RRP12_YEAST - dbPTM
RRP12_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RRP12_YEAST
UniProt AC Q12754
Protein Name Ribosomal RNA-processing protein 12
Gene Name RRP12
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1228
Subcellular Localization Cytoplasm . Nucleus, nucleolus .
Protein Description In association with GSP1, required for nuclear export of both pre-40S and pre-60S ribosomal subunits. Required for the late maturation of the 18S and 5.8S rRNA of the pre-40S ribosomes and for maturation of the 25S and 5.8S rRNA of the pre-60S ribosomes..
Protein Sequence MDQDKVAFLLELEDKLAKIRSQVNSKLENQKHIAIILTAVEENIAGQATNDVSKNIVNYIISFMSLLDQAVDPSTHEIKDIQLASSSTYLLDLIFHYSPKVLLRSKFSEILTKIAPCITAEKANAPLIRAAIGCLESLLIAQDAQAWNNTYDLNVTPKRGLQGILELSLDVRPKVRKRALDAVHAVLLNPPVAPTAEHVAAVFVADFCDKQLAGILNDLSNLSNKQLKAQKTKEDINASVMRSLRLITSVVSTGQWPSSQIEPLCDVLLGVTKSSEQYLVSASFECFESMFKTMAETTISSGLAENKYLRVLDTIFALKPSNVDTLLTKSWIAVVIKGMSTYATHQPLKALRKIPGVFHIMCTYLASETPEVYQAASQCLISILSESVKDDLLLYTPSVDEKVFKNVDEIISQIAKTFIDFLSIRYSHCSREILKILVAAFNKFRYRSNPHFLKSLKIVDTWRVNEEQFMDLRNEIELVIGASISAMGPEMILAEAPLNLDNPSSERPGRAWLLPLIRDYTKNANLATFQNELAPYIKSFQSKFDKVPEESIQLRVFQTIVDQIWSTLPRFCELPMDLRESFTDEFASELSSLLYSEVELRTTICHALKVLAESNVSYAEESSSHNVLLLQRFPISEAQKNIEYLSTKSTNLLAVLFNVYTQTTPNARSYILETIDQYLKITSKEDLEKTFNNVCGLLKNSMNEESSGNVNKEKKKPQLTATLLDLIICMITYLPVSSYSALFSMFSLTVNSADALIQKRAYRIITKLSELKSGSTAVAQFISDIENVMVDSASSVQTSAKAARLTAIKTIVELLPLDHLDFIVRTVAEVILSTKDVNEKSRETAFDTLICMGRKMNEPNGIIKLFQIPGYDPTTPDQSSSISEFFKIISAGLIGESQHMVSSSITGYACLVFEFKNELDSGILMDIYDTIELYLTSNSREIVKSAIGFTKVCVLGLPEELMRPKVPELLLKLLRWSHEHTGHFKAKVKHIIERLIRRFGYDYIEANFPEEDRRLLTNIRKMRNRNKRKDEEVTTGVSDVAATKGSRFMSAFDEAVYGSDEENDNGSDQEENVAGGKMKNGAKQFIVESGDNPLDLLDSQTLAHISSTRPKKFNKNQNRARFNDDAFNFDSEGKLVVKGQPKPSTNVDDPLSAVTSGINAYLEAVKSGPVRGQRNKLKFRKNGKDSDEFGDDDDGEKDSRLMRGRVNQGNKIGKHNKKGPKFKSRKKL
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
5Ubiquitination---MDQDKVAFLLEL
---CCHHHHHHHHHH		29.8117644757
15UbiquitinationFLLELEDKLAKIRSQ
HHHHHHHHHHHHHHH		40.7517644757
18UbiquitinationELEDKLAKIRSQVNS
HHHHHHHHHHHHHHH		49.4417644757
85PhosphorylationIKDIQLASSSTYLLD
CCCHHHCCCCHHHHH		33.1521551504
97PhosphorylationLLDLIFHYSPKVLLR
HHHHHHHCCHHHHHH		18.8721551504
98PhosphorylationLDLIFHYSPKVLLRS
HHHHHHCCHHHHHHH		15.0721551504
106AcetylationPKVLLRSKFSEILTK
HHHHHHHHHHHHHHH		46.6124489116
122AcetylationAPCITAEKANAPLIR
HHHCCHHHCCHHHHH		44.4724489116
210UbiquitinationFVADFCDKQLAGILN
HHHHHCHHHHHHHHH		48.6817644757
223PhosphorylationLNDLSNLSNKQLKAQ
HHHHHHCCHHHHHHH		46.3530377154
307AcetylationSSGLAENKYLRVLDT
CCCCCCCCHHHHHHH		36.8524489116
319UbiquitinationLDTIFALKPSNVDTL
HHHHHHCCCCCCCHH		42.8617644757
319AcetylationLDTIFALKPSNVDTL
HHHHHHCCCCCCCHH		42.8624489116
329UbiquitinationNVDTLLTKSWIAVVI
CCCHHCCHHHHHHHH		43.7017644757
