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Trichoplein keratin filament-binding protein (Protein TCHP) (Mitochondrial protein with oncostatic activity) (Mitostatin) (Tumor suppressor protein)

 TCHP_HUMAN              Reviewed;         498 AA.
Q9BT92; Q8NAG0;
26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
18-JUL-2018, entry version 123.
RecName: Full=Trichoplein keratin filament-binding protein;
Short=Protein TCHP;
AltName: Full=Mitochondrial protein with oncostatic activity;
Short=Mitostatin;
AltName: Full=Tumor suppressor protein;
Name=TCHP {ECO:0000312|EMBL:AAH04285.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH KRT5; KRT6A;
KRT8; KRT14; KRT16 AND KRT18, AND SUBCELLULAR LOCATION.
TISSUE=Liver {ECO:0000269|PubMed:15731013};
PubMed=15731013; DOI=10.1242/jcs.01667;
Nishizawa M., Izawa I., Inoko A., Hayashi Y., Nagata K., Yokoyama T.,
Usukura J., Inagaki M.;
"Identification of trichoplein, a novel keratin filament-binding
protein.";
J. Cell Sci. 118:1081-1090(2005).
[2] {ECO:0000312|EMBL:AAG12971.1}
NUCLEOTIDE SEQUENCE [MRNA].
Baffa R., Croce C.M., Gomella L.G., Iozzo R.V., Vecchione A.;
"A novel tumor suppressor gene at 12q (TS12Q).";
Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000312|EMBL:BAC03960.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Small intestine {ECO:0000312|EMBL:BAC03960.1};
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4] {ECO:0000312|EMBL:AAH04285.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin {ECO:0000312|EMBL:AAH04285.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANTS
PRO-44 AND LYS-93.
PubMed=18931701; DOI=10.1038/onc.2008.381;
Vecchione A., Fassan M., Anesti V., Morrione A., Goldoni S.,
Baldassarre G., Byrne D., D'Arca D., Palazzo J.P., Lloyd J.,
Scorrano L., Gomella L.G., Iozzo R.V., Baffa R.;
"MITOSTATIN, a putative tumor suppressor on chromosome 12q24.1, is
downregulated in human bladder and breast cancer.";
Oncogene 28:257-269(2009).
[6]
FUNCTION, INTERACTION WITH KCTD17, MUTAGENESIS OF LYS-50 AND LYS-57,
UBIQUITINATION AT LYS-50 AND LYS-57, AND UBIQUITINATION BY THE
BCR(KCTD17) COMPLEX.
PubMed=25270598; DOI=10.1038/ncomms6081;
Kasahara K., Kawakami Y., Kiyono T., Yonemura S., Kawamura Y., Era S.,
Matsuzaki F., Goshima N., Inagaki M.;
"Ubiquitin-proteasome system controls ciliogenesis at the initial step
of axoneme extension.";
Nat. Commun. 5:5081-5081(2014).
-!- FUNCTION: Tumor suppressor which has the ability to inhibit cell
growth and be pro-apoptotic during cell stress. Inhibits cell
growth in bladder and prostate cancer cells by a down-regulation
of HSPB1 by inhibiting its phosphorylation. May act as a 'capping'
or 'branching' protein for keratin filaments in the cell
periphery. May regulate K8/K18 filament and desmosome organization
mainly at the apical or peripheral regions of simple epithelial
cells (PubMed:15731013, PubMed:18931701). Is a negative regulator
of ciliogenesis (PubMed:25270598). {ECO:0000269|PubMed:15731013,
ECO:0000269|PubMed:18931701, ECO:0000269|PubMed:25270598}.
-!- SUBUNIT: Interacts specifically with keratin proteins including,
KRT5, KRT6A, KRT8, KRT14, KRT16 and KRT18 (PubMed:15731013).
Interacts with KCTD17 (PubMed:25270598).
{ECO:0000269|PubMed:15731013, ECO:0000269|PubMed:25270598}.
