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Protein

U3 small nucleolar RNA-associated protein 18 homolog

Gene

UTP18

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Involved in nucleolar processing of pre-18S ribosomal RNA.By similarity

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

rRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
U3 small nucleolar RNA-associated protein 18 homolog
Alternative name(s):
WD repeat-containing protein 50
Gene namesi
Name:UTP18
Synonyms:WDR50
ORF Names:CDABP0061, CGI-48
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:24274. UTP18.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134984104.

Polymorphism and mutation databases

BioMutaiUTP18.
DMDMi73920973.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 556556U3 small nucleolar RNA-associated protein 18 homologPRO_0000051405Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei121 – 1211PhosphoserineCombined sources
Modified residuei124 – 1241PhosphoserineCombined sources
Modified residuei204 – 2041PhosphothreonineCombined sources
Modified residuei205 – 2051PhosphoserineCombined sources
Modified residuei206 – 2061PhosphoserineCombined sources
Modified residuei210 – 2101PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9Y5J1.
MaxQBiQ9Y5J1.
PaxDbiQ9Y5J1.
PRIDEiQ9Y5J1.

2D gel databases

SWISS-2DPAGEQ9Y5J1.

PTM databases

iPTMnetiQ9Y5J1.
PhosphoSiteiQ9Y5J1.

Miscellaneous databases

PMAP-CutDBQ9Y5J1.

Expressioni

Gene expression databases

BgeeiQ9Y5J1.
CleanExiHS_UTP18.
ExpressionAtlasiQ9Y5J1. baseline and differential.
GenevisibleiQ9Y5J1. HS.

Organism-specific databases

HPAiHPA052378.

Interactioni

Protein-protein interaction databases

BioGridi119285. 22 interactions.
IntActiQ9Y5J1. 15 interactions.
MINTiMINT-3087088.
STRINGi9606.ENSP00000225298.

Structurei

3D structure databases

ProteinModelPortaliQ9Y5J1.
SMRiQ9Y5J1. Positions 249-459.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati249 – 28840WD 1Add
BLAST
Repeati293 – 33341WD 2Add
BLAST
Repeati339 – 38042WD 3Add
BLAST
Repeati381 – 41939WD 4Add
BLAST
Repeati421 – 46242WD 5Add
BLAST
Repeati471 – 51242WD 6Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat UTP18 family.Curated
Contains 6 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG2055. Eukaryota.
ENOG410YBWP. LUCA.
GeneTreeiENSGT00440000033919.
HOGENOMiHOG000242429.
HOVERGENiHBG082494.
InParanoidiQ9Y5J1.
KOiK14553.
OMAiRTRKCIH.
OrthoDBiEOG7C5M8J.
PhylomeDBiQ9Y5J1.
TreeFamiTF313426.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y5J1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPERRRRMK LDRRTGAKPK RKPGMRPDWK AGAGPGGPPQ KPAPSSQRKP
60 70 80 90 100
PARPSAAAAA IAVAAAEEER RLRQRNRLRL EEDKPAVERC LEELVFGDVE
110 120 130 140 150
NDEDALLRRL RGPRVQEHED SGDSEVENEA KGNFPPQKKP VWVDEEDEDE
160 170 180 190 200
EMVDMMNNRF RKDMMKNASE SKLSKDNLKK RLKEEFQHAM GGVPAWAETT
210 220 230 240 250
KRKTSSDDES EEDEDDLLQR TGNFISTSTS LPRGILKMKN CQHANAERPT
260 270 280 290 300
VARISSVQFH PGAQIVMVAG LDNAVSLFQV DGKTNPKIQS IYLERFPIFK
310 320 330 340 350
ACFSANGEEV LATSTHSKVL YVYDMLAGKL IPVHQVRGLK EKIVRSFEVS
360 370 380 390 400
PDGSFLLING IAGYLHLLAM KTKELIGSMK INGRVAASTF SSDSKKVYAS
410 420 430 440 450
SGDGEVYVWD VNSRKCLNRF VDEGSLYGLS IATSRNGQYV ACGSNCGVVN
460 470 480 490 500
IYNQDSCLQE TNPKPIKAIM NLVTGVTSLT FNPTTEILAI ASEKMKEAVR
510 520 530 540 550
LVHLPSCTVF SNFPVIKNKN ISHVHTMDFS PRSGYFALGN EKGKALMYRL

