ID AFF2_HUMAN Reviewed; 1311 AA. AC P51816; A2RTY4; B4DXD5; B7WNQ1; B7ZLD6; B7ZLD9; O43786; O60215; P78407; AC Q13521; Q14323; Q7Z2F7; Q7Z400; Q9UNA5; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 4. DT 27-MAR-2024, entry version 179. DE RecName: Full=AF4/FMR2 family member 2 {ECO:0000312|HGNC:HGNC:3776}; DE AltName: Full=Protein FMR-2; DE Short=FMR2P; DE AltName: Full=Protein Ox19; GN Name=AFF2 {ECO:0000312|HGNC:HGNC:3776}; Synonyms=FMR2, OX19; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Fetal brain, and Placenta; RX PubMed=8673085; DOI=10.1038/ng0596-105; RA Gecz J., Gedeon A.K., Sutherland G.R., Mulley J.C.; RT "Identification of the gene FMR2, associated with FRAXE mental RT retardation."; RL Nat. Genet. 13:105-108(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RC TISSUE=Brain; RX PubMed=8673086; DOI=10.1038/ng0596-109; RA Gu Y., Shen Y., Gibbs R.A., Nelson D.L.; RT "Identification of FMR2, a novel gene associated with the FRAXE CCG repeat RT and CpG island."; RL Nat. Genet. 13:109-113(1996). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). RC TISSUE=Fetal brain; RX PubMed=8824884; DOI=10.1093/hmg/5.2.275; RA Chakrabarti L., Knight S.J.L., Flannery A.V., Davies K.E.; RT "A candidate gene for mild mental handicap at the FRAXE fragile site."; RL Hum. Mol. Genet. 5:275-282(1996). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1). RX PubMed=9299237; DOI=10.1006/geno.1997.4867; RA Gecz J., Bielby S., Sutherland G.R., Mulley J.C.; RT "Gene structure and subcellular localization of FMR2, a member of a new RT family of putative transcription activators."; RL Genomics 44:201-213(1997). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=9467002; DOI=10.1093/hmg/7.3.441; RA Chakrabarti L., Bristulf J., Foss G.S., Davies K.E.; RT "Expression of the murine homologue of FMR2 in mouse brain and during RT development."; RL Hum. Mol. Genet. 7:441-448(1998). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [GENOMIC RP DNA] OF 526-896. RX PubMed=12777533; DOI=10.1093/molbev/msg134; RA Kitano T., Schwarz C., Nickel B., Paeaebo S.; RT "Gene diversity patterns at 10 X-chromosomal loci in humans and RT chimpanzees."; RL Mol. Biol. Evol. 20:1281-1289(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7). RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 5 AND 6). RC TISSUE=Cerebellum; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 348-421 (ISOFORM 1). RA Wang L., Thibodeau S.N.; RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases. RN [12] RP FUNCTION, SUBCELLULAR LOCATION, AND INVOLVEMENT IN XLID109. RX PubMed=19136466; DOI=10.1093/nar/gkn1058; RA Bensaid M., Melko M., Bechara E.G., Davidovic L., Berretta A., RA Catania M.V., Gecz J., Lalli E., Bardoni B.; RT "FRAXE-associated mental retardation protein (FMR2) is an RNA-binding RT protein with high affinity for G-quartet RNA forming structure."; RL Nucleic Acids Res. 37:1269-1279(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430 AND THR-517, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [14] RP INVOLVEMENT IN XLID109. RX PubMed=21739600; DOI=10.1002/ajmg.a.34122; RA Stettner G.M., Shoukier M., Hoger C., Brockmann K., Auber B.; RT "Familial intellectual disability and autistic behavior caused by a small RT FMR2 gene deletion."; RL Am. J. Med. Genet. A 155:2003-2007(2011). CC -!