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Reviewed, UniProtKB/Swiss-Prot O43818 (U3IP2_HUMAN)

Last modified January 19, 2010. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    U3 small nucleolar RNA-interacting protein 2
Alternative name(s):
    U3 small nucleolar ribonucleoprotein-associated 55 kDa protein
      Short name=U3 snoRNP-associated 55 kDa protein
      Short name=U3-55K
    RRP9 homolog
Gene names
Name: RRP9
Synonyms: RNU3IP2, U355K
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length475 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Component of a nucleolar small nuclear ribonucleoprotein particle (snoRNP) thought to participate in the processing and modification of pre-ribosomal RNA.

Subunit structure

Interacts specifically with the U3 small nucleolar RNA (U3 snoRNA). Binds a sub-fragment of the U3 snoRNA surrounding the B/C motif (3UBC). This association with the U3BC RNA is dependent on the binding of a protein called 15.5K to the box B/C motif. The association of the protein with the U3BC RNA was found to be also dependent on a conserved RNA structure that flanks the box B/C motif. Ref.5 Ref.6

Subcellular location

Nucleusnucleolus Ref.7.

Domain

The WD domains are required for nucleolar localization and U3 small nucleolar RNAs binding.

Sequence similarities

Belongs to the WD repeat RRP9 family.

Contains 7 WD repeats.

Ontologies

Keywords
   Biological processrRNA processing
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DomainRepeat
WD repeat
   LigandRNA-binding
   Molecular functionRibonucleoprotein
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processrRNA processing Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentnucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

small nuclear ribonucleoprotein complex Ref.1

Traceable author statement. Source: ProtInc

small nucleolar ribonucleoprotein complex Ref.1

Traceable author statement. Source: ProtInc

   Molecular functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 475475U3 small nucleolar RNA-interacting protein 2
PRO_0000051313

Regions

Repeat144 – 18340WD 1
Repeat197 – 23640WD 2
Repeat239 – 27840WD 3
Repeat281 – 32040WD 4
Repeat322 – 36039WD 5
Repeat374 – 41340WD 6
Repeat419 – 46042WD 7
Motif8 – 4033Nuclear localization signal Potential
Compositional bias47 – 10559Glu-rich

Amino acid modifications

Modified residue501Phosphoserine Ref.8 Ref.10 Ref.11 Ref.12
Modified residue511Phosphoserine Ref.8 Ref.10 Ref.11 Ref.12
Modified residue531Phosphoserine Ref.8 Ref.10 Ref.11 Ref.12
Modified residue571Phosphoserine Ref.10 Ref.12
Modified residue4751Phosphoserine Ref.9

Natural variations

Natural variant81R → G in a breast cancer sample; somatic mutation. Ref.13
VAR_035887
Natural variant3421A → E in a breast cancer sample; somatic mutation. Ref.13
VAR_035888

Sequences

Sequence LengthMass (Da)Tools
O43818-1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 3CD19F66EA75B627

FASTA47551,841
        10         20         30         40         50         60 
MSATAAARKR GKPASGAGAG AGAGKRRRKA DSAGDRGKSK GGGKMNEEIS SDSESESLAP 

        70         80         90        100        110        120 
RKPEEEEEEE LEETAQEKKL RLAKLYLEQL RQQEEEKAEA RAFEEDQVAG RLKEDVLEQR 

       130        140        150        160        170        180 
GRLQKLVAKE IQAPASADIR VLRGHQLSIT CLVVTPDDSA IFSAAKDCSI IKWSVESGRK 

       190        200        210        220        230        240 
LHVIPRAKKG AEGKPPGHSS HVLCMAISSD GKYLASGDRS KLILIWEAQS CQHLYTFTGH 

       250        260        270        280        290        300 
RDAVSGLAFR RGTHQLYSTS HDRSVKVWNV AENSYVETLF GHQDAVAALD ALSRECCVTA 

       310        320        330        340        350        360 
GGRDGTVRVW KIPEESQLVF YGHQGSIDCI HLINEEHMVS GADDGSVALW GLSKKRPLAL 

       370        380        390        400        410        420 
QREAHGLRGE PGLEQPFWIS SVAALLNTDL VATGSHSSCV RLWQCGEGFR QLDLLCDIPL 

