085 – 20851N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2096 ↔ 21251 PublicationPROSITE-ProRule annotation
Glycosylationi2136 – 21361N-linked (GlcNAc...)Sequence Analysis
Modified residuei2352 – 23521N6-acetyllysine1 Publication
Modified residuei2409 – 24091Phosphoserine5 Publications
Modified residuei2479 – 24791Phosphoserine3 Publications
Modified residuei2484 – 24841Phosphoserine10 Publications

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP11717.
PaxDbiP11717.
PRIDEiP11717.

PTM databases

PhosphoSiteiP11717.

Expressioni

Gene expression databases

BgeeiP11717.
CleanExiHS_IGF2R.
ExpressionAtlasiP11717. baseline and differential.
GenevestigatoriP11717.

Organism-specific databases

HPAiCAB009661.
HPA011332.

Interactioni

Subunit structurei

Binds HA-I and HA-II plasma membrane adapters By similarity. Interacts with DPP4; the interaction is direct. Binds GGA1, GGA2 and GGA3.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-1048580,EBI-1048580
GGA1Q9UJY52EBI-1048580,EBI-447141
IGF2P0134417EBI-1048580,EBI-7178764
PACS1Q6VY072EBI-1048580,EBI-2555014

Protein-protein interaction databases

BioGridi109703. 19 interactions.
DIPiDIP-6027N.
IntActiP11717. 13 interactions.
MINTiMINT-5004044.
STRINGi9606.ENSP00000349437.

Structurei

Secondary structure

1
2491
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni1514 – 15163
Beta strandi1517 – 15193
Turni1521 – 15233
Beta strandi1526 – 15283
Helixi1530 – 15323
Beta strandi1533 – 15364
Beta strandi1538 – 15425
Turni1543 – 15453
Beta strandi1546 – 15505
Beta strandi1552 – 15543
Beta strandi1558 – 15603
Beta strandi1563 – 15675
Turni1568 – 15703
Beta strandi1573 – 15764
Beta strandi1582 – 15843
Beta strandi1587 – 15926
Beta strandi1596 – 15983
Beta strandi1599 – 16013
Beta strandi1607 – 16148
Beta strandi1616 – 16183
Beta strandi1625 – 16306
Turni1631 – 16344
Beta strandi1635 – 16428
Helixi1643 – 16453
Beta strandi1653 – 16564
Beta strandi1659 – 16624
Helixi1664 – 16663
Beta strandi1669 – 16713
Beta strandi1673 – 16753
Beta strandi1690 – 16923
Beta strandi1694 – 16963
Beta strandi1711 – 17144
Beta strandi1717 – 17193
Beta strandi1722 – 17276
Beta strandi1732 – 17343
Beta strandi1735 – 17373
Beta strandi1743 – 17453
Beta strandi1759 – 17668
Beta strandi1775 – 17773
Turni1781 – 17833
Beta strandi1784 – 17918
Helixi1792 – 17943
Turni1801 – 18044
Beta strandi1805 – 18073
Turni1809 – 18113
Beta strandi1814 – 18163
Helixi1818 – 18214
Beta strandi1825 – 18295
Beta strandi1832 – 18365
Beta strandi1838 – 18403
Turni1845 – 18473
Beta strandi1850 – 18589
Beta strandi1863 – 187614
Turni1878 – 18803
Beta strandi1883 – 18886
Beta strandi1905 – 19095
Beta strandi1912 – 19165
Beta strandi1920 – 19245
Beta strandi1926 – 19327
Helixi1933 – 19364
Beta strandi1939 – 19435
Beta strandi1950 – 19578
Beta strandi1967 – 19726
Turni1973 – 19753
Beta strandi1976 – 19849
Beta strandi1995 – 20006
Beta strandi2002 – 20043
Helixi2005 – 20073
Beta strandi2011 – 20133
Beta strandi2015 – 20195
Beta strandi2022 – 20265
Beta strandi2043 – 20486
Beta strandi2054 – 20596
Helixi2060 – 20623
Beta strandi2064 – 20685
Beta strandi2071 – 20766
Beta strandi2089 – 20968
Beta strandi2098 – 210912
Turni2110 – 21134
Beta strandi2114 – 21218
Helixi2122 – 21243