- FUNCTION: RNA-binding protein. Might be involved in alternative CC splicing regulation through an interaction with G-quartet RNA CC structure. {ECO:0000269|PubMed:19136466}. CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:19136466}. CC Note=When splicing is inhibited, accumulates in enlarged speckles. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Comment=Additional isoforms seem to exist.; CC Name=1; CC IsoId=P51816-1; Sequence=Displayed; CC Name=2; CC IsoId=P51816-2; Sequence=VSP_000211, VSP_000212, VSP_000213; CC Name=3; CC IsoId=P51816-3; Sequence=VSP_000211, VSP_000212, VSP_000216; CC Name=4; CC IsoId=P51816-4; Sequence=VSP_000211, VSP_000212, VSP_000213, CC VSP_000214, VSP_000215; CC Name=5; CC IsoId=P51816-5; Sequence=VSP_000211, VSP_000213; CC Name=6; CC IsoId=P51816-6; Sequence=VSP_000212, VSP_000213; CC Name=7; CC IsoId=P51816-7; Sequence=VSP_043237, VSP_043238; CC -!- TISSUE SPECIFICITY: Brain (most abundant in hippocampus and amygdala), CC placenta and lung. CC -!- DISEASE: Intellectual developmental disorder, X-linked 109 (XLID109) CC [MIM:309548]: A form of mild to moderate intellectual disability CC associated with learning difficulties, communication deficits, CC attention problems, hyperactivity, and autistic behavior. It is CC associated with a fragile site on chromosome Xq28. Intellectual CC disability is characterized by significantly below average general CC intellectual functioning associated with impairments in adaptive CC behavior and manifested during the developmental period. CC {ECO:0000269|PubMed:19136466, ECO:0000269|PubMed:21739600}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. It is caused either by silencing of the AFF2 gene as a CC consequence of a CCG expansion located upstream of this gene or by CC deletion within the gene. Loss of AFF2 expression is correlated with CC FRAXE CCG(N) expansion. Normal individuals have 6-35 copies of the CC repeat, whereas cytogenetically positive, developmentally delayed males CC have more than 200 copies and show methylation of the associated CPG CC island. CC -!- SIMILARITY: Belongs to the AF4 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U48436; AAC82513.1; -; mRNA. DR EMBL; L76569; AAA99416.1; -; mRNA. DR EMBL; X95463; CAA64730.1; -; mRNA. DR EMBL; AF012624; AAB71534.1; -; Genomic_DNA. DR EMBL; AF012603; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012604; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012605; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012606; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012607; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012608; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012609; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012610; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012611; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012612; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012613; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012614; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012615; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012616; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012617; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012618; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012619; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012620; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012621; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012622; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AF012623; AAB71534.1; JOINED; Genomic_DNA. DR EMBL; AJ001550; CAA04822.1; -; mRNA. DR EMBL; AB102644; BAC81113.1; -; mRNA. DR EMBL; AB101711; BAC80300.1; -; Genomic_DNA. DR EMBL; AB101712; BAC80301.1; -; Genomic_DNA. DR EMBL; AB101713; BAC80302.1; -; Genomic_DNA. DR EMBL; AB101714; BAC80303.1; -; Genomic_DNA. DR EMBL; AB101715; BAC80304.1; -; Genomic_DNA. DR EMBL; AB101716; BAC80305.1; -; Genomic_DNA. DR EMBL; AB101717; BAC80306.1; -; Genomic_DNA. DR EMBL; AB101718; BAC80307.1; -; Genomic_DNA. DR EMBL; AB101719; BAC80308.1; -; Genomic_DNA. DR EMBL; AB101720; BAC80309.1; -; Genomic_DNA. DR EMBL; AB101721; BAC80310.1; -; Genomic_DNA. DR EMBL; AB101722; BAC80311.1; -; Genomic_DNA. DR EMBL; AB101723; BAC80312.1; -; Genomic_DNA. DR EMBL; AB101724; BAC80313.1; -; Genomic_DNA. DR EMBL; AB101725; BAC80314.1; -; Genomic_DNA. DR EMBL; AB101726; BAC80315.1; -; Genomic_DNA. DR EMBL; AB101727; BAC80316.1; -; Genomic_DNA. DR EMBL; AB101728; BAC80317.1; -; Genomic_DNA. DR EMBL; AB101729; BAC80318.1; -; Genomic_DNA. DR EMBL; AB101730; BAC80319.1; -; Genomic_DNA. DR EMBL; AK301927; BAG63347.1; -; mRNA. DR EMBL; AC002368; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC005731; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC006516; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC015552; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC231841; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471171; EAW61288.1; -; Genomic_DNA. DR EMBL; BC132683; AAI32684.1; -; mRNA. DR EMBL; BC143740; AAI43741.1; -; mRNA. DR EMBL; BC143744; AAI43745.1; -; mRNA. DR EMBL; AH008014; AAD45878.1; -; Genomic_DNA. DR CCDS; CCDS14684.1; -. [P51816-1] DR CCDS; CCDS55521.1; -. [P51816-7] DR CCDS; CCDS76040.1; -. [P51816-6] DR CCDS; CCDS78510.1; -. [P51816-3] DR RefSeq; NP_001162593.1; NM_001169122.1. [P51816-3] DR RefSeq; NP_001162594.1; NM_001169123.1. [P51816-5] DR RefSeq; NP_001162595.1; NM_001169124.1. [P51816-6] DR RefSeq; NP_001162596.1; NM_001169125.1. [P51816-2] DR RefSeq; NP_001164099.1; NM_001170628.1. [P51816-7] DR RefSeq; NP_002016.2; NM_002025.3. [P51816-1] DR AlphaFoldDB; P51816; -. DR SMR; P51816; -. DR BioGRID; 108620; 6. DR IntAct; P51816; 8. DR STRING; 9606.ENSP00000359489; -. DR GlyGen; P51816; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P51816; -. DR PhosphoSitePlus; P51816; -. DR BioMuta; AFF2; -. DR DMDM; 116241242; -. DR EPD; P51816; -. DR MassIVE; P51816; -. DR MaxQB; P51816; -. DR PaxDb; 9606-ENSP00000359489; -. DR PeptideAtlas; P51816; -. DR ProteomicsDB; 56419; -. [P51816-1] DR ProteomicsDB; 56420; -. [P51816-2] DR ProteomicsDB; 56421; -. [P51816-3] DR ProteomicsDB; 56422; -. [P51816-4] DR ProteomicsDB; 56423; -. [P51816-5] DR ProteomicsDB; 56424; -. [P51816-6] DR ProteomicsDB; 56425; -. [P51816-7] DR Antibodypedia; 529; 181 antibodies from 23 providers. DR DNASU; 2334; -. DR Ensembl; ENST00000286437.7; ENSP00000286437.5; ENSG00000155966.14. [P51816-7] DR Ensembl; ENST00000342251.7; ENSP00000345459.4; ENSG00000155966.14. [P51816-3] DR Ensembl; ENST00000370457.9; ENSP00000359486.6; ENSG00000155966.14. [P51816-6] DR Ensembl; ENST00000370458.5; ENSP00000359487.1; ENSG00000155966.14. [P51816-4] DR Ensembl; ENST00000370460.7; ENSP00000359489.2; ENSG00000155966.14. [P51816-1] DR GeneID; 