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O75691

- UTP20_HUMAN

UniProt

O75691 - UTP20_HUMAN

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Protein

Small subunit processome component 20 homolog

Gene

UTP20

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Involved in 18S pre-rRNA processing. Associates with U3 snoRNA.1 Publication

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: UniProtKB
  2. 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) Source: UniProtKB
  3. endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: UniProtKB
  4. negative regulation of cell proliferation Source: ProtInc
  5. rRNA processing Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

rRNA processing

Names & Taxonomyi

Protein namesi
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 namesi
Name:UTP20
Synonyms:DRIM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:17897. UTP20.

Subcellular locationi

Nucleusnucleolus 3 Publications
Note: Colocalizes with NCL in the nucleolus.

GO - Cellular componenti

  1. 90S preribosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. nucleolus Source: UniProtKB
  4. nucleoplasm Source: UniProtKB
  5. preribosome, small subunit precursor Source: UniProtKB
  6. small-subunit processome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2744 – 27463KKK → AAA: Inhibits nucleolar but not nuclear localization. 1 Publication
Mutagenesisi2744 – 27441K → A: Does not decrease nucleolar localization. 1 Publication
Mutagenesisi2745 – 27451K → A: Does not decrease nucleolar localization. 1 Publication
Mutagenesisi2746 – 27461K → A: Decreases nucleolar localization. 1 Publication
Mutagenesisi2748 – 27492KK → AA: Inhibits nucleolar but not nuclear localization. 1 Publication
Mutagenesisi2748 – 27481K → A: Does not decrease nucleolar localization. 1 Publication
Mutagenesisi2749 – 27491K → A: Decreases nucleolar localization. 1 Publication
Mutagenesisi2751 – 27511K → A: Does not decrease nucleolar localization. 1 Publication
Mutagenesisi2753 – 27531K → A: Does not decrease nucleolar localization. 1 Publication
Mutagenesisi2757 – 27604KKRK → AAAA: Inhibits nucleolar localization and decreases nuclear localization. 1 Publication
Mutagenesisi2757 – 27571K → A: Does not decrease nucleolar localization. 1 Publication
Mutagenesisi2758 – 27581K → A: Does not decrease nucleolar localization. 1 Publication
Mutagenesisi2760 – 27601K → A: Does not decrease nucleolar localization. 1 Publication

Organism-specific databases

PharmGKBiPA143485666.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 27852785Small subunit processome component 20 homologPRO_0000080011Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei788 – 7881Phosphoserine1 Publication
Modified residuei1741 – 17411Phosphothreonine4 Publications
Modified residuei2601 – 26011Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO75691.
PaxDbiO75691.
PRIDEiO75691.

2D gel databases

SWISS-2DPAGEO75691.

PTM databases

PhosphoSiteiO75691.

Expressioni

Tissue specificityi

Expressed in appendix, brain, colon, fetal liver, heart, ovary, pancreas, placenta, prostate, skeletal muscle, small intestine, spleen, testis and thymus.1 Publication

Gene expression databases

BgeeiO75691.
CleanExiHS_UTP20.
GenevestigatoriO75691.

Interactioni

Subunit structurei

Interacts with FBL and PPP1R26.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PPP1R26Q5T8A74EBI-356062,EBI-308500

Protein-protein interaction databases

BioGridi118152. 17 interactions.
IntActiO75691. 2 interactions.
MINTiMINT-1163597.
STRINGi9606.ENSP00000261637.

Structurei

3D structure databases

ProteinModelPortaliO75691.
SMRiO75691. Positions 1231-1256.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati165 – 20238HEAT 1Add
BLAST
Repeati1841 – 187838HEAT 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2744 – 277532Nuclear localization signalAdd
BLAST
Regioni2744 – 276118Nucleolar localization signalAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili2688 – 276578Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1319 – 13246Poly-Lys

Sequence similaritiesi

Belongs to the UTP20 family.Curated
Contains 2 HEAT repeats.Curated

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiNOG296791.
GeneTreeiENSGT00390000016813.
HOGENOMiHOG000168315.
HOVERGENiHBG094143.
InParanoidiO75691.
KOiK14772.
OMAiWLFDMVT.
OrthoDBiEOG7MWGVX.
PhylomeDBiO75691.
TreeFamiTF105652.

