ID RS27L_HUMAN Reviewed; 84 AA. AC Q71UM5; Q9BTJ1; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 09-JAN-2013, entry version 81. DE RecName: Full=40S ribosomal protein S27-like; GN Name=RPS27L; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Umbilical cord blood; RX MEDLINE=20499367; PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for RT 300 previously undefined genes expressed in CD34+ hematopoietic RT stem/progenitor cells."; RL Genome Res. 10:1546-1560(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND MASS RP SPECTROMETRY. 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 [4] 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., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- COFACTOR: Binds 1 zinc ion per subunit (Potential). CC -!- INTERACTION: CC Q00987:MDM2; NbExp=6; IntAct=EBI-355126, EBI-389668; CC -!- SIMILARITY: Belongs to the ribosomal protein S27e family. 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; AF070668; AAD20974.1; -; mRNA. DR EMBL; BC003667; AAH03667.1; -; mRNA. DR IPI; IPI00746004; -. DR RefSeq; NP_057004.1; NM_015920.3. DR UniGene; Hs.108957; -. DR ProteinModelPortal; Q71UM5; -. DR SMR; Q71UM5; 3-82. DR IntAct; Q71UM5; 9. DR MINT; MINT-1158751; -. DR STRING; Q71UM5; -. DR PhosphoSite; Q71UM5; -. DR DMDM; 51316258; -. DR PaxDb; Q71UM5; -. DR PRIDE; Q71UM5; -. DR DNASU; 51065; -. DR Ensembl; ENST00000330964; ENSP00000331019; ENSG00000185088. DR GeneID; 51065; -. DR KEGG; hsa:51065; -. DR UCSC; uc002aly.3; human. DR CTD; 51065; -. DR GeneCards; GC15M063445; -. DR HGNC; HGNC:18476; RPS27L. DR MIM; 612055; gene. DR neXtProt; NX_Q71UM5; -. DR PharmGKB; PA38546; -. DR eggNOG; COG2051; -. DR HOVERGEN; HBG000252; -. DR KO; K02978; -. DR OMA; AQTVVVC; -. DR OrthoDB; EOG4H19XB; -. DR GenomeRNAi; 51065; -. DR NextBio; 53659; -. DR ArrayExpress; Q71UM5; -. DR Bgee; Q71UM5; -. DR CleanEx; HS_RPS27L; -. DR Genevestigator; Q71UM5; -. DR GermOnline; ENSG00000185088; Homo sapiens. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0008494; F:translation activator activity; IDA:UniProtKB. DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB. DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IDA:UniProtKB. DR GO; GO:0031571; P:mitotic cell cycle G1/S transition DNA damage checkpoint; IMP:UniProtKB. DR GO; GO:0006412; P:translation; IDA:UniProtKB. DR Gene3D; 2.20.25.100; G3DSA:2.20.25.100; 1. DR InterPro; IPR000592; Ribosomal_S27e. DR InterPro; IPR023407; Ribosomal_S27e_Zn-bd_dom. DR InterPro; IPR011332; Ribosomal_zn-bd_dom. DR PANTHER; PTHR11594; PTHR11594; 1. DR Pfam; PF01667; Ribosomal_S27e; 1. DR ProDom; PD004466; Ribosomal_S27e; 1. DR SUPFAM; SSF57829; Ribosomal_zn-bd; 1. DR PROSITE; PS01168; RIBOSOMAL_S27E; 1. PE 1: Evidence at protein level; KW Complete proteome; Metal-binding; Phosphoprotein; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; Zinc; Zinc-finger. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 84 40S ribosomal protein S27-like. FT /FTId=PRO_0000149054. FT ZN_FING 38 60 C4-type. FT MOD_RES 27 27 Phosphoserine. FT CONFLICT 22 22 K -> E (in Ref. 2). SQ SEQUENCE 84 AA; 9477 MW; 271CCACFBB269E38 CRC64; MPLARDLLHP SLEEEKKKHK KKRLVQSPNS YFMDVKCPGC YKITTVFSHA QTVVLCVGCS TVLCQPTGGK ARLTEGCSFR RKQH //