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP11717.
SMRiP11717. Positions 41-467, 614-761, 1515-2128.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11717.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini41 – 23042264LumenalSequence AnalysisAdd
BLAST
Topological domaini2328 – 2491164CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei2305 – 232723HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati40 – 1891501Add
BLAST
Repeati190 – 3441552Add
BLAST
Repeati345 – 4891453Add
BLAST
Repeati490 – 6431544Add
BLAST
Repeati644 – 7831405Add
BLAST
Repeati784 – 9501676Add
BLAST
Repeati951 – 10991497Add
BLAST
Repeati1100 – 12431448Add
BLAST
Repeati1244 – 13841419Add
BLAST
Repeati1385 – 153214810Add
BLAST
Repeati1533 – 166613411Add
BLAST
Repeati1667 – 182015412Add
BLAST
Repeati1821 – 200818813Add
BLAST
Domaini1898 – 194447Fibronectin type-IIPROSITE-ProRule annotationAdd
BLAST
Repeati2009 – 213712914Add
BLAST
Repeati2165 – 228912515Add
BLAST

Domaini

Sequence similaritiesi

Belongs to the MRL1/IGF2R family.Curated
Contains 1 fibronectin type-II domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG260109.
GeneTreeiENSGT00390000013943.
HOGENOMiHOG000113638.
HOVERGENiHBG000334.
InParanoidiP11717.
KOiK06564.
OMAiVDCQVTD.
OrthoDBiEOG74BJRG.
PhylomeDBiP11717.
TreeFamiTF328963.

