ID FBX34_HUMAN Reviewed; 711 AA. AC Q9NWN3; Q2VPB5; Q4VBP5; Q86TY4; DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 15-MAR-2005, sequence version 2. DT 10-JUN-2026, entry version 162. DE RecName: Full=F-box only protein 34; GN Name=FBXO34; Synonyms=FBX34; 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 [LARGE SCALE MRNA]. RC TISSUE=Neuroblastoma; RA Li W.B., Gruber C., Jessee J., Polayes D.; RT "Full-length cDNA libraries and normalization."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ASN-470 AND PRO-533. RC TISSUE=Placenta; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 405-711, AND VARIANTS ASN-470 AND RP PRO-533. 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] OF 407-711, AND VARIANTS ASN-470 AND RP PRO-533. 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 [5] RP FUNCTION, AND FUNCTION (MICROBIAL INFECTION). RX PubMed=36285453; DOI=10.1080/22221751.2022.2140605; RA Yang X., Zhao X., Zhu Y., Xun J., Wen Q., Pan H., Yang J., Wang J., RA Liang Z., Shen X., Liang Y., Lin Q., Liang H., Li M., Chen J., Jiang S., RA Xu J., Lu H., Zhu H.; RT "FBXO34 promotes latent HIV-1 activation by post-transcriptional RT modulation."; RL Emerg. Microbes Infect. 11:2785-2799(2022). CC -!- FUNCTION: Substrate-recognition component of the SCF (SKP1-CUL1-F-box CC protein)-type E3 ubiquitin ligase complex promoting ubiquitination and CC proteasomal degradation of specific target proteins including HNRNPU CC (PubMed:36285453). Regulates both the G2/M transition and anaphase CC entry in meiotic oocytes (By similarity). CC {ECO:0000250|UniProtKB:Q80XI1, ECO:0000269|PubMed:36285453}. CC -!- FUNCTION: (Microbial infection) Plays a positive role in latent HIV-1 CC activation. Mechanistically, promotes hnRNP U/HNRNPU ubiquitination, CC which leads to its degradation and abolishment of the interaction CC between hnRNP U and HIV-1 Rev mRNA. {ECO:0000269|PubMed:36285453}. CC -!- SUBUNIT: Directly interacts with SKP1 and CUL1. {ECO:0000250}. CC -!- INTERACTION: CC Q9NWN3; P05187: ALPP; NbExp=3; IntAct=EBI-719816, EBI-1211484; CC Q9NWN3; P27658: COL8A1; NbExp=3; IntAct=EBI-719816, EBI-747133; CC Q9NWN3; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-719816, EBI-11988027; CC Q9NWN3; Q92915-2: FGF14; NbExp=3; IntAct=EBI-719816, EBI-12836320; CC Q9NWN3; Q6A162: KRT40; NbExp=3; IntAct=EBI-719816, EBI-10171697; CC Q9NWN3; P60412: KRTAP10-11; NbExp=3; IntAct=EBI-719816, EBI-10217483; CC Q9NWN3; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-719816, EBI-10172150; CC Q9NWN3; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-719816, EBI-10171774; CC Q9NWN3; P60329: KRTAP12-4; NbExp=4; IntAct=EBI-719816, EBI-10176396; CC Q9NWN3; Q9BYQ6: KRTAP4-11; NbExp=3; IntAct=EBI-719816, EBI-10302392; CC Q9NWN3; Q9BQ66: KRTAP4-12; NbExp=3; IntAct=EBI-719816, EBI-739863; CC Q9NWN3; Q9BYR2: KRTAP4-5; NbExp=5; IntAct=EBI-719816, EBI-11993254; CC Q9NWN3; Q6L8H2: KRTAP5-3; NbExp=3; IntAct=EBI-719816, EBI-11974251; CC Q9NWN3; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-719816, EBI-1044640; CC Q9NWN3; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-719816, EBI-1043191; CC Q9NWN3; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-719816, EBI-11958364; CC Q9NWN3; Q99750: MDFI; NbExp=3; IntAct=EBI-719816, EBI-724076; CC Q9NWN3; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-719816, EBI-742948; CC Q9NWN3; Q5JR59-3: MTUS2; NbExp=4; IntAct=EBI-719816, EBI-11522433; CC Q9NWN3; Q8WWZ8: OIT3; NbExp=3; IntAct=EBI-719816, EBI-10277776; CC Q9NWN3; B2RUY7: VWC2L; NbExp=3; IntAct=EBI-719816, EBI-11747707; CC -!- SEQUENCE CAUTION: CC Sequence=BAA91346.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAD62596.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; BX248268; CAD62596.1; ALT_INIT; mRNA. DR EMBL; BC095482; AAH95482.2; -; mRNA. DR EMBL; BC109120; AAI09121.1; -; mRNA. DR EMBL; BC109121; AAI09122.1; -; mRNA. DR EMBL; AK000732; BAA91346.1; ALT_INIT; mRNA. DR EMBL; CR457249; CAG33530.1; -; mRNA. DR CCDS; CCDS32086.1; -. DR RefSeq; NP_060413.2; NM_017943.3. DR RefSeq; NP_689417.1; NM_152231.2. DR RefSeq; XP_006720248.1; XM_006720185.4. DR RefSeq; XP_016876882.1; XM_017021393.3. DR RefSeq; XP_054232257.1; XM_054376282.1. DR RefSeq; XP_054232258.1; XM_054376283.1. DR AlphaFoldDB; Q9NWN3; -. DR BioGRID; 120359; 58. DR ComplexPortal; CPX-7975; SCF E3 ubiquitin ligase complex, FBXO34 variant. DR FunCoup; Q9NWN3; 634. DR IntAct; Q9NWN3; 35. DR STRING; 9606.ENSP00000313159; -. DR iPTMnet; Q9NWN3; -. DR PhosphoSitePlus; Q9NWN3; -. DR BioMuta; FBXO34; -. DR DMDM; 61252689; -. DR MassIVE; Q9NWN3; -. DR PaxDb; 9606-ENSP00000313159; -. DR PeptideAtlas; Q9NWN3; -. DR ProteomicsDB; 82956; -. DR Antibodypedia; 24028; 99 antibodies from 17 providers. DR DNASU; 55030; -. DR Ensembl; ENST00000313833.5; ENSP00000313159.4; ENSG00000178974.12. DR Ensembl; ENST00000440021.1; ENSP00000394117.1; ENSG00000178974.12. DR Ensembl; ENST00000679934.1; ENSP00000505918.1; ENSG00000178974.12. DR Ensembl; ENST00000680658.1; ENSP00000506499.1; ENSG00000178974.12. DR Ensembl; ENST00000680682.1; ENSP00000504946.1; ENSG00000178974.12. DR Ensembl; ENST00000681074.1; ENSP00000506304.1; ENSG00000178974.12. DR Ensembl; ENST00000681400.1; ENSP00000506349.1; ENSG00000178974.12. DR Ensembl; ENST00000681904.1; ENSP00000505815.1; ENSG00000178974.12. DR Ensembl; ENST00000855357.1; ENSP00000525416.1; ENSG00000178974.12. DR Ensembl; ENST00000855358.1; ENSP00000525417.1; ENSG00000178974.12. DR Ensembl; ENST00000855359.1; ENSP00000525418.1; ENSG00000178974.12. DR Ensembl; ENST00000855360.1; ENSP00000525419.1; ENSG00000178974.12. DR Ensembl; ENST00000855361.1; ENSP00000525420.1; ENSG00000178974.12. DR Ensembl; ENST00000918751.1; ENSP00000588810.1; ENSG00000178974.12. DR Ensembl; ENST00000918752.1; ENSP00000588811.1; ENSG00000178974.12. DR Ensembl; ENST00000969173.1; ENSP00000639232.1; ENSG00000178974.12. DR Ensembl; ENST00000969174.1; ENSP00000639233.1; ENSG00000178974.12. DR GeneID; 55030; -. DR KEGG; hsa:55030; -. DR MANE-Select; ENST00000313833.5; ENSP00000313159.4; NM_017943.4; NP_060413.2. DR UCSC; uc001xbu.4; human. DR AGR; HGNC:20201; -. DR ClinPGx; PA134910884; -. DR CTD; 55030; -. DR DisGeNET; 55030; -. DR GeneCards; FBXO34; -. DR HGNC; HGNC:20201; FBXO34. DR HPA; ENSG00000178974; Low tissue specificity. DR MIM; 609104; gene. DR OpenTargets; ENSG00000178974; -. DR VEuPathDB; HostDB:ENSG00000178974; -. DR eggNOG; ENOG502QRQQ; Eukaryota. DR GeneTree; ENSGT00530000064222; -. DR InParanoid; Q9NWN3; -. DR OMA; MKNSNRY; -. DR OrthoDB; 10052741at2759; -. DR PAN-GO; Q9NWN3; 0 GO annotations based on evolutionary models. DR PhylomeDB; Q9NWN3; -. DR PathwayCommons; Q9NWN3; -. DR SignaLink; Q9NWN3; -. DR Agora; ENSG00000178974; -. DR BioGRID-ORCS; 55030; 10 hits in 1198 CRISPR screens. DR ChiTaRS; FBXO34; human. DR GenomeRNAi; 55030; -. DR Pharos; Q9NWN3; Tdark. DR PRO; PR:Q9NWN3; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q9NWN3; protein. DR Bgee; ENSG00000178974; Expressed in secondary oocyte and 212 other cell types or tissues. DR ExpressionAtlas; Q9NWN3; baseline and differential. DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; NAS:ComplexPortal. DR CDD; cd22176; F-box_FBXO34; 1. DR InterPro; IPR036047; F-box-like_dom_sf. DR InterPro; IPR001810; F-box_dom. DR InterPro; IPR039594; FBXO34/46. DR PANTHER; PTHR16271:SF11; F-BOX ONLY PROTEIN 34; 1. DR PANTHER; PTHR16271; F-BOX ONLY PROTEIN 34/46 FAMILY MEMBER; 1. DR Pfam; PF12937; F-box-like; 1. DR SUPFAM; SSF81383; F-box domain; 1. DR PROSITE; PS50181; FBOX; 1. PE 1: Evidence at protein level; KW Proteomics identification; Reference proteome; Ubl conjugation pathway. FT CHAIN 1..711 FT /note="F-box only protein 34" FT /id="PRO_0000119926" FT DOMAIN 572..624 FT /note="F-box" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 249..271 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 337..372 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 494..529 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 10..23 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 354..364 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 432 FT /note="V -> A (in dbSNP:rs35070799)" FT /id="VAR_049047" FT VARIANT 470 FT /note="I -> N (in dbSNP:rs1045002)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4" FT /id="VAR_021489" FT VARIANT 533 FT /note="L -> P (in dbSNP:rs3742569)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4" FT /id="VAR_021490" FT VARIANT 704 FT /note="G -> V (in dbSNP:rs10138395)" FT /id="VAR_049048" SQ SEQUENCE 711 AA; 78711 MW; 6D289A9320AE9C42 CRC64; MHLKPYWKLQ KKEHPPEVSR ETQRTPMNHQ KAVNDETCKA SHITSSVFPS ASLGKASSRK PFGILSPNVL CSMSGKSPVE SSLNVKTKKN APSATIHQGE EEGPLDIWAV VKPGNTKEKI AFFASHQCSN RIGSMKIKSS WDIDGRATKR RKKSGDLKKA KVQVERMREV NSRCYQPEPF ACGIEHCSVH YVSDSGDGVY AGRPLSVIQM VAFLEQRASA LLASCSKNCT NSPAIVRFSG QSRGVPAVSE SYSAPGACEE PTERGNLEVG EPQSEPVRVL DMVAKLESEC LKRQGQREPG SLSRNNSFRR NVGRVLLANS TQADEGKTKK GVLEAPDTQV NPVGSVSVDC GPSRADRCSP KEDQAWDGAS QDCPPLPAGV SFHIDSAELE PGSQTAVKNS NRYDVEMTDE LVGLPFSSHT YSQASELPTD AVDCMSRELV SLTSRNPDQR KESLCISITV SKVDKDQPSI LNSCEDPVPG MLFFLPPGQH LSDYSQLNES TTKESSEASQ LEDAAGGDSA SEEKSGSAEP FVLPASSVES TLPVLEASSW KKQVSHDFLE TRFKIQQLLE PQQYMAFLPH HIMVKIFRLL PTKSLVALKC TCCYFKFIIE YYNIRPADSR WVRDPRYRED PCKQCKKKYV KGDVSLCRWH PKPYCQALPY GPGYWMCCHR SQKGFPGCKL GLHDNHWVPA CHSFNRAIHK KAKGTEAEEE Y //