PRPK_HUMAN - dbPTM
PRPK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRPK_HUMAN
UniProt AC Q96S44
Protein Name EKC/KEOPS complex subunit TP53RK {ECO:0000305}
Gene Name TP53RK {ECO:0000312|HGNC:HGNC:16197}
Organism Homo sapiens (Human).
Sequence Length 253
Subcellular Localization Cytoplasm . Nucleus .
Protein Description Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. [PubMed: 22912744]
Protein Sequence MAAARATTPADGEEPAPEAEALAAARERSSRFLSGLELVKQGAEARVFRGRFQGRAAVIKHRFPKGYRHPALEARLGRRRTVQEARALLRCRRAGISAPVVFFVDYASNCLYMEEIEGSVTVRDYIQSTMETEKTPQGLSNLAKTIGQVLARMHDEDLIHGDLTTSNMLLKPPLEQLNIVLIDFGLSFISALPEDKGVDLYVLEKAFLSTHPNTETVFEAFLKSYSTSSKKARPVLKKLDEVRLRGRKRSMVG
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
7Phosphorylation-MAAARATTPADGEE
-CCCCCCCCCCCCCC
27.9729255136
8PhosphorylationMAAARATTPADGEEP
CCCCCCCCCCCCCCC
18.5929255136
34PhosphorylationERSSRFLSGLELVKQ
HHHHHHHHHHHHHHC
38.3220068231
40UbiquitinationLSGLELVKQGAEARV
HHHHHHHHCCCCEEE
56.4921906983
121PhosphorylationEEIEGSVTVRDYIQS
EEECCCEEHHHHHHH
16.1224719451
129PhosphorylationVRDYIQSTMETEKTP
HHHHHHHHCCCCCCC
11.5819060867
132PhosphorylationYIQSTMETEKTPQGL
HHHHHCCCCCCCCHH
31.7719060867
134UbiquitinationQSTMETEKTPQGLSN
HHHCCCCCCCCHHHH
73.2921906983
135PhosphorylationSTMETEKTPQGLSNL
HHCCCCCCCCHHHHH
18.0225159151
140PhosphorylationEKTPQGLSNLAKTIG
CCCCCHHHHHHHHHH
36.3022817900
144UbiquitinationQGLSNLAKTIGQVLA
CHHHHHHHHHHHHHH
43.7921890473
201PhosphorylationEDKGVDLYVLEKAFL
CCCCCCEEEEEHHHH
9.8722817900
214PhosphorylationFLSTHPNTETVFEAF
HHHCCCCHHHHHHHH
37.1728985074
226PhosphorylationEAFLKSYSTSSKKAR
HHHHHHCCCCCCCHH
28.9828985074
238UbiquitinationKARPVLKKLDEVRLR
CHHHHHHHHHHHHHC
57.9424816145
250PhosphorylationRLRGRKRSMVG----
HHCCCCCCCCC----
22.3617712528

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
250SPhosphorylationKinaseAKT1P31749
PSP
250SPhosphorylationKinasePBKQ96KB5
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRPK_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 PRPK_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TPRKB_HUMANTPRKBphysical
12659830
P53_HUMANTP53physical
12659830
TPRKB_HUMANTPRKBphysical
22912744
OSGEP_HUMANOSGEPphysical
22912744
LAGE3_HUMANLAGE3physical
22912744
GON7_HUMANC14orf142physical
22912744
TPRKB_HUMANTPRKBphysical
22939629
AASD1_HUMANAARSD1physical
22863883
KBP_HUMANKIAA1279physical
22863883
TRMB_HUMANMETTL1physical
22863883
NIF3L_HUMANNIF3L1physical
22863883
NSUN2_HUMANNSUN2physical
22863883
PANK4_HUMANPANK4physical
22863883
KAPCB_HUMANPRKACBphysical
22863883
RAGP1_HUMANRANGAP1physical
22863883
SAE1_HUMANSAE1physical
22863883
SH3G1_HUMANSH3GL1physical
22863883
THG1_HUMANTHG1Lphysical
22863883
TM1L1_HUMANTOM1L1physical
22863883
TPD54_HUMANTPD52L2physical
22863883
UFM1_HUMANUFM1physical
22863883
SPSY_HUMANSMSphysical
23455922
LAGE3_HUMANLAGE3physical
23455922
NUP43_HUMANNUP43physical
23455922
INADL_HUMANINADLphysical
23455922
GON7_HUMANC14orf142physical
23455922
OSGEP_HUMANOSGEPphysical
23455922
TPRKB_HUMANTPRKBphysical
23455922
TPRKB_HUMANTPRKBphysical
26186194
GON7_HUMANC14orf142physical
26186194
OSGEP_HUMANOSGEPphysical
26186194
NUP43_HUMANNUP43physical
26186194
ARP19_HUMANARPP19physical
26344197
PRPS1_HUMANPRPS1physical
26344197
WDR4_HUMANWDR4physical
26344197
GON7_HUMANC14orf142physical
28514442
OSGEP_HUMANOSGEPphysical
28514442
TPRKB_HUMANTPRKBphysical
28514442
NUP43_HUMANNUP43physical
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 PRPK_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7; THR-8; SER-34;THR-129; THR-132; THR-135; SER-140 AND TYR-201, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-135, AND MASSSPECTROMETRY.

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