O75691 (UTP20_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Small subunit processome component 20 homolog

Alternative name(s):
Down-regulated in metastasis protein
Novel nucleolar protein 73
Short name=NNP73
Protein Key-1A6

Gene names

Name:	UTP20
Synonyms:	DRIM

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2785 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in 18S pre-rRNA processing. Associates with U3 snoRNA. Ref.8
Subunit structure	Interacts with FBL and PPP1R26. Ref.6 Ref.8
Subcellular location	Nucleus › nucleolus. Note: Colocalizes with NCL in the nucleolus. Ref.4 Ref.5 Ref.7
Tissue specificity	Expressed in appendix, brain, colon, fetal liver, heart, ovary, pancreas, placenta, prostate, skeletal muscle, small intestine, spleen, testis and thymus. Ref.1
Sequence similarities	Belongs to the UTP20 family. Contains 2 HEAT repeats.
Sequence caution	The sequence AAG35208.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	rRNA processing
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Inferred from sequence or structural similarity PubMed 17652137. Source: UniProtKB endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Inferred from sequence or structural similarity PubMed 15590835. Source: UniProtKB endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Inferred from sequence or structural similarity PubMed 17652137. Source: UniProtKB negative regulation of cell proliferation Traceable author statement Ref.1. Source: ProtInc
Cellular_component	90S preribosome Inferred from sequence or structural similarity PubMed 12150911. Source: UniProtKB cytoplasm Inferred from sequence or structural similarity PubMed 17652137. Source: UniProtKB nucleolus Inferred from direct assay Ref.7. Source: UniProtKB nucleoplasm Inferred from sequence or structural similarity PubMed 17652137. Source: UniProtKB preribosome, small subunit precursor Inferred from sequence or structural similarity PubMed 17652137. Source: UniProtKB small-subunit processome Inferred from sequence or structural similarity PubMed 15590835. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PPP1R26	Q5T8A7	4	EBI-356062,EBI-308500

