LS14B_HUMAN
ID LS14B_HUMAN Reviewed; 385 AA.
AC Q9BX40; Q6PFW8; Q96LH8;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protein LSM14 homolog B;
DE AltName: Full=RNA-associated protein 55B {ECO:0000303|PubMed:18723115};
DE Short=hRAP55B {ECO:0000303|PubMed:18723115};
GN Name=LSM14B {ECO:0000312|HGNC:HGNC:15887};
GN Synonyms=C20orf40 {ECO:0000312|HGNC:HGNC:15887},
GN FAM61B {ECO:0000312|HGNC:HGNC:15887}, RAP55B {ECO:0000303|PubMed:18723115};
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 3).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Ovary;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 57-361 (ISOFORM 1).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-115 AND SER-154, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP REVIEW.
RX PubMed=18723115; DOI=10.1016/j.biocel.2008.06.015;
RA Marnef A., Sommerville J., Ladomery M.R.;
RT "RAP55: insights into an evolutionarily conserved protein family.";
RL Int. J. Biochem. Cell Biol. 41:977-981(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165; SER-329 AND SER-349, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-248, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [12]
RP INTERACTION WITH DDX6.
RX PubMed=31422817; DOI=10.1016/j.ajhg.2019.07.010;
RA Balak C., Benard M., Schaefer E., Iqbal S., Ramsey K., Ernoult-Lange M.,
RA Mattioli F., Llaci L., Geoffroy V., Courel M., Naymik M., Bachman K.K.,
RA Pfundt R., Rump P., Ter Beest J., Wentzensen I.M., Monaghan K.G.,
RA McWalter K., Richholt R., Le Bechec A., Jepsen W., De Both M., Belnap N.,
RA Boland A., Piras I.S., Deleuze J.F., Szelinger S., Dollfus H., Chelly J.,
RA Muller J., Campbell A., Lal D., Rangasamy S., Mandel J.L., Narayanan V.,
RA Huentelman M., Weil D., Piton A.;
RT "Rare de novo missense variants in RNA helicase DDX6 cause intellectual
RT disability and dysmorphic features and lead to P-body defects and RNA
RT dysregulation.";
RL Am. J. Hum. Genet. 105:509-525(2019).
CC -!- FUNCTION: Required for oocyte meiotic maturation. May be involved in
CC the storage of translationally inactive mRNAs and protect them from
CC degradation (By similarity). Plays a role in control of mRNA
CC translation (By similarity). {ECO:0000250|UniProtKB:Q68FI1,
CC ECO:0000250|UniProtKB:Q8CGC4}.
CC -!- SUBUNIT: Component of a ribonucleoprotein (RNP) complex (By
CC similarity). Interacts with DDX6 (PubMed:31422817).
CC {ECO:0000250|UniProtKB:Q68FI1, ECO:0000269|PubMed:31422817}.
CC -!- INTERACTION:
CC Q9BX40-2; P14136: GFAP; NbExp=3; IntAct=EBI-19133880, EBI-744302;
CC Q9BX40-2; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-19133880, EBI-748420;
CC Q9BX40-2; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-19133880, EBI-1055254;
CC Q9BX40-2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-19133880, EBI-741158;
CC Q9BX40-2; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-19133880, EBI-11955057;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BX40-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BX40-2; Sequence=VSP_014660;
CC Name=3;
CC IsoId=Q9BX40-3; Sequence=VSP_014658, VSP_014659, VSP_014661,
CC VSP_014662;
CC -!- SIMILARITY: Belongs to the LSM14 family. {ECO:0000305}.
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DR EMBL; AK058202; BAB71714.1; -; mRNA.
DR EMBL; AL137077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057387; AAH57387.1; -; mRNA.
DR EMBL; BX354437; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS46626.1; -. [Q9BX40-1]
DR RefSeq; NP_653304.2; NM_144703.2. [Q9BX40-1]
DR AlphaFoldDB; Q9BX40; -.
DR SMR; Q9BX40; -.
DR BioGRID; 127252; 81.
DR IntAct; Q9BX40; 35.
DR MINT; Q9BX40; -.
DR STRING; 9606.ENSP00000279068; -.
DR iPTMnet; Q9BX40; -.
DR MetOSite; Q9BX40; -.
DR PhosphoSitePlus; Q9BX40; -.
DR BioMuta; LSM14B; -.
DR DMDM; 71151896; -.
DR EPD; Q9BX40; -.
DR jPOST; Q9BX40; -.
DR MassIVE; Q9BX40; -.
DR MaxQB; Q9BX40; -.
DR PaxDb; Q9BX40; -.
DR PeptideAtlas; Q9BX40; -.
DR PRIDE; Q9BX40; -.
DR ProteomicsDB; 79344; -. [Q9BX40-1]
DR ProteomicsDB; 79345; -. [Q9BX40-2]
DR ProteomicsDB; 79346; -. [Q9BX40-3]
DR Antibodypedia; 52743; 62 antibodies from 13 providers.
DR DNASU; 149986; -.
DR Ensembl; ENST00000279068.11; ENSP00000279068.5; ENSG00000149657.20. [Q9BX40-1]
DR GeneID; 149986; -.
DR KEGG; hsa:149986; -.
DR MANE-Select; ENST00000279068.11; ENSP00000279068.5; NM_144703.3; NP_653304.2.
DR UCSC; uc002ybt.3; human. [Q9BX40-1]
DR CTD; 149986; -.
DR GeneCards; LSM14B; -.
DR HGNC; HGNC:15887; LSM14B.
DR HPA; ENSG00000149657; Low tissue specificity.
DR neXtProt; NX_Q9BX40; -.
DR OpenTargets; ENSG00000149657; -.
DR PharmGKB; PA25754; -.
DR VEuPathDB; HostDB:ENSG00000149657; -.
DR eggNOG; KOG1073; Eukaryota.
DR GeneTree; ENSGT00940000156010; -.
DR HOGENOM; CLU_019221_0_0_1; -.
DR InParanoid; Q9BX40; -.
DR OMA; HPRWSPY; -.
DR OrthoDB; 1569369at2759; -.
DR PhylomeDB; Q9BX40; -.
DR TreeFam; TF313514; -.
DR PathwayCommons; Q9BX40; -.
DR SignaLink; Q9BX40; -.
DR BioGRID-ORCS; 149986; 10 hits in 1078 CRISPR screens.
DR ChiTaRS; LSM14B; human.
DR GenomeRNAi; 149986; -.
DR Pharos; Q9BX40; Tdark.
DR PRO; PR:Q9BX40; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9BX40; protein.
DR Bgee; ENSG00000149657; Expressed in sperm and 149 other tissues.
DR ExpressionAtlas; Q9BX40; baseline and differential.
DR Genevisible; Q9BX40; HS.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd01736; LSm14_N; 1.
DR InterPro; IPR025762; DFDF.
DR InterPro; IPR019050; FDF_dom.
DR InterPro; IPR025761; FFD_box.
DR InterPro; IPR025609; Lsm14-like_N.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR025768; TFG_box.
DR Pfam; PF09532; FDF; 1.
DR Pfam; PF12701; LSM14; 1.
DR SMART; SM01199; FDF; 1.
DR SMART; SM01271; LSM14; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
DR PROSITE; PS51512; DFDF; 1.
DR PROSITE; PS51513; FFD; 1.
DR PROSITE; PS51536; TFG; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Developmental protein; Isopeptide bond;
KW Methylation; Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Translation regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..385
FT /note="Protein LSM14 homolog B"
FT /id="PRO_0000187093"
FT DOMAIN 241..277
FT /note="DFDF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00845"
FT REGION 164..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 310..326
FT /note="FFD box"
FT MOTIF 330..350
FT /note="TFG box"
FT COMPBIAS 177..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 351
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8CGC4"
FT CROSSLNK 248
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..44
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014658"
FT VAR_SEQ 45..142
FT /note="SFGTEDRPTDRPAPPREEIYEYIIFRGSDIKDITVCEPPKAQHTLPQDPAIV
FT QSSLGSASASPFQPHVPYSPFRGMAPYGPLAASSLLSQQYAASLGL -> MAPYGPLAA
FT SSLLSQQYAASLGLEKLVSPPASAAASSPSSSPSPQPVSELDLSSEPQQLTAKGCLFCF
FT RSLFTYTQSHIVLFRVPTGPGTLEREEMER (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014659"
FT VAR_SEQ 143..220
FT /note="GAGFPSIPVGKSPMVEQAVQTGSADNLNAKKLLPGKGTTGTQLNGRQAQPSS
FT KTASDVVQPAAVQAQGQVNDENRRPQ -> EKLVSPPASAAASSPSSSPSPQPVSELDL
FT SSEPQQLTAKGNSSLGELHAVLQTILRARGKAADRMTVAVADHLPSPCS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014660"
FT VAR_SEQ 274..283
FT /note="KLNFKDDKAE -> RPILLLVFWT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014661"
FT VAR_SEQ 284..385
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014662"
FT CONFLICT 66
FT /note="Y -> N (in Ref. 4; BX354437)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="H -> N (in Ref. 4; BX354437)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="Y -> N (in Ref. 4; BX354437)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 385 AA; 42071 MW; 9F1216A57330EE32 CRC64;
MSGSSGTPYL GSKISLISKA QIRYEGILYT IDTDNSTVAL AKVRSFGTED RPTDRPAPPR
EEIYEYIIFR GSDIKDITVC EPPKAQHTLP QDPAIVQSSL GSASASPFQP HVPYSPFRGM
APYGPLAASS LLSQQYAASL GLGAGFPSIP VGKSPMVEQA VQTGSADNLN AKKLLPGKGT
TGTQLNGRQA QPSSKTASDV VQPAAVQAQG QVNDENRRPQ RRRSGNRRTR NRSRGQNRPT
NVKENTIKFE GDFDFESANA QFNREELDKE FKKKLNFKDD KAEKGEEKDL AVVTQSAEAP
AEEDLLGPNC YYDKSKSFFD NISSELKTSS RRTTWAEERK LNTETFGVSG RFLRGRSSRG
GFRGGRGNGT TRRNPTSHRA GTGRV
