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LIN37_HUMAN
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   03-AUG-2022, entry version 146.
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};
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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   PDBsum; 7N40; -.
DR   AlphaFoldDB; Q96GY3; -.
DR   SMR; Q96GY3; -.
DR   BioGRID; 121008; 91.
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; Q96GY3; -.
DR   PeptideAtlas; Q96GY3; -.
DR   PRIDE; Q96GY3; -.
DR   ProteomicsDB; 76683; -.
DR   Antibodypedia; 65388; 70 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   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; CPSVREP; -.
DR   OrthoDB; 1278998at2759; -.
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; 82 hits in 1048 CRISPR screens.
DR   ChiTaRS; LIN37; human.
DR   GenomeRNAi; 55957; -.
DR   Pharos; Q96GY3; Tdark.
DR   PRO; PR:Q96GY3; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q96GY3; protein.
DR   Bgee; ENSG00000267796; Expressed in right hemisphere of cerebellum and 95 other tissues.
DR   ExpressionAtlas; Q96GY3; baseline and differential.
DR   Genevisible; Q96GY3; HS.
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; PTHR31336; 1.
DR   Pfam; PF15306; LIN37; 1.
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"
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
 
 
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