TMOD3_HUMAN
ID TMOD3_HUMAN Reviewed; 352 AA.
AC Q9NYL9; B2R6G7; Q9NT43; Q9NZR0;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Tropomodulin-3;
DE AltName: Full=Ubiquitous tropomodulin;
DE Short=U-Tmod;
GN Name=TMOD3;
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 [MRNA].
RA Conley C.A., Fowler V.M.;
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10662549; DOI=10.1006/geno.1999.6061;
RA Cox P.R., Zoghbi H.Y.;
RT "Sequencing, expression analysis, and mapping of three unique human
RT tropomodulin genes and their mouse orthologs.";
RL Genomics 63:97-107(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 264-352.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP PROTEIN SEQUENCE OF 318-328, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Blocks the elongation and depolymerization of the actin
CC filaments at the pointed end. The Tmod/TM complex contributes to the
CC formation of the short actin protofilament, which in turn defines the
CC geometry of the membrane skeleton (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to the N-terminus of tropomyosin and to actin.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10662549}.
CC -!- SIMILARITY: Belongs to the tropomodulin family. {ECO:0000305}.
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DR EMBL; AF237631; AAF45299.1; -; mRNA.
DR EMBL; AF177171; AAF31670.1; -; mRNA.
DR EMBL; AK312569; BAG35464.1; -; mRNA.
DR EMBL; BC020542; AAH20542.1; -; mRNA.
DR EMBL; AL137543; CAB70801.1; -; mRNA.
DR CCDS; CCDS10145.1; -.
DR PIR; T46384; T46384.
DR RefSeq; NP_055362.1; NM_014547.4.
DR RefSeq; XP_016877576.1; XM_017022087.1.
DR RefSeq; XP_016877577.1; XM_017022088.1.
DR AlphaFoldDB; Q9NYL9; -.
DR SMR; Q9NYL9; -.
DR BioGRID; 118899; 209.
DR IntAct; Q9NYL9; 120.
DR MINT; Q9NYL9; -.
DR STRING; 9606.ENSP00000308753; -.
DR GlyGen; Q9NYL9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NYL9; -.
DR MetOSite; Q9NYL9; -.
DR PhosphoSitePlus; Q9NYL9; -.
DR SwissPalm; Q9NYL9; -.
DR BioMuta; TMOD3; -.
DR DMDM; 23396884; -.
DR OGP; Q9NYL9; -.
DR EPD; Q9NYL9; -.
DR jPOST; Q9NYL9; -.
DR MassIVE; Q9NYL9; -.
DR MaxQB; Q9NYL9; -.
DR PaxDb; Q9NYL9; -.
DR PeptideAtlas; Q9NYL9; -.
DR PRIDE; Q9NYL9; -.
DR ProteomicsDB; 83252; -.
DR TopDownProteomics; Q9NYL9; -.
DR Antibodypedia; 978; 156 antibodies from 28 providers.
DR DNASU; 29766; -.
DR Ensembl; ENST00000308580.12; ENSP00000308753.7; ENSG00000138594.14.
DR GeneID; 29766; -.
DR KEGG; hsa:29766; -.
DR MANE-Select; ENST00000308580.12; ENSP00000308753.7; NM_014547.5; NP_055362.1.
DR UCSC; uc002abn.4; human.
DR CTD; 29766; -.
DR DisGeNET; 29766; -.
DR GeneCards; TMOD3; -.
DR HGNC; HGNC:11873; TMOD3.
DR HPA; ENSG00000138594; Low tissue specificity.
DR MIM; 605112; gene.
DR neXtProt; NX_Q9NYL9; -.
DR OpenTargets; ENSG00000138594; -.
DR PharmGKB; PA36574; -.
DR VEuPathDB; HostDB:ENSG00000138594; -.
DR eggNOG; KOG3735; Eukaryota.
DR GeneTree; ENSGT00940000158280; -.
DR HOGENOM; CLU_031052_0_1_1; -.
DR InParanoid; Q9NYL9; -.
DR OMA; NTHVKHF; -.
DR OrthoDB; 1025132at2759; -.
DR PhylomeDB; Q9NYL9; -.
DR TreeFam; TF315841; -.
DR PathwayCommons; Q9NYL9; -.
DR Reactome; R-HSA-390522; Striated Muscle Contraction.
DR Reactome; R-HSA-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-HSA-9696264; RND3 GTPase cycle.
DR SignaLink; Q9NYL9; -.
DR BioGRID-ORCS; 29766; 16 hits in 1074 CRISPR screens.
DR ChiTaRS; TMOD3; human.
DR GeneWiki; TMOD3; -.
DR GenomeRNAi; 29766; -.
DR Pharos; Q9NYL9; Tbio.
DR PRO; PR:Q9NYL9; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9NYL9; protein.
DR Bgee; ENSG00000138594; Expressed in amniotic fluid and 182 other tissues.
DR ExpressionAtlas; Q9NYL9; baseline and differential.
DR Genevisible; Q9NYL9; HS.
DR GO; GO:0005912; C:adherens junction; HDA:BHF-UCL.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0030016; C:myofibril; IBA:GO_Central.
DR GO; GO:0005865; C:striated muscle thin filament; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; HDA:BHF-UCL.
DR GO; GO:0005523; F:tropomyosin binding; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0048821; P:erythrocyte development; IEA:Ensembl.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:Ensembl.
DR GO; GO:0006936; P:muscle contraction; IBA:GO_Central.
DR GO; GO:0030239; P:myofibril assembly; IBA:GO_Central.
DR GO; GO:0051694; P:pointed-end actin filament capping; IEA:InterPro.
DR GO; GO:1901992; P:positive regulation of mitotic cell cycle phase transition; IEA:Ensembl.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR004934; TMOD.
DR InterPro; IPR030133; TMOD3.
DR PANTHER; PTHR10901; PTHR10901; 1.
DR PANTHER; PTHR10901:SF18; PTHR10901:SF18; 1.
DR Pfam; PF03250; Tropomodulin; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..352
FT /note="Tropomodulin-3"
FT /id="PRO_0000186134"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT CONFLICT 27
FT /note="T -> S (in Ref. 2; AAF31670)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 352 AA; 39595 MW; 8B7F2122C1BE9855 CRC64;
MALPFRKDLE KYKDLDEDEL LGNLSETELK QLETVLDDLD PENALLPAGF RQKNQTSKST
TGPFDREHLL SYLEKEALEH KDREDYVPYT GEKKGKIFIP KQKPVQTFTE EKVSLDPELE
EALTSASDTE LCDLAAILGM HNLITNTKFC NIMGSSNGVD QEHFSNVVKG EKILPVFDEP
PNPTNVEESL KRTKENDAHL VEVNLNNIKN IPIPTLKDFA KALETNTHVK CFSLAATRSN
DPVATAFAEM LKVNKTLKSL NVESNFITGV GILALIDALR DNETLAELKI DNQRQQLGTA
VELEMAKMLE ENTNILKFGY QFTQQGPRTR AANAITKNND LVRKRRVEGD HQ
