TPPP3_HUMAN
ID TPPP3_HUMAN Reviewed; 176 AA.
AC Q9BW30; Q49AH9; Q9Y326; Q9Y6H0;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Tubulin polymerization-promoting protein family member 3 {ECO:0000303|PubMed:19633818};
DE AltName: Full=TPPP/p20 {ECO:0000303|PubMed:17105200};
GN Name=TPPP3 {ECO:0000303|PubMed:19633818, ECO:0000312|HGNC:HGNC:24162};
GN ORFNames=CGI-38 {ECO:0000303|PubMed:10810093};
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=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17105200; DOI=10.1021/bi061305e;
RA Vincze O., Toekesi N., Olah J., Hlavanda E., Zotter A., Horvath I.,
RA Lehotzky A., Tirian L., Medzihradszky K.F., Kovacs J., Orosz F., Ovadi J.;
RT "Tubulin polymerization promoting proteins (TPPPs): members of a new family
RT with distinct structures and functions.";
RL Biochemistry 45:13818-13826(2006).
RN [5]
RP FUNCTION.
RX PubMed=19633818; DOI=10.1007/s11010-009-0208-0;
RA Zhou W., Wang X., Li L., Feng X., Yang Z., Zhang W., Hu R.;
RT "Depletion of tubulin polymerization promoting protein family member 3
RT suppresses HeLa cell proliferation.";
RL Mol. Cell. Biochem. 333:91-98(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=30667362; DOI=10.1530/joe-18-0459;
RA Shukla V., Kaushal J.B., Sankhwar P., Manohar M., Dwivedi A.;
RT "Inhibition of TPPP3 attenuates beta-catenin/NF-kappaB/COX-2 signaling in
RT endometrial stromal cells and impairs decidualization.";
RL J. Endocrinol. 240:417-429(2019).
RN [8]
RP STRUCTURE BY NMR.
RG Northeast structural genomics consortium (NESG);
RT "Solution NMR structure of tubulin polymerization-promoting protein family
RT member 3 from Homo sapiens.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Regulator of microtubule dynamic that has microtubule
CC bundling activity (PubMed:17105200, PubMed:19633818). Required for
CC embryo implantation; possibly by regulating beta-catenin (By
CC similarity). Also required for decidualization via regulation of beta-
CC catenin (PubMed:30667362). {ECO:0000250|UniProtKB:Q9CRB6,
CC ECO:0000269|PubMed:17105200, ECO:0000269|PubMed:19633818,
CC ECO:0000269|PubMed:30667362}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:30667362}.
CC Cytoplasm, cytoskeleton {ECO:0000305|PubMed:17105200}.
CC -!- TISSUE SPECIFICITY: Expressed in endometrium during the mid-secretory
CC phase (LH + 7) (at protein level). {ECO:0000269|PubMed:30667362}.
CC -!- SIMILARITY: Belongs to the TPPP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD44478.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF132972; AAD27747.1; -; mRNA.
DR EMBL; AF078846; AAD44478.1; ALT_FRAME; mRNA.
DR EMBL; BC000691; AAH00691.1; -; mRNA.
DR CCDS; CCDS10835.1; -.
DR RefSeq; NP_057048.2; NM_015964.3.
DR RefSeq; NP_057224.2; NM_016140.3.
DR PDB; 2JRF; NMR; -; A=1-176.
DR PDBsum; 2JRF; -.
DR AlphaFoldDB; Q9BW30; -.
DR BMRB; Q9BW30; -.
DR SMR; Q9BW30; -.
DR BioGRID; 119673; 10.
DR IntAct; Q9BW30; 2.
DR STRING; 9606.ENSP00000462435; -.
DR GlyGen; Q9BW30; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BW30; -.
DR PhosphoSitePlus; Q9BW30; -.
DR BioMuta; TPPP3; -.
DR DMDM; 28380040; -.
DR jPOST; Q9BW30; -.
DR MassIVE; Q9BW30; -.
DR MaxQB; Q9BW30; -.
DR PaxDb; Q9BW30; -.
DR PeptideAtlas; Q9BW30; -.
DR PRIDE; Q9BW30; -.
DR ProteomicsDB; 79252; -.
DR Antibodypedia; 29534; 198 antibodies from 25 providers.
DR DNASU; 51673; -.
DR Ensembl; ENST00000290942.9; ENSP00000290942.5; ENSG00000159713.11.
DR Ensembl; ENST00000393957.7; ENSP00000377529.2; ENSG00000159713.11.