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2785	2785	Small subunit processome component 20 homolog		PRO_0000080011
Regions
	Repeat	165 – 202	38	HEAT 1
	Repeat	1841 – 1878	38	HEAT 2
	Region	2744 – 2775	32	Nuclear localization signal
	Region	2744 – 2761	18	Nucleolar localization signal
	Coiled coil	2688 – 2765	78	Potential
	Compositional bias	1319 – 1324	6	Poly-Lys
Amino acid modifications
	Modified residue	788	1	Phosphoserine Ref.9
	Modified residue	1741	1	Phosphothreonine Ref.9 Ref.10 Ref.11 Ref.14
	Modified residue	2601	1	Phosphoserine Ref.12 Ref.14
Natural variations
	Natural variant	120	1	M → T. Corresponds to variant rs2290723 [ dbSNP | Ensembl ].		VAR_055135
	Natural variant	502	1	S → C. Corresponds to variant rs4764643 [ dbSNP | Ensembl ].		VAR_022162
	Natural variant	1645	1	K → I in a breast cancer sample; somatic mutation. Ref.15		VAR_036274
	Natural variant	1882	1	L → Q. Ref.1 Corresponds to variant rs10082778 [ dbSNP | Ensembl ].		VAR_055136
	Natural variant	2452	1	I → F in a breast cancer sample; somatic mutation. Ref.15		VAR_036275
	Natural variant	2612	1	E → Q. Corresponds to variant rs1061436 [ dbSNP | Ensembl ].		VAR_022163
Experimental info
	Mutagenesis	2744 – 2746	3	KKK → AAA: Inhibits nucleolar but not nuclear localization. Ref.7
	Mutagenesis	2744	1	K → A: Does not decrease nucleolar localization. Ref.7
	Mutagenesis	2745	1	K → A: Does not decrease nucleolar localization. Ref.7
	Mutagenesis	2746	1	K → A: Decreases nucleolar localization. Ref.7
	Mutagenesis	2748 – 2749	2	KK → AA: Inhibits nucleolar but not nuclear localization. Ref.7
	Mutagenesis	2748	1	K → A: Does not decrease nucleolar localization. Ref.7
	Mutagenesis	2749	1	K → A: Decreases nucleolar localization. Ref.7
	Mutagenesis	2751	1	K → A: Does not decrease nucleolar localization. Ref.7
	Mutagenesis	2753	1	K → A: Does not decrease nucleolar localization. Ref.7
	Mutagenesis	2757 – 2760	4	KKRK → AAAA: Inhibits nucleolar localization and decreases nuclear localization. Ref.7
	Mutagenesis	2757	1	K → A: Does not decrease nucleolar localization. Ref.7
	Mutagenesis	2758	1	K → A: Does not decrease nucleolar localization. Ref.7
	Mutagenesis	2760	1	K → A: Does not decrease nucleolar localization. Ref.7
	Sequence conflict	1505	1	A → P in CAA07243. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O75691 [UniParc]. Last modified May 18, 2010. Version 3. Checksum: 0CE63611C8440E0D	FASTA	2,785	318,385
	10 20 30 40 50 60 MKTKPVSHKT ENTYRFLTFA ERLGNVNIDI IHRIDRTASY EEEVETYFFE GLLKWRELNL 70 80 90 100 110 120 TEHFGKFYKE VIDKCQSFNQ LVYHQNEIVQ SLKTHLQVKN SFAYQPLLDL VVQLARDLQM 130 140 150 160 170 180 DFYPHFPEFF LTITSILETQ DTELLEWAFT SLSYLYKYLW RLMVKDMSSI YSMYSTLLAH 190 200 210 220 230 240 KKLHIRNFAA ESFTFLMRKV SDKNALFNLM FLDLDKHPEK VEGVGQLLFE MCKGVRNMFH 250 260 270 280 290 300 SCTGQAVKLI LRKLGPVTET ETQLPWMLIG ETLKNMVKST VSYISKEHFG TFFECLQESL 310 320 330 340 350 360 LDLHTKVTKT NCCESSEQIK RLLETYLILV KHGSGTKIPT PADVCKVLSQ TLQVASLSTS 370 380 390 400 410 420 CWETLLDVIS ALILGENVSL PETLIKETIE KIFESRFEKR LIFSFSEVMF AMKQFEQLFL 430 440 450 460 470 480 PSFLSYIVNC FLIDDAVVKD EALAILAKLI LNKAAPPTAG SMAIEKYPLV FSPQMVGFYI 490 500 510 520 530 540 KQKKTRSKGR NEQFPVLDHL LSIIKLPPNK DTTYLSQSWA ALVVLPHIRP LEKEKVIPLV 550 560 570 580 590 600 TGFIEALFMT VDKGSFGKGN LFVLCQAVNT LLSLEESSEL LHLVPVERVK NLVLTFPLEP 610 620 630 640 650 660 SVLLLTDLYY QRLALCGCKG PLSQEALMEL FPKLQANIST GVSKIRLLTI RILNHFDVQL 670 680 690 700 710 720 PESMEDDGLS ERQSVFAILR QAELVPATVN DYREKLLHLR KLRHDVVQTA VPDGPLQEVP 730 740 750 760 770 780 LRYLLGMLYI NFSALWDPVI ELISSHAHEM ENKQFWKVYY EHLEKAATHA EKELQNDMTD 790 800 810 820 830 840 