2334; -. DR KEGG; hsa:2334; -. DR MANE-Select; ENST00000370460.7; ENSP00000359489.2; NM_002025.4; NP_002016.2. DR UCSC; uc004fco.4; human. [P51816-1] DR AGR; HGNC:3776; -. DR CTD; 2334; -. DR DisGeNET; 2334; -. DR GeneCards; AFF2; -. DR HGNC; HGNC:3776; AFF2. DR HPA; ENSG00000155966; Tissue enhanced (bone marrow, epididymis, placenta). DR MalaCards; AFF2; -. DR MIM; 300806; gene. DR MIM; 309548; phenotype. DR neXtProt; NX_P51816; -. DR OpenTargets; ENSG00000155966; -. DR Orphanet; 100973; FRAXE intellectual disability. DR PharmGKB; PA28192; -. DR VEuPathDB; HostDB:ENSG00000155966; -. DR eggNOG; ENOG502QUIB; Eukaryota. DR GeneTree; ENSGT00950000182974; -. DR HOGENOM; CLU_006484_0_0_1; -. DR InParanoid; P51816; -. DR OMA; PKEKESM; -. DR OrthoDB; 4254515at2759; -. DR PhylomeDB; P51816; -. DR TreeFam; TF326216; -. DR PathwayCommons; P51816; -. DR SignaLink; P51816; -. DR SIGNOR; P51816; -. DR BioGRID-ORCS; 2334; 16 hits in 766 CRISPR screens. DR ChiTaRS; AFF2; human. DR GeneWiki; AFF2; -. DR GenomeRNAi; 2334; -. DR Pharos; P51816; Tbio. DR PRO; PR:P51816; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P51816; Protein. DR Bgee; ENSG00000155966; Expressed in cortical plate and 121 other cell types or tissues. DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB. DR GO; GO:0002151; F:G-quadruplex RNA binding; ISS:UniProtKB. DR GO; GO:0007420; P:brain development; TAS:ProtInc. DR GO; GO:0007611; P:learning or memory; IEA:Ensembl. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl. DR GO; GO:0035063; P:nuclear speck organization; IMP:MGI. DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI. DR GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR Gene3D; 6.10.250.2670; -; 1. DR InterPro; IPR007797; AF4/FMR2. DR InterPro; IPR043640; AF4/FMR2_CHD. DR InterPro; IPR043639; AF4_int. DR PANTHER; PTHR10528; AF4/FMR2 FAMILY MEMBER; 1. DR PANTHER; PTHR10528:SF18; AF4_FMR2 FAMILY MEMBER 2; 1. DR Pfam; PF05110; AF-4; 1. DR Pfam; PF18875; AF4_int; 1. DR Pfam; PF18876; AFF4_CHD; 1. DR Genevisible; P51816; HS. PE 1: Evidence at protein level; KW Alternative splicing; Intellectual disability; mRNA processing; KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding; KW Triplet repeat expansion. FT CHAIN 1..1311 FT /note="AF4/FMR2 family member 2" FT /id="PRO_0000215912" FT REGION 94..187 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 204..229 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 377..417 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 457..530 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 574..726 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 818..867 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 881..943 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 94..115 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 162..187 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 477..512 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 587..613 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 626..640 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 641..656 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 657..713 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 852..867 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 896..913 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 430 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 