IGF2R

IGF2R
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1E6F, 1GP0, 1GP3, 1GQB, 1JPL, 1JWG, 1LF8, 2CNJ, 2V5N, 2V5O, 2V5P, 2L29, 2L2A, 2M68, 5IEI, 2M6T
Identifikatori
Aliasi	IGF2R
Vanjski ID-jevi	OMIM: 147280 MGI: 96435 HomoloGene: 676 GeneCards: IGF2R
Lokacija gena (čovjek)
Hrom.	Hromosom 6 (čovjek)
Kraj	160,113,507 bp
Lokacija gena (miš)
Hrom.	Hromosom 17 (miš)
Kraj	12,988,551 bp
Obrazac RNK ekspresije
	; ;
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• retinoic acid binding; • insulin-like growth factor binding; • G protein-coupled receptor activity; • transporter activity; • phosphoprotein binding; • insulin-like growth factor-activated receptor activity; • insulin-like growth factor II binding; • mannose binding; • vezivanje identičnih proteina; • vezivanje enzima; • G-protein alpha-subunit binding; • GO:0001948, GO:0016582 vezivanje za proteine; • kringle domain binding; • signaling receptor activity;
Ćelijska komponenta	• citoplazma; • integral component of membrane; • endozom; • late endosome; • membrana; • focal adhesion; • clathrin coat; • endocytic vesicle; • integral component of plasma membrane; • cell surface; • lysosomal membrane; • trans-Golđijeva mreža; • early endosome; • nuclear envelope lumen; • perinuklearno područje citoplazme; • trans-Golgi network transport vesicle; • Lizozom; • Egzosom; • jedro; • trans-Golgi network membrane; • transport vesicle; • Vanćelijsko; • Golđijev aparat; • ćelijska membrana; • clathrin-coated vesicle membrane; • secretory granule membrane; • clathrin-coated vesicle;
Biološki proces	• regulation of apoptotic process; • G protein-coupled receptor signaling pathway; • response to retinoic acid; • post-embryonic development; • receptor-mediated endocytosis; • animal organ regeneration; • Spermatogeneza; • positive regulation of apoptotic process; • liver development; • GO:0072468 Transdukcija signala; • insulin-like growth factor receptor signaling pathway; • neutrophil degranulation; • membrane organization; • GO:0015915 transport; • post-Golgi vesicle-mediated transport; • lysosomal transport;
	Izvori:Amigo / QuickGO
Ortolozi
	3482
	16004
	ENSG00000197081
	ENSMUSG00000023830
	P11717
	Q07113
	NM_000876
	NM_010515
	NP_000867
	NP_034645
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Receptor insulinolikog faktora rasta 2 (IGF2R), znan i kao kation-neovisni receptor manoza-6-fosfata (CI-MPR) jest protein koji je kod ljudi kodiran genom IGF2R.^[5]^[6] IGF2R je multifunkcionalni proteinski receptor koji se veže insulinski faktor rasta 2 (IGF2) na ćelijskoj površini i manoza-6-fosfat (M6P) označeni protein u trans-Golgijevoj mreži.^[6]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je 2.491 aminokiselina, а molekulska težina 274.375 Da.^[7]