Family and domain databases

Gene3Di2.10.10.10. 1 hit.
2.70.130.10. 16 hits.
InterProiIPR000479. CIMR.
IPR000562. FN_type2_col-bd.
IPR013806. Kringle-like.
IPR009011. Man6P_isomerase_rcpt-bd_dom.
[Graphical view]
PfamiPF00878. CIMR. 15 hits.
PF00040. fn2. 1 hit.
[Graphical view]
SMARTiSM00059. FN2. 1 hit.
[Graphical view]
SUPFAMiSSF50911. SSF50911. 16 hits.
SSF57440. SSF57440. 1 hit.
PROSITEiPS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11717-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGAAAGRSPH LGPAPARRPQ RSLLLLQLLL LVAAPGSTQA QAAPFPELCS
60 70 80 90 100
YTWEAVDTKN NVLYKINICG SVDIVQCGPS SAVCMHDLKT RTYHSVGDSV
110 120 130 140 150
LRSATRSLLE FNTTVSCDQQ GTNHRVQSSI AFLCGKTLGT PEFVTATECV
160 170 180 190 200
HYFEWRTTAA CKKDIFKANK EVPCYVFDEE LRKHDLNPLI KLSGAYLVDD
210 220 230 240 250
SDPDTSLFIN VCRDIDTLRD PGSQLRACPP GTAACLVRGH QAFDVGQPRD
260 270 280 290 300
GLKLVRKDRL VLSYVREEAG KLDFCDGHSP AVTITFVCPS ERREGTIPKL
310 320 330 340 350
TAKSNCRYEI EWITEYACHR DYLESKTCSL SGEQQDVSID LTPLAQSGGS
360 370 380 390 400
SYISDGKEYL FYLNVCGETE IQFCNKKQAA VCQVKKSDTS QVKAAGRYHN
410 420 430 440 450
QTLRYSDGDL TLIYFGGDEC SSGFQRMSVI NFECNKTAGN DGKGTPVFTG
460 470 480 490 500
EVDCTYFFTW DTEYACVKEK EDLLCGATDG KKRYDLSALV RHAEPEQNWE
510 520 530 540 550
AVDGSQTETE KKHFFINICH RVLQEGKARG CPEDAAVCAV DKNGSKNLGK
560 570 580 590 600
FISSPMKEKG NIQLSYSDGD DCGHGKKIKT NITLVCKPGD LESAPVLRTS
610 620 630 640 650
GEGGCFYEFE WHTAAACVLS KTEGENCTVF DSQAGFSFDL SPLTKKNGAY
660 670 680 690 700
KVETKKYDFY INVCGPVSVS PCQPDSGACQ VAKSDEKTWN LGLSNAKLSY
710 720 730 740 750
YDGMIQLNYR GGTPYNNERH TPRATLITFL CDRDAGVGFP EYQEEDNSTY
760 770 780 790 800
NFRWYTSYAC PEEPLECVVT DPSTLEQYDL SSLAKSEGGL GGNWYAMDNS
810 820 830 840 850
GEHVTWRKYY INVCRPLNPV PGCNRYASAC QMKYEKDQGS FTEVVSISNL
860 870 880 890 900
GMAKTGPVVE DSGSLLLEYV NGSACTTSDG RQTTYTTRIH LVCSRGRLNS
910 920 930 940 950
HPIFSLNWEC VVSFLWNTEA ACPIQTTTDT DQACSIRDPN SGFVFNLNPL
960 970 980 990 1000
NSSQGYNVSG IGKIFMFNVC GTMPVCGTIL GKPASGCEAE TQTEELKNWK
1010 1020 1030 1040 1050
PARPVGIEKS LQLSTEGFIT LTYKGPLSAK GTADAFIVRF VCNDDVYSGP
1060 1070 1080 1090 1100
LKFLHQDIDS GQGIRNTYFE FETALACVPS PVDCQVTDLA GNEYDLTGLS
1110 1120 1130 1140 1150
TVRKPWTAVD TSVDGRKRTF YLSVCNPLPY IPGCQGSAVG SCLVSEGNSW
1160 1170 1180 1190 1200
NLGVVQMSPQ AAANGSLSIM YVNGDKCGNQ RFSTRITFEC AQISGSPAFQ
1210 1220 1230 1240 1250
LQDGCEYVFI WRTVEACPVV RVEGDNCEVK DPRHGNLYDL KPLGLNDTIV
1260 1270 1280 1290 1300
SAGEYTYYFR VCGKLSSDVC PTSDKSKVVS SCQEKREPQG FHKVAGLLTQ
1310 1320 1330 1340 1350
KLTYENGLLK MNFTGGDTCH KVYQRSTAIF FYCDRGTQRP VFLKETSDCS
1360 1370 1380 1390 1400
YLFEWRTQYA CPPFDLTECS FKDGAGNSFD LSSLSRYSDN WEAITGTGDP
1410 1420 1430 1440 1450
EHYLINVCKS LAPQAGTEPC PPEAAACLLG GSKPVNLGRV RDGPQWRDGI
1460 1470 1480 1490 1500
IVLKYVDGDL CPDGIRKKST TIRFTCSESQ VNSRPMFISA VEDCEYTFAW
1510 1520 1530 1540 1550
