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U3 small nucleolar RNA-associated protein 14 homolog A (Antigen NY-CO-16) (Serologically defined colon cancer antigen 16)

 UT14A_HUMAN             Reviewed;         771 AA.
Q9BVJ6; A8K7A3; A8MVQ1; B4DQ08; E9PEL7; Q5JYF1;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
10-OCT-2018, entry version 148.
RecName: Full=U3 small nucleolar RNA-associated protein 14 homolog A;
AltName: Full=Antigen NY-CO-16;
AltName: Full=Serologically defined colon cancer antigen 16;
Name=UTP14A; Synonyms=SDCCAG16;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
GLY-771.
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2).
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cervix, Eye, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=12429849; DOI=10.1091/mbc.E02-05-0271;
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C.,
Greco A., Hochstrasser D.F., Diaz J.-J.;
"Functional proteomic analysis of human nucleolus.";
Mol. Biol. Cell 13:4100-4109(2002).
[6]
TISSUE SPECIFICITY.
PubMed=15289605; DOI=10.1073/pnas.0401130101;
Rohozinski J., Bishop C.E.;
"The mouse juvenile spermatogonial depletion (jsd) phenotype is due to
a mutation in the X-derived retrogene, mUtp14b.";
Proc. Natl. Acad. Sci. U.S.A. 101:11695-11700(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-31; SER-52;
SER-77; SER-405; SER-407 AND SER-445, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-31 AND SER-437,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; THR-205; SER-445;
SER-453 AND SER-569, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-407; SER-437;
SER-445 AND SER-453, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29; SER-31; SER-52;
SER-77; SER-81; SER-437; SER-445; SER-453 AND SER-569, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29 AND SER-31, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-733, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-122; LYS-449; LYS-519 AND
LYS-733, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[19]
VARIANT LEU-120 DEL.
PubMed=23033978; DOI=10.1056/NEJMoa1206524;
de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P.,
Gilissen C., del Rosario M., Hoischen A., Scheffer H., de Vries B.B.,
Brunner H.G., Veltman J.A., Vissers L.E.;
"Diagnostic exome sequencing in persons with severe intellectual
disability.";
N. Engl. J. Med. 367:1921-1929(2012).
-!- FUNCTION: May be required for ribosome biogenesis. {ECO:0000250}.
-!- INTERACTION:
O95257:GADD45G; NbExp=3; IntAct=EBI-473284, EBI-448202;
Q8NB12:SMYD1; NbExp=3; IntAct=EBI-473284, EBI-8463848;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:12429849}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9BVJ6-1; Sequence=Displayed;
Name=2;
IsoId=Q9BVJ6-2; Sequence=VSP_014475, VSP_014476;
Note=Gene prediction based on EST data. No experimental
confirmation available.;
Name=3;
IsoId=Q9BVJ6-3; Sequence=VSP_046389;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:15289605}.
-!- PTM: Citrullinated by PADI4. {ECO:0000250}.
-!- MISCELLANEOUS: The human genome also contains the UTP14C gene, an
autosomal retrotransposed copy of this X-linked gene. Evolution of
autosomal retrogenes from X-linked progenitors compensates for X-
chromosome silencing during male meiosis.
-!- SIMILARITY: Belongs to the UTP14 family. {ECO:0000305}.
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EMBL; AK291918; BAF84607.1; -; mRNA.
EMBL; AK298578; BAG60770.1; -; mRNA.
EMBL; AL034405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471107; EAX11820.1; -; Genomic_DNA.
EMBL; BC001149; AAH01149.1; -; mRNA.
EMBL; BC009649; AAH09649.1; -; mRNA.
EMBL; BC014987; AAH14987.1; -; mRNA.
CCDS; CCDS14615.1; -. [Q9BVJ6-1]
CCDS; CCDS55489.1; -. [Q9BVJ6-3]
RefSeq; NP_001159693.1; NM_001166221.1. [Q9BVJ6-3]
RefSeq; NP_006640.2; NM_006649.3. [Q9BVJ6-1]
UniGene; Hs.458598; -.
ProteinModelPortal; Q9BVJ6; -.
SMR; Q9BVJ6; -.
BioGrid; 116026; 110.