C: Cistein

D: Asparaginska kiselina

E: Glutaminska kiselina

F: Fenilalanin

G: Glicin

H: Histidin

I: Izoleucin

K: Lizin

L: Leucin

M: Metionin

N: Asparagin

P: Prolin

Q: Glutamin

R: Arginin

S: Serin

T: Treonin

V: Valin

W: Triptofan

Y: Tirozin

10	20	30	40	50
MGAAAGRSPH	LGPAPARRPQ	RSLLLLQLLL	LVAAPGSTQA	QAAPFPELCS
YTWEAVDTKN	NVLYKINICG	SVDIVQCGPS	SAVCMHDLKT	RTYHSVGDSV
LRSATRSLLE	FNTTVSCDQQ	GTNHRVQSSI	AFLCGKTLGT	PEFVTATECV
HYFEWRTTAA	CKKDIFKANK	EVPCYVFDEE	LRKHDLNPLI	KLSGAYLVDD
SDPDTSLFIN	VCRDIDTLRD	PGSQLRACPP	GTAACLVRGH	QAFDVGQPRD
GLKLVRKDRL	VLSYVREEAG	KLDFCDGHSP	AVTITFVCPS	ERREGTIPKL
TAKSNCRYEI	EWITEYACHR	DYLESKTCSL	SGEQQDVSID	LTPLAQSGGS
SYISDGKEYL	FYLNVCGETE	IQFCNKKQAA	VCQVKKSDTS	QVKAAGRYHN
QTLRYSDGDL	TLIYFGGDEC	SSGFQRMSVI	NFECNKTAGN	DGKGTPVFTG
EVDCTYFFTW	DTEYACVKEK	EDLLCGATDG	KKRYDLSALV	RHAEPEQNWE
AVDGSQTETE	KKHFFINICH	RVLQEGKARG	CPEDAAVCAV	DKNGSKNLGK
FISSPMKEKG	NIQLSYSDGD	DCGHGKKIKT	NITLVCKPGD	LESAPVLRTS
GEGGCFYEFE	WHTAAACVLS	KTEGENCTVF	DSQAGFSFDL	SPLTKKNGAY
KVETKKYDFY	INVCGPVSVS	PCQPDSGACQ	VAKSDEKTWN	LGLSNAKLSY
YDGMIQLNYR	GGTPYNNERH	TPRATLITFL	CDRDAGVGFP	EYQEEDNSTY
NFRWYTSYAC	PEEPLECVVT	DPSTLEQYDL	SSLAKSEGGL	GGNWYAMDNS
GEHVTWRKYY	INVCRPLNPV	PGCNRYASAC	QMKYEKDQGS	FTEVVSISNL
GMAKTGPVVE	DSGSLLLEYV	NGSACTTSDG	RQTTYTTRIH	LVCSRGRLNS
HPIFSLNWEC	VVSFLWNTEA	ACPIQTTTDT	DQACSIRDPN	SGFVFNLNPL
NSSQGYNVSG	IGKIFMFNVC	GTMPVCGTIL	GKPASGCEAE	TQTEELKNWK
PARPVGIEKS	LQLSTEGFIT	LTYKGPLSAK	GTADAFIVRF	VCNDDVYSGP
LKFLHQDIDS	GQGIRNTYFE	FETALACVPS	PVDCQVTDLA	GNEYDLTGLS
TVRKPWTAVD	TSVDGRKRTF	YLSVCNPLPY	IPGCQGSAVG	SCLVSEGNSW
NLGVVQMSPQ	AAANGSLSIM	YVNGDKCGNQ	RFSTRITFEC	AQISGSPAFQ
LQDGCEYVFI	WRTVEACPVV	RVEGDNCEVK	DPRHGNLYDL	KPLGLNDTIV
SAGEYTYYFR	VCGKLSSDVC	PTSDKSKVVS	SCQEKREPQG	FHKVAGLLTQ
KLTYENGLLK	MNFTGGDTCH	KVYQRSTAIF	FYCDRGTQRP	VFLKETSDCS
YLFEWRTQYA	CPPFDLTECS	FKDGAGNSFD	LSSLSRYSDN	WEAITGTGDP
EHYLINVCKS	LAPQAGTEPC	PPEAAACLLG	GSKPVNLGRV	RDGPQWRDGI
IVLKYVDGDL	CPDGIRKKST	TIRFTCSESQ	VNSRPMFISA	VEDCEYTFAW
PTATACPMKS	NEHDDCQVTN	PSTGHLFDLS	SLSGRAGFTA	AYSEKGLVYM
SICGENENCP	PGVGACFGQT	RISVGKANKR	LRYVDQVLQL	VYKDGSPCPS
KSGLSYKSVI	SFVCRPEARP	TNRPMLISLD	KQTCTLFFSW	HTPLACEQAT
ECSVRNGSSI	VDLSPLIHRT	GGYEAYDESE	DDASDTNPDF	YINICQPLNP
MHGVPCPAGA	AVCKVPIDGP	PIDIGRVAGP	PILNPIANEI	YLNFESSTPC
LADKHFNYTS	LIAFHCKRGV	SMGTPKLLRT	SECDFVFEWE	TPVVCPDEVR
MDGCTLTDEQ	LLYSFNLSSL	STSTFKVTRD	SRTYSVGVCT	FAVGPEQGGC
KDGGVCLLSG	TKGASFGRLQ	SMKLDYRHQD	EAVVLSYVNG	DRCPPETDDG
VPCVFPFIFN	GKSYEECIIE	SRAKLWCSTT	ADYDRDHEWG	FCRHSNSYRT
SSIIFKCDED	EDIGRPQVFS	EVRGCDVTFE	WKTKVVCPPK	KLECKFVQKH
KTYDLRLLSS	LTGSWSLVHN	GVSYYINLCQ	KIYKGPLGCS	ERASICRRTT
TGDVQVLGLV	HTQKLGVIGD	KVVVTYSKGY	PCGGNKTASS	VIELTCTKTV
GRPAFKRFDI	DSCTYYFSWD	SRAACAVKPQ	EVQMVNGTIT	NPINGKSFSL
GDIYFKLFRA	SGDMRTNGDN	YLYEIQLSSI	TSSRNPACSG	ANICQVKPND
QHFSRKVGTS	DKTKYYLQDG	DLDVVFASSS	KCGKDKTKSV	SSTIFFHCDP
LVEDGIPEFS	HETADCQYLF	SWYTSAVCPL	GVGFDSENPG	DDGQMHKGLS
ERSQAVGAVL	SLLLVALTCC	LLALLLYKKE	RRETVISKLT	TCCRRSSNVS
YKYSKVNKEE	ETDENETEWL	MEEIQLPPPR	QGKEGQENGH	ITTKSVKALS
SLHGDDQDSE	DEVLTIPEVK	VHSGRGAGAE	SSHPVRNAQS	NALQEREDDR
VGLVRGEKAR	KGKSSSAQQK	TVSSTKLVSF	HDDSDEDLLH	I

Struktura

Strukturno, IGF2R je transmembranski protein tipa I (to jest, ima jedan transmembranski domen sa svojim C-terminalom na citoplazmatskoj strani lipidne membrane s velikim vanćelijskim/lumenskim domenom i relativno kratkim citoplazmatskim repom.^[8] Vanćelijski domen sastoji se od male regije homologne kolagen-vezujućem domenu fibronektina i od petnaest ponavljanja sa približno 147 aminokiselinskih ostataka. Svako od ovih ponavljanja homologno je vancitoplazmatskom domenu sa 157 ostataka receptora za manozu 6-fosfat. Vezivanje za IGF2 posreduje se kroz jedno od ponavljanja, dok su dva različita ponavljanja odgovorna za vezivanje za manoza-6-fosfat. IGF2R je veličine približno 300 kDa; čini se da postoji i funkcionira kao dimer.

Funkcija

IGF2R ima funkciju uklanjanja IGF2 sa ćelijske površine radi slabljenja signalizacije i transporta lizosomnih kiselohidrolaznih prekursora iz Golgijevog aparata u lizosom. Nakon vezanja IGF2 na ćelijskoj površini, IGF2R se akumuliraju u tvoreći klatrinom obložene vezikule i internalizirane. U lumenu trans-Golgijeve mreže, IGF2R veže teret označen kao M6P.^[8] IGF2R (vezani za njihov teret) prepoznaju porodicu GGA, adapterskih klatrinskih proteina i akumuliraju se u tvoreći vezikule obložene klatrinom.^[9] IGF2R sa ćelijske površine i iz Golgijevog aparata šalju se u rani endosom gdje, u njegovom relativno niskom pH okruženju, IGF2R oslobađaju svoj teret. IGF2R se reciklira natrag u Golgijevom aparatu, pomoću kompleksa retromera, opet putem interakcije s GGA i vezikulama. Proteini iz terea se zatim transportuju do lizosoma, preko kasnog endosoma nezavisno od IGF2R.

Interakcije

Pokazano je da receptor faktora rasta sličan insulinu stupa u interakciju s M6PRBP1.^[10]^[11]

Evolucija

Funkcija receptora insulinolikog faktora rasta 2 evoluirala je iz kationski neovisnog receptora manoza 6-fosfata i prvi put se vidi u Monotremata. Mjesto vezanja IGF-2 vjerovatno je stečeno slučajno, stvaranjem klastera za pojačavanje mjesta egzonske prerade u egzonu 34, što je vjerojatno bilo potrebno zbog nekoliko kilobaza insercije ponavljajućih elemenata u prethodnom intronu. Zatim je uslijedilo šestostruko sazrijevanje afiniteta tokom evolucije, podudarajući se s početkom utiskivanja i u skladu s teorijom roditeljske protivrječnosti.^[12]

Također pogledajte

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000197081 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000023830 - Ensembl, maj 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Oshima A, Nolan CM, Kyle JW, Grubb JH, Sly WS (februar 1988). "The human cation-independent mannose 6-phosphate receptor. Cloning and sequence of the full-length cDNA and expression of functional receptor in COS cells". J. Biol. Chem. 263 (5): 2553–62. doi:10.1016/S0021-9258(18)69243-9. PMID 2963003.
^ ^a ^b Laureys G, Barton DE, Ullrich A, Francke U (oktobar 1988). "Chromosomal mapping of the gene for the type II insulin-like growth factor receptor/cation-independent mannose 6-phosphate receptor in man and mouse". Genomics. 3 (3): 224–9. doi:10.1016/0888-7543(88)90083-3. PMID 2852162.
^ "UniProt, P11717" (jezik: engleski). Pristupljeno 8. 10. 2021.
^ ^a ^b Ghosh P, Dahms NM, Kornfeld S (mart 2003). "Mannose 6-phosphate receptors: new twists in the tale". Nat. Rev. Mol. Cell Biol. 4 (3): 202–12. doi:10.1038/nrm1050. PMID 12612639. S2CID 16991464.
^ Ghosh P, Kornfeld S (juli 2004). "The GGA proteins: key players in protein sorting at the trans-Golgi network". Eur. J. Cell Biol. 83 (6): 257–62. doi:10.1078/0171-9335-00374. PMID 15511083.
^ Díaz E, Pfeffer SR (maj 1998). "TIP47: a cargo selection device for mannose 6-phosphate receptor trafficking". Cell. 93 (3): 433–43. doi:10.1016/S0092-8674(00)81171-X. PMID 9590177. S2CID 17161071.
^ Orsel JG, Sincock PM, Krise JP, Pfeffer SR (august 2000). "Recognition of the 300-kDa mannose 6-phosphate receptor cytoplasmic domain by 47-kDa tail-interacting protein". Proc. Natl. Acad. Sci. U.S.A. 97 (16): 9047–51. Bibcode:2000PNAS...97.9047O. doi:10.1073/pnas.160251397. PMC 16819. PMID 10908666.
^ Williams C, Hoppe HJ, Rezgui D, Strickland M, Forbes BE, Grutzner F, Frago S, Ellis RZ, Wattana-Amorn P, Prince SN, Zaccheo OJ, Nolan CM, Mungall AJ, Jones EY, Crump MP, Hassan AB (novembar 2012). "Exon splice enhancer primes IGF2:IGF2R binding site structure and function evolution". Science. 338 (6111): 1209–1213. Bibcode:2012Sci...338.1209W. doi:10.1126/science.1228633. PMC 4658703. PMID 23197533.

