FA98B_HUMAN
ID FA98B_HUMAN Reviewed; 433 AA.
AC Q52LJ0; A8MUW5; Q8N935;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein FAM98B;
GN Name=FAM98B;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [4]
RP SUBCELLULAR LOCATION.
RX PubMed=18445686; DOI=10.1242/jcs.019174;
RA Tegha-Dunghu J., Neumann B., Reber S., Krause R., Erfle H., Walter T.,
RA Held M., Rogers P., Hupfeld K., Ruppert T., Ellenberg J., Gruss O.J.;
RT "EML3 is a nuclear microtubule-binding protein required for the correct
RT alignment of chromosomes in metaphase.";
RL J. Cell Sci. 121:1718-1726(2008).
RN [5]
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., Buerckstuemmer 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 [6]
RP IDENTIFICATION IN THE TRNA SPLICING LIGASE COMPLEX.
RX PubMed=21311021; DOI=10.1126/science.1197847;
RA Popow J., Englert M., Weitzer S., Schleiffer A., Mierzwa B., Mechtler K.,
RA Trowitzsch S., Will C.L., Luhrmann R., Soll D., Martinez J.;
RT "HSPC117 is the essential subunit of a human tRNA splicing ligase
RT complex.";
RL Science 331:760-764(2011).
RN [7]
RP IDENTIFICATION IN THE TRNA SPLICING LIGASE COMPLEX.
RX PubMed=24870230; DOI=10.1038/nature13284;
RA Popow J., Jurkin J., Schleiffer A., Martinez J.;
RT "Analysis of orthologous groups reveals archease and DDX1 as tRNA splicing
RT factors.";
RL Nature 511:104-107(2014).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=24608264; DOI=10.1371/journal.pone.0090957;
RA Perez-Gonzalez A., Pazo A., Navajas R., Ciordia S., Rodriguez-Frandsen A.,
RA Nieto A.;
RT "hCLE/C14orf166 associates with DDX1-HSPC117-FAM98B in a novel
RT transcription-dependent shuttling RNA-transporting complex.";
RL PLoS ONE 9:E90957-E90957(2014).
RN [9]
RP FUNCTION, INTERACTION WITH FAM98A, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=28040436; DOI=10.1016/j.biocel.2016.12.013;
RA Akter K.A., Mansour M.A., Hyodo T., Senga T.;
RT "FAM98A associates with DDX1-C14orf166-FAM98B in a novel complex involved
RT in colorectal cancer progression.";
RL Int. J. Biochem. Cell Biol. 84:1-13(2017).
CC -!- FUNCTION: Positively stimulates PRMT1-induced protein arginine
CC dimethylated arginine methylation (PubMed:28040436). Promotes
CC colorectal cancer cell malignancy (PubMed:28040436).
CC {ECO:0000269|PubMed:28040436}.
CC -!- SUBUNIT: Homodimer (PubMed:28040436). Component of the tRNA-splicing
CC ligase complex (PubMed:21311021, PubMed:24870230). Interacts with
CC FAM98A (PubMed:28040436). {ECO:0000269|PubMed:21311021,
CC ECO:0000269|PubMed:24870230, ECO:0000269|PubMed:28040436}.
CC -!- INTERACTION:
CC Q52LJ0; Q9Y224: RTRAF; NbExp=2; IntAct=EBI-1043130, EBI-1104547;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24608264}. Cytoplasm
CC {ECO:0000269|PubMed:18445686, ECO:0000269|PubMed:24608264}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2;
CC IsoId=Q52LJ0-2; Sequence=Displayed;
CC Name=1;
CC IsoId=Q52LJ0-1; Sequence=VSP_060151, VSP_060152;
CC -!- TISSUE SPECIFICITY: Expressed strongly in colorectal cancer tissues
CC compared to wild-type colon samples (at protein level)
CC (PubMed:28040436). Expressed strongly in colorectal cancer tissues
CC compared to wild-type colon samples (PubMed:28040436).
CC {ECO:0000269|PubMed:28040436}.
CC -!- MISCELLANEOUS: [Isoform 1]: Dubious isoform due to intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FAM98 family. {ECO:0000305}.
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DR EMBL; AK095745; BAC04621.1; -; mRNA.
DR EMBL; AC109631; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC116158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC093898; AAH93898.1; -; mRNA.
DR CCDS; CCDS10047.2; -. [Q52LJ0-2]
DR RefSeq; NP_775882.2; NM_173611.3. [Q52LJ0-2]
DR AlphaFoldDB; Q52LJ0; -.
DR BioGRID; 129661; 84.
DR ComplexPortal; CPX-6411; tRNA-splicing ligase complex.
DR CORUM; Q52LJ0; -.
DR DIP; DIP-50585N; -.
DR IntAct; Q52LJ0; 25.
DR MINT; Q52LJ0; -.
DR STRING; 9606.ENSP00000380734; -.
DR GlyGen; Q52LJ0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q52LJ0; -.
DR MetOSite; Q52LJ0; -.