455PhosphorylationSNPHFLKSLKIVDTW
CCHHHHHHCCEEEEE		36.7219795423
461PhosphorylationKSLKIVDTWRVNEEQ
HHCCEEEEEECCHHH		12.3219795423
522UbiquitinationPLIRDYTKNANLATF
HHHHHHHCCCCHHHH		48.0822817900
538UbiquitinationNELAPYIKSFQSKFD
HHHHHHHHHHHHHHC		39.1017644757
546AcetylationSFQSKFDKVPEESIQ
HHHHHHCCCCHHHHH		63.9224489116
583PhosphorylationMDLRESFTDEFASEL
CCHHHHCHHHHHHHH		43.8523749301
588PhosphorylationSFTDEFASELSSLLY
HCHHHHHHHHHHHHH		44.3723749301
595PhosphorylationSELSSLLYSEVELRT
HHHHHHHHHHHHHHH		14.2123749301
596PhosphorylationELSSLLYSEVELRTT
HHHHHHHHHHHHHHH		34.8323749301
640AcetylationFPISEAQKNIEYLST
CCCCHHHHHHHHHHC		67.9324489116
767AcetylationRAYRIITKLSELKSG
HHHHHHHHHHHHCCC		39.3424489116
773PhosphorylationTKLSELKSGSTAVAQ
HHHHHHCCCCHHHHH		51.0730377154
841PhosphorylationTKDVNEKSRETAFDT
CCCCCHHHHHHHHHH		29.2119823750
844PhosphorylationVNEKSRETAFDTLIC
CCHHHHHHHHHHHHH		31.3619823750
848PhosphorylationSRETAFDTLICMGRK
HHHHHHHHHHHCCCC		16.1519823750
875PhosphorylationIPGYDPTTPDQSSSI
CCCCCCCCCCCCCCH		30.2030377154
880PhosphorylationPTTPDQSSSISEFFK
CCCCCCCCCHHHHHH		26.5130377154
944AcetylationSNSREIVKSAIGFTK
CCCHHHHHHHHCCCC		39.5724489116
1029UbiquitinationMRNRNKRKDEEVTTG
HHHCCCCCCCCCCCC		71.7217644757
1035PhosphorylationRKDEEVTTGVSDVAA
CCCCCCCCCHHHHHC		40.5424961812
1038PhosphorylationEEVTTGVSDVAATKG
CCCCCCHHHHHCCCC		27.9324961812
1043PhosphorylationGVSDVAATKGSRFMS
CHHHHHCCCCHHHHH		26.6324961812
1044UbiquitinationVSDVAATKGSRFMSA
HHHHHCCCCHHHHHH		50.6017644757
1046PhosphorylationDVAATKGSRFMSAFD
HHHCCCCHHHHHHHH		24.7325371407
1050PhosphorylationTKGSRFMSAFDEAVY
CCCHHHHHHHHHHHH		24.0723749301
1057PhosphorylationSAFDEAVYGSDEEND
HHHHHHHHCCCCCCC		20.2628152593
1059PhosphorylationFDEAVYGSDEENDNG
HHHHHHCCCCCCCCC		24.9417330950
1067PhosphorylationDEENDNGSDQEENVA
CCCCCCCCCCCCCCC		42.2317330950
1083AcetylationGKMKNGAKQFIVESG
CCCCCCCCEEEEECC		47.3325381059
1083UbiquitinationGKMKNGAKQFIVESG
CCCCCCCCEEEEECC		47.3317644757
1099PhosphorylationNPLDLLDSQTLAHIS
CCHHHCCHHHHHHHH		25.6521440633
1101PhosphorylationLDLLDSQTLAHISST
HHHCCHHHHHHHHCC		29.8421440633
1106PhosphorylationSQTLAHISSTRPKKF
HHHHHHHHCCCCCCC		18.7830377154
1111UbiquitinationHISSTRPKKFNKNQN
HHHCCCCCCCCCCCC		67.7017644757
1112UbiquitinationISSTRPKKFNKNQNR
HHCCCCCCCCCCCCC		57.7717644757
1115AcetylationTRPKKFNKNQNRARF
CCCCCCCCCCCCCCC		64.1425381059
1131PhosphorylationDDAFNFDSEGKLVVK
CCCCCCCCCCCEEEC		44.0828889911
1152PhosphorylationTNVDDPLSAVTSGIN
CCCCCHHHHHHHHHH		26.5321551504
1156PhosphorylationDPLSAVTSGINAYLE
CHHHHHHHHHHHHHH		30.9521551504
1186PhosphorylationFRKNGKDSDEFGDDD
CCCCCCCCCCCCCCC		42.3925521595
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 RRP12_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RRP12_YEAST !!
