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Protein FAM168A (Tongue cancer chemotherapy resistance-associated protein 1)

 F168A_HUMAN             Reviewed;         244 AA.
Q92567; A2ICY2; A2ID81; Q86UG2;
26-APR-2004, integrated into UniProtKB/Swiss-Prot.
26-APR-2004, sequence version 2.
22-NOV-2017, entry version 128.
RecName: Full=Protein FAM168A;
AltName: Full=Tongue cancer chemotherapy resistance-associated protein 1;
Name=FAM168A; Synonyms=KIAA0280, TCRP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
He Z., Zhou M., Liu X.;
"Cloning and characterization of a novel gene TCRP1 associated with
tongue cancer chemotherapy resistance.";
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9039502; DOI=10.1093/dnares/3.5.321;
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
Tanaka A., Kotani H., Miyajima N., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. VI.
The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by
analysis of cDNA clones from cell line KG-1 and brain.";
DNA Res. 3:321-329(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Spleen;
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Blood;
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]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[6]
FUNCTION, AND INVOLVEMENT IN DISEASE.
PubMed=21334329; DOI=10.1016/j.febslet.2010.12.045;
Gu Y., Fan S., Xiong Y., Peng B., Zheng G., Yu Y., Ouyang Y., He Z.;
"Cloning and functional characterization of TCRP1, a novel gene
mediating resistance to cisplatin in an oral squamous cell carcinoma
cell line.";
FEBS Lett. 585:881-887(2011).
[7]
FUNCTION, AND INVOLVEMENT IN DISEASE.
PubMed=21603883; DOI=10.1007/s11010-011-0880-8;
Gu Y., Fan S., Liu B., Zheng G., Yu Y., Ouyang Y., He Z.;
"TCRP1 promotes radioresistance of oral squamous cell carcinoma cells
via Akt signal pathway.";
Mol. Cell. Biochem. 357:107-113(2011).
[8]
INTERACTION WITH FAM168B.
PubMed=22771904; DOI=10.1016/j.febslet.2012.06.043;
Mishra M., Lee S., Lin M.K., Yamashita T., Heese K.;
"Characterizing the neurite outgrowth inhibitory effect of Mani.";
FEBS Lett. 586:3018-3023(2012).
[9]
FUNCTION, AND INTERACTION WITH AKT1 AND MT1X.
PubMed=23251525; DOI=10.1371/journal.pone.0051413;
Peng B., Gu Y., Xiong Y., Zheng G., He Z.;
"Microarray-assisted pathway analysis identifies MT1X & NFkappaB as
mediators of TCRP1-associated resistance to cisplatin in oral squamous
cell carcinoma.";
PLoS ONE 7:E51413-E51413(2012).
[10]
FUNCTION, INVOLVEMENT IN DISEASE, AND INTERACTION WITH POLB.
PubMed=25260657; DOI=10.1007/s11010-014-2217-x;
Liu X., Wang C., Gu Y., Zhang Z., Zheng G., He Z.;
"TCRP1 contributes to cisplatin resistance by preventing Pol beta
degradation in lung cancer cells.";
Mol. Cell. Biochem. 398:175-183(2015).
-!- FUNCTION: In cancer context, protects cells from induced-DNA
damage and apoptosis. Acts, at least in part, through
PI3K/AKT/NFKB signaling pathway and by preventing POLB
degradation. Decreases POLB ubiquitation and stabilizes its
protein levels. {ECO:0000269|PubMed:21334329,
ECO:0000269|PubMed:21603883, ECO:0000269|PubMed:23251525,
ECO:0000269|PubMed:25260657}.
-!- SUBUNIT: Interacts with POLB (PubMed:25260657). Interacts with
AKT1 and MT1X (PubMed:23251525). May interact with FAM168B
(PubMed:22771904). {ECO:0000269|PubMed:22771904,
ECO:0000269|PubMed:23251525, ECO:0000269|PubMed:25260657}.
