RRS1_HUMAN - dbPTM
RRS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RRS1_HUMAN
UniProt AC Q15050
Protein Name Ribosome biogenesis regulatory protein homolog
Gene Name RRS1
Organism Homo sapiens (Human).
Sequence Length 365
Subcellular Localization Nucleus, nucleolus .
Protein Description Involved in ribosomal large subunit assembly. May regulate the localization of the 5S RNP/5S ribonucleoprotein particle to the nucleolus..
Protein Sequence MEGQSVEELLAKAEQDEAEKLQRITVHKELELQFDLGNLLASDRNPPTGLRCAGPTPEAELQALARDNTQLLINQLWQLPTERVEEAIVARLPEPTTRLPREKPLPRPRPLTRWQQFARLKGIRPKKKTNLVWDEVSGQWRRRWGYQRARDDTKEWLIEVPGNADPLEDQFAKRIQAKKERVAKNELNRLRNLARAHKMQLPSAAGLHPTGHQSKEELGRAMQVAKVSTASVGRFQERLPKEKVPRGSGKKRKFQPLFGDFAAEKKNQLELLRVMNSKKPQLDVTRATNKQMREEDQEEAAKRRKMSQKGKRKGGRQGPGGKRKGGPPSQGGKRKGGLGGKMNSGPPGLGGKRKGGQRPGGKRRK
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
1Acetylation-------MEGQSVEE
-------CCCCCHHH
13.5722223895
5Phosphorylation---MEGQSVEELLAK
---CCCCCHHHHHHH
42.2125159151
20UbiquitinationAEQDEAEKLQRITVH
HHHHHHHHHHHHHHC
57.9033845483
20AcetylationAEQDEAEKLQRITVH
HHHHHHHHHHHHHHC
57.9025953088
52GlutathionylationNPPTGLRCAGPTPEA
CCCCCCCCCCCCCHH
6.5422555962
56PhosphorylationGLRCAGPTPEAELQA
CCCCCCCCCHHHHHH
32.6125850435
129PhosphorylationGIRPKKKTNLVWDEV
CCCCCCCCCCCEECC
42.5425690035
137PhosphorylationNLVWDEVSGQWRRRW
CCCEECCCCHHHHHH
24.1825690035
146PhosphorylationQWRRRWGYQRARDDT
HHHHHHCCHHCCCCC
6.46-
153PhosphorylationYQRARDDTKEWLIEV
CHHCCCCCCCEEEEC
34.84-
154SumoylationQRARDDTKEWLIEVP
HHCCCCCCCEEEECC
54.6228112733
173AcetylationPLEDQFAKRIQAKKE
HHHHHHHHHHHHHHH
51.8526051181
173UbiquitinationPLEDQFAKRIQAKKE
HHHHHHHHHHHHHHH
51.8532015554
184SumoylationAKKERVAKNELNRLR
HHHHHHHHHHHHHHH
48.36-
184SumoylationAKKERVAKNELNRLR
HHHHHHHHHHHHHHH
48.36-
184UbiquitinationAKKERVAKNELNRLR
HHHHHHHHHHHHHHH
48.3624816145
203PhosphorylationAHKMQLPSAAGLHPT
HHHCCCCCCCCCCCC
39.0728555341
215UbiquitinationHPTGHQSKEELGRAM
CCCCCCCHHHHHHHH
48.9533845483
215AcetylationHPTGHQSKEELGRAM
CCCCCCCHHHHHHHH
48.9526051181
226SumoylationGRAMQVAKVSTASVG
HHHHHHHHHHHHHHH
37.5528112733
228PhosphorylationAMQVAKVSTASVGRF
HHHHHHHHHHHHHHH
19.9728348404
229PhosphorylationMQVAKVSTASVGRFQ
HHHHHHHHHHHHHHH
26.4128348404
231PhosphorylationVAKVSTASVGRFQER
HHHHHHHHHHHHHHH
25.7825159151
265UbiquitinationFGDFAAEKKNQLELL
HCHHHHHHHHHHHHH
52.9132015554
2652-HydroxyisobutyrylationFGDFAAEKKNQLELL
HCHHHHHHHHHHHHH
52.91-
265AcetylationFGDFAAEKKNQLELL
HCHHHHHHHHHHHHH
52.9126051181
266SumoylationGDFAAEKKNQLELLR
CHHHHHHHHHHHHHH
41.2428112733
266UbiquitinationGDFAAEKKNQLELLR
CHHHHHHHHHHHHHH
41.2433845483
273CitrullinationKNQLELLRVMNSKKP
HHHHHHHHHHCCCCC
37.96-
273CitrullinationKNQLELLRVMNSKKP
HHHHHHHHHHCCCCC
37.96-
279UbiquitinationLRVMNSKKPQLDVTR
HHHHCCCCCCHHHHH
37.5033845483
290AcetylationDVTRATNKQMREEDQ
HHHHHHHHHHHHHHH
40.9126051181
302UbiquitinationEDQEEAAKRRKMSQK
HHHHHHHHHHHHHHH
60.8424816145
302AcetylationEDQEEAAKRRKMSQK
HHHHHHHHHHHHHHH
60.8426051181
307PhosphorylationAAKRRKMSQKGKRKG
HHHHHHHHHHHHCCC
31.60-
313AcetylationMSQKGKRKGGRQGPG
HHHHHHCCCCCCCCC
70.027483953
322AcetylationGRQGPGGKRKGGPPS
CCCCCCCCCCCCCCC
57.777483963
324UbiquitinationQGPGGKRKGGPPSQG
CCCCCCCCCCCCCCC
72.24-
329PhosphorylationKRKGGPPSQGGKRKG
CCCCCCCCCCCCCCC
44.59-
333AcetylationGPPSQGGKRKGGLGG
CCCCCCCCCCCCCCC
58.7326051181
335AcetylationPSQGGKRKGGLGGKM
CCCCCCCCCCCCCCC
61.9025953088
341UbiquitinationRKGGLGGKMNSGPPG
CCCCCCCCCCCCCCC
32.8624816145
341AcetylationRKGGLGGKMNSGPPG
CCCCCCCCCCCCCCC
32.8625953088
344PhosphorylationGLGGKMNSGPPGLGG
CCCCCCCCCCCCCCC
49.5325159151
352AcetylationGPPGLGGKRKGGQRP
CCCCCCCCCCCCCCC
49.4925953088

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

Oops, there are no upstream regulatory protein records of RRS1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RRS1_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 RRS1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
U2AF1_HUMANU2AF1physical
22939629
RS7_HUMANRPS7physical
22939629
U2AF2_HUMANU2AF2physical
22939629
TPR_HUMANTPRphysical
22939629
RS4X_HUMANRPS4Xphysical
22939629
RS6_HUMANRPS6physical
22939629
EBP2_HUMANEBNA1BP2physical
26344197
MK67I_HUMANNIFKphysical
26344197
NMD3_HUMANNMD3physical
26344197
NOC2L_HUMANNOC2Lphysical
26344197
NOP2_HUMANNOP2physical
26344197
RPF2_HUMANRPF2physical
26344197
RL11_HUMANRPL11physical
26344197
RL37A_HUMANRPL37Aphysical
26344197
RRP15_HUMANRRP15physical
26344197
H2A2C_HUMANHIST2H2ACphysical
28514442
RS3_HUMANRPS3physical
28514442
ABC3C_HUMANAPOBEC3Cphysical
28514442
PURB_HUMANPURBphysical
28514442
U2AF2_HUMANU2AF2physical
28514442
RS2_HUMANRPS2physical
28514442
RL37A_HUMANRPL37Aphysical
28514442
RS18_HUMANRPS18physical
28514442
YBOX1_HUMANYBX1physical
28514442
LIN41_HUMANTRIM71physical
28514442
RS16_HUMANRPS16physical
28514442
NSA2_HUMANNSA2physical
28514442
RL3_HUMANRPL3physical
28514442
RT31_HUMANMRPS31physical
28514442
RLA1_HUMANRPLP1physical
28514442
RLA2_HUMANRPLP2physical
28514442
RS19_HUMANRPS19physical
28514442
NUCL_HUMANNCLphysical
28514442
RL18_HUMANRPL18physical
28514442
CDK12_HUMANCDK12physical
28514442
RT35_HUMANMRPS35physical
28514442
RS5_HUMANRPS5physical
28514442
RS15_HUMANRPS15physical
28514442
RPF2_HUMANRPF2physical
28514442
NPM_HUMANNPM1physical
28514442
RL18A_HUMANRPL18Aphysical
28514442
MKRN1_HUMANMKRN1physical
28514442
RS10_HUMANRPS10physical
28514442
RS25_HUMANRPS25physical
28514442
RS28_HUMANRPS28physical
28514442
RS9_HUMANRPS9physical
28514442
RS3A_HUMANRPS3Aphysical
28514442
RT09_HUMANMRPS9physical
28514442
RS24_HUMANRPS24physical
28514442
RL8_HUMANRPL8physical
28514442
RL7A_HUMANRPL7Aphysical
28514442
RL4_HUMANRPL4physical
28514442
RL6_HUMANRPL6physical
28514442
RBMS1_HUMANRBMS1physical
28514442
RS20_HUMANRPS20physical
28514442
RM52_HUMANMRPL52physical
28514442
ZCRB1_HUMANZCRB1physical
28514442
DHX30_HUMANDHX30physical
28514442
RS14_HUMANRPS14physical
28514442
RL34_HUMANRPL34physical
28514442
STAU1_HUMANSTAU1physical
28514442
SREK1_HUMANSREK1physical
28514442
RL35A_HUMANRPL35Aphysical
28514442
RBM4_HUMANRBM4physical
28514442
MK67I_HUMANNIFKphysical
28514442
SF3B1_HUMANSF3B1physical
28514442
DHX57_HUMANDHX57physical
28514442
RT29_HUMANDAP3physical
28514442
BRX1_HUMANBRIX1physical
28514442
GLE1_HUMANGLE1physical
28514442
RL23A_HUMANRPL23Aphysical
28514442
SRSF5_HUMANSRSF5physical
28514442
NOG1_HUMANGTPBP4physical
28514442
RLA0_HUMANRPLP0physical
28514442
SF3B4_HUMANSF3B4physical
28514442
RL31_HUMANRPL31physical
28514442
RS13_HUMANRPS13physical
28514442
RBM34_HUMANRBM34physical
28514442
RL10A_HUMANRPL10Aphysical
28514442
C1QBP_HUMANC1QBPphysical
28514442
RL13A_HUMANRPL13Aphysical
28514442
RSSA_HUMANRPSAphysical
28514442
RL14_HUMANRPL14physical
28514442
BMS1_HUMANBMS1physical
28514442
DKC1_HUMANDKC1physical
28514442
RT16_HUMANMRPS16physical
28514442
RS17_HUMANRPS17physical
28514442
ZCCHV_HUMANZC3HAV1physical
28514442
CH033_HUMANC8orf33physical
28514442
NOP56_HUMANNOP56physical
28514442
PUM3_HUMANKIAA0020physical
28514442
RL35_HUMANRPL35physical
28514442
NOC4L_HUMANNOC4Lphysical
28514442
SPB1_HUMANFTSJ3physical
28514442
IF2B1_HUMANIGF2BP1physical
28514442
RS8_HUMANRPS8physical
28514442
RL32_HUMANRPL32physical
28514442
RS12_HUMANRPS12physical
28514442
YBOX3_HUMANYBX3physical
28514442
DDX21_HUMANDDX21physical
28514442
RM32_HUMANMRPL32physical
28514442
PTCD3_HUMANPTCD3physical
28514442
RL29_HUMANRPL29physical
28514442
RL27_HUMANRPL27physical
28514442
RBM19_HUMANRBM19physical
28514442
RL17_HUMANRPL17physical
28514442
MPP10_HUMANMPHOSPH10physical
28514442
PURA_HUMANPURAphysical
28514442
RL9_HUMANRPL9physical
28514442
NOP53_HUMANGLTSCR2physical
28514442
RL13_HUMANRPL13physical
28514442
GLYR1_HUMANGLYR1physical
28514442
KRR1_HUMANKRR1physical
28514442
ZN512_HUMANZNF512physical
28514442
MOV10_HUMANMOV10physical
28514442
KNOP1_HUMANKNOP1physical
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 RRS1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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-344, AND MASSSPECTROMETRY.

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