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Protein

Ribosomal RNA processing protein 1 homolog B

Gene

RRP1B

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

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. negative regulation of phosphatase activity Source: UniProtKB
  2. rRNA processing Source: InterPro
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal RNA processing protein 1 homolog B
Alternative name(s):
RRP1-like protein B
Gene namesi
Name:RRP1B
Synonyms:KIAA0179
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 21

Organism-specific databases

HGNCiHGNC:23818. RRP1B.

Subcellular locationi

  1. Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. euchromatin Source: Ensembl
  3. heterochromatin Source: Ensembl
  4. nucleolus Source: HPA
  5. nucleus Source: UniProtKB
  6. preribosome, small subunit precursor Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162402138.

Polymorphism and mutation databases

BioMutaiRRP1B.
DMDMi296452976.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 758758Ribosomal RNA processing protein 1 homolog BPRO_0000050729Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei245 – 2451Phosphoserine7 Publications
Modified residuei350 – 3501Phosphoserine4 Publications
Modified residuei392 – 3921Phosphoserine2 Publications
Modified residuei394 – 3941Phosphoserine1 Publication
Modified residuei395 – 3951Phosphoserine1 Publication
Modified residuei452 – 4521Phosphoserine1 Publication
Modified residuei458 – 4581Phosphoserine1 Publication
Modified residuei513 – 5131Phosphoserine3 Publications
Modified residuei652 – 6521N6-acetyllysine1 Publication
Modified residuei702 – 7021Phosphoserine2 Publications
Modified residuei706 – 7061Phosphoserine3 Publications
Modified residuei712 – 7121CitrullineBy similarity
Modified residuei728 – 7281Phosphothreonine1 Publication
Modified residuei732 – 7321Phosphoserine4 Publications
Modified residuei735 – 7351Phosphoserine2 Publications
Modified residuei736 – 7361Phosphoserine1 Publication

Post-translational modificationi

Citrullinated by PADI4.By similarity

Keywords - PTMi

Acetylation, Citrullination, Phosphoprotein

Proteomic databases

MaxQBiQ14684.
PaxDbiQ14684.
PRIDEiQ14684.

2D gel databases

SWISS-2DPAGEQ14684.

PTM databases

PhosphoSiteiQ14684.

Expressioni

Gene expression databases

BgeeiQ14684.
CleanExiHS_RRP1B.
GenevestigatoriQ14684.

Organism-specific databases

HPAiHPA017893.
HPA020324.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
LSM1O151161EBI-372051,EBI-347619

Protein-protein interaction databases

BioGridi116708. 53 interactions.
IntActiQ14684. 12 interactions.
MINTiMINT-3029999.
STRINGi9606.ENSP00000339145.

Structurei

3D structure databases

ProteinModelPortaliQ14684.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi402 – 4065Poly-Lys

Sequence similaritiesi

Belongs to the RRP1 family.Curated

Phylogenomic databases

eggNOGiNOG299406.
GeneTreeiENSGT00390000011821.
HOGENOMiHOG000070179.
HOVERGENiHBG098014.
InParanoidiQ14684.
KOiK14849.
OMAiQKPLHGV.
OrthoDBiEOG718KC8.
PhylomeDBiQ14684.
TreeFamiTF315294.

Family and domain databases

InterProiIPR010301. Nop52.
[Graphical view]
PANTHERiPTHR13026. PTHR13026. 1 hit.
PfamiPF05997. Nop52. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q14684-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAPAMQPAEI QFAQRLASSE KGIRDRAVKK LRQYISVKTQ RETGGFSQEE
60 70 80 90 100
LLKIWKGLFY CMWVQDEPLL QEELANTIAQ LVHAVNNSAA QHLFIQTFWQ
110 120 130 140 150
TMNREWKGID RLRLDKYYML IRLVLRQSFE VLKRNGWEES RIKVFLDVLM
160 170 180 190 200
KEVLCPESQS PNGVRFHFID IYLDELSKVG GKELLADQNL KFIDPFCKIA
210 220 230 240 250
AKTKDHTLVQ TIARGVFEAI VDQSPFVPEE TMEEQKTKVG DGDLSAEEIP
260 270 280 290 300
ENEVSLRRAV SKKKTALGKN HSRKDGLSDE RGRDDCGTFE DTGPLLQFDY
310 320 330 340 350
KAVADRLLEM TSRKNTPHFN RKRLSKLIKK FQDLSEGSSI SQLSFAEDIS
360 370 380 390 400
ADEDDQILSQ GKHKKKGNKL LEKTNLEKEK GSRVFCVEEE DSESSLQKRR
410 420 430 440 450
RKKKKKHHLQ PENPGPGGAA PSLEQNRGRE PEASGLKALK ARVAEPGAEA
460 470 480 490 500
TSSTGEESGS EHPPAVPMHN KRKRPRKKSP RAHREMLESA VLPPEDMSQS
510 520 530 540 550
GPSGSHPQGP RGSPTGGAQL LKRKRKLGVV PVNGSGLSTP AWPPLQQEGP
560 570 580 590 600
PTGPAEGANS HTTLPQRRRL QKKKAGPGSL ELCGLPSQKT ASLKKRKKMR
610 620 630 640 650
VMSNLVEHNG VLESEAGQPQ ALGSSGTCSS LKKQKLRAES DFVKFDTPFL
660 670 680 690 700
PKPLFFRRAK SSTATHPPGP AVQLNKTPSS SKKVTFGLNR NMTAEFKKTD
710 720 730 740 750
KSILVSPTGP SRVAFDPEQK PLHGVLKTPT SSPASSPLVA KKPLTTTPRR

RPRAMDFF
Length:758
Mass (Da):84,428
Last modified:May 18, 2010 - v3
Checksum:i738117A7062054F2
GO
Isoform 2 (identifier: Q14684-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     51-68: Missing.

Note: No experimental confirmation available.

Show »
Length:740
Mass (Da):82,176
Checksum:i7D39CB77AA4BE255
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti436 – 4361L → P in BAA11496 (PubMed:8724849).Curated
Sequence conflicti436 – 4361L → P in AAH28386 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei51 – 6818Missing in isoform 2. 1 PublicationVSP_007801Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D80001 mRNA. Translation: BAA11496.1. Different initiation.
AP001052 Genomic DNA. No translation available.
BC028386 mRNA. Translation: AAH28386.1.
CCDSiCCDS33577.1. [Q14684-1]
RefSeqiNP_055871.1. NM_015056.2. [Q14684-1]
UniGeneiHs.565725.

Genome annotation databases

EnsembliENST00000340648; ENSP00000339145; ENSG00000160208. [Q14684-1]
GeneIDi23076.
KEGGihsa:23076.
UCSCiuc002zdk.3. human. [Q14684-1]

Polymorphism and mutation databases

BioMutaiRRP1B.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D80001 mRNA. Translation: BAA11496.1. Different initiation.
AP001052 Genomic DNA. No translation available.
BC028386 mRNA. Translation: AAH28386.1.
CCDSiCCDS33577.1. [Q14684-1]
RefSeqiNP_055871.1. NM_015056.2. [Q14684-1]
UniGeneiHs.565725.

3D structure databases

ProteinModelPortaliQ14684.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116708. 53 interactions.
IntActiQ14684. 12 interactions.
MINTiMINT-3029999.
STRINGi9606.ENSP00000339145.

PTM databases

PhosphoSiteiQ14684.

Polymorphism and mutation databases

BioMutaiRRP1B.
DMDMi296452976.

2D gel databases

SWISS-2DPAGEQ14684.

Proteomic databases

MaxQBiQ14684.
PaxDbiQ14684.
PRIDEiQ14684.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000340648; ENSP00000339145; ENSG00000160208. [Q14684-1]
GeneIDi23076.
KEGGihsa:23076.
UCSCiuc002zdk.3. human. [Q14684-1]

Organism-specific databases

CTDi23076.
GeneCardsiGC21P045079.
H-InvDBHIX0016154.
HGNCiHGNC:23818. RRP1B.
HPAiHPA017893.
HPA020324.
MIMi610654. gene.
neXtProtiNX_Q14684.
PharmGKBiPA162402138.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG299406.
GeneTreeiENSGT00390000011821.
HOGENOMiHOG000070179.
HOVERGENiHBG098014.
InParanoidiQ14684.
KOiK14849.
OMAiQKPLHGV.
OrthoDBiEOG718KC8.
PhylomeDBiQ14684.
TreeFamiTF315294.

Miscellaneous databases

ChiTaRSiRRP1B. human.
GeneWikiiRRP1B.
GenomeRNAii23076.
NextBioi44187.
PROiQ14684.
SOURCEiSearch...

Gene expression databases

BgeeiQ14684.
CleanExiHS_RRP1B.
GenevestigatoriQ14684.

Family and domain databases

InterProiIPR010301. Nop52.
[Graphical view]
PANTHERiPTHR13026. PTHR13026. 1 hit.
PfamiPF05997. Nop52. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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-350, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRRP1B_HUMAN
AccessioniPrimary (citable) accession number: Q14684
Secondary accession number(s): Q8TBZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 18, 2010
Last modified: April 29, 2015
This is version 138 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 21
    Human chromosome 21: 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

External Data

Dasty 3

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 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.