PTATACPMKS NEHDDCQVTN PSTGHLFDLS SLSGRAGFTA AYSEKGLVYM
1560 1570 1580 1590 1600
SICGENENCP PGVGACFGQT RISVGKANKR LRYVDQVLQL VYKDGSPCPS
1610 1620 1630 1640 1650
KSGLSYKSVI SFVCRPEARP TNRPMLISLD KQTCTLFFSW HTPLACEQAT
1660 1670 1680 1690 1700
ECSVRNGSSI VDLSPLIHRT GGYEAYDESE DDASDTNPDF YINICQPLNP
1710 1720 1730 1740 1750
MHGVPCPAGA AVCKVPIDGP PIDIGRVAGP PILNPIANEI YLNFESSTPC
1760 1770 1780 1790 1800
LADKHFNYTS LIAFHCKRGV SMGTPKLLRT SECDFVFEWE TPVVCPDEVR
1810 1820 1830 1840 1850
MDGCTLTDEQ LLYSFNLSSL STSTFKVTRD SRTYSVGVCT FAVGPEQGGC
1860 1870 1880 1890 1900
KDGGVCLLSG TKGASFGRLQ SMKLDYRHQD EAVVLSYVNG DRCPPETDDG
1910 1920 1930 1940 1950
VPCVFPFIFN GKSYEECIIE SRAKLWCSTT ADYDRDHEWG FCRHSNSYRT
1960 1970 1980 1990 2000
SSIIFKCDED EDIGRPQVFS EVRGCDVTFE WKTKVVCPPK KLECKFVQKH
2010 2020 2030 2040 2050
KTYDLRLLSS LTGSWSLVHN GVSYYINLCQ KIYKGPLGCS ERASICRRTT
2060 2070 2080 2090 2100
TGDVQVLGLV HTQKLGVIGD KVVVTYSKGY PCGGNKTASS VIELTCTKTV
2110 2120 2130 2140 2150
GRPAFKRFDI DSCTYYFSWD SRAACAVKPQ EVQMVNGTIT NPINGKSFSL
2160 2170 2180 2190 2200
GDIYFKLFRA SGDMRTNGDN YLYEIQLSSI TSSRNPACSG ANICQVKPND
2210 2220 2230 2240 2250
QHFSRKVGTS DKTKYYLQDG DLDVVFASSS KCGKDKTKSV SSTIFFHCDP
2260 2270 2280 2290 2300
LVEDGIPEFS HETADCQYLF SWYTSAVCPL GVGFDSENPG DDGQMHKGLS
2310 2320 2330 2340 2350
ERSQAVGAVL SLLLVALTCC LLALLLYKKE RRETVISKLT TCCRRSSNVS
2360 2370 2380 2390 2400
YKYSKVNKEE ETDENETEWL MEEIQLPPPR QGKEGQENGH ITTKSVKALS
2410 2420 2430 2440 2450
SLHGDDQDSE DEVLTIPEVK VHSGRGAGAE SSHPVRNAQS NALQEREDDR
2460 2470 2480 2490
VGLVRGEKAR KGKSSSAQQK TVSSTKLVSF HDDSDEDLLH I
Length:2,491
Mass (Da):274,375
Last modified:January 11, 2011 - v3
Checksum:i3841ADE559B48057
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti254 – 2541L → V in AAA59866. (PubMed:2963003)Curated
Sequence conflicti510 – 5101E → K in AAA59866. (PubMed:2963003)Curated
Sequence conflicti612 – 6121H → R in CAA68395. (PubMed:2957598)Curated
Sequence conflicti612 – 6121H → R in AAF16870. 1 PublicationCurated
Sequence conflicti845 – 8451V → A in AAA59866. (PubMed:2963003)Curated
Sequence conflicti1489 – 14891S → N in AAA59866. (PubMed:2963003)Curated
Sequence conflicti1703 – 17031G → A in CAA68395. (PubMed:2957598)Curated
Sequence conflicti1703 – 17031G → A in AAF16870. 1 PublicationCurated
Sequence conflicti2026 – 20261I → M in AAA59866. (PubMed:2963003)Curated
Sequence conflicti2075 – 20751T → M in AAA59866. (PubMed:2963003)Curated
Sequence conflicti2156 – 21561K → N in AAA59866. (PubMed:2963003)Curated
Sequence conflicti2160 – 21601A → E in AAA59866. (PubMed:2963003)Curated
Sequence conflicti2176 – 21761Q → L in AAA59866. (PubMed:2963003)Curated
Sequence conflicti2330 – 23301E → K in AAA59866. (PubMed:2963003)Curated
Sequence conflicti2335 – 23351V → M in AAA59866. (PubMed:2963003)Curated
Sequence conflicti2341 – 23411T → S in AAA59866. (PubMed:2963003)Curated
