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Q14684 (RRP1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribosomal RNA processing protein 1 homolog B
Alternative name(s):
RRP1-like protein B
Gene names
Name:RRP1B
Synonyms:KIAA0179
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length758 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Nucleusnucleolus Ref.4.

Post-translational modification

Citrullinated by PADI4 By similarity.

Sequence similarities

Belongs to the RRP1 family.

Sequence caution

The sequence BAA11496.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LSM1O151161EBI-372051,EBI-347619

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14684-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q14684-2)

The sequence of this isoform differs from the canonical sequence as follows:
     51-68: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 758758Ribosomal RNA processing protein 1 homolog B
PRO_0000050729

Regions

Compositional bias402 – 4065Poly-Lys

Amino acid modifications

Modified residue2451Phosphoserine Ref.5 Ref.7 Ref.8 Ref.9 Ref.11 Ref.13 Ref.15
Modified residue3501Phosphoserine Ref.9 Ref.11 Ref.13
Modified residue3921Phosphoserine Ref.6 Ref.9
Modified residue3941Phosphoserine Ref.9
Modified residue3951Phosphoserine Ref.9
Modified residue4521Phosphoserine Ref.9
Modified residue4581Phosphoserine Ref.9
Modified residue5131Phosphoserine Ref.6 Ref.13 Ref.15
Modified residue6521N6-acetyllysine Ref.12
Modified residue7021Phosphoserine Ref.9 Ref.13
Modified residue7061Phosphoserine Ref.9 Ref.13 Ref.15
Modified residue7121Citrulline By similarity
Modified residue7281Phosphothreonine Ref.15
Modified residue7321Phosphoserine Ref.9 Ref.11 Ref.13 Ref.15
Modified residue7351Phosphoserine Ref.11 Ref.13
Modified residue7361Phosphoserine Ref.9

Natural variations

Alternative sequence51 – 6818Missing in isoform 2.
VSP_007801

Experimental info

Sequence conflict4361L → P in BAA11496. Ref.1
Sequence conflict4361L → P in AAH28386. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: 738117A7062054F2

FASTA75884,428
        10         20         30         40         50         60 
MAPAMQPAEI QFAQRLASSE KGIRDRAVKK LRQYISVKTQ RETGGFSQEE LLKIWKGLFY 

        70         80         90        100        110        120 
CMWVQDEPLL QEELANTIAQ LVHAVNNSAA QHLFIQTFWQ TMNREWKGID RLRLDKYYML 

       130        140        150        160        170        180 
IRLVLRQSFE VLKRNGWEES RIKVFLDVLM KEVLCPESQS PNGVRFHFID IYLDELSKVG 

       190        200        210        220        230        240 
GKELLADQNL KFIDPFCKIA AKTKDHTLVQ TIARGVFEAI VDQSPFVPEE TMEEQKTKVG 

       250        260        270        280        290        300 
DGDLSAEEIP ENEVSLRRAV SKKKTALGKN HSRKDGLSDE RGRDDCGTFE DTGPLLQFDY 

       310        320        330        340        350        360 
KAVADRLLEM TSRKNTPHFN RKRLSKLIKK FQDLSEGSSI SQLSFAEDIS ADEDDQILSQ 

       370        380        390        400        410        420 
GKHKKKGNKL LEKTNLEKEK GSRVFCVEEE DSESSLQKRR RKKKKKHHLQ PENPGPGGAA 

       430        440        450        460        470        480 
PSLEQNRGRE PEASGLKALK ARVAEPGAEA TSSTGEESGS EHPPAVPMHN KRKRPRKKSP 

       490        500        510        520        530        540 
RAHREMLESA VLPPEDMSQS GPSGSHPQGP RGSPTGGAQL LKRKRKLGVV PVNGSGLSTP 

       550        560        570        580        590        600 
AWPPLQQEGP PTGPAEGANS HTTLPQRRRL QKKKAGPGSL ELCGLPSQKT ASLKKRKKMR 

       610        620        630        640        650        660 
VMSNLVEHNG VLESEAGQPQ ALGSSGTCSS LKKQKLRAES DFVKFDTPFL PKPLFFRRAK 

       670        680        690        700        710        720 
SSTATHPPGP AVQLNKTPSS SKKVTFGLNR NMTAEFKKTD KSILVSPTGP SRVAFDPEQK 

       730        740        750 
PLHGVLKTPT SSPASSPLVA KKPLTTTPRR RPRAMDFF 

« Hide

Isoform 2 [UniParc].

Checksum: 7D39CB77AA4BE255
Show »

FASTA74082,176

References

[1]"Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Bone marrow.
[2]"The DNA sequence of human chromosome 21."
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A. expand/collapse author list , Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.
Nature 405:311-319(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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] (ISOFORM 1).
Tissue: Testis.
[4]"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].
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-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392 AND SER-513, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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-245, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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 SER-245; SER-350; SER-392; SER-394; SER-395; SER-452; SER-458; SER-702; SER-706; SER-732 AND SER-736, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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].
[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 SER-245; SER-350; SER-732 AND SER-735, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-652, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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-245; SER-350; SER-513; SER-702; SER-706; SER-732 AND SER-735, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[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 SER-245; SER-513; SER-706; THR-728 AND SER-732, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D80001 mRNA. Translation: BAA11496.1. Different initiation.
AP001052 Genomic DNA. No translation available.
BC028386 mRNA. Translation: AAH28386.1.
RefSeqNP_055871.1. NM_015056.2.
UniGeneHs.565725.

3D structure databases

ProteinModelPortalQ14684.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116708. 46 interactions.
IntActQ14684. 12 interactions.
MINTMINT-3029999.
STRING9606.ENSP00000339145.

PTM databases

PhosphoSiteQ14684.

Polymorphism databases

DMDM296452976.

2D gel databases

SWISS-2DPAGEQ14684.

Proteomic databases

PaxDbQ14684.
PRIDEQ14684.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340648; ENSP00000339145; ENSG00000160208. [Q14684-1]
GeneID23076.
KEGGhsa:23076.
UCSCuc002zdk.3. human. [Q14684-1]

Organism-specific databases

CTD23076.
GeneCardsGC21P045079.
H-InvDBHIX0016154.
HGNCHGNC:23818. RRP1B.
HPAHPA017893.
HPA020324.
MIM610654. gene.
neXtProtNX_Q14684.
PharmGKBPA162402138.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG299406.
HOGENOMHOG000070179.
HOVERGENHBG098014.
InParanoidQ14684.
KOK14849.
OMAMTAEFKK.
OrthoDBEOG718KC8.
PhylomeDBQ14684.
TreeFamTF315294.

Gene expression databases

BgeeQ14684.
CleanExHS_RRP1B.
GenevestigatorQ14684.

Family and domain databases

InterProIPR010301. Nop52.
[Graphical view]
PANTHERPTHR13026. PTHR13026. 1 hit.
PfamPF05997. Nop52. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRRP1B.
GenomeRNAi23076.
NextBio44187.
PROQ14684.
SOURCESearch...

Entry information

Entry nameRRP1B_HUMAN
AccessionPrimary (citable) accession number: Q14684
Secondary accession number(s): Q8TBZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM