ID UT14A_HUMAN Reviewed; 771 AA. AC Q9BVJ6; A8K7A3; A8MVQ1; B4DQ08; E9PEL7; Q5JYF1; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 27-MAR-2024, entry version 181. DE RecName: Full=U3 small nucleolar RNA-associated protein 14 homolog A; DE AltName: Full=Antigen NY-CO-16; DE AltName: Full=Serologically defined colon cancer antigen 16; GN Name=UTP14A; Synonyms=SDCCAG16; 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] (ISOFORMS 1 AND 3), AND VARIANT RP GLY-771. 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2). RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cervix, Eye, and Muscle; 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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=12429849; DOI=10.1091/mbc.e02-05-0271; RA Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., RA Greco A., Hochstrasser D.F., Diaz J.-J.; RT "Functional proteomic analysis of human nucleolus."; RL Mol. Biol. Cell 13:4100-4109(2002). RN [6] RP TISSUE SPECIFICITY. RX PubMed=15289605; DOI=10.1073/pnas.0401130101; RA Rohozinski J., Bishop C.E.; RT "The mouse juvenile spermatogonial depletion (jsd) phenotype is due to a RT mutation in the X-derived retrogene, mUtp14b."; RL Proc. Natl. Acad. Sci. U.S.A. 101:11695-11700(2004). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-31; SER-52; SER-77; RP SER-405; SER-407 AND SER-445, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [11] RP IDENTIFICATION BY MASS 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-31 AND SER-437, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; THR-205; SER-445; SER-453 RP AND SER-569, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-407; SER-437; RP SER-445 AND SER-453, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-31; SER-52; SER-77; RP SER-81; SER-437; SER-445; SER-453 AND SER-569, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-31, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-733, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [18] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-122; LYS-449; LYS-519 AND RP LYS-733, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [19] RP INTERACTION WITH DHX37. RX PubMed=30582406; DOI=10.1080/15476286.2018.1556149; RA Choudhury P., Hackert P., Memet I., Sloan K.E., Bohnsack M.T.; RT "The human RNA helicase DHX37 is required for release of the U3 snoRNP from RT pre-ribosomal particles."; RL RNA Biol. 16:54-68(2019). RN [20] RP VARIANT LEU-120 DEL. RX PubMed=23033978; DOI=10.1056/nejmoa1206524; RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G., RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C., RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G., RA Veltman J.A., Vissers L.E.; RT "Diagnostic exome sequencing in persons with severe intellectual RT disability."; RL N. Engl. J. Med. 367:1921-1929(2012). CC -!- FUNCTION: May be required for ribosome biogenesis. {ECO:0000250}. CC -!- SUBUNIT: Interacts with DHX37. {ECO:0000269|PubMed:30582406}. CC -!- INTERACTION: CC Q9BVJ6; P01023: A2M; NbExp=3; IntAct=EBI-473284, EBI-640741; CC Q9BVJ6; Q06481-5: APLP2; NbExp=3; IntAct=EBI-473284, EBI-25646567; CC Q9BVJ6; P05067: APP; NbExp=3; IntAct=EBI-473284, EBI-77613; CC Q9BVJ6; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-473284, EBI-702390; CC Q9BVJ6; Q13867: BLMH; NbExp=3; IntAct=EBI-473284, EBI-718504; CC Q9BVJ6; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-473284, EBI-1383687; CC Q9BVJ6; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-473284, EBI-9087876; CC Q9BVJ6; O14576-2: DYNC1I1; NbExp=3; IntAct=EBI-473284, EBI-25840445; CC Q9BVJ6; O95257: GADD45G; NbExp=3; IntAct=EBI-473284, EBI-448202; CC Q9BVJ6; P42858: HTT; NbExp=4; IntAct=EBI-473284, EBI-466029; CC Q9BVJ6; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-473284, EBI-1055254; CC Q9BVJ6; O95751: LDOC1; NbExp=3; IntAct=EBI-473284, EBI-740738; CC Q9BVJ6; P25800: LMO1; NbExp=3; IntAct=EBI-473284, EBI-8639312; CC Q9BVJ6; P63000: RAC1; NbExp=3; IntAct=EBI-473284, EBI-413628; CC Q9BVJ6; Q8NB12: SMYD1; NbExp=4; IntAct=EBI-473284, EBI-8463848; CC Q9BVJ6; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-473284, EBI-6116822; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9BVJ6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BVJ6-2; Sequence=VSP_014475, VSP_014476; CC Name=3; CC IsoId=Q9BVJ6-3; Sequence=VSP_046389; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. CC {ECO:0000269|PubMed:15289605}. CC -!- PTM: Citrullinated by PADI4. {ECO:0000250}. CC -!- MISCELLANEOUS: The human genome also contains the UTP14C gene, an CC autosomal retrotransposed copy of this X-linked gene. Evolution of CC autosomal retrogenes from X-linked progenitors compensates for X- CC chromosome silencing during male meiosis. CC -!- SIMILARITY: Belongs to the UTP14 family. {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; AK291918; BAF84607.1; -; mRNA. DR EMBL; AK298578; BAG60770.1; -; mRNA. DR EMBL; AL034405; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471107; EAX11820.1; -; Genomic_DNA. DR EMBL; BC001149; AAH01149.1; -; mRNA. DR EMBL; BC009649; AAH09649.1; -; mRNA. DR EMBL; BC014987; AAH14987.1; -; mRNA. DR CCDS; CCDS14615.1; -. [Q9BVJ6-1] DR CCDS; CCDS55489.1; -. [Q9BVJ6-3] DR RefSeq; NP_001159693.1; NM_001166221.1. [Q9BVJ6-3] DR RefSeq; NP_006640.2; NM_006649.3. [Q9BVJ6-1] DR PDB; 7MQ8; EM; 3.60 A; SS=1-771. DR PDB; 7MQ9; EM; 3.87 A; SS=1-771. DR PDB; 7MQA; EM; 2.70 A; SS=1-771. DR PDB; 7WTS; EM; 3.20 A; 5=1-771. DR PDBsum; 7MQ8; -. DR PDBsum; 7MQ9; -. DR PDBsum; 7MQA; -. DR PDBsum; 7WTS; -. DR AlphaFoldDB; Q9BVJ6; -. DR EMDB; EMD-23936; -. DR EMDB; EMD-23937; -. DR EMDB; EMD-23938; -. DR EMDB; EMD-32799; -. DR SMR; Q9BVJ6; -. DR BioGRID; 116026; 226. DR ComplexPortal; CPX-2511; Small ribosomal subunit processome. DR DIP; DIP-32505N; -. DR IntAct; Q9BVJ6; 83. DR MINT; Q9BVJ6; -. DR STRING; 9606.ENSP00000377944; -. DR GlyGen; Q9BVJ6; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9BVJ6; -. DR PhosphoSitePlus; Q9BVJ6; -. DR SwissPalm; Q9BVJ6; -. DR BioMuta; UTP14A; -. DR DMDM; 68566226; -. DR CPTAC; CPTAC-5932; -. DR CPTAC; CPTAC-5933; -. DR EPD; Q9BVJ6; -. DR jPOST; Q9BVJ6; -. DR MassIVE; Q9BVJ6; -. DR MaxQB; Q9BVJ6; -. DR PaxDb; 9606-ENSP00000377944; -. DR PeptideAtlas; Q9BVJ6; -. DR ProteomicsDB; 19917; -. DR ProteomicsDB; 79210; -. [Q9BVJ6-1] DR ProteomicsDB; 79211; -. [Q9BVJ6-2] DR Pumba; Q9BVJ6; -. DR Antibodypedia; 30118; 183 antibodies from 27 providers. DR CPTC; Q9BVJ6; 1 antibody. DR DNASU; 10813; -. DR Ensembl; ENST00000394422.8; ENSP00000377944.3; ENSG00000156697.13. [Q9BVJ6-1] DR Ensembl; ENST00000425117.6; ENSP00000388669.2; ENSG00000156697.13. [Q9BVJ6-3] DR GeneID; 10813; -. DR KEGG; hsa:10813; -. DR MANE-Select; ENST00000394422.8; ENSP00000377944.3; NM_006649.4; NP_006640.2. DR UCSC; uc004euz.4; human. [Q9BVJ6-1] DR AGR; HGNC:10665; -. DR CTD; 10813; -. DR DisGeNET; 10813; -. DR GeneCards; UTP14A; -. DR HGNC; HGNC:10665; UTP14A. DR HPA; ENSG00000156697; Low tissue specificity. DR MIM; 300508; gene. DR neXtProt; NX_Q9BVJ6; -. DR OpenTargets; ENSG00000156697; -. DR PharmGKB; PA35595; -. DR VEuPathDB; HostDB:ENSG00000156697; -. DR eggNOG; KOG2172; Eukaryota. DR GeneTree; ENSGT00390000008142; -. DR HOGENOM; CLU_012635_1_0_1; -. DR InParanoid; Q9BVJ6; -. DR OMA; QVIEPMD; -. DR OrthoDB; 5480898at2759; -. DR PhylomeDB; Q9BVJ6; -. DR TreeFam; TF314531; -. DR PathwayCommons; Q9BVJ6; -. DR Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol. DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol. DR SignaLink; Q9BVJ6; -. DR BioGRID-ORCS; 10813; 262 hits in 790 CRISPR screens. DR ChiTaRS; UTP14A; human. DR GeneWiki; UTP14A; -. DR GenomeRNAi; 10813; -. DR Pharos; Q9BVJ6; Tbio. DR PRO; PR:Q9BVJ6; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q9BVJ6; Protein. DR Bgee; ENSG00000156697; Expressed in oocyte and 189 other cell types or tissues. DR ExpressionAtlas; Q9BVJ6; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0032040; C:small-subunit processome; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0006364; P:rRNA processing; IEA:InterPro. DR InterPro; IPR006709; SSU_processome_Utp14. DR PANTHER; PTHR14150; U3 SMALL NUCLEOLAR RNA-ASSOCIATED PROTEIN 14; 1. DR PANTHER; PTHR14150:SF14; U3 SMALL NUCLEOLAR RNA-ASSOCIATED PROTEIN 14 HOMOLOG A; 1. DR Pfam; PF04615; Utp14; 1. DR SWISS-2DPAGE; Q9BVJ6; -. DR Genevisible; Q9BVJ6; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Citrullination; Coiled coil; KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; KW Ribosome biogenesis; Ubl conjugation. FT CHAIN 1..771 FT /note="U3 small nucleolar RNA-associated protein 14 homolog FT A" FT /id="PRO_0000065733" FT REGION 23..49 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 334..355 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 367..557 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 740..771 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 40..67 FT /evidence="ECO:0000255" FT COILED 216..290 FT /evidence="ECO:0000255" FT COILED 317..347 FT /evidence="ECO:0000255" FT COMPBIAS 385..438 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 439..460 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 462..476 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 490..527 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 29 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 31 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 52 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 77 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 81 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 205 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 405 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 407 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 433 FT /note="Citrulline" FT /evidence="ECO:0000250" FT MOD_RES 437 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 445 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 453 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 569 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 589 FT /note="Citrulline" FT /evidence="ECO:0000250" FT CROSSLNK 122 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 449 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 519 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 733 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..12 FT /note="MTANRLAESLLA -> MKGDFRKKKSEA (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_014475" FT VAR_SEQ 13..180 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_014476" FT VAR_SEQ 128..179 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046389" FT VARIANT 120 FT /note="Missing" FT /evidence="ECO:0000269|PubMed:23033978" FT /id="VAR_078693" FT VARIANT 487 FT /note="V -> A (in dbSNP:rs2281278)" FT /id="VAR_022811" FT VARIANT 771 FT /note="D -> G (in dbSNP:rs1055032)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_069181" FT HELIX 221..246 FT /evidence="ECO:0007829|PDB:7WTS" FT HELIX 250..262 FT /evidence="ECO:0007829|PDB:7WTS" FT STRAND 629..633 FT /evidence="ECO:0007829|PDB:7WTS" SQ SEQUENCE 771 AA; 87978 MW; DF82C264BA6486FE CRC64; MTANRLAESL LALSQQEELA DLPKDYLLSE SEDEGDNDGE RKHQKLLEAI SSLDGKNRRK LAERSEASLK VSEFNVSSEG SGEKLVLADL LEPVKTSSSL ATVKKQLSRV KSKKTVELPL NKEEIERIHR EVAFNKTAQV LSKWDPVVLK NRQAEQLVFP LEKEEPAIAP IEHVLSGWKA RTPLEQEIFN LLHKNKQPVT DPLLTPVEKA SLRAMSLEEA KMRRAELQRA RALQSYYEAK ARREKKIKSK KYHKVVKKGK AKKALKEFEQ LRKVNPAAAL EELEKIEKAR MMERMSLKHQ NSGKWAKSKA IMAKYDLEAR QAMQEQLSKN KELTQKLQVA SESEEEEGGT EDVEELLVPD VVNEVQMNAD GPNPWMLRSC TSDTKEAATQ EDPEQLPELE AHGVSESEGE ERPVAEEEIL LREFEERRSL RKRSELSQDA EPAGSQETKD SGSQEVLSEL RVLSQKLKEN HQSRKQKASS EGTIPQVQRE EPAPEEEEPL LLQRPERVQT LEELEELGKE ECFQNKELPR PVLEGQQSER TPNNRPDAPK EKKKKEQMID LQNLLTTQSP SVKSLAVPTI EELEDEEERN HRQMIKEAFA GDDVIRDFLK EKREAVEASK PKDVDLTLPG WGEWGGVGLK PSAKKRRRFL IKAPEGPPRK DKNLPNVIIN EKRNIHAAAH QVRVLPYPFT HHWQFERTIQ TPIGSTWNTQ RAFQKLTTPK VVTKPGHIIN PIKAEDVGYR SSSRSDLSVI QRNPKRITTR HKKQLKKCSV D //