-!- INTERACTION:
Q6P1W5:C1orf94; NbExp=3; IntAct=EBI-7957930, EBI-946029;
Q13137:CALCOCO2; NbExp=3; IntAct=EBI-7957930, EBI-739580;
O75553:DAB1; NbExp=3; IntAct=EBI-7957930, EBI-7875264;
Q15038:DAZAP2; NbExp=3; IntAct=EBI-7957930, EBI-724310;
Q86UW9:DTX2; NbExp=6; IntAct=EBI-7957930, EBI-740376;
Q9P2K6:KLHL42; NbExp=3; IntAct=EBI-7957930, EBI-739890;
Q96HR8:NAF1; NbExp=3; IntAct=EBI-7957930, EBI-2515597;
Q96DC9:OTUB2; NbExp=3; IntAct=EBI-7957930, EBI-746259;
Q96BN8:OTULIN; NbExp=3; IntAct=EBI-7957930, EBI-750730;
P86479:PRR20C; NbExp=3; IntAct=EBI-7957930, EBI-10172814;
Q9Y2K5-2:R3HDM2; NbExp=3; IntAct=EBI-7957930, EBI-10326419;
Q93062:RBPMS; NbExp=5; IntAct=EBI-7957930, EBI-740322;
Q93062-3:RBPMS; NbExp=4; IntAct=EBI-11978259, EBI-740343;
Q9NWF9:RNF216; NbExp=4; IntAct=EBI-11978259, EBI-723313;
Q15637:SF1; NbExp=3; IntAct=EBI-7957930, EBI-744603;
Q8WU79:SMAP2; NbExp=3; IntAct=EBI-7957930, EBI-2822515;
Q5TAL4:SNRPC; NbExp=3; IntAct=EBI-7957930, EBI-10246938;
O75177:SS18L1; NbExp=4; IntAct=EBI-7957930, EBI-744674;
Q86VP1:TAX1BP1; NbExp=3; IntAct=EBI-7957930, EBI-529518;
Q92734:TFG; NbExp=4; IntAct=EBI-11978259, EBI-357061;
Q15025:TNIP1; NbExp=3; IntAct=EBI-7957930, EBI-357849;
Q9BSL1:UBAC1; NbExp=4; IntAct=EBI-11978259, EBI-749370;
Q8TF42:UBASH3B; NbExp=3; IntAct=EBI-7957930, EBI-1380492;
P0CG48:UBC; NbExp=4; IntAct=EBI-11978259, EBI-3390054;
Q13404:UBE2V1; NbExp=3; IntAct=EBI-7957930, EBI-1050671;
A5D8V6:VPS37C; NbExp=3; IntAct=EBI-7957930, EBI-2559305;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q92567-1; Sequence=Displayed;
Name=2;
IsoId=Q92567-2; Sequence=VSP_010095;
Name=3;
IsoId=Q92567-3; Sequence=VSP_010095, VSP_034630;
-!- DISEASE: Note=Associated with cisplatin (DDP)-resistance and
radioresistance in the treatment of lung cancer as well as oral
squamous cell carcinoma and poor clinical outcome in patients.
{ECO:0000269|PubMed:21334329, ECO:0000269|PubMed:21603883,
ECO:0000269|PubMed:23251525, ECO:0000269|PubMed:25260657}.
-!- SIMILARITY: Belongs to the FAM168 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA13408.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; EF363480; ABM69287.1; -; mRNA.
EMBL; EF197985; ABM69272.1; -; mRNA.
EMBL; D87470; BAA13408.1; ALT_INIT; mRNA.
EMBL; AK292054; BAF84743.1; -; mRNA.
EMBL; BC052341; AAH52341.1; -; mRNA.
CCDS; CCDS41689.1; -. [Q92567-2]
CCDS; CCDS66165.1; -. [Q92567-3]
CCDS; CCDS73346.1; -. [Q92567-1]
RefSeq; NP_001272979.1; NM_001286050.1. [Q92567-1]
RefSeq; NP_001272980.1; NM_001286051.1. [Q92567-3]
RefSeq; NP_055974.1; NM_015159.2. [Q92567-2]
UniGene; Hs.475334; -.