-!- INTERACTION:
P0C7W6:CCDC172; NbExp=5; IntAct=EBI-740781, EBI-2548868;
Q01850:CDR2; NbExp=5; IntAct=EBI-740781, EBI-1181367;
Q8WWB3:DYDC1; NbExp=5; IntAct=EBI-740781, EBI-740680;
Q2KHM9:KIAA0753; NbExp=3; IntAct=EBI-740781, EBI-2805604;
P19012:KRT15; NbExp=4; IntAct=EBI-740781, EBI-739566;
Q6A162:KRT40; NbExp=3; IntAct=EBI-740781, EBI-10171697;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-740781, EBI-741037;
Q8TD10:MIPOL1; NbExp=3; IntAct=EBI-740781, EBI-2548751;
Q13064:MKRN3; NbExp=5; IntAct=EBI-740781, EBI-2340269;
Q15742:NAB2; NbExp=5; IntAct=EBI-740781, EBI-8641936;
Q9UHB4:NDOR1; NbExp=5; IntAct=EBI-740781, EBI-10249760;
Q9Y5B8:NME7; NbExp=10; IntAct=EBI-740781, EBI-744782;
P14373:TRIM27; NbExp=3; IntAct=EBI-740781, EBI-719493;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:15731013}. Cytoplasm
{ECO:0000269|PubMed:18931701}. Cell membrane
{ECO:0000305|PubMed:15731013, ECO:0000305|PubMed:18931701}.
Mitochondrion {ECO:0000269|PubMed:18931701}. Cell junction,
desmosome {ECO:0000269|PubMed:15731013}.
-!- TISSUE SPECIFICITY: Expressed at high levels in normal urothelial
and breast epithelial cells. Also expressed in the smooth muscle
and endothelial cells. Reduced expression seen in advanced bladder
and breast carcinomas (at protein level). Ubiquitous. Expressed at
highest levels in the heart, skeletal muscle, kidney, liver and
testis. {ECO:0000269|PubMed:18931701}.
-!- PTM: Ubiquitinated. Ubiquitination by the BCR(KCTD17) E3 ubiquitin
ligase complex results in proteasomal degradation, and induces
ciliogenesis. {ECO:0000269|PubMed:25270598}.
-!- SIMILARITY: Belongs to the TCHP family. {ECO:0000305}.
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EMBL; AY007230; AAG12971.1; -; mRNA.
EMBL; AK092736; BAC03960.1; -; mRNA.
EMBL; BC004285; AAH04285.1; -; mRNA.
CCDS; CCDS9137.1; -.
RefSeq; NP_001137324.1; NM_001143852.1.
RefSeq; NP_115676.1; NM_032300.4.
RefSeq; XP_011537138.1; XM_011538836.2.
RefSeq; XP_011537139.1; XM_011538837.2.
UniGene; Hs.410924; -.
ProteinModelPortal; Q9BT92; -.
BioGrid; 123987; 52.
IntAct; Q9BT92; 78.
MINT; Q9BT92; -.
STRING; 9606.ENSP00000324404; -.
iPTMnet; Q9BT92; -.
PhosphoSitePlus; Q9BT92; -.
BioMuta; TCHP; -.
DMDM; 74733103; -.
EPD; Q9BT92; -.
MaxQB; Q9BT92; -.
PaxDb; Q9BT92; -.
PeptideAtlas; Q9BT92; -.
PRIDE; Q9BT92; -.
ProteomicsDB; 78961; -.
DNASU; 84260; -.
Ensembl; ENST00000312777; ENSP00000324404; ENSG00000139437.
Ensembl; ENST00000405876; ENSP00000384520; ENSG00000139437.
Ensembl; ENST00000544838; ENSP00000440838; ENSG00000139437.
GeneID; 84260; -.
KEGG; hsa:84260; -.
UCSC; uc001tpn.4; human.
CTD; 84260; -.
DisGeNET; 84260; -.
EuPathDB; HostDB:ENSG00000139437.17; -.
GeneCards; TCHP; -.
HGNC; HGNC:28135; TCHP.
HPA; HPA038638; -.
HPA; HPA061543; -.
MIM; 612654; gene.
neXtProt; NX_Q9BT92; -.
OpenTargets; ENSG00000139437; -.
PharmGKB; PA143485629; -.
eggNOG; ENOG410IIAX; Eukaryota.
eggNOG; ENOG410ZEPV; LUCA.
GeneTree; ENSGT00730000111170; -.
HOGENOM; HOG000006708; -.
HOVERGEN; HBG097262; -.
InParanoid; Q9BT92; -.
KO; K16811; -.
OMA; DQNSRYF; -.
