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P11717

- MPRI_HUMAN

UniProt

P11717 - MPRI_HUMAN

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Protein

Cation-independent mannose-6-phosphate receptor

Gene
IGF2R, MPRI
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. 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
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; Single-pass type I membrane protein
Note: Colocalized with DPP4 in internalized cytoplasmic vesicles adjacent to the cell surface.1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini41 – 23042264Lumenal Reviewed predictionAdd
BLAST
Transmembranei2305 – 232723Helical; Reviewed predictionAdd
BLAST
Topological domaini2328 – 2491164Cytoplasmic Reviewed predictionAdd
BLAST

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. nuclear envelope lumen Source: Ensembl
  11. perinuclear region of cytoplasm Source: Ensembl
  12. 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 ↔ 69 By similarity
Disulfide bondi77 ↔ 84 By similarity
Glycosylationi112 – 1121N-linked (GlcNAc...)1 Publication
Disulfide bondi117 ↔ 149 By similarity
Disulfide bondi134 ↔ 161 By similarity
Disulfide bondi174 ↔ 212 By similarity
Disulfide bondi228 ↔ 235 By similarity
Disulfide bondi275 ↔ 306 By similarity
Disulfide bondi288 ↔ 318 By similarity
Disulfide bondi328 ↔ 366 By similarity
Disulfide bondi374 ↔ 382 By similarity
Glycosylationi400 – 4001N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi420 ↔ 454 By similarity
Disulfide bondi434 ↔ 466 By similarity
Glycosylationi435 – 4351N-linked (GlcNAc...) Reviewed prediction
Glycosylationi543 – 5431N-linked (GlcNAc...) Reviewed prediction
Glycosylationi581 – 5811N-linked (GlcNAc...)1 Publication
Glycosylationi626 – 6261N-linked (GlcNAc...)1 Publication
Disulfide bondi627 ↔ 664 By similarity
Disulfide bondi672 ↔ 679 By similarity
Disulfide bondi731 ↔ 760 By similarity
Glycosylationi747 – 7471N-linked (GlcNAc...)2 Publications
Glycosylationi871 – 8711N-linked (GlcNAc...) Reviewed prediction
Glycosylationi951 – 9511N-linked (GlcNAc...) Reviewed prediction
Glycosylationi957 – 9571N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1164 – 11641N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1246 – 12461N-linked (GlcNAc...)1 Publication
Glycosylationi1312 – 13121N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1516 ↔ 15531 Publication
Disulfide bondi1559 ↔ 15661 Publication
Disulfide bondi1598 ↔ 16341 Publication
Disulfide bondi1614 ↔ 16461 Publication
Disulfide bondi1652 ↔ 16951 Publication
Glycosylationi1656 – 16561N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1706 ↔ 17131 Publication
Disulfide bondi1750 ↔ 17831 Publication
Glycosylationi1757 – 17571N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1766 ↔ 17951 Publication
Disulfide bondi1804 ↔ 18391 Publication
Glycosylationi1816 – 18161N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1850 ↔ 18561 Publication
Disulfide bondi1893 ↔ 19751 Publication
Disulfide bondi1903 ↔ 19271 Publication
Disulfide bondi1917 ↔ 19421 Publication
Disulfide bondi1957 ↔ 19871 Publication
Disulfide bondi1994 ↔ 20291 Publication
Disulfide bondi2039 ↔ 20461 Publication
Disulfide bondi2082 ↔ 21131 Publication
Glycosylationi2085 – 20851N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2096 ↔ 21251 Publication
Glycosylationi2136 – 21361N-linked (GlcNAc...) Reviewed prediction
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 GGA3.2 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.

Miscellaneous databases

EvolutionaryTraceiP11717.

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-IIAdd
BLAST
Repeati2009 – 213712914Add
BLAST
Repeati2165 – 228912515Add
BLAST

Domaini

Sequence similaritiesi

Belongs to the MRL1/IGF2R family.

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

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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

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 conflict

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

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

« 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: September 3, 2014
This is version 164 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

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