AFF2_HUMAN
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 03-AUG-2022, entry version 170.
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 -!- INTERACTION:
CC P51816; O00629: KPNA4; NbExp=3; IntAct=EBI-1754468, EBI-396343;
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}.
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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; 3.
DR IntAct; P51816; 8.
DR STRING; 9606.ENSP00000359489; -.
DR iPTMnet; P51816; -.
DR PhosphoSitePlus; P51816; -.
DR BioMuta; AFF2; -.
DR DMDM; 116241242; -.
DR EPD; P51816; -.
DR MassIVE; P51816; -.
DR MaxQB; P51816; -.
DR PaxDb; P51816; -.
DR PeptideAtlas; P51816; -.
DR PRIDE; 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; 162 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 CTD; 2334; -.
DR DisGeNET; 2334; -.
DR GeneCards; AFF2; -.
DR HGNC; HGNC:3776; AFF2.
DR HPA; ENSG00000155966; Tissue enhanced (bone marrow, brain, 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; THSSAPM; -.
DR OrthoDB; 558558at2759; -.
DR PhylomeDB; P51816; -.
DR TreeFam; TF326216; -.
DR PathwayCommons; P51816; -.
DR SignaLink; P51816; -.
DR SIGNOR; P51816; -.
DR BioGRID-ORCS; 2334; 16 hits in 689 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 120 other tissues.
DR Genevisible; P51816; HS.
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 InterPro; IPR007797; AF4/FMR2.
DR InterPro; IPR043640; AF4/FMR2_CHD.
DR InterPro; IPR043639; AF4_int.
DR PANTHER; PTHR10528; PTHR10528; 1.
DR Pfam; PF18876; AF-4_C; 1.
DR Pfam; PF18875; AF4_int; 1.
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