DIP; DIP-32505N; -.
IntAct; Q9BVJ6; 54.
MINT; Q9BVJ6; -.
STRING; 9606.ENSP00000377944; -.
iPTMnet; Q9BVJ6; -.
PhosphoSitePlus; Q9BVJ6; -.
BioMuta; UTP14A; -.
DMDM; 68566226; -.
SWISS-2DPAGE; Q9BVJ6; -.
EPD; Q9BVJ6; -.
MaxQB; Q9BVJ6; -.
PaxDb; Q9BVJ6; -.
PeptideAtlas; Q9BVJ6; -.
PRIDE; Q9BVJ6; -.
ProteomicsDB; 79210; -.
ProteomicsDB; 79211; -. [Q9BVJ6-2]
DNASU; 10813; -.
Ensembl; ENST00000394422; ENSP00000377944; ENSG00000156697. [Q9BVJ6-1]
Ensembl; ENST00000425117; ENSP00000388669; ENSG00000156697. [Q9BVJ6-3]
GeneID; 10813; -.
KEGG; hsa:10813; -.
UCSC; uc004euz.4; human. [Q9BVJ6-1]
CTD; 10813; -.
EuPathDB; HostDB:ENSG00000156697.12; -.
GeneCards; UTP14A; -.
HGNC; HGNC:10665; UTP14A.
HPA; HPA047217; -.
HPA; HPA054023; -.
MIM; 300508; gene.
neXtProt; NX_Q9BVJ6; -.
OpenTargets; ENSG00000156697; -.
PharmGKB; PA35595; -.
eggNOG; KOG2172; Eukaryota.
eggNOG; COG5644; LUCA.
GeneTree; ENSGT00390000008142; -.
HOGENOM; HOG000231396; -.
HOVERGEN; HBG056550; -.
InParanoid; Q9BVJ6; -.
KO; K14567; -.
OMA; TTLPGWG; -.
OrthoDB; EOG091G0DC1; -.
PhylomeDB; Q9BVJ6; -.
TreeFam; TF314531; -.
Reactome; R-HSA-6790901; rRNA modification in the nucleus and cytosol.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
ChiTaRS; UTP14A; human.
GeneWiki; UTP14A; -.
GenomeRNAi; 10813; -.
PRO; PR:Q9BVJ6; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000156697; Expressed in 211 organ(s), highest expression level in oocyte.
CleanEx; HS_UTP14A; -.
ExpressionAtlas; Q9BVJ6; baseline and differential.
Genevisible; Q9BVJ6; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0032040; C:small-subunit processome; IBA:GO_Central.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central.
GO; GO:0006364; P:rRNA processing; TAS:Reactome.
InterPro; IPR006709; SSU_processome_Utp14.
PANTHER; PTHR14150; PTHR14150; 1.
Pfam; PF04615; Utp14; 1.
1: Evidence at protein level;
Alternative splicing; Citrullination; Coiled coil; Complete proteome;
Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Ribosome biogenesis; Ubl conjugation.
CHAIN 1 771 U3 small nucleolar RNA-associated protein
14 homolog A.
/FTId=PRO_0000065733.
COILED 40 67 {ECO:0000255}.
COILED 216 290 {ECO:0000255}.
COILED 317 347 {ECO:0000255}.
MOD_RES 29 29 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 31 31 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 52 52 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 81 81 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 205 205 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 405 405 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 407 407 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 433 433 Citrulline. {ECO:0000250}.
MOD_RES 437 437 Phosphoserine.
{ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 445 445 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 453 453 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 569 569 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 589 589 Citrulline. {ECO:0000250}.
CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 449 449 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 519 519 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 733 733 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 12 MTANRLAESLLA -> MKGDFRKKKSEA (in isoform
2). {ECO:0000305}.
/FTId=VSP_014475.
VAR_SEQ 13 180 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_014476.
VAR_SEQ 128 179 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046389.
VARIANT 120 120 Missing. {ECO:0000269|PubMed:23033978}.
/FTId=VAR_078693.
VARIANT 487 487 V -> A (in dbSNP:rs2281278).
/FTId=VAR_022811.
VARIANT 771 771 D -> G (in dbSNP:rs1055032).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_069181.
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


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