DR PhosphoSitePlus; Q52LJ0; -.
DR SwissPalm; Q52LJ0; -.
DR BioMuta; FAM98B; -.
DR DMDM; 74735811; -.
DR EPD; Q52LJ0; -.
DR jPOST; Q52LJ0; -.
DR MassIVE; Q52LJ0; -.
DR MaxQB; Q52LJ0; -.
DR PaxDb; Q52LJ0; -.
DR PeptideAtlas; Q52LJ0; -.
DR PRIDE; Q52LJ0; -.
DR ProteomicsDB; 2137; -.
DR ProteomicsDB; 62424; -. [Q52LJ0-1]
DR Antibodypedia; 2032; 106 antibodies from 20 providers.
DR DNASU; 283742; -.
DR Ensembl; ENST00000397609.6; ENSP00000380734.2; ENSG00000171262.11. [Q52LJ0-2]
DR Ensembl; ENST00000491535.5; ENSP00000453166.1; ENSG00000171262.11. [Q52LJ0-1]
DR GeneID; 283742; -.
DR KEGG; hsa:283742; -.
DR MANE-Select; ENST00000397609.6; ENSP00000380734.2; NM_173611.4; NP_775882.2.
DR UCSC; uc001zkb.3; human. [Q52LJ0-2]
DR CTD; 283742; -.
DR DisGeNET; 283742; -.
DR GeneCards; FAM98B; -.
DR HGNC; HGNC:26773; FAM98B.
DR HPA; ENSG00000171262; Low tissue specificity.
DR MIM; 616142; gene.
DR neXtProt; NX_Q52LJ0; -.
DR OpenTargets; ENSG00000171262; -.
DR PharmGKB; PA142671778; -.
DR VEuPathDB; HostDB:ENSG00000171262; -.
DR eggNOG; KOG3973; Eukaryota.
DR GeneTree; ENSGT00440000037341; -.
DR HOGENOM; CLU_038408_1_1_1; -.
DR InParanoid; Q52LJ0; -.
DR OMA; NDQQWIS; -.
DR OrthoDB; 800008at2759; -.
DR PhylomeDB; Q52LJ0; -.
DR TreeFam; TF320308; -.
DR BioCyc; MetaCyc:ENSG00000171262-MON; -.
DR PathwayCommons; Q52LJ0; -.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR SignaLink; Q52LJ0; -.
DR BioGRID-ORCS; 283742; 248 hits in 1090 CRISPR screens.
DR ChiTaRS; FAM98B; human.
DR GenomeRNAi; 283742; -.
DR Pharos; Q52LJ0; Tdark.
DR PRO; PR:Q52LJ0; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q52LJ0; protein.
DR Bgee; ENSG00000171262; Expressed in upper arm skin and 194 other tissues.
DR ExpressionAtlas; Q52LJ0; baseline and differential.
DR Genevisible; Q52LJ0; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0072669; C:tRNA-splicing ligase complex; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0008276; F:protein methyltransferase activity; IMP:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0006479; P:protein methylation; IMP:UniProtKB.
DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IC:ComplexPortal.
DR InterPro; IPR018797; FAM98.
DR PANTHER; PTHR31353; PTHR31353; 1.
DR Pfam; PF10239; DUF2465; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Nucleus; Reference proteome.
FT CHAIN 1..433
FT /note="Protein FAM98B"
FT /id="PRO_0000187188"
FT REGION 303..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 301..330
FT /note="LMGRVPDRGGRPNEIEPPPPEMPPWQKRQE -> GVSFSTVENELMISYLMF
FT LQILVYFSFMSW (in isoform 1)"
FT /id="VSP_060151"
FT VAR_SEQ 331..433
FT /note="Missing (in isoform 1)"
FT /id="VSP_060152"
FT CONFLICT 22
FT /note="A -> T (in Ref. 1; BAC04621)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 433 AA; 45547 MW; 4A46D5F04FAB2530 CRC64;
MRGPEPGPQP TMEGDVLDTL EALGYKGPLL EEQALTKAAE GGLSSPEFSE LCIWLGSQIK
SLCNLEESIT SAGRDDLESF QLEISGFLKE MACPYSVLIS GDIKDRLKKK EDCLKLLLFL
STELQASQIL QNKKHKNSQL DKNSEVYQEV QAMFDTLGIP KSTTSDIPHM LNQVESKVKD
ILSKVQKNHV GKPLLKMDLN SEQAEQLERI NDALSCEYEC RRRMLMKRLD VTVQSFGWSD
RAKVKTDDIA RIYQPKRYAL SPKTTITMAH LLAAREDLSK IIRTSSGTSR EKTACAINKV
LMGRVPDRGG RPNEIEPPPP EMPPWQKRQE GGGGRGGWGG GGGGGGRGGG GGGGGRGGWG
GGGGGWGGGG GGGGGWGGGG GGGRGGFQGR GDYGGRGGYG GRGGYGGRGY GDPYGGGGGG
GGGGGGGGGY RRY
