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 27-MAR-2024, entry version 176. 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}, TIP30 GN {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, PubMed:10698937) thought to be CC 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="https://atlasgeneticsoncology.org/gene/40894/HTATIP2"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 61. DR IntAct; Q9BUP3; 29. DR MINT; Q9BUP3; -. DR STRING; 9606.ENSP00000392985; -. DR DrugBank; DB11077; Polyethylene glycol 400. DR GlyGen; Q9BUP3; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000392985; -. DR PeptideAtlas; Q9BUP3; -. DR ProteomicsDB; 79117; -. [Q9BUP3-1] DR ProteomicsDB; 79118; -. [Q9BUP3-2] DR ProteomicsDB; 79119; -. [Q9BUP3-3] DR Pumba; Q9BUP3; -. DR Antibodypedia; 1770; 311 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 AGR; HGNC:16637; -. 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; DWPQLTI; -. DR OrthoDB; 150138at2759; -. DR PhylomeDB; Q9BUP3; -. DR TreeFam; TF312849; -. DR PathwayCommons; Q9BUP3; -. DR SignaLink; Q9BUP3; -. DR BioGRID-ORCS; 10553; 18 hits in 1169 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 209 other cell types or tissues. DR ExpressionAtlas; Q9BUP3; baseline and differential. 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 CDD; cd05250; CC3_like_SDR_a; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR PANTHER; PTHR14097; OXIDOREDUCTASE HTATIP2; 1. DR PANTHER; PTHR14097:SF7; OXIDOREDUCTASE HTATIP2; 1. DR Pfam; PF13460; NAD_binding_10; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR Genevisible; Q9BUP3; HS. 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 (in 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 FT metastatis-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 //