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P11717

- MPRI_HUMAN

UniProt

P11717 - MPRI_HUMAN

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
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    8. receptor activity Source: ProtInc
    9. retinoic acid binding Source: Ensembl
    10. 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

    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: UniProt
    7. integral component of plasma membrane Source: ProtInc
    8. late endosome Source: Ensembl
    9. lysosomal membrane Source: UniProtKB-SubCell
    10. membrane Source: UniProtKB
    11. nuclear envelope lumen Source: Ensembl
    12. perinuclear region of cytoplasm Source: Ensembl
    13. trans-Golgi network transport vesicle Source: MGI

    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

    ArrayExpressiP11717.
    BgeeiP11717.
    CleanExiHS_IGF2R.
    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.
    HOGENOMiHOG000113638.
    HOVERGENiHBG000334.
    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

    MGAAAGRSPH LGPAPARRPQ RSLLLLQLLL LVAAPGSTQA QAAPFPELCS     50
    YTWEAVDTKN NVLYKINICG SVDIVQCGPS SAVCMHDLKT RTYHSVGDSV 100
    LRSATRSLLE FNTTVSCDQQ GTNHRVQSSI AFLCGKTLGT PEFVTATECV 150
    HYFEWRTTAA CKKDIFKANK EVPCYVFDEE LRKHDLNPLI KLSGAYLVDD 200
    SDPDTSLFIN VCRDIDTLRD PGSQLRACPP GTAACLVRGH QAFDVGQPRD 250
    GLKLVRKDRL VLSYVREEAG KLDFCDGHSP AVTITFVCPS ERREGTIPKL 300
    TAKSNCRYEI EWITEYACHR DYLESKTCSL SGEQQDVSID LTPLAQSGGS 350
    SYISDGKEYL FYLNVCGETE IQFCNKKQAA VCQVKKSDTS QVKAAGRYHN 400
    QTLRYSDGDL TLIYFGGDEC SSGFQRMSVI NFECNKTAGN DGKGTPVFTG 450
    EVDCTYFFTW DTEYACVKEK EDLLCGATDG KKRYDLSALV RHAEPEQNWE 500
    AVDGSQTETE KKHFFINICH RVLQEGKARG CPEDAAVCAV DKNGSKNLGK 550
    FISSPMKEKG NIQLSYSDGD DCGHGKKIKT NITLVCKPGD LESAPVLRTS 600
    GEGGCFYEFE WHTAAACVLS KTEGENCTVF DSQAGFSFDL SPLTKKNGAY 650
    KVETKKYDFY INVCGPVSVS PCQPDSGACQ VAKSDEKTWN LGLSNAKLSY 700
    YDGMIQLNYR GGTPYNNERH TPRATLITFL CDRDAGVGFP EYQEEDNSTY 750
    NFRWYTSYAC PEEPLECVVT DPSTLEQYDL SSLAKSEGGL GGNWYAMDNS 800
    GEHVTWRKYY INVCRPLNPV PGCNRYASAC QMKYEKDQGS FTEVVSISNL 850
    GMAKTGPVVE DSGSLLLEYV NGSACTTSDG RQTTYTTRIH LVCSRGRLNS 900
    HPIFSLNWEC VVSFLWNTEA ACPIQTTTDT DQACSIRDPN SGFVFNLNPL 950
    NSSQGYNVSG IGKIFMFNVC GTMPVCGTIL GKPASGCEAE TQTEELKNWK 1000
    PARPVGIEKS LQLSTEGFIT LTYKGPLSAK GTADAFIVRF VCNDDVYSGP 1050
    LKFLHQDIDS GQGIRNTYFE FETALACVPS PVDCQVTDLA GNEYDLTGLS 1100
    TVRKPWTAVD TSVDGRKRTF YLSVCNPLPY IPGCQGSAVG SCLVSEGNSW 1150
    NLGVVQMSPQ AAANGSLSIM YVNGDKCGNQ RFSTRITFEC AQISGSPAFQ 1200
    LQDGCEYVFI WRTVEACPVV RVEGDNCEVK DPRHGNLYDL KPLGLNDTIV 1250
    SAGEYTYYFR VCGKLSSDVC PTSDKSKVVS SCQEKREPQG FHKVAGLLTQ 1300
    KLTYENGLLK MNFTGGDTCH KVYQRSTAIF FYCDRGTQRP VFLKETSDCS 1350
    YLFEWRTQYA CPPFDLTECS FKDGAGNSFD LSSLSRYSDN WEAITGTGDP 1400
    EHYLINVCKS LAPQAGTEPC PPEAAACLLG GSKPVNLGRV RDGPQWRDGI 1450
    IVLKYVDGDL CPDGIRKKST TIRFTCSESQ VNSRPMFISA VEDCEYTFAW 1500
    PTATACPMKS NEHDDCQVTN PSTGHLFDLS SLSGRAGFTA AYSEKGLVYM 1550
    SICGENENCP PGVGACFGQT RISVGKANKR LRYVDQVLQL VYKDGSPCPS 1600
    KSGLSYKSVI SFVCRPEARP TNRPMLISLD KQTCTLFFSW HTPLACEQAT 1650
    ECSVRNGSSI VDLSPLIHRT GGYEAYDESE DDASDTNPDF YINICQPLNP 1700
    MHGVPCPAGA AVCKVPIDGP PIDIGRVAGP PILNPIANEI YLNFESSTPC 1750
    LADKHFNYTS LIAFHCKRGV SMGTPKLLRT SECDFVFEWE TPVVCPDEVR 1800
    MDGCTLTDEQ LLYSFNLSSL STSTFKVTRD SRTYSVGVCT FAVGPEQGGC 1850
    KDGGVCLLSG TKGASFGRLQ SMKLDYRHQD EAVVLSYVNG DRCPPETDDG 1900
    VPCVFPFIFN GKSYEECIIE SRAKLWCSTT ADYDRDHEWG FCRHSNSYRT 1950
    SSIIFKCDED EDIGRPQVFS EVRGCDVTFE WKTKVVCPPK KLECKFVQKH 2000
    KTYDLRLLSS LTGSWSLVHN GVSYYINLCQ KIYKGPLGCS ERASICRRTT 2050
    TGDVQVLGLV HTQKLGVIGD KVVVTYSKGY PCGGNKTASS VIELTCTKTV 2100
    GRPAFKRFDI DSCTYYFSWD SRAACAVKPQ EVQMVNGTIT NPINGKSFSL 2150
    GDIYFKLFRA SGDMRTNGDN YLYEIQLSSI TSSRNPACSG ANICQVKPND 2200
    QHFSRKVGTS DKTKYYLQDG DLDVVFASSS KCGKDKTKSV SSTIFFHCDP 2250
    LVEDGIPEFS HETADCQYLF SWYTSAVCPL GVGFDSENPG DDGQMHKGLS 2300
    ERSQAVGAVL SLLLVALTCC LLALLLYKKE RRETVISKLT TCCRRSSNVS 2350
    YKYSKVNKEE ETDENETEWL MEEIQLPPPR QGKEGQENGH ITTKSVKALS 2400
    SLHGDDQDSE DEVLTIPEVK VHSGRGAGAE SSHPVRNAQS NALQEREDDR 2450
    VGLVRGEKAR KGKSSSAQQK TVSSTKLVSF HDDSDEDLLH I 2491
    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.

    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.
    HOGENOMi HOG000113638.
    HOVERGENi HBG000334.
    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

    ArrayExpressi P11717.
    Bgeei P11717.
    CleanExi HS_IGF2R.
    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

    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 1, 2014
    This is version 165 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