Family and domain databases

Gene3Di1.25.10.10. 5 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR011430. DRIM.
[Graphical view]
PfamiPF07539. DRIM. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 12 hits.

Sequencei

Sequence statusi: Complete.

O75691 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKTKPVSHKT ENTYRFLTFA ERLGNVNIDI IHRIDRTASY EEEVETYFFE
60 70 80 90 100
GLLKWRELNL TEHFGKFYKE VIDKCQSFNQ LVYHQNEIVQ SLKTHLQVKN
110 120 130 140 150
SFAYQPLLDL VVQLARDLQM DFYPHFPEFF LTITSILETQ DTELLEWAFT
160 170 180 190 200
SLSYLYKYLW RLMVKDMSSI YSMYSTLLAH KKLHIRNFAA ESFTFLMRKV
210 220 230 240 250
SDKNALFNLM FLDLDKHPEK VEGVGQLLFE MCKGVRNMFH SCTGQAVKLI
260 270 280 290 300
LRKLGPVTET ETQLPWMLIG ETLKNMVKST VSYISKEHFG TFFECLQESL
310 320 330 340 350
LDLHTKVTKT NCCESSEQIK RLLETYLILV KHGSGTKIPT PADVCKVLSQ
360 370 380 390 400
TLQVASLSTS CWETLLDVIS ALILGENVSL PETLIKETIE KIFESRFEKR
410 420 430 440 450
LIFSFSEVMF AMKQFEQLFL PSFLSYIVNC FLIDDAVVKD EALAILAKLI
460 470 480 490 500
LNKAAPPTAG SMAIEKYPLV FSPQMVGFYI KQKKTRSKGR NEQFPVLDHL
510 520 530 540 550
LSIIKLPPNK DTTYLSQSWA ALVVLPHIRP LEKEKVIPLV TGFIEALFMT
560 570 580 590 600
VDKGSFGKGN LFVLCQAVNT LLSLEESSEL LHLVPVERVK NLVLTFPLEP
610 620 630 640 650
SVLLLTDLYY QRLALCGCKG PLSQEALMEL FPKLQANIST GVSKIRLLTI
660 670 680 690 700
RILNHFDVQL PESMEDDGLS ERQSVFAILR QAELVPATVN DYREKLLHLR
710 720 730 740 750
KLRHDVVQTA VPDGPLQEVP LRYLLGMLYI NFSALWDPVI ELISSHAHEM
760 770 780 790 800
ENKQFWKVYY EHLEKAATHA EKELQNDMTD EKSVGDESWE QTQEGDVGAL
810 820 830 840 850
YHEQLALKTD CQERLDHTNF RFLLWRALTK FPERVEPRSR ELSPLFLRFI
860 870 880 890 900
NNEYYPADLQ VAPTQDLRRK GKGMVAEEIE EEPAAGDDEE LEEEAVPQDE
910 920 930 940 950
SSQKKKTRRA AAKQLIAHLQ VFSKFSNPRA LYLESKLYEL YLQLLLHQDQ
960 970 980 990 1000
MVQKITLDCI MTYKHPHVLP YRENLQRLLE DRSFKEEIVH FSISEDNAVV
1010 1020 1030 1040 1050
KTAHRADLFP ILMRILYGRM KNKTGSKTQG KSASGTRMAI VLRFLAGTQP
1060 1070 1080 1090 1100
EEIQIFLDLL FEPVRHFKNG ECHSAVIQAV EDLDLSKVLP LGRQHGILNS
1110 1120 1130 1140 1150
LEIVLKNISH LISAYLPKIL QILLCMTATV SHILDQREKI QLRFINPLKN
1160 1170 1180 1190 1200
LRRLGIKMVT DIFLDWESYQ FRTEEIDAVF HGAVWPQISR LGSESQYSPT
1210 1220 1230 1240 1250
PLLKLISIWS RNARYFPLLA KQKPGHPECD ILTNVFAILS AKNLSDATAS
1260 1270 1280 1290 1300
IVMDIVDDLL NLPDFEPTET VLNLLVTGCV YPGIAENIGE SITIGGRLIL
1310 1320 1330 1340 1350
PHVPAILQYL SKTTISAEKV KKKKNRAQVS KELGILSKIS KFMKDKEQSS
1360 1370 1380 1390 1400
VLITLLLPFL HRGNIAEDTE VDILVTVQNL LKHCVDPTSF LKPIAKLFSV
1410 1420 1430 1440 1450
IKNKLSRKLL CTVFETLSDF ESGLKYITDV VKLNAFDQRH LDDINFDVRF
1460 1470 1480 1490 1500
ETFQTITSYI KEMQIVDVNY LIPVMHNCFY NLELGDMSLS DNASMCLMSI
1510 1520 1530 1540 1550
IKKLAALNVT EKDYREIIHR SLLEKLRKGL KSQTESIQQD YTTILSCLIQ
1560 1570 1580 1590 1600
TFPNQLEFKD LVQLTHYHDP EMDFFENMKH IQIHRRARAL KKLAKQLMEG
1610 1620 1630 1640 1650
KVVLSSKSLQ NYIMPYAMTP IFDEKMLKHE NITTAATEII GAICKHLSWS
1660 1670 1680 1690 1700
AYMYYLKHFI HVLQTGQINQ KLGVSLLVIV LEAFHFDHKT LEEQMGKIEN
1710 1720 1730 1740 1750
EENAIEAIEL PEPEAMELER VDEEEKEYTC KSLSDNGQPG TPDPADSGGT
1760 1770 1780 1790 1800
SAKESECITK PVSFLPQNKE EIERTIKNIQ GTITGDILPR LHKCLASTTK
1810 1820 1830 1840 1850
REEEHKLVKS KVVNDEEVVR VPLAFAMVKL MQSLPQEVME ANLPSILLKV
1860 1870 1880 1890 1900
CALLKNRAQE IRDIARSTLA KIIEDLGVHF LLYVLKELQT TLVRGYQVHV
1910 1920 1930 1940 1950
LTFTVHMLLQ GLTNKLQVGD LDSCLDIMIE IFNHELFGAV AEEKEVKQIL
1960 1970 1980 1990 2000
SKVMEARRSK SYDSYEILGK FVGKDQVTKL ILPLKEILQN TTSLKLARKV
2010 2020 2030 2040 2050
HETLRRITVG LIVNQEMTAE SILLLSYGLI SENLPLLTEK EKNPVAPAPD
2060 2070 2080 2090 2100
PRLPPQSCLL LPPTPVRGGQ KAVVSRKTNM HIFIESGLRL LHLSLKTSKI
2110 2120 2130 2140 2150
KSSGECVLEM LDPFVSLLID CLGSMDVKVI TGALQCLIWV LRFPLPSIET
2160 2170 2180 2190 2200
KAEQLTKHLF LLLKDYAKLG AARGQNFHLV VNCFKCVTIL VKKVKSYQIT
2210 2220 2230 2240 2250
EKQLQVLLAY AEEDIYDTSR QATAFGLLKA ILSRKLLVPE IDEVMRKVSK
2260 2270 2280 2290 2300
LAVSAQSEPA RVQCRQVFLK YILDYPLGDK LRPNLEFMLA QLNYEHETGR
2310 2320 2330 2340 2350
ESTLEMIAYL FDTFPQGLLH ENCGMFFIPL CLMTINDDSA TCKKMASMTI
2360 2370 2380 2390 2400
KSLLGKISLE KKDWLFDMVT TWFGAKKRLN RQLAALICGL FVESEGVDFE
2410 2420 2430 2440 2450
KRLGTVLPVI EKEIDPENFK DIMEETEEKA ADRLLFSFLT LITKLIKECN
2460 2470 2480 2490 2500
IIQFTKPAET LSKIWSHVHS HLRHPHNWVW LTAAQIFGLL FASCQPEELI
2510 2520 2530 2540 2550
QKWNTKKTKK HLPEPVAIKF LASDLDQKMK SISLASCHQL HSKFLDQSLG
2560 2570 2580 2590 2600
EQVVKNLLFA AKVLYLLELY CEDKQSKIKE DLEEQEALED GVACADEKAE
2610 2620 2630 2640 2650
SDGEEKEEVK EELGRPATLL WLIQKLSRIA KLEAAYSPRN PLKRTCIFKF
2660 2670 2680 2690 2700
LGAVAMDLGI DKVKPYLPMI IAPLFRELNS TYSEQDPLLK NLSQEIIELL
2710 2720 2730 2740 2750
KKLVGLESFS LAFASVQKQA NEKRALRKKR KALEFVTNPD IAAKKKMKKH
2760 2770 2780
KNKSEAKKRK IEFLRPGYKA KRQKSHSLKD LAMVE
Length:2,785
Mass (Da):318,385
Last modified:May 18, 2010 - v3
Checksum:i0CE63611C8440E0D
GO

Sequence cautioni

The sequence AAG35208.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1505 – 15051A → P in CAA07243. (PubMed:9673349)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti120 – 1201M → T.
Corresponds to variant rs2290723 [ dbSNP | Ensembl ].
VAR_055135
Natural varianti502 – 5021S → C.
Corresponds to variant rs4764643 [ dbSNP | Ensembl ].
VAR_022162
Natural varianti1645 – 16451K → I in a breast cancer sample; somatic mutation. 1 Publication
VAR_036274
Natural varianti1882 – 18821L → Q.1 Publication
Corresponds to variant rs10082778 [ dbSNP | Ensembl ].
VAR_055136
Natural varianti2452 – 24521I → F in a breast cancer sample; somatic mutation. 1 Publication
VAR_036275
Natural varianti2612 – 26121E → Q.
Corresponds to variant rs1061436 [ dbSNP | Ensembl ].
VAR_022163

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ006778 mRNA. Translation: CAA07243.1.
AC063948 Genomic DNA. No translation available.
AC063951 Genomic DNA. No translation available.
AF072718 mRNA. Translation: AAG35208.1. Different initiation.
CCDSiCCDS9081.1.
RefSeqiNP_055318.2. NM_014503.2.
UniGeneiHs.295732.

Genome annotation databases

EnsembliENST00000261637; ENSP00000261637; ENSG00000120800.
GeneIDi27340.
KEGGihsa:27340.
UCSCiuc001tia.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ006778 mRNA. Translation: CAA07243.1 .
AC063948 Genomic DNA. No translation available.
AC063951 Genomic DNA. No translation available.
AF072718 mRNA. Translation: AAG35208.1 . Different initiation.
CCDSi CCDS9081.1.
RefSeqi NP_055318.2. NM_014503.2.
UniGenei Hs.295732.

3D structure databases

ProteinModelPortali O75691.
SMRi O75691. Positions 1231-1256.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118152. 17 interactions.
IntActi O75691. 2 interactions.
MINTi MINT-1163597.
STRINGi 9606.ENSP00000261637.

PTM databases

PhosphoSitei O75691.

2D gel databases

SWISS-2DPAGE O75691.

Proteomic databases

MaxQBi O75691.
PaxDbi O75691.
PRIDEi O75691.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261637 ; ENSP00000261637 ; ENSG00000120800 .
GeneIDi 27340.
KEGGi hsa:27340.
UCSCi uc001tia.1. human.

Organism-specific databases

CTDi 27340.
GeneCardsi GC12P101673.
H-InvDB HIX0010919.
HGNCi HGNC:17897. UTP20.
MIMi 612822. gene.
neXtProti NX_O75691.
PharmGKBi PA143485666.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG296791.
GeneTreei ENSGT00390000016813.
HOGENOMi HOG000168315.
HOVERGENi HBG094143.
InParanoidi O75691.
KOi K14772.
OMAi WLFDMVT.
OrthoDBi EOG7MWGVX.
PhylomeDBi O75691.
TreeFami TF105652.

Miscellaneous databases

GeneWikii UTP20.
GenomeRNAii 27340.
NextBioi 50408.
PROi O75691.
SOURCEi Search...

Gene expression databases

Bgeei O75691.
CleanExi HS_UTP20.
Genevestigatori O75691.

Family and domain databases

Gene3Di 1.25.10.10. 5 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR011430. DRIM.
[Graphical view ]
Pfami PF07539. DRIM. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 12 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1741, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  13. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-1645 AND PHE-2452.

Entry informationi

Entry nameiUTP20_HUMAN
AccessioniPrimary (citable) accession number: O75691
Secondary accession number(s): Q9H3H4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3