EKSVGDESWE QTQEGDVGAL YHEQLALKTD CQERLDHTNF RFLLWRALTK FPERVEPRSR 850 860 870 880 890 900 ELSPLFLRFI NNEYYPADLQ VAPTQDLRRK GKGMVAEEIE EEPAAGDDEE LEEEAVPQDE 910 920 930 940 950 960 SSQKKKTRRA AAKQLIAHLQ VFSKFSNPRA LYLESKLYEL YLQLLLHQDQ MVQKITLDCI 970 980 990 1000 1010 1020 MTYKHPHVLP YRENLQRLLE DRSFKEEIVH FSISEDNAVV KTAHRADLFP ILMRILYGRM 1030 1040 1050 1060 1070 1080 KNKTGSKTQG KSASGTRMAI VLRFLAGTQP EEIQIFLDLL FEPVRHFKNG ECHSAVIQAV 1090 1100 1110 1120 1130 1140 EDLDLSKVLP LGRQHGILNS LEIVLKNISH LISAYLPKIL QILLCMTATV SHILDQREKI 1150 1160 1170 1180 1190 1200 QLRFINPLKN LRRLGIKMVT DIFLDWESYQ FRTEEIDAVF HGAVWPQISR LGSESQYSPT 1210 1220 1230 1240 1250 1260 PLLKLISIWS RNARYFPLLA KQKPGHPECD ILTNVFAILS AKNLSDATAS IVMDIVDDLL 1270 1280 1290 1300 1310 1320 NLPDFEPTET VLNLLVTGCV YPGIAENIGE SITIGGRLIL PHVPAILQYL SKTTISAEKV 1330 1340 1350 1360 1370 1380 KKKKNRAQVS KELGILSKIS KFMKDKEQSS VLITLLLPFL HRGNIAEDTE VDILVTVQNL 1390 1400 1410 1420 1430 1440 LKHCVDPTSF LKPIAKLFSV IKNKLSRKLL CTVFETLSDF ESGLKYITDV VKLNAFDQRH 1450 1460 1470 1480 1490 1500 LDDINFDVRF ETFQTITSYI KEMQIVDVNY LIPVMHNCFY NLELGDMSLS DNASMCLMSI 1510 1520 1530 1540 1550 1560 IKKLAALNVT EKDYREIIHR SLLEKLRKGL KSQTESIQQD YTTILSCLIQ TFPNQLEFKD 1570 1580 1590 1600 1610 1620 LVQLTHYHDP EMDFFENMKH IQIHRRARAL KKLAKQLMEG KVVLSSKSLQ NYIMPYAMTP 1630 1640 1650 1660 1670 1680 IFDEKMLKHE NITTAATEII GAICKHLSWS AYMYYLKHFI HVLQTGQINQ KLGVSLLVIV 1690 1700 1710 1720 1730 1740 LEAFHFDHKT LEEQMGKIEN EENAIEAIEL PEPEAMELER VDEEEKEYTC KSLSDNGQPG 1750 1760 1770 1780 1790 1800 TPDPADSGGT SAKESECITK PVSFLPQNKE EIERTIKNIQ GTITGDILPR LHKCLASTTK 1810 1820 1830 1840 1850 1860 REEEHKLVKS KVVNDEEVVR VPLAFAMVKL MQSLPQEVME ANLPSILLKV CALLKNRAQE 1870 1880 1890 1900 1910 1920 IRDIARSTLA KIIEDLGVHF LLYVLKELQT TLVRGYQVHV LTFTVHMLLQ GLTNKLQVGD 1930 1940 1950 1960 1970 1980 LDSCLDIMIE IFNHELFGAV AEEKEVKQIL SKVMEARRSK SYDSYEILGK FVGKDQVTKL 1990 2000 2010 2020 2030 2040 ILPLKEILQN TTSLKLARKV HETLRRITVG LIVNQEMTAE SILLLSYGLI SENLPLLTEK 2050 2060 2070 2080 2090 2100 EKNPVAPAPD PRLPPQSCLL LPPTPVRGGQ KAVVSRKTNM HIFIESGLRL LHLSLKTSKI 2110 2120 2130 2140 2150 2160 KSSGECVLEM LDPFVSLLID CLGSMDVKVI TGALQCLIWV LRFPLPSIET KAEQLTKHLF 2170 2180 2190 2200 2210 2220 LLLKDYAKLG AARGQNFHLV VNCFKCVTIL VKKVKSYQIT EKQLQVLLAY AEEDIYDTSR 2230 2240 2250 2260 2270 2280 QATAFGLLKA ILSRKLLVPE IDEVMRKVSK LAVSAQSEPA RVQCRQVFLK YILDYPLGDK 2290 2300 2310 2320 2330 2340 LRPNLEFMLA QLNYEHETGR ESTLEMIAYL FDTFPQGLLH ENCGMFFIPL CLMTINDDSA 2350 2360 2370 2380 2390 2400 TCKKMASMTI KSLLGKISLE KKDWLFDMVT TWFGAKKRLN RQLAALICGL FVESEGVDFE 2410 2420 2430 2440 2450 2460 KRLGTVLPVI EKEIDPENFK DIMEETEEKA ADRLLFSFLT LITKLIKECN IIQFTKPAET 2470 2480 2490 2500 2510 2520 LSKIWSHVHS HLRHPHNWVW LTAAQIFGLL FASCQPEELI QKWNTKKTKK HLPEPVAIKF 2530 2540 2550 2560 2570 2580 LASDLDQKMK SISLASCHQL HSKFLDQSLG EQVVKNLLFA AKVLYLLELY CEDKQSKIKE 2590 2600 2610 2620 2630 2640 DLEEQEALED GVACADEKAE SDGEEKEEVK EELGRPATLL WLIQKLSRIA KLEAAYSPRN 2650 2660 2670 2680 2690 2700 PLKRTCIFKF LGAVAMDLGI DKVKPYLPMI IAPLFRELNS TYSEQDPLLK NLSQEIIELL 2710 2720 2730 2740 2750 2760 KKLVGLESFS LAFASVQKQA NEKRALRKKR KALEFVTNPD IAAKKKMKKH KNKSEAKKRK 2770 2780 IEFLRPGYKA KRQKSHSLKD LAMVE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Differential gene expression in mammary carcinoma cell lines: identification of DRIM, a new gene down-regulated in metastasis." Schwirzke M., Gnirke A., Bork P., Tarin D., Weidle U.H. Anticancer Res. 18:1409-1421(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT GLN-1882.
[2]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Key-1A6." Ke Y., Hagiwara K., Zhao H., Ning T., Su X.L., Mcmenamin H., Lu G.R., Wang B., Harris C.C. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1883-2785.
[4]	"Directed proteomic analysis of the human nucleolus." Andersen J.S., Lyon C.E., Fox A.H., Leung A.K.L., Lam Y.W., Steen H., Mann M., Lamond A.I. Curr. Biol. 12:1-11(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[5]	"Functional proteomic analysis of human nucleolus." Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J. Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"KIAA0649, a 1A6/DRIM-interacting protein with the oncogenic potential." Yang L., Zhao J., Lu W., Li Y., Du X., Ning T., Lu G., Ke Y. Biochem. Biophys. Res. Commun. 334:884-890(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PPP1R26.
[7]	"Mapping nucleolar localization sequences of 1A6/DRIM." Liu J., Du X., Ke Y. FEBS Lett. 580:1405-1410(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF 2744-LYS--LYS-2746; LYS-2744; LYS-2745; LYS-2746; 2748-LYS-LYS-2749; LYS-2748; LYS-2749; LYS-2751; LYS-2753; 2757-LYS--LYS-2760; LYS-2757; LYS-2758 AND LYS-2760.
[8]	"Human 1A6/DRIM, the homolog of yeast Utp20, functions in the 18S rRNA processing." Wang Y., Liu J., Zhao H., Lue W., Zhao J., Yang L., Li N., Du X., Ke Y. Biochim. Biophys. Acta 1773:863-868(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH FBL.
[9]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-788 AND THR-1741, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1741, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1741, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2601, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1741 AND SER-2601, MASS SPECTROMETRY.
[15]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-1645 AND PHE-2452.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ006778 mRNA. Translation: CAA07243.1. AC063948 Genomic DNA. No translation available. AC063951 Genomic DNA. No translation available. AF072718 mRNA. Translation: AAG35208.1. Different initiation.
IPI	IPI00004970.
RefSeq	NP_055318.2. NM_014503.2.
UniGene	Hs.295732.
3D structure databases
ProteinModelPortal	O75691.
SMR	O75691. Positions 2113-2141.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75691. 2 interactions.
MINT	MINT-1163597.
STRING	9606.ENSP00000261637.
PTM databases
PhosphoSite	O75691.
2D gel databases
SWISS-2DPAGE	O75691.
Proteomic databases
PaxDb	O75691.
PRIDE	O75691.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000261637; ENSP00000261637; ENSG00000120800.
GeneID	27340.
KEGG	hsa:27340.
UCSC	uc001tia.1. human.
Organism-specific databases
CTD	27340.
GeneCards	GC12P101673.
H-InvDB	HIX0010919.
HGNC	HGNC:17897. UTP20.
MIM	612822. gene.
neXtProt	NX_O75691.
PharmGKB	PA143485666.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG296791.
HOGENOM	HOG000168315.
HOVERGEN	HBG094143.
InParanoid	O75691.
KO	K14772.
OMA	YFPLLAK.
OrthoDB	EOG41C6VB.
PhylomeDB	O75691.
Gene expression databases
Bgee	O75691.
CleanEx	HS_UTP20.
Genevestigator	O75691.
GermOnline	ENSG00000120800. Homo sapiens.
Family and domain databases
Gene3D	1.25.10.10. 5 hits.
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR011430. DRIM. [Graphical view]
Pfam	PF07539. DRIM. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 2 hits.
PROSITE	PS50077. HEAT_REPEAT. False negative. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	27340.
NextBio	50408.
SOURCE	Search...

Entry information

Entry name

UTP20_HUMAN

Accession

Primary (citable) accession number: O75691
Secondary accession number(s): Q9H3H4

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 99 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.