ID A8MQB8_HUMAN Unreviewed; 582 AA.
AC A8MQB8;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Fragile X messenger ribonucleoprotein 1 {ECO:0000313|Ensembl:ENSP00000359508.1};
GN Name=FMR1 {ECO:0000313|Ensembl:ENSP00000359508.1};
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 {ECO:0000313|Ensembl:ENSP00000359508.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000359508.1, ECO:0000313|Proteomes:UP000005640}
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 [2] {ECO:0007829|PubMed:20068231}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [3] {ECO:0007829|PubMed:21269460}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [4] {ECO:0007829|PubMed:22814378}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [5] {ECO:0007829|PubMed:24275569}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [6] {ECO:0000313|Ensembl:ENSP00000359508.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cell projection,
CC dendrite {ECO:0000256|ARBA:ARBA00004279}. Cell projection, dendritic
CC spine {ECO:0000256|ARBA:ARBA00004552}. Cell projection, filopodium tip
CC {ECO:0000256|ARBA:ARBA00004495}. Cell projection, growth cone
CC {ECO:0000256|ARBA:ARBA00004624}. Cell projection, neuron projection
CC {ECO:0000256|ARBA:ARBA00004487}. Chromosome, centromere
CC {ECO:0000256|ARBA:ARBA00004584}. Cytoplasm, Cytoplasmic
CC ribonucleoprotein granule {ECO:0000256|ARBA:ARBA00004331}. Cytoplasm,
CC Stress granule {ECO:0000256|ARBA:ARBA00004210}. Cytoplasm, perinuclear
CC region {ECO:0000256|ARBA:ARBA00004556}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}. Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}. Perikaryon
CC {ECO:0000256|ARBA:ARBA00004484}. Presynaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034111}. Synapse, synaptosome
CC {ECO:0000256|ARBA:ARBA00034102}. Synaptic cell membrane
CC {ECO:0000256|ARBA:ARBA00034109}.
CC -!- SIMILARITY: Belongs to the FMR1 family.
CC {ECO:0000256|ARBA:ARBA00006633}.
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DR EMBL; KC877972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KC877974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF454876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF495784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF510171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L29074; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A8MQB8; -.
DR SMR; A8MQB8; -.
DR IntAct; A8MQB8; 2.
DR EPD; A8MQB8; -.
DR MassIVE; A8MQB8; -.
DR MaxQB; A8MQB8; -.
DR PeptideAtlas; A8MQB8; -.
DR ProteomicsDB; 1944; -.
DR Antibodypedia; 3246; 834 antibodies from 45 providers.
DR Ensembl; ENST00000370477.5; ENSP00000359508.1; ENSG00000102081.16.
DR UCSC; uc065blo.1; human.
DR HGNC; HGNC:3775; FMR1.
DR VEuPathDB; HostDB:ENSG00000102081; -.
DR GeneTree; ENSGT00950000183189; -.
DR ChiTaRS; FMR1; human.
DR Proteomes; UP000005640; Chromosome X.
DR Bgee; ENSG00000102081; Expressed in caput epididymis and 213 other cell types or tissues.
DR ExpressionAtlas; A8MQB8; baseline and differential.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0032433; C:filopodium tip; IEA:UniProtKB-SubCell.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR CDD; cd22506; KH_I_FMR1_rpt1; 1.
DR CDD; cd22509; KH_I_FMR1_rpt2; 1.
DR CDD; cd22512; KH_I_FMR1_rpt3; 1.
DR CDD; cd20471; Tudor_Agenet_FMR1_rpt1; 1.
DR CDD; cd20474; Tudor_Agenet_FMR1_rpt2; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 3.
DR InterPro; IPR008395; Agenet-like_dom.
DR InterPro; IPR040148; FMR1.
DR InterPro; IPR022034; FMR1-like_C_core.
DR InterPro; IPR032196; FMR1_C2.
DR InterPro; IPR040472; FMRP_KH0.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR047438; KH_I_FMR1_rpt1.
DR InterPro; IPR047440; KH_I_FMR1_rpt2.
DR InterPro; IPR047431; Tudor_Agenet_FMR1_rpt1.
DR InterPro; IPR047436; Tudor_Agenet_FMR1_rpt2.
DR InterPro; IPR041560; Tudor_FRM1.
DR PANTHER; PTHR10603; FRAGILE X MENTAL RETARDATION SYNDROME-RELATED PROTEIN; 1.
DR PANTHER; PTHR10603:SF4; SYNAPTIC FUNCTIONAL REGULATOR FMR1; 1.
DR Pfam; PF05641; Agenet; 1.
DR Pfam; PF16098; FXMR_C2; 1.
DR Pfam; PF12235; FXMRP1_C_core; 1.
DR Pfam; PF00013; KH_1; 2.
DR Pfam; PF17904; KH_9; 1.
DR Pfam; PF18336; Tudor_FRX1; 1.
DR SMART; SM00322; KH; 2.
DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 2.
DR PROSITE; PS51641; AGENET_LIKE; 2.
DR PROSITE; PS50084; KH_TYPE_1; 2.
PE 1: Evidence at protein level;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Centromere {ECO:0000256|ARBA:ARBA00023328};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187};
KW mRNA transport {ECO:0000256|ARBA:ARBA00022816};
KW Neurogenesis {ECO:0000256|ARBA:ARBA00022902};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteomics identification {ECO:0007829|EPD:A8MQB8,
KW ECO:0007829|MaxQB:A8MQB8};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Repressor {ECO:0000256|ARBA:ARBA00022491};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00117}; Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Synaptosome {ECO:0000256|ARBA:ARBA00022599};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 4..50
FT /note="Agenet-like"
FT /evidence="ECO:0000259|PROSITE:PS51641"
FT DOMAIN 63..115
FT /note="Agenet-like"
FT /evidence="ECO:0000259|PROSITE:PS51641"
FT REGION 325..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 516..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..571
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 582 AA; 65822 MW; A2F295E12184C3D0 CRC64;
MEELVVEVRG SNGAFYKAFV KDVHEDSITV AFENNWQPDR QIPFHDVRFP PPVGYNKDIN
ESDEVEVYSR ANEKEPCCWW LAKVRMIKGE FYVIEYAACD ATYNEIVTIE RLRSVNPNKP
ATKDTFHKIK LDVPEDLRQM CAKEAAHKDF KKAVGAFSVT YDPENYQLVI LSINEVTSKR
AHMLIDMHFR SLRTKLSLIM RNEEASKQLE SSRQLASRFH EQFIVREDLM GLAIGTHGAN
IQQARKVPGV TAIDLDEDTC TFHIYGEDQD AVKKARSFLE FAEDVIQVPR NLVGKVIGKN
GKLIQEIVDK SGVVRVRIEA ENEKNVPQEE EIMPPNSLPS NNSRVGPNAP EEKKHLDIKE
NSTHFSQPNS TKVQRGMVPF VFVGTKDSIA NATVLLDYHL NYLKEVDQLR LERLQIDEQL
RQIGASSRPP PNRTDKEKSY VTDDGQGMGR GSRPYRNRGH GRRGPGYTSE SDHRDELSDW
SLAPTEEERE SFLRRGDGRR RGGGGRGQGG RGRGGGFKGN DDHSRTDNRP RNPREAKGRT
TDGSLQNTSS EGSRLRTGKD RNQKKEKPDS VDGQQPLVNG VP
//