DR Ensembl; ENST00000562206.1; ENSP00000457275.1; ENSG00000159713.11.
DR Ensembl; ENST00000564104.5; ENSP00000462435.1; ENSG00000159713.11.
DR GeneID; 51673; -.
DR KEGG; hsa:51673; -.
DR MANE-Select; ENST00000393957.7; ENSP00000377529.2; NM_015964.4; NP_057048.2.
DR UCSC; uc002esz.5; human.
DR CTD; 51673; -.
DR DisGeNET; 51673; -.
DR GeneCards; TPPP3; -.
DR HGNC; HGNC:24162; TPPP3.
DR HPA; ENSG00000159713; Tissue enhanced (fallopian).
DR MIM; 616957; gene.
DR neXtProt; NX_Q9BW30; -.
DR OpenTargets; ENSG00000159713; -.
DR PharmGKB; PA162406823; -.
DR VEuPathDB; HostDB:ENSG00000159713; -.
DR eggNOG; KOG4070; Eukaryota.
DR GeneTree; ENSGT00940000153875; -.
DR HOGENOM; CLU_091734_0_0_1; -.
DR InParanoid; Q9BW30; -.
DR OMA; PKASGHE; -.
DR OrthoDB; 1317210at2759; -.
DR PhylomeDB; Q9BW30; -.
DR TreeFam; TF314440; -.
DR PathwayCommons; Q9BW30; -.
DR SignaLink; Q9BW30; -.
DR BioGRID-ORCS; 51673; 11 hits in 1061 CRISPR screens.
DR ChiTaRS; TPPP3; human.
DR EvolutionaryTrace; Q9BW30; -.
DR GenomeRNAi; 51673; -.
DR Pharos; Q9BW30; Tbio.
DR PRO; PR:Q9BW30; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9BW30; protein.
DR Bgee; ENSG00000159713; Expressed in right uterine tube and 99 other tissues.
DR ExpressionAtlas; Q9BW30; baseline and differential.
DR Genevisible; Q9BW30; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR GO; GO:0046697; P:decidualization; IMP:UniProtKB.
DR GO; GO:0007566; P:embryo implantation; ISS:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; IDA:UniProtKB.
DR GO; GO:0046785; P:microtubule polymerization; IEA:InterPro.
DR GO; GO:0032273; P:positive regulation of protein polymerization; IBA:GO_Central.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR008907; P25-alpha.
DR InterPro; IPR030795; TPPP3.
DR PANTHER; PTHR12932; PTHR12932; 1.
DR PANTHER; PTHR12932:SF16; PTHR12932:SF16; 1.
DR Pfam; PF05517; p25-alpha; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Cytoskeleton; Microtubule;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..176
FT /note="Tubulin polymerization-promoting protein family
FT member 3"
FT /id="PRO_0000221138"
FT REGION 132..152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CONFLICT 7
FT /note="M -> I (in Ref. 2; AAD44478)"
FT /evidence="ECO:0000305"
FT CONFLICT 10..11
FT /note="LE -> PK (in Ref. 2; AAD44478)"
FT /evidence="ECO:0000305"
FT CONFLICT 52..54
FT /note="GTD -> TP (in Ref. 2; AAD44478)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="K -> G (in Ref. 2; AAD44478)"
FT /evidence="ECO:0000305"
FT CONFLICT 88
FT /note="K -> Q (in Ref. 1; AAD27747)"
FT /evidence="ECO:0000305"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:2JRF"
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:2JRF"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:2JRF"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:2JRF"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:2JRF"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:2JRF"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:2JRF"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:2JRF"
FT HELIX 72..86
FT /evidence="ECO:0007829|PDB:2JRF"
FT HELIX 92..101
FT /evidence="ECO:0007829|PDB:2JRF"
FT TURN 102..105
FT /evidence="ECO:0007829|PDB:2JRF"
FT STRAND 108..112
FT /evidence="ECO:0007829|PDB:2JRF"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:2JRF"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:2JRF"
FT TURN 146..150
FT /evidence="ECO:0007829|PDB:2JRF"
SQ SEQUENCE 176 AA; 18985 MW; 20EA146E93FB1ADF CRC64;
MAASTDMAGL EESFRKFAIH GDPKASGQEM NGKNWAKLCK DCKVADGKSV TGTDVDIVFS
KVKGKSARVI NYEEFKKALE ELATKRFKGK SKEEAFDAIC QLVAGKEPAN VGVTKAKTGG
AVDRLTDTSR YTGSHKERFD ESGKGKGIAG RQDILDDSGY VSAYKNAGTY DAKVKK