       430        440        450        460        470 
VGFINSLKFS SSGDFLVAGV GQEHRLGRWW RIKEARNSVC IIPLRRVPVP PAAGS 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and characterization of the human U3 small nucleolar ribonucleoprotein complex-associated 55-kilodalton protein."
Pluk H., Soffner J., Luehrmann R., van Venrooij W.J.
Mol. Cell. Biol. 18:488-498(1998) [PubMed: 9418896] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 102-113 AND 267-273.
Tissue: Teratocarcinoma.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]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. expand/collapse author list , 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Skin.
[5]"Interaction of the U3-55k protein with U3 snoRNA is mediated by the box B/C motif of U3 and the WD repeats of U3-55k."
Lukowiak A.A., Granneman S., Mattox S.A., Speckmann W.A., Jones K., Pluk H., van Venrooij W.J., Terns R.M., Terns M.P.
Nucleic Acids Res. 28:3462-3471(2000) [PubMed: 10982864] [Abstract]
Cited for: INTERACTION WITH U3 SNRNA.
[6]"The hU3-55K protein requires 15.5K binding to the box B/C motif as well as flanking RNA elements for its association with the U3 small nucleolar RNA in Vitro."
Granneman S., Pruijn G.J.M., Horstman W., van Venrooij W.J., Luehrmann R., Watkins N.J.
J. Biol. Chem. 277:48490-48500(2002) [PubMed: 12381732] [Abstract]
Cited for: INTERACTION WITH U3 SNRNA.
[7]"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: 12429849] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-51 AND SER-53, MASS SPECTROMETRY.
Tissue: Epithelium.
[9]"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis."
Wang B., Malik R., Nigg E.A., Korner R.
Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, MASS SPECTROMETRY.
[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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-51; SER-53 AND SER-57, MASS SPECTROMETRY.
[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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-51 AND SER-53, MASS SPECTROMETRY.
[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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-51; SER-53 AND SER-57, MASS SPECTROMETRY.
Tissue: T-cell.
[13]"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. expand/collapse author list , 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: 16959974] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLY-8 AND GLU-342.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ001340 mRNA. Translation: CAA04687.1.
AK313696 mRNA. Translation: BAG36443.1.
CH471055 Genomic DNA. Translation: EAW65159.1.
BC001113 mRNA. Translation: AAH01113.1.
BC009879 mRNA. Translation: AAH09879.1.
BC010048 mRNA. Translation: AAH10048.1.
BC023662 mRNA. Translation: AAH23662.2.
IPIIPI00217862.
RefSeqNP_004695.1.
UniGeneHs.153768

3D structure databases

SMRO43818. Positions 139-446.
ModBaseSearch...

Protein-protein interaction databases

IntActO43818. 1 interaction.
STRINGO43818.

PTM databases

PhosphoSiteO43818.

2-D gel databases

SWISS-2DPAGEO43818.
DOSAC-COBS-2DPAGEO43818.

Proteomic databases

PeptideAtlasO43818.
PRIDEO43818.

Genome annotation databases

EnsemblENST00000232888; ENSP00000232888; ENSG00000114767; Homo sapiens. [Genome view]
GeneID9136.
KEGGhsa:9136.
UCSCuc003dbw.1. human.

Organism-specific databases

CTD9136.
GeneCardsGC03M051943.
H-InvDBHIX0003335.
HGNCHGNC:16829. RRP9.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG06018.
HOGENOMHBG713247.
HOVERGENO43818.
InParanoidO43818.
OMAWISSVAA.
OrthoDBEOG9DNHQG.
PhylomeDBO43818.

Gene expression databases

ArrayExpressO43818.
BgeeO43818.
CleanExHS_RRP9.
GenevestigatorO43818.
GermOnlineENSG00000114767. Homo sapiens.

Family and domain databases

InterProIPR020472. G-protein_beta_WD-40_rep_reg.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR011046. WD40_repeat-like_dom.
IPR019782. WD40_repeat_2.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
IPR019781. WD40_repeat_sg.
[Graphical view]
Gene3DG3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
PfamPF00400. WD40. 6 hits.
[Graphical view]
PRINTSPR00320. GPROTEINBRPT.
SMARTSM00320. WD40. 6 hits.
[Graphical view]
PROSITEPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 5 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio34259.

Entry information

Entry nameU3IP2_HUMAN
AccessionPrimary (citable) accession number: O43818
Secondary accession number(s): B2R996, Q8IZ30
Entry history
Integrated into UniProtKB/Swiss-Prot: October 10, 2003
Last sequence update: June 1, 1998
Last modified: January 19, 2010
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents