UT14A_HUMAN
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 03-AUG-2022, entry version 172.
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}.
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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 PDBsum; 7MQ8; -.
DR PDBsum; 7MQ9; -.
DR PDBsum; 7MQA; -.
DR AlphaFoldDB; Q9BVJ6; -.
DR SMR; Q9BVJ6; -.
DR BioGRID; 116026; 204.
DR DIP; DIP-32505N; -.
DR IntAct; Q9BVJ6; 80.
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 BioMuta; UTP14A; -.
DR DMDM; 68566226; -.
DR SWISS-2DPAGE; Q9BVJ6; -.
DR EPD; Q9BVJ6; -.
DR jPOST; Q9BVJ6; -.
DR MassIVE; Q9BVJ6; -.
DR MaxQB; Q9BVJ6; -.
DR PaxDb; Q9BVJ6; -.
DR PeptideAtlas; Q9BVJ6; -.
DR PRIDE; Q9BVJ6; -.
DR ProteomicsDB; 19917; -.
DR ProteomicsDB; 79210; -. [Q9BVJ6-1]
DR ProteomicsDB; 79211; -. [Q9BVJ6-2]
DR Antibodypedia; 30118; 167 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 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; RESKWAK; -.
DR OrthoDB; 370022at2759; -.
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; 243 hits in 716 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 187 other tissues.
DR ExpressionAtlas; Q9BVJ6; baseline and differential.
DR Genevisible; Q9BVJ6; HS.
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; PTHR14150; 1.
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"
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
