MRT4_HUMAN - dbPTM
MRT4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MRT4_HUMAN
UniProt AC Q9UKD2
Protein Name mRNA turnover protein 4 homolog {ECO:0000250|UniProtKB:P33201}
Gene Name MRTO4
Organism Homo sapiens (Human).
Sequence Length 239
Subcellular Localization Nucleus, nucleolus . Cytoplasm . Shuttles between the nucleus and the cytoplasm.
Protein Description Component of the ribosome assembly machinery. Nuclear paralog of the ribosomal protein P0, it binds pre-60S subunits at an early stage of assembly in the nucleolus, and is replaced by P0 in cytoplasmic pre-60S subunits and mature 80S ribosomes..
Protein Sequence MPKSKRDKKVSLTKTAKKGLELKQNLIEELRKCVDTYKYLFIFSVANMRNSKLKDIRNAWKHSRMFFGKNKVMMVALGRSPSDEYKDNLHQVSKRLRGEVGLLFTNRTKEEVNEWFTKYTEMDYARAGNKAAFTVSLDPGPLEQFPHSMEPQLRQLGLPTALKRGVVTLLSDYEVCKEGDVLTPEQARVLKLFGYEMAEFKVTIKYMWDSQSGRFQQMGDDLPESASESTEESDSEDDD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
5Acetylation---MPKSKRDKKVSL
---CCCCHHCCCCCC		71.4019824413
8AcetylationMPKSKRDKKVSLTKT
CCCCHHCCCCCCCHH		60.1419824421
9AcetylationPKSKRDKKVSLTKTA
CCCHHCCCCCCCHHH		41.1519824429
11PhosphorylationSKRDKKVSLTKTAKK
CHHCCCCCCCHHHHH		38.9226425664
13PhosphorylationRDKKVSLTKTAKKGL
HCCCCCCCHHHHHHH		20.8826270265
23AcetylationAKKGLELKQNLIEEL
HHHHHHHHHHHHHHH		27.9726822725
23UbiquitinationAKKGLELKQNLIEEL
HHHHHHHHHHHHHHH		27.97-
232-HydroxyisobutyrylationAKKGLELKQNLIEEL
HHHHHHHHHHHHHHH		27.97-
31MethylationQNLIEELRKCVDTYK
HHHHHHHHHHHHHHH		33.34115483843
32UbiquitinationNLIEELRKCVDTYKY
HHHHHHHHHHHHHHH		51.76-
39PhosphorylationKCVDTYKYLFIFSVA
HHHHHHHHHHHHHHH		9.0920068231
44PhosphorylationYKYLFIFSVANMRNS
HHHHHHHHHHHCCCC		18.5920068231
51PhosphorylationSVANMRNSKLKDIRN
HHHHCCCCCHHHHHH		29.0620068231
69AcetylationHSRMFFGKNKVMMVA
HHHHHCCCCCEEEEE		48.7325953088
71UbiquitinationRMFFGKNKVMMVALG
HHHCCCCCEEEEECC		34.69-
80PhosphorylationMMVALGRSPSDEYKD
EEEECCCCCCHHHHH		27.2723401153
82PhosphorylationVALGRSPSDEYKDNL
EECCCCCCHHHHHHH		44.3030266825
85PhosphorylationGRSPSDEYKDNLHQV
CCCCCHHHHHHHHHH		28.7428152594
86AcetylationRSPSDEYKDNLHQVS
CCCCHHHHHHHHHHH		37.7926051181
86UbiquitinationRSPSDEYKDNLHQVS
CCCCHHHHHHHHHHH		37.7921906983
93PhosphorylationKDNLHQVSKRLRGEV
HHHHHHHHHHHHHCC		12.8928152594
942-HydroxyisobutyrylationDNLHQVSKRLRGEVG
HHHHHHHHHHHHCCE		57.50-
94AcetylationDNLHQVSKRLRGEVG
HHHHHHHHHHHHCCE		57.5025953088
94UbiquitinationDNLHQVSKRLRGEVG
HHHHHHHHHHHHCCE		57.5021906983
105PhosphorylationGEVGLLFTNRTKEEV
HCCEEEEECCCHHHH		24.62-
109AcetylationLLFTNRTKEEVNEWF
EEEECCCHHHHHHHH		48.9526051181
109SumoylationLLFTNRTKEEVNEWF
EEEECCCHHHHHHHH		48.95-
109UbiquitinationLLFTNRTKEEVNEWF
EEEECCCHHHHHHHH		48.95-
109SumoylationLLFTNRTKEEVNEWF
EEEECCCHHHHHHHH		48.95-
118AcetylationEVNEWFTKYTEMDYA
HHHHHHHHHHHHHHH		40.4726051181
126MethylationYTEMDYARAGNKAAF
HHHHHHHHCCCCEEE		36.48115483847
130UbiquitinationDYARAGNKAAFTVSL
HHHHCCCCEEEEEEE		39.93-
160PhosphorylationLRQLGLPTALKRGVV
HHHCCCCHHHHHCCE		50.0620068231
163AcetylationLGLPTALKRGVVTLL
CCCCHHHHHCCEECC		44.6425953088
163UbiquitinationLGLPTALKRGVVTLL
CCCCHHHHHCCEECC		44.64-
1632-HydroxyisobutyrylationLGLPTALKRGVVTLL
CCCCHHHHHCCEECC		44.64-
168PhosphorylationALKRGVVTLLSDYEV
HHHHCCEECCCCHHH		21.4120860994
171PhosphorylationRGVVTLLSDYEVCKE
HCCEECCCCHHHHCC		41.0620860994
177UbiquitinationLSDYEVCKEGDVLTP
CCCHHHHCCCCCCCH		70.66-
177AcetylationLSDYEVCKEGDVLTP
CCCHHHHCCCCCCCH		70.6626051181
183PhosphorylationCKEGDVLTPEQARVL
HCCCCCCCHHHHHHH		25.3221815630
191UbiquitinationPEQARVLKLFGYEMA
HHHHHHHHHHCCEEE		38.62-
205AcetylationAEFKVTIKYMWDSQS
EEEEEEEEEEECCCC		21.4926051181
225PhosphorylationMGDDLPESASESTEE
CCCCCCCCCCCCCCC		34.8420363803
227PhosphorylationDDLPESASESTEESD
CCCCCCCCCCCCCCC		41.1620363803
229PhosphorylationLPESASESTEESDSE
CCCCCCCCCCCCCCC		38.3320363803
230PhosphorylationPESASESTEESDSED
CCCCCCCCCCCCCCC		39.4620363803
233PhosphorylationASESTEESDSEDDD-
CCCCCCCCCCCCCC-		39.9620363803
235PhosphorylationESTEESDSEDDD---
CCCCCCCCCCCC---		52.8020363803
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
229SPhosphorylationKinaseCSNK2A1P68400
GPS
233SPhosphorylationKinaseCSNK2A1P68400
GPS
235SPhosphorylationKinaseCSNK2A1P68400
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MRT4_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of MRT4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XPO5_HUMANXPO5physical
21048991
XPO1_HUMANXPO1physical
21048991
NMD3_HUMANNMD3physical
21048991
RL23A_HUMANRPL23Aphysical
21048991
RLP24_HUMANRSL24D1physical
21048991
SPB1_HUMANFTSJ3physical
22939629
RL31_HUMANRPL31physical
22939629
VAPA_HUMANVAPAphysical
22939629
BRX1_HUMANBRIX1physical
26344197
DDX24_HUMANDDX24physical
26344197
U5S1_HUMANEFTUD2physical
26344197
IF2B_HUMANEIF2S2physical
26344197
FBRL_HUMANFBLphysical
26344197
SPB1_HUMANFTSJ3physical
26344197
NOG2_HUMANGNL2physical
26344197
NOG1_HUMANGTPBP4physical
26344197
PUM3_HUMANKIAA0020physical
26344197
RM01_HUMANMRPL1physical
26344197
NH2L1_HUMANNHP2L1physical
26344197
MK67I_HUMANNIFKphysical
26344197
NOC2L_HUMANNOC2Lphysical
26344197
NOL10_HUMANNOL10physical
26344197
NOP2_HUMANNOP2physical
26344197
NSA2_HUMANNSA2physical
26344197
PESC_HUMANPES1physical
26344197
RL10A_HUMANRPL10Aphysical
26344197
RL27_HUMANRPL27physical
26344197
RL5_HUMANRPL5physical
26344197
RRP15_HUMANRRP15physical
26344197
SDA1_HUMANSDAD1physical
26344197
SPT5H_HUMANSUPT5Hphysical
26344197
WDR12_HUMANWDR12physical
26344197
H12_HUMANHIST1H1Cphysical
28514442
NOG1_HUMANGTPBP4physical
28514442
NSA2_HUMANNSA2physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MRT4_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory