HTAI2_HUMAN
ID HTAI2_HUMAN Reviewed; 242 AA.
AC Q9BUP3; A8K7S7; D3DQY8; O15383; O60520; O95345; Q53GC1; Q53GG2; Q6IBI3;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Oxidoreductase HTATIP2;
DE EC=1.1.1.-;
DE AltName: Full=30 kDa HIV-1 TAT-interacting protein;
DE AltName: Full=HIV-1 TAT-interactive protein 2;
GN Name=HTATIP2 {ECO:0000312|HGNC:HGNC:16637};
GN Synonyms=CC3 {ECO:0000312|EMBL:AAB84360.1},
GN TIP30 {ECO:0000303|PubMed:9482853};
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] {ECO:0000305, ECO:0000312|EMBL:AAB84360.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP VARIANT ARG-197.
RC TISSUE=Lung cancer {ECO:0000269|PubMed:9174052};
RX PubMed=9174052; DOI=10.1038/sj.onc.1201059;
RA Shtivelman E.;
RT "A link between metastasis and resistance to apoptosis of variant small
RT cell lung carcinoma.";
RL Oncogene 14:2167-2173(1997).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAC39694.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH HIV-1 TAT
RP (MICROBIAL INFECTION).
RC TISSUE=Pancreatic islet;
RX PubMed=9482853; DOI=10.1073/pnas.95.5.2146;
RA Xiao H., Tao Y., Greenblatt J., Roeder R.G.;
RT "A cofactor, TIP30, specifically enhances HIV-1 Tat-activated
RT transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:2146-2151(1998).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAC78331.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND INTERACTION WITH
RP PSMD4.
RC TISSUE=Placenta {ECO:0000312|EMBL:AAC78331.1};
RX PubMed=10611237; DOI=10.1128/mcb.20.2.583-593.2000;
RA Whitman S., Wang X., Shalaby R., Shtivelman E.;
RT "Alternatively spliced products CC3 and TC3 have opposing effects on
RT apoptosis.";
RL Mol. Cell. Biol. 20:583-593(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Synovium;
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 [5] {ECO:0000305, ECO:0000312|EMBL:CAG33102.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305, ECO:0000312|EMBL:CAG33102.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Small intestine {ECO:0000312|EMBL:BAD96730.1};
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [8] {ECO:0000305, ECO:0000312|EMBL:CAG33102.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9] {ECO:0000305, ECO:0000312|EMBL:AAH15358.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP ARG-197.
RC TISSUE=Cervix {ECO:0000312|EMBL:AAH15358.1}, and Skin;
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 [10] {ECO:0000305}
RP MUTAGENESIS OF 28-GLY--GLY-31.
RX PubMed=10698937; DOI=10.1093/emboj/19.5.956;
RA Xiao H., Palhan V., Yang Y., Roeder R.G.;
RT "TIP30 has an intrinsic kinase activity required for up-regulation of a
RT subset of apoptotic genes.";
RL EMBO J. 19:956-963(2000).
RN [11] {ECO:0000305}
RP FUNCTION.
RX PubMed=11313954; DOI=10.1038/sj.onc.1204075;
RA NicAmhlaoibh R., Shtivelman E.;
RT "Metastasis suppressor CC3 inhibits angiogenic properties of tumor cells in
RT vitro.";
RL Oncogene 20:270-275(2001).
RN [12] {ECO:0000305}
RP TISSUE SPECIFICITY, VARIANTS SER-106; TYR-108; THR-116; VAL-134 AND
RP ILE-144, MUTAGENESIS OF ARG-106, AND CHARACTERIZATION OF VARIANT VAL-134.
RX PubMed=14695192;
RA Ito M., Jiang C., Krumm K., Zhang X., Pecha J., Zhao J., Guo Y.,
RA Roeder R.G., Xiao H.;
RT "TIP30 deficiency increases susceptibility to tumorigenesis.";
RL Cancer Res. 63:8763-8767(2003).
RN [13] {ECO:0000305}
RP INTERACTION WITH NCOA5.
RX PubMed=15073177; DOI=10.1074/jbc.m401809200;
RA Jiang C., Ito M., Piening V., Bruck K., Roeder R.G., Xiao H.;
RT "TIP30 interacts with an estrogen receptor alpha-interacting coactivator
RT CIA and regulates c-myc transcription.";
RL J. Biol. Chem. 279:27781-27789(2004).
RN [14] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH XPO4; IPO5; IPO7;
RP IPO9; KPNB1; GCN1L1 AND LRPPRC.
RX PubMed=15282309; DOI=10.1128/mcb.24.16.7091-7101.2004;
RA King F.W., Shtivelman E.;
RT "Inhibition of nuclear import by the proapoptotic protein CC3.";
RL Mol. Cell. Biol. 24:7091-7101(2004).
RN [15]
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 [16]
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).
RN [17] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
RX PubMed=15728189; DOI=10.1074/jbc.m501113200;
RA El Omari K., Bird L.E., Nichols C.E., Ren J., Stammers D.K.;
RT "Crystal structure of CC3 (TIP30): implications for its role as a tumor
RT suppressor.";
RL J. Biol. Chem. 280:18229-18236(2005).
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] ARG-197, AND IDENTIFICATION BY MASS
RP 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 [19]
RP VARIANT ARG-197.
RX PubMed=24237036; DOI=10.1021/pr400544j;
RA Song C., Wang F., Cheng K., Wei X., Bian Y., Wang K., Tan Y., Wang H.,
RA Ye M., Zou H.;
RT "Large-scale quantification of single amino-acid variations by a variation-
RT associated database search strategy.";
RL J. Proteome Res. 13:241-248(2014).
CC -!- FUNCTION: Oxidoreductase required for tumor suppression. NADPH-bound
CC form inhibits nuclear import by competing with nuclear import
CC substrates for binding to a subset of nuclear transport receptors. May
CC act as a redox sensor linked to transcription through regulation of
CC nuclear import. Isoform 1 is a metastasis suppressor with proapoptotic
CC as well as antiangiogenic properties. Isoform 2 has an antiapoptotic
CC effect. {ECO:0000269|PubMed:10611237, ECO:0000269|PubMed:11313954,
CC ECO:0000269|PubMed:15282309, ECO:0000269|PubMed:9174052}.
CC -!- SUBUNIT: Monomer. Binds nuclear transport receptors XPO4, IPO5/RANBP5,
CC IPO7, IPO9 and KPNB1 as well as GCN1L1/GCN1 and LRPPRC probably through
CC their HEAT repeats. Binds NCOA5/CIA. Isoform 2 binds the proteasome
CC subunit PSMD4/s5a through its N-terminus. {ECO:0000269|PubMed:15073177,
CC ECO:0000269|PubMed:15282309}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-1 Tat (via activation
CC domain). {ECO:0000269|PubMed:9482853}.
CC -!- INTERACTION:
CC Q9BUP3; P54852: EMP3; NbExp=3; IntAct=EBI-13625358, EBI-3907816;
CC Q9BUP3-3; Q8TB40: ABHD4; NbExp=3; IntAct=EBI-12937691, EBI-7131019;
CC Q9BUP3-3; Q13520: AQP6; NbExp=3; IntAct=EBI-12937691, EBI-13059134;
CC Q9BUP3-3; Q08426: EHHADH; NbExp=3; IntAct=EBI-12937691, EBI-2339219;
CC Q9BUP3-3; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-12937691, EBI-18304435;
CC Q9BUP3-3; Q8N6M3: FITM2; NbExp=3; IntAct=EBI-12937691, EBI-11722638;
CC Q9BUP3-3; O00258: GET1; NbExp=3; IntAct=EBI-12937691, EBI-18908258;
CC Q9BUP3-3; Q8NBQ5: HSD17B11; NbExp=3; IntAct=EBI-12937691, EBI-1052304;
CC Q9BUP3-3; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-12937691, EBI-10266796;
CC Q9BUP3-3; Q9HDC5: JPH1; NbExp=3; IntAct=EBI-12937691, EBI-465137;
CC Q9BUP3-3; Q9NQG6: MIEF1; NbExp=3; IntAct=EBI-12937691, EBI-740987;
CC Q9BUP3-3; Q9H2K0: MTIF3; NbExp=3; IntAct=EBI-12937691, EBI-3923617;
CC Q9BUP3-3; Q9UKF7-2: PITPNC1; NbExp=3; IntAct=EBI-12937691, EBI-14223623;
CC Q9BUP3-3; Q99541: PLIN2; NbExp=3; IntAct=EBI-12937691, EBI-2115275;
CC Q9BUP3-3; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-12937691, EBI-7545592;
CC Q9BUP3-3; Q86VR2: RETREG3; NbExp=3; IntAct=EBI-12937691, EBI-10192441;
CC Q9BUP3-3; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-12937691, EBI-2623095;
CC Q9BUP3-3; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-12937691, EBI-18159983;
CC Q9BUP3-3; Q12893: TMEM115; NbExp=3; IntAct=EBI-12937691, EBI-8633987;
CC Q9BUP3-3; Q9Y320: TMX2; NbExp=3; IntAct=EBI-12937691, EBI-6447886;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15282309}. Nucleus
CC envelope {ECO:0000269|PubMed:15282309}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:9174052}; Synonyms=CC3
CC {ECO:0000303|PubMed:9174052};
CC IsoId=Q9BUP3-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:10611237, ECO:0000305}; Synonyms=TC3
CC {ECO:0000303|PubMed:10611237};
CC IsoId=Q9BUP3-2; Sequence=VSP_051864, VSP_051865;
CC Name=3;
CC IsoId=Q9BUP3-3; Sequence=VSP_038339;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest level in liver. High levels in
CC lung, skeletal muscle, pancreas and placenta. Moderate levels in heart
CC and kidney. Low levels in brain. Not expressed or low levels in variant
CC small cell lung carcinomas, 33% of hepatocellular carcinomas and
CC neuroblastomas. {ECO:0000269|PubMed:14695192,
CC ECO:0000269|PubMed:9174052}.
CC -!- DOMAIN: Unique C-terminus confers high proteasome-dependent instability
CC to isoform 2. {ECO:0000269|PubMed:10611237}.
CC -!- MISCELLANEOUS: [Isoform 2]: Mutagenesis of Leu-154 and Leu-157 or Cys-
CC 158, Cys-160 and Cys-161 abolishes antiapoptotic effect. {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:9482853 and PubMed:10698937) thought to
CC be a transcriptional coregulator with protein kinase activity. However,
CC crystal structure reveals a short chain dehydrogenase/reductase fold
CC binding NADPH rather than ATP. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/HTATIP2ID40894ch11p15.html";
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DR EMBL; U69161; AAB84360.1; -; mRNA.
DR EMBL; AF039103; AAC39694.1; -; mRNA.
DR EMBL; AF092095; AAC78331.1; -; mRNA.
DR EMBL; AK292092; BAF84781.1; -; mRNA.
DR EMBL; CR456821; CAG33102.1; -; mRNA.
DR EMBL; AK223010; BAD96730.1; -; mRNA.
DR EMBL; AK222969; BAD96689.1; -; mRNA.
DR EMBL; AC025972; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471064; EAW68338.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68339.1; -; Genomic_DNA.
DR EMBL; BC002439; AAH02439.2; -; mRNA.
DR EMBL; BC015358; AAH15358.1; -; mRNA.
DR CCDS; CCDS44553.1; -. [Q9BUP3-3]
DR CCDS; CCDS53613.1; -. [Q9BUP3-2]
DR CCDS; CCDS7852.1; -. [Q9BUP3-1]
DR RefSeq; NP_001091990.1; NM_001098520.1. [Q9BUP3-3]
DR RefSeq; NP_001091991.1; NM_001098521.1. [Q9BUP3-1]
DR RefSeq; NP_001091992.1; NM_001098522.1. [Q9BUP3-1]
DR RefSeq; NP_001091993.1; NM_001098523.1. [Q9BUP3-2]
DR RefSeq; NP_006401.3; NM_006410.4. [Q9BUP3-1]
DR PDB; 2BKA; X-ray; 1.70 A; A=1-242.
DR PDBsum; 2BKA; -.
DR AlphaFoldDB; Q9BUP3; -.
DR SMR; Q9BUP3; -.
DR BioGRID; 115804; 39.
DR IntAct; Q9BUP3; 28.
DR MINT; Q9BUP3; -.
DR STRING; 9606.ENSP00000392985; -.
DR DrugBank; DB11077; Polyethylene glycol 400.
DR iPTMnet; Q9BUP3; -.
DR PhosphoSitePlus; Q9BUP3; -.
DR SwissPalm; Q9BUP3; -.
