Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
MRTO4 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
MRTO4 Involved in mRNA turnover and ribosome assembly. Belongs to the ribosomal protein L10P family. Note: This description may include information from UniProtKB.
Protein type: Nucleolus
Chromosomal Location of Human Ortholog: 1p36.13
Cellular Component: nuclear membrane; nucleolus; nucleus
Biological Process: ribosome biogenesis and assembly
Reference #:  Q9UKD2 (UniProtKB)
Alt. Names/Synonyms: 60S acidic ribosomal protein PO; C1orf33; dJ657E11.4; mRNA turnover 4 homolog (S. cerevisiae); mRNA turnover protein 4 homolog; MRT4; MRT4, mRNA turnover 4, homolog; MRTO4; ribosomal protein, large, P0-like
Gene Symbols: MRTO4
Molecular weight: 27,560 Da
Basal Isoelectric point: 8.34  Predict pI for various phosphorylation states
Select Structure to View Below

MRTO4

Protein Structure Not Found.


STRING  |  Wikipedia  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  Phospho.ELM  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K5-ac ___MPKSkRDkkVSL
0 1 K8-ac MPKSkRDkkVSLTKT
0 1 K9-ac PKSkRDkkVSLTKTA
0 1 Y39-p KCVDTYKyLFIFsVA
0 1 S44-p YKyLFIFsVANMRNs
0 1 S51-p sVANMRNsKLKDIRN
0 1 K69-ac HSRMFFGkNKVMMVA
0 3 S80-p MMVALGRsPsDEykD
0 1 S82-p VALGRsPsDEykDNL
0 1 Y85-p GRsPsDEykDNLHQV
0 1 K86-ac RsPsDEykDNLHQVS
0 1 K86-ub RsPsDEykDNLHQVS
0 1 K94-ub DNLHQVSkRLRGEVG
0 1 T105-p GEVGLLFtNRTKEEV
0 1 T160-p LRQLGLPtALkRGVV
0 1 K163-ac LGLPtALkRGVVTLL
0 1 K177-ub LSDYEVCkEGDVLTP
0 3 S225-p MGDDLPEsASEsTEE
0 3 S229-p LPEsASEsTEEsDsE
0 3 S233-p ASEsTEEsDsEDDD_
0 2 S235-p EsTEEsDsEDDD___
  mouse

 
K5 ___MPKSKRDKKVSL
K8 MPKSKRDKKVSLTKT
K9 PKSKRDKKVSLTKTA
Y39 KCVDTYKYLFIFSVA
S44 YKYLFIFSVANMRNS
S51 SVANMRNSKLKDIRN
K69 HSRMFFGKNKVMMVA
S80 MMVALGRSPSDEYKD
S82 VALGRSPSDEYKDNL
Y85 GRSPSDEYKDNLHQV
K86 RSPSDEYKDNLHQVS
K86 RSPSDEYKDNLHQVS
K94 DNLHQVSKKLRGEVG
T105 GEVGLLFTNRTKEEV
T160 LRQLGLPTALKKGVV
K163 LGLPTALKKGVVTLL
K177 LSDYEVCKEGDVLTP
S225-p MDDDLPEsAPEsEGE
S229-p LPEsAPEsEGEsEEE
S233-p APEsEGEsEEEDDS_
- gap
  rat

 
- gap
- gap
- gap
- gap
- gap
S4 ____MRNSKLKDIRN
K22-ac HSRMFFGkNKVMMVA
S33 MMVALGRSPSDEYKD
S35 VALGRSPSDEYKDNL
Y38 GRSPSDEYKDNLHQV
K39 RSPSDEYKDNLHQVS
K39 RSPSDEYKDNLHQVS
K47 DNLHQVSKKLRGEVG
T58 GEVGLLFTNRTKEEV
T113 LRQLGLPTALKKGVV
K116 LGLPTALKKGVVTLL
K130 LSDYEVCKEGDVLTP
S178-p MDDDLPEsAPEsEGE
S182-p LPEsAPEsEGEsEEE
S186-p APEsEGEsEEEEDDS
- gap
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.