HHYSDF
Length:556
Mass (Da):62,004
Last modified:August 30, 2005 - v3
Checksum:i800139F974F4EDF6
GO

Sequence cautioni

The sequence AAD34043.1 differs from that shown. Reason: Frameshift at position 19. Curated
The sequence AAG01999.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti543 – 55614GKALM…HYSDF → ARP in AAD34043 (PubMed:10810093).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151806 mRNA. Translation: AAD34043.1. Frameshift.
BC025276 mRNA. Translation: AAH25276.2.
AY007138 mRNA. Translation: AAG01999.1. Different initiation.
CCDSiCCDS42362.1.
RefSeqiNP_057085.2. NM_016001.2.
UniGeneiHs.709327.

Genome annotation databases

EnsembliENST00000225298; ENSP00000225298; ENSG00000011260.
GeneIDi51096.
KEGGihsa:51096.
UCSCiuc002its.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151806 mRNA. Translation: AAD34043.1. Frameshift.
BC025276 mRNA. Translation: AAH25276.2.
AY007138 mRNA. Translation: AAG01999.1. Different initiation.
CCDSiCCDS42362.1.
RefSeqiNP_057085.2. NM_016001.2.
UniGeneiHs.709327.

3D structure databases

ProteinModelPortaliQ9Y5J1.
SMRiQ9Y5J1. Positions 249-459.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119285. 22 interactions.
IntActiQ9Y5J1. 15 interactions.
MINTiMINT-3087088.
STRINGi9606.ENSP00000225298.

PTM databases

iPTMnetiQ9Y5J1.
PhosphoSiteiQ9Y5J1.

Polymorphism and mutation databases

BioMutaiUTP18.
DMDMi73920973.

2D gel databases

SWISS-2DPAGEQ9Y5J1.

Proteomic databases

EPDiQ9Y5J1.
MaxQBiQ9Y5J1.
PaxDbiQ9Y5J1.
PRIDEiQ9Y5J1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000225298; ENSP00000225298; ENSG00000011260.
GeneIDi51096.
KEGGihsa:51096.
UCSCiuc002its.4. human.

Organism-specific databases

CTDi51096.
GeneCardsiUTP18.
HGNCiHGNC:24274. UTP18.
HPAiHPA052378.
MIMi612816. gene.
neXtProtiNX_Q9Y5J1.
PharmGKBiPA134984104.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2055. Eukaryota.
ENOG410YBWP. LUCA.
GeneTreeiENSGT00440000033919.
HOGENOMiHOG000242429.
HOVERGENiHBG082494.
InParanoidiQ9Y5J1.
KOiK14553.
OMAiRTRKCIH.
OrthoDBiEOG7C5M8J.
PhylomeDBiQ9Y5J1.
TreeFamiTF313426.

Miscellaneous databases

ChiTaRSiUTP18. human.
GeneWikiiUTP18.
GenomeRNAii51096.
NextBioi53793.
PMAP-CutDBQ9Y5J1.
PROiQ9Y5J1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y5J1.
CleanExiHS_UTP18.
ExpressionAtlasiQ9Y5J1. baseline and differential.
GenevisibleiQ9Y5J1. HS.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 1 hit.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skin.
  3. "Pediatric leukemia cDNA sequencing project."
    Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A., Margolin J.F.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 162-556.
    Tissue: Leukemia.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-204; SER-205; SER-206 AND SER-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  9. "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].
  10. "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 SER-206 AND SER-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  11. "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-121; SER-124 AND SER-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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 SER-121; SER-124; THR-204; SER-206 AND SER-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-124; THR-204 AND SER-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiUTP18_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5J1
Secondary accession number(s): Q9H4N6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: August 30, 2005
Last modified: May 11, 2016
This is version 154 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 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.