Sequence conflicti2410 – 24101E → T in AAA59866. (PubMed:2963003)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti91 – 911R → H.1 Publication
Corresponds to variant rs8191704 [ dbSNP | Ensembl ].
VAR_021304
Natural varianti203 – 2031P → L.1 Publication
Corresponds to variant rs8191746 [ dbSNP | Ensembl ].
VAR_020470
Natural varianti231 – 2311G → D.1 Publication
Corresponds to variant rs8191753 [ dbSNP | Ensembl ].
VAR_021305
Natural varianti252 – 2521L → V.1 Publication
Corresponds to variant rs8191754 [ dbSNP | Ensembl ].
VAR_020471
Natural varianti273 – 2731D → G.1 Publication
Corresponds to variant rs8191758 [ dbSNP | Ensembl ].
VAR_021306
Natural varianti512 – 5121K → Q.1 Publication
Corresponds to variant rs8191776 [ dbSNP | Ensembl ].
VAR_021307
Natural varianti529 – 5291R → Q.
Corresponds to variant rs6413489 [ dbSNP | Ensembl ].
VAR_020472
Natural varianti604 – 6041G → S.1 Publication
Corresponds to variant rs8191797 [ dbSNP | Ensembl ].
VAR_020473
Natural varianti724 – 7241A → T.1 Publication
Corresponds to variant rs6413491 [ dbSNP | Ensembl ].
VAR_020474
Natural varianti817 – 8171L → V.1 Publication
Corresponds to variant rs8191808 [ dbSNP | Ensembl ].
VAR_021308
Natural varianti856 – 8561G → S.1 Publication
Corresponds to variant rs8191819 [ dbSNP | Ensembl ].
VAR_020475
Natural varianti1107 – 11071T → M.1 Publication
Corresponds to variant rs8191842 [ dbSNP | Ensembl ].
VAR_020476
Natural varianti1124 – 11241V → I.1 Publication
Corresponds to variant rs8191843 [ dbSNP | Ensembl ].
VAR_021309
Natural varianti1184 – 11841T → S.1 Publication
Corresponds to variant rs8191844 [ dbSNP | Ensembl ].
VAR_020477
Natural varianti1254 – 12541E → A.
Corresponds to variant rs2230043 [ dbSNP | Ensembl ].
VAR_050428
Natural varianti1315 – 13151G → E.1 Publication
Corresponds to variant rs8191859 [ dbSNP | Ensembl ].
VAR_021310
Natural varianti1335 – 13351R → H.1 Publication
Corresponds to variant rs8191860 [ dbSNP | Ensembl ].
VAR_021311
Natural varianti1395 – 13951T → S.
Corresponds to variant rs2230048 [ dbSNP | Ensembl ].
VAR_050429
Natural varianti1619 – 16191R → G.4 Publications
Corresponds to variant rs629849 [ dbSNP | Ensembl ].
VAR_021312
Natural varianti1696 – 16961Q → R.
Corresponds to variant rs11552587 [ dbSNP | Ensembl ].
VAR_050430
Natural varianti1832 – 18321R → H.1 Publication
Corresponds to variant rs8191904 [ dbSNP | Ensembl ].
VAR_021313
Natural varianti1860 – 18601G → D.1 Publication
Corresponds to variant rs8191905 [ dbSNP | Ensembl ].
VAR_021314
Natural varianti1908 – 19081I → M.1 Publication
Corresponds to variant rs8191908 [ dbSNP | Ensembl ].
VAR_021315
Natural varianti2020 – 20201N → S.1 Publication
Corresponds to variant rs1805075 [ dbSNP | Ensembl ].
VAR_014722
Natural varianti2459 – 24591A → V.1 Publication
Corresponds to variant rs8191955 [ dbSNP | Ensembl ].
VAR_021316

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS5273.1.
PIRiA28372.
RefSeqiNP_000867.2. NM_000876.2.
UniGeneiHs.487062.

Genome annotation databases

EnsembliENST00000356956; ENSP00000349437; ENSG00000197081.
GeneIDi3482.
KEGGihsa:3482.
UCSCiuc003qta.3. human.

Polymorphism databases

DMDMi317373416.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS5273.1.
PIRi A28372.
RefSeqi NP_000867.2. NM_000876.2.
UniGenei Hs.487062.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
1JPL X-ray 2.40 E/F/G/H 2480-2491 [» ]
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 [» ]
ProteinModelPortali P11717.
SMRi P11717. Positions 41-467, 614-761, 1515-2128.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109703. 19 interactions.
DIPi DIP-6027N.
IntActi P11717. 13 interactions.
MINTi MINT-5004044.
STRINGi 9606.ENSP00000349437.

Chemistry

BindingDBi P11717.
ChEMBLi CHEMBL3240.
DrugBanki DB01277. Mecasermin.

PTM databases

PhosphoSitei P11717.

Polymorphism databases

DMDMi 317373416.

Proteomic databases

MaxQBi P11717.
PaxDbi P11717.
PRIDEi P11717.

Protocols and materials databases

DNASUi 3482.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356956 ; ENSP00000349437 ; ENSG00000197081 .
GeneIDi 3482.
KEGGi hsa:3482.
UCSCi uc003qta.3. human.

Organism-specific databases

CTDi 3482.
GeneCardsi GC06P160390.
HGNCi HGNC:5467. IGF2R.
HPAi CAB009661.
HPA011332.
MIMi 147280. gene.
neXtProti NX_P11717.
PharmGKBi PA29701.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG260109.
GeneTreei ENSGT00390000013943.
HOGENOMi HOG000113638.
HOVERGENi HBG000334.
InParanoidi P11717.
KOi K06564.
OMAi VDCQVTD.
OrthoDBi EOG74BJRG.
PhylomeDBi P11717.
TreeFami TF328963.

Enzyme and pathway databases

Reactomei REACT_19400. Golgi Associated Vesicle Biogenesis.
SignaLinki P11717.

Miscellaneous databases

ChiTaRSi IGF2R. human.
EvolutionaryTracei P11717.
GeneWikii Insulin-like_growth_factor_2_receptor.
GenomeRNAii 3482.
NextBioi 13692.
PROi P11717.
SOURCEi Search...

Gene expression databases

Bgeei P11717.
CleanExi HS_IGF2R.
ExpressionAtlasi P11717. baseline and differential.
Genevestigatori P11717.

Family and domain databases

Gene3Di 2.10.10.10. 1 hit.
2.70.130.10. 16 hits.
InterProi IPR000479. CIMR.
IPR000562. FN_type2_col-bd.
IPR013806. Kringle-like.
IPR009011. Man6P_isomerase_rcpt-bd_dom.
[Graphical view ]
Pfami PF00878. CIMR. 15 hits.
PF00040. fn2. 1 hit.
[Graphical view ]
SMARTi SM00059. FN2. 1 hit.
[Graphical view ]
SUPFAMi SSF50911. SSF50911. 16 hits.
SSF57440. SSF57440. 1 hit.
PROSITEi PS00023. FN2_1. 1 hit.
PS51092. FN2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, 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. 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. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 1508-2128 ALONE AND IN COMPLEX WITH IGF2, DISULFIDE BONDS.

Entry informationi

Entry nameiMPRI_HUMAN
AccessioniPrimary (citable) accession number: P11717
Secondary accession number(s): Q7Z7G9, Q96PT5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 11, 2011
Last modified: October 29, 2014
This is version 166 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3