DR BioMuta; HTATIP2; -.
DR DMDM; 317373366; -.
DR EPD; Q9BUP3; -.
DR jPOST; Q9BUP3; -.
DR MassIVE; Q9BUP3; -.
DR MaxQB; Q9BUP3; -.
DR PaxDb; Q9BUP3; -.
DR PeptideAtlas; Q9BUP3; -.
DR PRIDE; Q9BUP3; -.
DR ProteomicsDB; 79117; -. [Q9BUP3-1]
DR ProteomicsDB; 79118; -. [Q9BUP3-2]
DR ProteomicsDB; 79119; -. [Q9BUP3-3]
DR Antibodypedia; 1770; 284 antibodies from 33 providers.
DR DNASU; 10553; -.
DR Ensembl; ENST00000419348.6; ENSP00000392985.2; ENSG00000109854.14. [Q9BUP3-3]
DR Ensembl; ENST00000421577.6; ENSP00000397752.2; ENSG00000109854.14. [Q9BUP3-1]
DR Ensembl; ENST00000443524.6; ENSP00000387876.2; ENSG00000109854.14. [Q9BUP3-1]
DR Ensembl; ENST00000451739.7; ENSP00000394259.2; ENSG00000109854.14. [Q9BUP3-1]
DR Ensembl; ENST00000530266.5; ENSP00000436548.1; ENSG00000109854.14. [Q9BUP3-2]
DR Ensembl; ENST00000532081.1; ENSP00000432107.1; ENSG00000109854.14. [Q9BUP3-2]
DR Ensembl; ENST00000532505.1; ENSP00000432338.1; ENSG00000109854.14. [Q9BUP3-2]
DR GeneID; 10553; -.
DR KEGG; hsa:10553; -.
DR MANE-Select; ENST00000451739.7; ENSP00000394259.2; NM_001098522.2; NP_001091992.1.
DR UCSC; uc001mpx.3; human. [Q9BUP3-1]
DR CTD; 10553; -.
DR DisGeNET; 10553; -.
DR GeneCards; HTATIP2; -.
DR HGNC; HGNC:16637; HTATIP2.
DR HPA; ENSG00000109854; Low tissue specificity.
DR MIM; 605628; gene.
DR neXtProt; NX_Q9BUP3; -.
DR OpenTargets; ENSG00000109854; -.
DR PharmGKB; PA29539; -.
DR VEuPathDB; HostDB:ENSG00000109854; -.
DR eggNOG; KOG4039; Eukaryota.
DR GeneTree; ENSGT00390000008184; -.
DR HOGENOM; CLU_1906034_0_0_1; -.
DR InParanoid; Q9BUP3; -.
DR OMA; FCCIGTT; -.
DR OrthoDB; 1601023at2759; -.
DR PhylomeDB; Q9BUP3; -.
DR TreeFam; TF312849; -.
DR PathwayCommons; Q9BUP3; -.
DR SignaLink; Q9BUP3; -.
DR BioGRID-ORCS; 10553; 18 hits in 1090 CRISPR screens.
DR ChiTaRS; HTATIP2; human.
DR EvolutionaryTrace; Q9BUP3; -.
DR GeneWiki; HTATIP2; -.
DR GenomeRNAi; 10553; -.
DR Pharos; Q9BUP3; Tbio.
DR PRO; PR:Q9BUP3; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9BUP3; protein.
DR Bgee; ENSG00000109854; Expressed in jejunal mucosa and 207 other tissues.
DR ExpressionAtlas; Q9BUP3; baseline and differential.
DR Genevisible; Q9BUP3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0051170; P:import into nucleus; IDA:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IDA:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:MGI.
DR GO; GO:0045765; P:regulation of angiogenesis; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR InterPro; IPR016040; NAD(P)-bd_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR Pfam; PF13460; NAD_binding_10; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Angiogenesis; Apoptosis;
KW Cytoplasm; Developmental protein; Differentiation; Host-virus interaction;
KW NADP; Nucleus; Oxidoreductase; Reference proteome; Tumor suppressor.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..242
FT /note="Oxidoreductase HTATIP2"
FT /id="PRO_0000072544"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000303|PubMed:15728189"
FT ACT_SITE 147
FT /evidence="ECO:0000303|PubMed:15728189"
FT BINDING 19..52
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:15728189"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000303|PubMed:15728189"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 1
FT /note="M -> MAGPAALSAAAAAALAAALLLLRREDPGPGAGPSM (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_038339"
FT VAR_SEQ 102..133
FT /note="EGFVRVDRDYVLKSAELAKAGGCKHFNLLSSK -> VRKAYALFPFCWPVIS
FT RILFLLTLFLCACCNA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10611237, ECO:0000303|Ref.5"
FT /id="VSP_051864"
FT VAR_SEQ 134..242
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10611237, ECO:0000303|Ref.5"
FT /id="VSP_051865"
FT VARIANT 106
FT /note="R -> S (in a hepatocellular carcinoma sample)"
FT /evidence="ECO:0000269|PubMed:14695192"
FT /id="VAR_023713"
FT VARIANT 108
FT /note="D -> Y (in a hepatocellular carcinoma sample)"
FT /evidence="ECO:0000269|PubMed:14695192"
FT /id="VAR_023714"
FT VARIANT 116
FT /note="A -> T (in a hepatocellular carcinoma sample;
FT dbSNP:rs761113892)"
FT /evidence="ECO:0000269|PubMed:14695192"
FT /id="VAR_023715"
FT VARIANT 134
FT /note="G -> V (in a hepatocellular carcinoma sample;
FT reduces protein stability)"
FT /evidence="ECO:0000269|PubMed:14695192"
FT /id="VAR_023716"
FT VARIANT 144
FT /note="L -> I (in a hepatocellular carcinoma sample)"
FT /evidence="ECO:0000269|PubMed:14695192"
FT /id="VAR_023717"
FT VARIANT 197
FT /note="S -> R (highly associated with hepatocellular
FT carcinoma (HCC) progression; dbSNP:rs3824886)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:24237036, ECO:0000269|PubMed:9174052,
FT ECO:0007744|PubMed:21269460"
FT /id="VAR_023718"
FT MUTAGEN 28..31
FT /note="GETG->VETA: Loss of proapoptotic and metastatis-
FT inhibiting effect."
FT /evidence="ECO:0000269|PubMed:10698937"
FT MUTAGEN 106
FT /note="R->H: Loss of association with nucleus."
FT /evidence="ECO:0000269|PubMed:14695192"
FT CONFLICT 87
FT /note="V -> F (in Ref. 5; CAG33102)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="L -> P (in Ref. 6; BAD96730)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="W -> R (in Ref. 2; AAC39694)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="F -> L (in Ref. 1; AAB84360)"
FT /evidence="ECO:0000305"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:2BKA"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:2BKA"
FT HELIX 29..41
FT /evidence="ECO:0007829|PDB:2BKA"
FT STRAND 45..53
FT /evidence="ECO:0007829|PDB:2BKA"
FT HELIX 60..64
FT /evidence="ECO:0007829|PDB:2BKA"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:2BKA"
FT HELIX 72..82
FT /evidence="ECO:0007829|PDB:2BKA"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:2BKA"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:2BKA"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:2BKA"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:2BKA"
FT HELIX 142..155
FT /evidence="ECO:0007829|PDB:2BKA"
FT STRAND 160..166
FT /evidence="ECO:0007829|PDB:2BKA"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:2BKA"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:2BKA"
FT HELIX 179..188
FT /evidence="ECO:0007829|PDB:2BKA"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:2BKA"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:2BKA"
FT HELIX 203..214
FT /evidence="ECO:0007829|PDB:2BKA"
FT STRAND 220..226
FT /evidence="ECO:0007829|PDB:2BKA"
FT HELIX 227..233
FT /evidence="ECO:0007829|PDB:2BKA"
SQ SEQUENCE 242 AA; 27049 MW; 6A26E4A095243678 CRC64;
MAETEALSKL REDFRMQNKS VFILGASGET GRVLLKEILE QGLFSKVTLI GRRKLTFDEE
AYKNVNQEVV DFEKLDDYAS AFQGHDVGFC CLGTTRGKAG AEGFVRVDRD YVLKSAELAK
AGGCKHFNLL SSKGADKSSN FLYLQVKGEV EAKVEELKFD RYSVFRPGVL LCDRQESRPG
EWLVRKFFGS LPDSWASGHS VPVVTVVRAM LNNVVRPRDK QMELLENKAI HDLGKAHGSL
KP