517 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT VAR_SEQ 1..32 FT /note="MDLFDFFRDWDLEQQCHYEQDRSALKKREWER -> MKFKRRHQAFPSFFKM FT KVSLPSDPSCVEEILR (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043237" FT VAR_SEQ 33..391 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043238" FT VAR_SEQ 57..60 FT /note="Missing (in isoform 2, isoform 3, isoform 4 and FT isoform 5)" FT /evidence="ECO:0000303|PubMed:12777533, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8673086, FT ECO:0000303|PubMed:8824884, ECO:0000303|PubMed:9467002" FT /id="VSP_000211" FT VAR_SEQ 364..392 FT /note="Missing (in isoform 2, isoform 3, isoform 4 and FT isoform 6)" FT /evidence="ECO:0000303|PubMed:12777533, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8673086, FT ECO:0000303|PubMed:8824884, ECO:0000303|PubMed:9467002" FT /id="VSP_000212" FT VAR_SEQ 416..421 FT /note="Missing (in isoform 2, isoform 4, isoform 5 and FT isoform 6)" FT /evidence="ECO:0000303|PubMed:12777533, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8824884, FT ECO:0000303|PubMed:9467002" FT /id="VSP_000213" FT VAR_SEQ 466 FT /note="N -> K (in isoform 4)" FT /evidence="ECO:0000303|PubMed:8824884" FT /id="VSP_000214" FT VAR_SEQ 467..1311 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:8824884" FT /id="VSP_000215" FT VAR_SEQ 970..971 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:8673086" FT /id="VSP_000216" FT VARIANT 1185 FT /note="L -> M (in dbSNP:rs12858959)" FT /id="VAR_028217" FT CONFLICT 195 FT /note="D -> A (in Ref. 3; CAA64730)" FT /evidence="ECO:0000305" FT CONFLICT 470 FT /note="A -> V (in Ref. 2; AAA99416)" FT /evidence="ECO:0000305" FT CONFLICT 548 FT /note="Q -> P (in Ref. 1; AAC82513, 2; AAA99416 and 4; FT AAB71534)" FT /evidence="ECO:0000305" FT CONFLICT 1043 FT /note="T -> M (in Ref. 10; AAI32684/AAI43741/AAI43745)" FT /evidence="ECO:0000305" SQ SEQUENCE 1311 AA; 144771 MW; B5310BC074F893CB CRC64; MDLFDFFRDW DLEQQCHYEQ DRSALKKREW ERRNQEVQQE DDLFSSGFDL FGEPYKVAEY TNKGDALANR VQNTLGNYDE MKNLLTNHSN QNHLVGIPKN SVPQNPNNKN EPSFFPEQKN RIIPPHQDNT HPSAPMPPPS VVILNSTLIH SNRKSKPEWS RDSHNPSTVL ASQASGQPNK MQTLTQDQSQ AKLEDFFVYP AEQPQIGEVE ESNPSAKEDS NPNSSGEDAF KEIFQSNSPE ESEFAVQAPG SPLVASSLLA PSSGLSVQNF PPGLYCKTSM GQQKPTAYVR PMDGQDQAPD ISPTLKPSIE FENSFGNLSF GTLLDGKPSA ASSKTKLPKF TILQTSEVSL PSDPSCVEEI LREMTHSWPT PLTSMHTAGH SEQSTFSIPG QESQHLTPGF TLQKWNDPTT RASTKSVSFK SMLEDDLKLS SDEDDLEPVK TLTTQCTATE LYQAVEKAKP RNNPVNPPLA TPQPPPAVQA SGGSGSSSES ESSSESDSDT ESSTTDSESN EAPRVATPEP EPPSTNKWQL DKWLNKVTSQ NKSFICGQNE TPMETISLPP PIIQPMEVQM KVKTNASQVP AEPKERPLLS LIREKARPRP TQKIPETKAL KHKLSTTSET VSQRTIGKKQ PKKVEKNTST DEFTWPKPNI TSSTPKEKES VELHDPPRGR NKATAHKPAP RKEPRPNIPL APEKKKYRGP GKIVPKSREF IETDSSTSDS NTDQEETLQI KVLPPCIISG GNTAKSKEIC GASLTLSTLM SSSGSNNNLS ISNEEPTFSP IPVMQTEILS PLRDHENLKN LWVKIDLDLL SRVPGHSSLH AAPAKPDHKE TATKPKRQTA VTAVEKPAPK GKRKHKPIEV AEKIPEKKQR LEEATTICLL PPCISPAPPH KPPNTRENNS SRRANRRKEE KLFPPPLSPL PEDPPRRRNV SGNNGPFGQD KNIAMTGQIT STKPKRTEGK FCATFKGISV NEGDTPKKAS SATITVTNTA IATATVTATA IVTTTVTATA TATATTTTTT TTISTITSTI TTGLMDSSHL EMTSWAALPL LSSSSTNVRR PKLTFDDSVH NADYYMQEAK KLKHKADALF EKFGKAVNYA DAALSFTECG NAMERDPLEA KSPYTMYSET VELLRYAMRL KNFASPLASD GDKKLAVLCY RCLSLLYLRM FKLKKDHAMK YSRSLMEYFK QNASKVAQIP SPWVSNGKNT PSPVSLNNVS PINAMGNCNN GPVTIPQRIH HMAASHVNIT SNVLRGYEHW DMADKLTREN KEFFGDLDTL MGPLTQHSSM TNLVRYVRQG LCWLRIDAHL L //