ID LIN37_HUMAN Reviewed; 246 AA. AC Q96GY3; A8KAQ1; O14557; Q7Z2T9; DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 155. DE RecName: Full=Protein lin-37 homolog; DE AltName: Full=Antolefinin; GN Name=LIN37; ORFNames=MSTP064; 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]. 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=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Eye; 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 92-246. RC TISSUE=Aorta; RA Qin B.M., Sheng H., Liu Y.Q., Liu B., Zhao B., Wang X.Y., Zhang Q., RA Xu Y.Y., Song L., Je Y., Gao Y., Zhang C.L., Hui R.T.; RT "Homo sapiens normal aorta MST064."; RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases. RN [5] RP IDENTIFICATION IN THE DREAM COMPLEX. RX PubMed=17671431; DOI=10.4161/cc.6.15.4512; RA Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C., von Eyss B., RA Gagrica S., Haenel F., Brehm A., Gaubatz S.; RT "LINC, a human complex that is related to pRB-containing complexes in RT invertebrates regulates the expression of G2/M genes."; RL Cell Cycle 6:1903-1913(2007). RN [6] RP IDENTIFICATION IN THE DREAM COMPLEX. RX PubMed=17531812; DOI=10.1016/j.molcel.2007.04.015; RA Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K., RA Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.; RT "Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex RT represses human cell cycle-dependent genes in quiescence."; RL Mol. Cell 26:539-551(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-167, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; SER-182 AND SER-202, 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-138; SER-182 AND SER-202, 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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 [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [13] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-5 AND LYS-7, AND IDENTIFICATION RP BY MASS 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). CC -!- SUBUNIT: Component of the DREAM complex (also named LINC complex) at CC least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2, CC RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent CC cells where it represses cell cycle-dependent genes. It dissociates in CC S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds CC to MYBL2. {ECO:0000269|PubMed:17531812, ECO:0000269|PubMed:17671431}. CC -!- INTERACTION: CC Q96GY3; O95273: CCNDBP1; NbExp=3; IntAct=EBI-748884, EBI-748961; CC Q96GY3; Q01850: CDR2; NbExp=3; IntAct=EBI-748884, EBI-1181367; CC Q96GY3; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-748884, EBI-739624; CC Q96GY3; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-748884, EBI-2125614; CC Q96GY3; Q15323: KRT31; NbExp=3; IntAct=EBI-748884, EBI-948001; CC Q96GY3; Q6A162: KRT40; NbExp=3; IntAct=EBI-748884, EBI-10171697; CC Q96GY3; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-748884, EBI-741037; CC Q96GY3; P43360: MAGEA6; NbExp=6; IntAct=EBI-748884, EBI-1045155; CC Q96GY3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-748884, EBI-16439278; CC Q96GY3; Q5VU43-2: PDE4DIP; NbExp=3; IntAct=EBI-748884, EBI-9640281; CC Q96GY3; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-748884, EBI-302345; CC Q96GY3; O43586: PSTPIP1; NbExp=3; IntAct=EBI-748884, EBI-1050964; CC Q96GY3; Q8IYF3: TEX11; NbExp=2; IntAct=EBI-748884, EBI-742397; CC Q96GY3; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-748884, EBI-1105213; CC Q96GY3; Q13077: TRAF1; NbExp=3; IntAct=EBI-748884, EBI-359224; CC Q96GY3; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-748884, EBI-2130429; CC Q96GY3; P36508: ZNF76; NbExp=3; IntAct=EBI-748884, EBI-7254550; CC -!- SEQUENCE CAUTION: CC Sequence=AAB81199.