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F168A_HUMAN
ID   F168A_HUMAN             Reviewed;         244 AA.
AC   Q92567; A2ICY2; A2ID81; Q86UG2;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2004, sequence version 2.
DT   03-AUG-2022, entry version 157.
DE   RecName: Full=Protein FAM168A;
DE   AltName: Full=Tongue cancer chemotherapy resistance-associated protein 1;
GN   Name=FAM168A; Synonyms=KIAA0280, TCRP1;
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] (ISOFORMS 2 AND 3).
RA   He Z., Zhou M., Liu X.;
RT   "Cloning and characterization of a novel gene TCRP1 associated with tongue
RT   cancer chemotherapy resistance.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA   Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA   Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT   "Prediction of the coding sequences of unidentified human genes. VI. The
RT   coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT   cDNA clones from cell line KG-1 and brain.";
RL   DNA Res. 3:321-329(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Spleen;
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] (ISOFORM 2).
RC   TISSUE=Blood;
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   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   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   [6]
RP   FUNCTION, AND INVOLVEMENT IN DISEASE.
RX   PubMed=21334329; DOI=10.1016/j.febslet.2010.12.045;
RA   Gu Y., Fan S., Xiong Y., Peng B., Zheng G., Yu Y., Ouyang Y., He Z.;
RT   "Cloning and functional characterization of TCRP1, a novel gene mediating
RT   resistance to cisplatin in an oral squamous cell carcinoma cell line.";
RL   FEBS Lett. 585:881-887(2011).
RN   [7]
RP   FUNCTION, AND INVOLVEMENT IN DISEASE.
RX   PubMed=21603883; DOI=10.1007/s11010-011-0880-8;
RA   Gu Y., Fan S., Liu B., Zheng G., Yu Y., Ouyang Y., He Z.;
RT   "TCRP1 promotes radioresistance of oral squamous cell carcinoma cells via
RT   Akt signal pathway.";
RL   Mol. Cell. Biochem. 357:107-113(2011).
RN   [8]
RP   INTERACTION WITH FAM168B.
RX   PubMed=22771904; DOI=10.1016/j.febslet.2012.06.043;
RA   Mishra M., Lee S., Lin M.K., Yamashita T., Heese K.;
RT   "Characterizing the neurite outgrowth inhibitory effect of Mani.";
RL   FEBS Lett. 586:3018-3023(2012).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH AKT1 AND MT1X.
RX   PubMed=23251525; DOI=10.1371/journal.pone.0051413;
RA   Peng B., Gu Y., Xiong Y., Zheng G., He Z.;
RT   "Microarray-assisted pathway analysis identifies MT1X & NFkappaB as
RT   mediators of TCRP1-associated resistance to cisplatin in oral squamous cell
RT   carcinoma.";
RL   PLoS ONE 7:E51413-E51413(2012).
RN   [10]
RP   FUNCTION, INVOLVEMENT IN DISEASE, AND INTERACTION WITH POLB.
RX   PubMed=25260657; DOI=10.1007/s11010-014-2217-x;
RA   Liu X., Wang C., Gu Y., Zhang Z., Zheng G., He Z.;
RT   "TCRP1 contributes to cisplatin resistance by preventing Pol beta
RT   degradation in lung cancer cells.";
RL   Mol. Cell. Biochem. 398:175-183(2015).
CC   -!- FUNCTION: In cancer context, protects cells from induced-DNA damage and
CC       apoptosis. Acts, at least in part, through PI3K/AKT/NFKB signaling
CC       pathway and by preventing POLB degradation. Decreases POLB ubiquitation
CC       and stabilizes its protein levels. {ECO:0000269|PubMed:21334329,
CC       ECO:0000269|PubMed:21603883, ECO:0000269|PubMed:23251525,
CC       ECO:0000269|PubMed:25260657}.
CC   -!- SUBUNIT: Interacts with POLB (PubMed:25260657). Interacts with AKT1 and
CC       MT1X (PubMed:23251525). May interact with FAM168B (PubMed:22771904).
CC       {ECO:0000269|PubMed:22771904, ECO:0000269|PubMed:23251525,
CC       ECO:0000269|PubMed:25260657}.
CC   -!- INTERACTION:
CC       Q92567; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-7957930, EBI-946029;
CC       Q92567; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-7957930, EBI-739580;
CC       Q92567; O75553: DAB1; NbExp=3; IntAct=EBI-7957930, EBI-7875264;
CC       Q92567; Q15038: DAZAP2; NbExp=3; IntAct=EBI-7957930, EBI-724310;
CC       Q92567; Q86UW9: DTX2; NbExp=6; IntAct=EBI-7957930, EBI-740376;
CC       Q92567; Q9P2K6: KLHL42; NbExp=3; IntAct=EBI-7957930, EBI-739890;
CC       Q92567; Q96HR8: NAF1; NbExp=3; IntAct=EBI-7957930, EBI-2515597;
CC       Q92567; Q96DC9: OTUB2; NbExp=5; IntAct=EBI-7957930, EBI-746259;
CC       Q92567; Q96BN8: OTULIN; NbExp=3; IntAct=EBI-7957930, EBI-750730;
CC       Q92567; P86479: PRR20C; NbExp=3; IntAct=EBI-7957930, EBI-10172814;
CC       Q92567; Q9Y2K5-2: R3HDM2; NbExp=3; IntAct=EBI-7957930, EBI-10326419;
CC       Q92567; Q93062: RBPMS; NbExp=5; IntAct=EBI-7957930, EBI-740322;
CC       Q92567; Q15637: SF1; NbExp=4; IntAct=EBI-7957930, EBI-744603;
CC       Q92567; Q8WU79: SMAP2; NbExp=3; IntAct=EBI-7957930, EBI-2822515;
CC       Q92567; Q5TAL4: SNRPC; NbExp=3; IntAct=EBI-7957930, EBI-10246938;
CC       Q92567; O75177: SS18L1; NbExp=4; IntAct=EBI-7957930, EBI-744674;
CC       Q92567; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-7957930, EBI-529518;
CC       Q92567; Q15025: TNIP1; NbExp=3; IntAct=EBI-7957930, EBI-357849;
CC       Q92567; Q8TF42: UBASH3B; NbExp=4; IntAct=EBI-7957930, EBI-1380492;
CC       Q92567; Q13404: UBE2V1; NbExp=4; IntAct=EBI-7957930, EBI-1050671;
CC       Q92567; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-7957930, EBI-2559305;
CC       Q92567-2; Q9NXW9: ALKBH4; NbExp=3; IntAct=EBI-11978259, EBI-8637516;
CC       Q92567-2; P54253: ATXN1; NbExp=3; IntAct=EBI-11978259, EBI-930964;
CC       Q92567-2; P0C7T5: ATXN1L; NbExp=3; IntAct=EBI-11978259, EBI-8624731;
CC       Q92567-2; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-11978259, EBI-11983447;
CC       Q92567-2; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-11978259, EBI-12809220;
CC       Q92567-2; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-11978259, EBI-1383687;
CC       Q92567-2; Q15038: DAZAP2; NbExp=5; IntAct=EBI-11978259, EBI-724310;
CC       Q92567-2; Q96GG9: DCUN1D1; NbExp=5; IntAct=EBI-11978259, EBI-740086;
CC       Q92567-2; Q86UW9: DTX2; NbExp=3; IntAct=EBI-11978259, EBI-740376;
CC       Q92567-2; O95208-2: EPN2; NbExp=3; IntAct=EBI-11978259, EBI-12135243;
CC       Q92567-2; I6L9I8: EPN3; NbExp=3; IntAct=EBI-11978259, EBI-12866582;
CC       Q92567-2; A1KXE4-2: FAM168B; NbExp=3; IntAct=EBI-11978259, EBI-12193763;
CC       Q92567-2; A0A0S2Z4Q4: HGS; NbExp=3; IntAct=EBI-11978259, EBI-16429135;
CC       Q92567-2; O14964: HGS; NbExp=8; IntAct=EBI-11978259, EBI-740220;
CC       Q92567-2; O00291: HIP1; NbExp=3; IntAct=EBI-11978259, EBI-473886;
CC       Q92567-2; O43593: HR; NbExp=3; IntAct=EBI-11978259, EBI-2880706;
CC       Q92567-2; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-11978259, EBI-12811111;
CC       Q92567-2; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-11978259, EBI-1048945;
CC       Q92567-2; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-11978259, EBI-10241353;
CC       Q92567-2; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-11978259, EBI-9996449;
CC       Q92567-2; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-11978259, EBI-3957694;
CC       Q92567-2; Q3LI66: KRTAP6-2; NbExp=5; IntAct=EBI-11978259, EBI-11962084;
CC       Q92567-2; Q8IUC3: KRTAP7-1; NbExp=3; IntAct=EBI-11978259, EBI-18394498;
CC       Q92567-2; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-11978259, EBI-10261141;