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 RRP12_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HSP79_YEASTSSE2physical
16554755
PRP2_YEASTPRP2physical
16554755
YP216_YEASTYPL216Wphysical
16554755
RS17A_YEASTRPS17Aphysical
16429126
RS4A_YEASTRPS4Aphysical
16429126
RS4B_YEASTRPS4Aphysical
16429126
RS8A_YEASTRPS8Aphysical
16429126
RS8B_YEASTRPS8Aphysical
16429126
RS3A2_YEASTRPS1Bphysical
16429126
RL17A_YEASTRPL17Aphysical
16429126
RL28_YEASTRPL28physical
16429126
RL3_YEASTRPL3physical
16429126
RL7B_YEASTRPL7Bphysical
16429126
RL27A_YEASTRPL27Aphysical
16429126
RL5_YEASTRPL5physical
16429126
HSP72_YEASTSSA2physical
19536198
HSP71_YEASTSSA1physical
19536198
SSB1_YEASTSSB1physical
19536198
UTP20_YEASTUTP20physical
21482668
RRP5_YEASTRRP5physical
21482668
YJ9I_YEASTYJR141Wphysical
21482668
NAT10_YEASTKRE33physical
21482668
IMB3_YEASTPSE1physical
21482668
TSR1_YEASTTSR1physical
21482668
YBT1_YEASTYBT1physical
21482668
PRP22_YEASTPRP22physical
21482668
UTP4_YEASTUTP4physical
21482668
RIO1_YEASTRIO1physical
21482668
ENP1_YEASTENP1physical
21482668
NOB1_YEASTNOB1physical
21482668
RIO2_YEASTRIO2physical
21482668
RIR2_YEASTRNR2physical
21482668
SML1_YEASTSML1genetic
21482668
RIR1_YEASTRNR1genetic
21482668
NOP53_YEASTNOP53physical
25877921
LOC1_YEASTLOC1physical
25877921
MAK21_YEASTMAK21physical
25877921
NOP4_YEASTNOP4physical
25877921
NSA2_YEASTNSA2physical
25877921
EBP2_YEASTEBP2physical
25877921
RLP7_YEASTRLP7physical
25877921
HAP3_YEASTHAP3genetic
27708008
SHE1_YEASTSHE1genetic
27708008
ODPB_YEASTPDB1genetic
27708008
MTU1_YEASTSLM3genetic
27708008
RLA1_YEASTRPP1Agenetic
27708008
S2538_YEASTYDL119Cgenetic
27708008
RM01_YEASTMRPL1genetic
27708008
UME6_YEASTUME6genetic
27708008
OMS1_YEASTOMS1genetic
27708008
BCS1_YEASTBCS1genetic
27708008
RLA4_YEASTRPP2Bgenetic
27708008
RV167_YEASTRVS167genetic
27708008
STP1_YEASTSTP1genetic
27708008
YGY5_YEASTYGL235Wgenetic
27708008
CHO2_YEASTCHO2genetic
27708008
MED20_YEASTSRB2genetic
27708008
GIC1_YEASTGIC1genetic
27708008
COX23_YEASTCOX23genetic
27708008
DAL81_YEASTDAL81genetic
27708008
FABG_YEASTOAR1genetic
27708008
CYT2_YEASTCYT2genetic
27708008
HAP4_YEASTHAP4genetic
27708008
COXM1_YEASTCMC1genetic
27708008
RM49_YEASTMRP49genetic
27708008
DCOR_YEASTSPE1genetic
27708008
COX12_YEASTCOX12genetic
27708008
RCF1_YEASTRCF1genetic
27708008
ATP18_YEASTATP18genetic
27708008
MSS1_YEASTMSS1genetic
27708008
COX5A_YEASTCOX5Agenetic
27708008
ODP2_YEASTLAT1genetic
27708008
SWS2_YEASTSWS2genetic
27708008
ATP23_YEASTATP23genetic
27708008
CYC2_YEASTCYC2genetic
27708008
COQ7_YEASTCAT5genetic
27708008
LIPA_YEASTLIP5genetic
27708008
FABD_YEASTMCT1genetic
27708008
MNE1_YEASTMNE1genetic
27708008
HAP5_YEASTHAP5genetic
27708008
RTC6_YEASTRTC6genetic
27708008
MDL2_YEASTMDL2genetic
27708008
QCR2_YEASTQCR2genetic
27708008
NOP4_YEASTNOP4physical
27077951
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RRP12_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1067, AND MASSSPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1186, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1067, AND MASSSPECTROMETRY.

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