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; 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; AK293116; BAF85805.1; -; mRNA. DR EMBL; AC002398; AAB81199.1; ALT_SEQ; Genomic_DNA. DR EMBL; AD000671; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC009071; AAH09071.1; -; mRNA. DR EMBL; AF162447; AAQ13584.1; -; mRNA. DR CCDS; CCDS62642.1; -. DR PIR; T00702; T00702. DR RefSeq; NP_061977.1; NM_019104.2. DR PDB; 7N40; X-ray; 2.55 A; C=92-130. DR PDB; 7R1D; EM; 3.50 A; B=1-246. DR PDBsum; 7N40; -. DR PDBsum; 7R1D; -. DR AlphaFoldDB; Q96GY3; -. DR EMDB; EMD-14239; -. DR SMR; Q96GY3; -. DR BioGRID; 121008; 93. DR ComplexPortal; CPX-2366; Myb-MuvB transcriptional activation complex. DR ComplexPortal; CPX-2368; DREAM transcriptional repressor complex, RBL1 variant. DR ComplexPortal; CPX-7461; DREAM transcriptional repressor complex, RBL2 variant. DR ComplexPortal; CPX-7462; Myb-MuvB-FOXM1 transcriptional activation complex. DR CORUM; Q96GY3; -. DR IntAct; Q96GY3; 43. DR MINT; Q96GY3; -. DR STRING; 9606.ENSP00000301159; -. DR GlyGen; Q96GY3; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q96GY3; -. DR PhosphoSitePlus; Q96GY3; -. DR BioMuta; LIN37; -. DR EPD; Q96GY3; -. DR jPOST; Q96GY3; -. DR MassIVE; Q96GY3; -. DR MaxQB; Q96GY3; -. DR PaxDb; 9606-ENSP00000301159; -. DR PeptideAtlas; Q96GY3; -. DR ProteomicsDB; 76683; -. DR Pumba; Q96GY3; -. DR Antibodypedia; 65388; 76 antibodies from 18 providers. DR DNASU; 55957; -. DR Ensembl; ENST00000301159.14; ENSP00000301159.7; ENSG00000267796.8. DR GeneID; 55957; -. DR KEGG; hsa:55957; -. DR MANE-Select; ENST00000301159.14; ENSP00000301159.7; NM_019104.3; NP_061977.1. DR UCSC; uc021usw.1; human. DR AGR; HGNC:33234; -. DR CTD; 55957; -. DR DisGeNET; 55957; -. DR GeneCards; LIN37; -. DR HGNC; HGNC:33234; LIN37. DR HPA; ENSG00000267796; Low tissue specificity. DR neXtProt; NX_Q96GY3; -. DR OpenTargets; ENSG00000267796; -. DR PharmGKB; PA162394016; -. DR VEuPathDB; HostDB:ENSG00000267796; -. DR eggNOG; ENOG502QV4J; Eukaryota. DR GeneTree; ENSGT00390000002748; -. DR InParanoid; Q96GY3; -. DR OMA; RGHWLKH; -. DR OrthoDB; 4188657at2759; -. DR PhylomeDB; Q96GY3; -. DR TreeFam; TF329230; -. DR PathwayCommons; Q96GY3; -. DR Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex. DR Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1. DR Reactome; R-HSA-1538133; G0 and Early G1. DR Reactome; R-HSA-156711; Polo-like kinase mediated events. DR Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition. DR Reactome; R-HSA-69205; G1/S-Specific Transcription. DR Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry. DR SignaLink; Q96GY3; -. DR BioGRID-ORCS; 55957; 89 hits in 1129 CRISPR screens. DR ChiTaRS; LIN37; human. DR GenomeRNAi; 55957; -. DR Pharos; Q96GY3; Tbio. DR PRO; PR:Q96GY3; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q96GY3; Protein. DR Bgee; ENSG00000267796; Expressed in right hemisphere of cerebellum and 97 other cell types or tissues. DR ExpressionAtlas; Q96GY3; baseline and differential. DR GO; GO:0031523; C:Myb complex; IBA:GO_Central. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0017053; C:transcription repressor complex; IEA:InterPro. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central. DR InterPro; IPR028226; LIN37. DR PANTHER; PTHR31336; LIN37 HOMOLOG; 1. DR PANTHER; PTHR31336:SF3; PROTEIN LIN-37 HOMOLOG; 1. DR Pfam; PF15306; LIN37; 1. DR Genevisible; Q96GY3; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Isopeptide bond; Phosphoprotein; KW Reference proteome; Ubl conjugation. FT CHAIN 1..246 FT /note="Protein lin-37 homolog" FT /id="PRO_0000238479" FT REGION 37..90 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 129..209 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 162..176 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 135 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9D8N6" FT MOD_RES 138 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 167 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 182 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332" FT MOD_RES 202 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT CROSSLNK 5 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 7 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 16 FT /note="A -> V (in dbSNP:rs170758)" FT /id="VAR_061674" FT VARIANT 172 FT /note="P -> S (in dbSNP:rs35617825)" FT /id="VAR_051093" FT STRAND 96..99 FT /evidence="ECO:0007829|PDB:7N40" FT STRAND 102..105 FT /evidence="ECO:0007829|PDB:7N40" FT HELIX 106..108 FT /evidence="ECO:0007829|PDB:7N40" FT HELIX 115..123 FT /evidence="ECO:0007829|PDB:7N40" SQ SEQUENCE 246 AA; 28383 MW; 8718E1C8FB13C446 CRC64; MFPVKVKVEK SELEMAKARN QLDAVLQCLL EKSHMDRERL DEEAGKTPSD THNKDCSIAA TGKRPSARFP HQRRKKRREM DDGLAEGGPQ RSNTYVIKLF DRSVDLAQFS ENTPLYPICR AWMRNSPSVR ERECSPSSPL PPLPEDEEGS EVTNSKSRDV YKLPPPTPPG PPGDACRSRI PSPLQPEMQG TPDDEPSEPE PSPSTLIYRN MQRWKRIRQR WKEASHRNQL RYSESMKILR EMYERQ //