Dopunska literatura

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Hawkes C, Kar S (2004). "The insulin-like growth factor-II/mannose-6-phosphate receptor: structure, distribution and function in the central nervous system". Brain Res. Brain Res. Rev. 44 (2–3): 117–40. doi:10.1016/j.brainresrev.2003.11.002. PMID 15003389. S2CID 20434586.
Scott CD, Firth SM (2005). "The role of the M6P/IGF-II receptor in cancer: tumor suppression or garbage disposal?". Horm. Metab. Res. 36 (5): 261–71. doi:10.1055/s-2004-814477. PMID 15156403.
Antoniades HN, Galanopoulos T, Neville-Golden J, Maxwell M (1992). "Expression of insulin-like growth factors I and II and their receptor mRNAs in primary human astrocytomas and meningiomas; in vivo studies using in situ hybridization and immunocytochemistry". Int. J. Cancer. 50 (2): 215–22. doi:10.1002/ijc.2910500210. PMID 1370435. S2CID 22632952.
Zhou J, Bondy C (1992). "Insulin-like growth factor-II and its binding proteins in placental development". Endocrinology. 131 (3): 1230–40. doi:10.1210/en.131.3.1230. PMID 1380437.
Morgan DO, Edman JC, Standring DN, Fried VA, Smith MC, Roth RA, Rutter WJ (1987). "Insulin-like growth factor II receptor as a multifunctional binding protein". Nature. 329 (6137): 301–7. Bibcode:1987Natur.329..301M. doi:10.1038/329301a0. PMID 2957598. S2CID 4308631.
Oshima A, Nolan CM, Kyle JW, Grubb JH, Sly WS (1988). "The human cation-independent mannose 6-phosphate receptor. Cloning and sequence of the full-length cDNA and expression of functional receptor in COS cells". J. Biol. Chem. 263 (5): 2553–62. doi:10.1016/S0021-9258(18)69243-9. PMID 2963003.
De Souza AT, Hankins GR, Washington MK, Orton TC, Jirtle RL (1996). "M6P/IGF2R gene is mutated in human hepatocellular carcinomas with loss of heterozygosity". Nat. Genet. 11 (4): 447–9. doi:10.1038/ng1295-447. PMID 7493029. S2CID 21787312.
Ilvesmäki V, Blum WF, Voutilainen R (1994). "Insulin-like growth factor binding proteins in the human adrenal gland". Mol. Cell. Endocrinol. 97 (1–2): 71–9. doi:10.1016/0303-7207(93)90212-3. PMID 7511544. S2CID 22503525.
De Souza AT, Hankins GR, Washington MK, Fine RL, Orton TC, Jirtle RL (1995). "Frequent loss of heterozygosity on 6q at the mannose 6-phosphate/insulin-like growth factor II receptor locus in human hepatocellular tumors". Oncogene. 10 (9): 1725–9. PMID 7753549.
Schmidt B, Kiecke-Siemsen C, Waheed A, Braulke T, von Figura K (1995). "Localization of the insulin-like growth factor II binding site to amino acids 1508-1566 in repeat 11 of the mannose 6-phosphate/insulin-like growth factor II receptor". J. Biol. Chem. 270 (25): 14975–82. doi:10.1074/jbc.270.25.14975. PMID 7797478.
Rao PH, Murty VV, Gaidano G, Hauptschein R, Dalla-Favera R, Chaganti RS (1994). "Subregional mapping of 8 single copy loci to chromosome 6 by fluorescence in situ hybridization". Cytogenet. Cell Genet. 66 (4): 272–3. doi:10.1159/000133710. PMID 8162705.
Ishiwata T, Bergmann U, Kornmann M, Lopez M, Beger HG, Korc M (1997). "Altered expression of insulin-like growth factor II receptor in human pancreatic cancer". Pancreas. 15 (4): 367–73. doi:10.1097/00006676-199711000-00006. PMID 9361090. S2CID 42073680.
Tikkanen R, Peltola M, Oinonen C, Rouvinen J, Peltonen L (1998). "Several cooperating binding sites mediate the interaction of a lysosomal enzyme with phosphotransferase". EMBO J. 16 (22): 6684–93. doi:10.1093/emboj/16.22.6684. PMC 1170273. PMID 9362483.
Nykjaer A, Christensen EI, Vorum H, Hager H, Petersen CM, Røigaard H, Min HY, Vilhardt F, Møller LB, Kornfeld S, Gliemann J (1998). "Mannose 6-Phosphate/Insulin-like Growth Factor–II Receptor Targets the Urokinase Receptor to Lysosomes via a Novel Binding Interaction". J. Cell Biol. 141 (3): 815–28. doi:10.1083/jcb.141.3.815. PMC 2132758. PMID 9566979.
Díaz E, Pfeffer SR (1998). "TIP47: a cargo selection device for mannose 6-phosphate receptor trafficking". Cell. 93 (3): 433–43. doi:10.1016/S0092-8674(00)81171-X. PMID 9590177. S2CID 17161071.
Wan L, Molloy SS, Thomas L, Liu G, Xiang Y, Rybak SL, Thomas G (1998). "PACS-1 defines a novel gene family of cytosolic sorting proteins required for trans-Golgi network localization". Cell. 94 (2): 205–16. doi:10.1016/S0092-8674(00)81420-8. PMID 9695949. S2CID 15027198.
Killian JK, Jirtle RL (1999). "Genomic structure of the human M6P/IGF2 receptor". Mamm. Genome. 10 (1): 74–7. CiteSeerX 10.1.1.564.5806. doi:10.1007/s003359900947. PMID 9892739. S2CID 20181915.
Kumar S, Hand AT, Connor JR, Dodds RA, Ryan PJ, Trill JJ, Fisher SM, Nuttall ME, Lipshutz DB, Zou C, Hwang SM, Votta BJ, James IE, Rieman DJ, Gowen M, Lee JC (1999). "Identification and cloning of a connective tissue growth factor-like cDNA from human osteoblasts encoding a novel regulator of osteoblast functions". J. Biol. Chem. 274 (24): 17123–31. doi:10.1074/jbc.274.24.17123. PMID 10358067.

Vanjski linkovi

Insulin-Like-Growth-Factor II Receptor na US National Library of Medicine Medical Subject Headings (MeSH)

Kategoruja:Receptori

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000197081 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000023830 - Ensembl, maj 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid2963003-5] Oshima A, Nolan CM, Kyle JW, Grubb JH, Sly WS (februar 1988). "The human cation-independent mannose 6-phosphate receptor. Cloning and sequence of the full-length cDNA and expression of functional receptor in COS cells". J. Biol. Chem. 263 (5): 2553–62. doi:10.1016/S0021-9258(18)69243-9. PMID 2963003.

[pmid2852162-6] Laureys G, Barton DE, Ullrich A, Francke U (oktobar 1988). "Chromosomal mapping of the gene for the type II insulin-like growth factor receptor/cation-independent mannose 6-phosphate receptor in man and mouse". Genomics. 3 (3): 224–9. doi:10.1016/0888-7543(88)90083-3. PMID 2852162.

[UniProt-7] "UniProt, P11717" (jezik: engleski). Pristupljeno 8. 10. 2021.

[pmid12612639-8] Ghosh P, Dahms NM, Kornfeld S (mart 2003). "Mannose 6-phosphate receptors: new twists in the tale". Nat. Rev. Mol. Cell Biol. 4 (3): 202–12. doi:10.1038/nrm1050. PMID 12612639. S2CID 16991464.

[pmid15511083-9] Ghosh P, Kornfeld S (juli 2004). "The GGA proteins: key players in protein sorting at the trans-Golgi network". Eur. J. Cell Biol. 83 (6): 257–62. doi:10.1078/0171-9335-00374. PMID 15511083.

[pmid9590177-10] Díaz E, Pfeffer SR (maj 1998). "TIP47: a cargo selection device for mannose 6-phosphate receptor trafficking". Cell. 93 (3): 433–43. doi:10.1016/S0092-8674(00)81171-X. PMID 9590177. S2CID 17161071.

[pmid10908666-11] Orsel JG, Sincock PM, Krise JP, Pfeffer SR (august 2000). "Recognition of the 300-kDa mannose 6-phosphate receptor cytoplasmic domain by 47-kDa tail-interacting protein". Proc. Natl. Acad. Sci. U.S.A. 97 (16): 9047–51. Bibcode:2000PNAS...97.9047O. doi:10.1073/pnas.160251397. PMC 16819. PMID 10908666.

[PMID_23197533-12] Williams C, Hoppe HJ, Rezgui D, Strickland M, Forbes BE, Grutzner F, Frago S, Ellis RZ, Wattana-Amorn P, Prince SN, Zaccheo OJ, Nolan CM, Mungall AJ, Jones EY, Crump MP, Hassan AB (novembar 2012). "Exon splice enhancer primes IGF2:IGF2R binding site structure and function evolution". Science. 338 (6111): 1209–1213. Bibcode:2012Sci...338.1209W. doi:10.1126/science.1228633. PMC 4658703. PMID 23197533.

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