ProteinModelPortal; Q92567; -.
SMR; Q92567; -.
BioGrid; 116810; 85.
IntAct; Q92567; 60.
MINT; MINT-8383567; -.
STRING; 9606.ENSP00000348852; -.
iPTMnet; Q92567; -.
PhosphoSitePlus; Q92567; -.
DMDM; 46576628; -.
EPD; Q92567; -.
MaxQB; Q92567; -.
PaxDb; Q92567; -.
PeptideAtlas; Q92567; -.
PRIDE; Q92567; -.
DNASU; 23201; -.
Ensembl; ENST00000064778; ENSP00000064778; ENSG00000054965. [Q92567-1]
Ensembl; ENST00000356467; ENSP00000348852; ENSG00000054965. [Q92567-2]
Ensembl; ENST00000450446; ENSP00000390501; ENSG00000054965. [Q92567-3]
GeneID; 23201; -.
KEGG; hsa:23201; -.
UCSC; uc001oty.3; human. [Q92567-1]
CTD; 23201; -.
DisGeNET; 23201; -.
EuPathDB; HostDB:ENSG00000054965.10; -.
GeneCards; FAM168A; -.
H-InvDB; HIX0009919; -.
HGNC; HGNC:28999; FAM168A.
HPA; HPA037580; -.
MIM; 616316; gene.
neXtProt; NX_Q92567; -.
OpenTargets; ENSG00000054965; -.
PharmGKB; PA162387077; -.
eggNOG; ENOG410IHUV; Eukaryota.
eggNOG; ENOG410XR79; LUCA.
GeneTree; ENSGT00390000005140; -.
HOGENOM; HOG000073527; -.
HOVERGEN; HBG052179; -.
InParanoid; Q92567; -.
OMA; CATEGTF; -.
OrthoDB; EOG091G0P0L; -.
PhylomeDB; Q92567; -.
TreeFam; TF331128; -.
GenomeRNAi; 23201; -.
PRO; PR:Q92567; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000054965; -.
CleanEx; HS_FAM168A; -.
Genevisible; Q92567; HS.
GO; GO:1905053; P:positive regulation of base-excision repair; IDA:UniProtKB.
InterPro; IPR029247; FAM168A/MANI.
PANTHER; PTHR31844; PTHR31844; 1.
Pfam; PF14944; TCRP1; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Complete proteome; Methylation;
Reference proteome.
CHAIN 1 244 Protein FAM168A.
/FTId=PRO_0000050742.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 102 102 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q8BGZ2}.
VAR_SEQ 51 59 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.1}.
/FTId=VSP_010095.
VAR_SEQ 102 208 RYTAGTPYKVPPTQSNTAPPPYSPSPNPYQTAMYPIRSAYP
QQNLYAQGAYYTQPVYAAQPHVIHHTTVVQPNSIPSAIYPA
PVAAPRTNGVAMGMVAGTTMAMSAG -> S (in
isoform 3). {ECO:0000303|Ref.1}.
/FTId=VSP_034630.
SEQUENCE 244 AA; 26184 MW; 60E3E9621665D30C CRC64;
MNPVYSPVQP GAPYGNPKNM AYTGYPTAYP AAAPAYNPSL YPTNSPSYAP EFQFLHSAYA
TLLMKQAWPQ NSSSCGTEGT FHLPVDTGTE NRTYQASSAA FRYTAGTPYK VPPTQSNTAP
PPYSPSPNPY QTAMYPIRSA YPQQNLYAQG AYYTQPVYAA QPHVIHHTTV VQPNSIPSAI
YPAPVAAPRT NGVAMGMVAG TTMAMSAGTL LTTPQHTAIG AHPVSMPTYR AQGTPAYSYV
PPHW


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