CC       Q92567-2; Q14847-2: LASP1; NbExp=3; IntAct=EBI-11978259, EBI-9088686;
CC       Q92567-2; O14770-4: MEIS2; NbExp=3; IntAct=EBI-11978259, EBI-8025850;
CC       Q92567-2; Q96HR8: NAF1; NbExp=3; IntAct=EBI-11978259, EBI-2515597;
CC       Q92567-2; Q13952-2: NFYC; NbExp=3; IntAct=EBI-11978259, EBI-11956831;
CC       Q92567-2; Q96DC9: OTUB2; NbExp=3; IntAct=EBI-11978259, EBI-746259;
CC       Q92567-2; Q96BN8: OTULIN; NbExp=3; IntAct=EBI-11978259, EBI-750730;
CC       Q92567-2; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-11978259, EBI-11022007;
CC       Q92567-2; Q9UBV8: PEF1; NbExp=3; IntAct=EBI-11978259, EBI-724639;
CC       Q92567-2; P78337: PITX1; NbExp=3; IntAct=EBI-11978259, EBI-748265;
CC       Q92567-2; Q96CS7: PLEKHB2; NbExp=3; IntAct=EBI-11978259, EBI-373552;
CC       Q92567-2; O75360: PROP1; NbExp=3; IntAct=EBI-11978259, EBI-9027467;
CC       Q92567-2; P86480: PRR20D; NbExp=3; IntAct=EBI-11978259, EBI-12754095;
CC       Q92567-2; Q9UIG5-2: PSORS1C1; NbExp=3; IntAct=EBI-11978259, EBI-14831475;
CC       Q92567-2; Q9NWB1-5: RBFOX1; NbExp=4; IntAct=EBI-11978259, EBI-12123390;
CC       Q92567-2; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-11978259, EBI-740343;
CC       Q92567-2; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-11978259, EBI-11987469;
CC       Q92567-2; Q9BQY4: RHOXF2; NbExp=6; IntAct=EBI-11978259, EBI-372094;
CC       Q92567-2; Q9NWF9: RNF216; NbExp=3; IntAct=EBI-11978259, EBI-723313;
CC       Q92567-2; P62979: RPS27A; NbExp=3; IntAct=EBI-11978259, EBI-357375;
CC       Q92567-2; Q96T21: SECISBP2; NbExp=3; IntAct=EBI-11978259, EBI-954116;
CC       Q92567-2; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-11978259, EBI-529518;
CC       Q92567-2; Q7Z6R9: TFAP2D; NbExp=3; IntAct=EBI-11978259, EBI-11952651;
CC       Q92567-2; Q92734: TFG; NbExp=3; IntAct=EBI-11978259, EBI-357061;
CC       Q92567-2; Q01085-2: TIAL1; NbExp=5; IntAct=EBI-11978259, EBI-11064654;
CC       Q92567-2; Q13470-2: TNK1; NbExp=3; IntAct=EBI-11978259, EBI-11018037;
CC       Q92567-2; Q9H0E2: TOLLIP; NbExp=3; IntAct=EBI-11978259, EBI-74615;
CC       Q92567-2; P62987: UBA52; NbExp=3; IntAct=EBI-11978259, EBI-357304;
CC       Q92567-2; Q9BSL1: UBAC1; NbExp=3; IntAct=EBI-11978259, EBI-749370;
CC       Q92567-2; P0CG48: UBC; NbExp=3; IntAct=EBI-11978259, EBI-3390054;
CC       Q92567-2; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-11978259, EBI-947187;
CC       Q92567-2; Q9BZV1: UBXN6; NbExp=3; IntAct=EBI-11978259, EBI-1993899;
CC       Q92567-2; O94888: UBXN7; NbExp=3; IntAct=EBI-11978259, EBI-1993627;
CC       Q92567-2; Q5VVQ6: YOD1; NbExp=5; IntAct=EBI-11978259, EBI-2510804;
CC       Q92567-2; Q9BYJ9: YTHDF1; NbExp=3; IntAct=EBI-11978259, EBI-1051237;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q92567-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q92567-2; Sequence=VSP_010095;
CC       Name=3;
CC         IsoId=Q92567-3; Sequence=VSP_010095, VSP_034630;
CC   -!- DISEASE: Note=Associated with cisplatin (DDP)-resistance and
CC       radioresistance in the treatment of lung cancer as well as oral
CC       squamous cell carcinoma and poor clinical outcome in patients.
CC       {ECO:0000269|PubMed:21334329, ECO:0000269|PubMed:21603883,
CC       ECO:0000269|PubMed:23251525, ECO:0000269|PubMed:25260657}.
CC   -!- SIMILARITY: Belongs to the FAM168 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA13408.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; EF363480; ABM69287.1; -; mRNA.
DR   EMBL; EF197985; ABM69272.1; -; mRNA.
DR   EMBL; D87470; BAA13408.1; ALT_INIT; mRNA.
DR   EMBL; AK292054; BAF84743.1; -; mRNA.
DR   EMBL; BC052341; AAH52341.1; -; mRNA.
DR   CCDS; CCDS41689.1; -. [Q92567-2]
DR   CCDS; CCDS66165.1; -. [Q92567-3]
DR   CCDS; CCDS73346.1; -. [Q92567-1]
DR   RefSeq; NP_001272979.1; NM_001286050.1. [Q92567-1]
DR   RefSeq; NP_001272980.1; NM_001286051.1. [Q92567-3]
DR   RefSeq; NP_055974.1; NM_015159.2. [Q92567-2]
DR   AlphaFoldDB; Q92567; -.
DR   BioGRID; 116810; 138.
DR   IntAct; Q92567; 82.
DR   MINT; Q92567; -.
DR   STRING; 9606.ENSP00000064778; -.
DR   GlyGen; Q92567; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q92567; -.
DR   PhosphoSitePlus; Q92567; -.
DR   BioMuta; FAM168A; -.
DR   DMDM; 46576628; -.
DR   EPD; Q92567; -.
DR   jPOST; Q92567; -.
DR   MassIVE; Q92567; -.
DR   MaxQB; Q92567; -.
DR   PaxDb; Q92567; -.
DR   PeptideAtlas; Q92567; -.
DR   PRIDE; Q92567; -.
DR   ProteomicsDB; 75324; -. [Q92567-1]
DR   ProteomicsDB; 75325; -. [Q92567-2]
DR   ProteomicsDB; 75326; -. [Q92567-3]
DR   Antibodypedia; 50128; 41 antibodies from 13 providers.
DR   DNASU; 23201; -.
DR   Ensembl; ENST00000064778.8; ENSP00000064778.4; ENSG00000054965.11. [Q92567-1]
DR   Ensembl; ENST00000356467.5; ENSP00000348852.4; ENSG00000054965.11. [Q92567-2]
DR   Ensembl; ENST00000450446.6; ENSP00000390501.2; ENSG00000054965.11. [Q92567-3]
DR   GeneID; 23201; -.
DR   KEGG; hsa:23201; -.
DR   MANE-Select; ENST00000356467.5; ENSP00000348852.4; NM_015159.3; NP_055974.1. [Q92567-2]
DR   UCSC; uc001oty.3; human. [Q92567-1]
DR   CTD; 23201; -.
DR   DisGeNET; 23201; -.
DR   GeneCards; FAM168A; -.
DR   HGNC; HGNC:28999; FAM168A.
DR   HPA; ENSG00000054965; Low tissue specificity.
DR   MIM; 616316; gene.
DR   neXtProt; NX_Q92567; -.
DR   OpenTargets; ENSG00000054965; -.
DR   PharmGKB; PA162387077; -.
DR   VEuPathDB; HostDB:ENSG00000054965; -.
DR   eggNOG; ENOG502QRTA; Eukaryota.
DR   GeneTree; ENSGT00390000005140; -.
DR   HOGENOM; CLU_065824_1_0_1; -.
DR   InParanoid; Q92567; -.
DR   OMA; MPTMGMV; -.
DR   OrthoDB; 1348118at2759; -.
DR   PhylomeDB; Q92567; -.
DR   TreeFam; TF331128; -.
DR   PathwayCommons; Q92567; -.
DR   SignaLink; Q92567; -.
DR   BioGRID-ORCS; 23201; 80 hits in 1079 CRISPR screens.
DR   ChiTaRS; FAM168A; human.
DR   GenomeRNAi; 23201; -.
DR   Pharos; Q92567; Tbio.
DR   PRO; PR:Q92567; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q92567; protein.
DR   Bgee; ENSG00000054965; Expressed in cortical plate and 199 other tissues.
DR   Genevisible; Q92567; HS.
DR   GO; GO:1905053; P:positive regulation of base-excision repair; IDA:UniProtKB.
DR   InterPro; IPR029247; FAM168A/MANI.
DR   PANTHER; PTHR31844; PTHR31844; 1.
DR   Pfam; PF14944; TCRP1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Methylation; Reference proteome.
FT   CHAIN           1..244
FT                   /note="Protein FAM168A"
FT                   /id="PRO_0000050742"
FT   REGION          107..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:19413330"
FT   MOD_RES         102
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BGZ2"
FT   VAR_SEQ         51..59
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT                   /id="VSP_010095"
FT   VAR_SEQ         102..208
FT                   /note="RYTAGTPYKVPPTQSNTAPPPYSPSPNPYQTAMYPIRSAYPQQNLYAQGAYY
FT                   TQPVYAAQPHVIHHTTVVQPNSIPSAIYPAPVAAPRTNGVAMGMVAGTTMAMSAG ->
FT                   S (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_034630"
SQ   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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