OrthoDB; EOG091G0FWB; -.
PhylomeDB; Q9BT92; -.
TreeFam; TF329032; -.
ChiTaRS; TCHP; human.
GeneWiki; TCHP; -.
GenomeRNAi; 84260; -.
PRO; PR:Q9BT92; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000139437; -.
CleanEx; HS_TCHP; -.
ExpressionAtlas; Q9BT92; baseline and differential.
Genevisible; Q9BT92; HS.
GO; GO:0045179; C:apical cortex; IDA:HGNC.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0097539; C:ciliary transition fiber; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
GO; GO:0045095; C:keratin filament; IDA:HGNC.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO; GO:1902018; P:negative regulation of cilium assembly; IMP:UniProtKB.
InterPro; IPR026773; TCHP.
PANTHER; PTHR31183:SF2; PTHR31183:SF2; 1.
1: Evidence at protein level;
Apoptosis; Cell junction; Cell membrane;
Cilium biogenesis/degradation; Coiled coil; Complete proteome;
Cytoplasm; Cytoskeleton; Isopeptide bond; Membrane; Mitochondrion;
Polymorphism; Reference proteome; Tumor suppressor; Ubl conjugation.
CHAIN 1 498 Trichoplein keratin filament-binding
protein.
/FTId=PRO_0000292609.
REGION 73 498 Interaction with keratin proteins.
{ECO:0000269|PubMed:15731013}.
REGION 259 425 Trichohyalin/plectin homology domain.
{ECO:0000269|PubMed:15731013}.
COILED 11 39 {ECO:0000255}.
COILED 66 136 {ECO:0000255}.
COILED 163 353 {ECO:0000255}.
COILED 380 479 {ECO:0000255}.
COMPBIAS 70 482 Glu-rich. {ECO:0000255}.
CROSSLNK 50 50 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000305|PubMed:25270598}.
CROSSLNK 57 57 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000305|PubMed:25270598}.
VARIANT 44 44 S -> P (in a gastric carcinoma sample;
dbSNP:rs202208566).
{ECO:0000269|PubMed:18931701}.
/FTId=VAR_064056.
VARIANT 93 93 E -> K (in a pancreatic carcinoma sample;
dbSNP:rs200027650).
{ECO:0000269|PubMed:18931701}.
/FTId=VAR_064057.
VARIANT 127 127 K -> R (in dbSNP:rs10774978).
/FTId=VAR_053924.
VARIANT 417 417 E -> K (in dbSNP:rs16940680).
/FTId=VAR_053925.
MUTAGEN 50 50 K->R: Decreased ubiquitination. Negative
effect on ubiquitination is higher when
associated with R-57.
{ECO:0000269|PubMed:25270598}.
MUTAGEN 57 57 K->R: Decreased ubiquitination. Negative
effect on ubiquitination is higher when
associated with R-50.
{ECO:0000269|PubMed:25270598}.
CONFLICT 326 326 A -> V (in Ref. 3; BAC03960).
{ECO:0000305}.
SEQUENCE 498 AA; 61072 MW; 7D1E8A66C56516F8 CRC64;
MALPTLPSYW CSQQRLNQQL ARQREQEARL RQQWEQNSRY FRMSDICSSK QAEWSSKTSY
QRSMHAYQRE KMKEEKRRSL EARREKLRQL MQEEQDLLAR ELEELRLSMN LQERRIREQH
GKLKSAKEEQ RKLIAEQLLY EHWKKNNPKL REMELDLHQK HVVNSWEMQK EEKKQQEATA
EQENKRYENE YERARREALE RMKAEEERRQ LEDKLQAEAL LQQMEELKLK EVEATKLKKE
QENLLKQRWE LERLEEERKQ MEAFRQKAEL GRFLRHQYNA QLSRRTQQIQ EELEADRRIL
QALLEKEDES QRLHLARREQ VMADVAWMKQ AIEEQLQLER AREAELQMLL REEAKEMWEK
REAEWARERS ARDRLMSEVL TGRQQQIQEK IEQNRRAQEE SLKHREQLIR NLEEVRELAR
REKEESEKLK SARKQELEAQ VAERRLQAWE ADQQEEEEEE EARRVEQLSD ALLQQEAETM
AEQGYRPKPY GHPKIAWN


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