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Protein

RRP15-like protein

Gene

RRP15

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

Names & Taxonomyi

Protein namesi
Recommended name:
RRP15-like protein
Alternative name(s):
Ribosomal RNA-processing protein 15
Gene namesi
Name:RRP15
Synonyms:KIAA0507
ORF Names:CGI-115
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:24255. RRP15.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162402123.

Polymorphism and mutation databases

BioMutaiRRP15.
DMDMi124053370.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 282281RRP15-like proteinPRO_0000273213Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei9 – 91CitrullineBy similarity
Modified residuei11 – 111PhosphoserineCombined sources
Modified residuei58 – 581PhosphoserineCombined sources
Modified residuei67 – 671PhosphoserineCombined sources
Modified residuei104 – 1041PhosphothreonineCombined sources
Cross-linki239 – 239Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei266 – 2661PhosphoserineCombined sources
Modified residuei276 – 2761PhosphoserineCombined sources
Modified residuei280 – 2801PhosphoserineCombined sources

Post-translational modificationi

Citrullinated by PADI4.By similarity

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9Y3B9.
MaxQBiQ9Y3B9.
PaxDbiQ9Y3B9.
PRIDEiQ9Y3B9.

PTM databases

iPTMnetiQ9Y3B9.
PhosphoSiteiQ9Y3B9.

Miscellaneous databases

PMAP-CutDBQ9Y3B9.

Expressioni

Gene expression databases

BgeeiQ9Y3B9.
CleanExiHS_RRP15.
GenevisibleiQ9Y3B9. HS.

Organism-specific databases

HPAiHPA024639.

Interactioni

Protein-protein interaction databases

BioGridi119224. 29 interactions.
IntActiQ9Y3B9. 12 interactions.
MINTiMINT-3085803.
STRINGi9606.ENSP00000355899.

Structurei

3D structure databases

ProteinModelPortaliQ9Y3B9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili108 – 14437Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the RRP15 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG2974. Eukaryota.
ENOG4111R78. LUCA.
GeneTreeiENSGT00390000001960.
HOGENOMiHOG000047445.
HOVERGENiHBG056607.
InParanoidiQ9Y3B9.
OMAiGTNMGWA.
OrthoDBiEOG73V6MV.
PhylomeDBiQ9Y3B9.
TreeFamiTF106119.

Family and domain databases

InterProiIPR012459. Rrp15.
[Graphical view]
PANTHERiPTHR13245. PTHR13245. 1 hit.
PfamiPF07890. Rrp15p. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Y3B9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAAPDSRV SEEENLKKTP KKKMKMVTGA VASVLEDEAT DTSDSEGSCG
60 70 80 90 100
SEKDHFYSDD DAIEADSEGD AEPCDKENEN DGESSVGTNM GWADAMAKVL
110 120 130 140 150
NKKTPESKPT ILVKNKKLEK EKEKLKQERL EKIKQRDKRL EWEMMCRVKP
160 170 180 190 200
DVVQDKETER NLQRIATRGV VQLFNAVQKH QKNVDEKVKE AGSSMRKRAK
210 220 230 240 250
LISTVSKKDF ISVLRGMDGS TNETASSRKK PKAKQTEVKS EEGPGWTILR
260 270 280
DDFMMGASMK DWDKESDGPD DSRPESASDS DT
Length:282
Mass (Da):31,484
Last modified:January 23, 2007 - v2
Checksum:i3FB1E3D861FB938F
GO

Sequence cautioni

The sequence AAD34110.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH20641.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti23 – 231K → N in AAD34110 (PubMed:10810093).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321A → V.
Corresponds to variant rs34358288 [ dbSNP | Ensembl ].
VAR_053813
Natural varianti149 – 1491K → N.
Corresponds to variant rs11118075 [ dbSNP | Ensembl ].
VAR_030112
Natural varianti230 – 2301K → R.
Corresponds to variant rs3737978 [ dbSNP | Ensembl ].
VAR_030113

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC020641 mRNA. Translation: AAH20641.1. Different initiation.
AF151873 mRNA. Translation: AAD34110.1. Different initiation.
CCDSiCCDS1520.2.
RefSeqiNP_057136.2. NM_016052.3.
UniGeneiHs.660109.

Genome annotation databases

EnsembliENST00000366932; ENSP00000355899; ENSG00000067533.
GeneIDi51018.
KEGGihsa:51018.
UCSCiuc001hlj.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC020641 mRNA. Translation: AAH20641.1. Different initiation.
AF151873 mRNA. Translation: AAD34110.1. Different initiation.
CCDSiCCDS1520.2.
RefSeqiNP_057136.2. NM_016052.3.
UniGeneiHs.660109.

3D structure databases

ProteinModelPortaliQ9Y3B9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119224. 29 interactions.
IntActiQ9Y3B9. 12 interactions.
MINTiMINT-3085803.
STRINGi9606.ENSP00000355899.

PTM databases

iPTMnetiQ9Y3B9.
PhosphoSiteiQ9Y3B9.

Polymorphism and mutation databases

BioMutaiRRP15.
DMDMi124053370.

Proteomic databases

EPDiQ9Y3B9.
MaxQBiQ9Y3B9.
PaxDbiQ9Y3B9.
PRIDEiQ9Y3B9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366932; ENSP00000355899; ENSG00000067533.
GeneIDi51018.
KEGGihsa:51018.
UCSCiuc001hlj.3. human.

Organism-specific databases

CTDi51018.
GeneCardsiRRP15.
HGNCiHGNC:24255. RRP15.
HPAiHPA024639.
MIMi611193. gene.
neXtProtiNX_Q9Y3B9.
PharmGKBiPA162402123.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2974. Eukaryota.
ENOG4111R78. LUCA.
GeneTreeiENSGT00390000001960.
HOGENOMiHOG000047445.
HOVERGENiHBG056607.
InParanoidiQ9Y3B9.
OMAiGTNMGWA.
OrthoDBiEOG73V6MV.
PhylomeDBiQ9Y3B9.
TreeFamiTF106119.

Miscellaneous databases

ChiTaRSiRRP15. human.
GeneWikiiRRP15.
GenomeRNAii51018.
PMAP-CutDBQ9Y3B9.
PROiQ9Y3B9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y3B9.
CleanExiHS_RRP15.
GenevisibleiQ9Y3B9. HS.

Family and domain databases

InterProiIPR012459. Rrp15.
[Graphical view]
PANTHERiPTHR13245. PTHR13245. 1 hit.
PfamiPF07890. Rrp15p. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "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: Testis.
  2. "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] OF 13-282.
  3. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104; SER-266; SER-276 AND SER-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND THR-104, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-58; SER-67 AND SER-266, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-239, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRRP15_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3B9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 113 of the entry and version 2 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 1
    Human chromosome 1: 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

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.