KRR1_HUMAN - dbPTM
KRR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KRR1_HUMAN
UniProt AC Q13601
Protein Name KRR1 small subunit processome component homolog
Gene Name KRR1
Organism Homo sapiens (Human).
Sequence Length 381
Subcellular Localization Cytoplasm . Nucleus . Nucleus, nucleolus . Translocates from cytoplasm to nucleus after exposure to HIV-1 virus or HIV-1 protein VPR or induction by hydrocortisone and dexamethasone in the absence of HIV-1 protein VPR (Ref.6).
Protein Description Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (By similarity)..
Protein Sequence MASPSLERPEKGAGKSEFRNQKPKPENQDESELLTVPDGWKEPAFSKEDNPRGLLEESSFATLFPKYREAYLKECWPLVQKALNEHHVNATLDLIEGSMTVCTTKKTFDPYIIIRARDLIKLLARSVSFEQAVRILQDDVACDIIKIGSLVRNKERFVKRRQRLIGPKGSTLKALELLTNCYIMVQGNTVSAIGPFSGLKEVRKVVLDTMKNIHPIYNIKSLMIKRELAKDSELRSQSWERFLPQFKHKNVNKRKEPKKKTVKKEYTPFPPPQPESQIDKELASGEYFLKANQKKRQKMEAIKAKQAEAISKRQEERNKAFIPPKEKPIVKPKEASTETKIDVASIKEKVKKAKNKKLGALTAEEIALKMEADEKKKKKKK
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
2Acetylation------MASPSLERP
------CCCCCCCCC		30.1021406692
3Phosphorylation-----MASPSLERPE
-----CCCCCCCCCC		17.4529255136
5Phosphorylation---MASPSLERPEKG
---CCCCCCCCCCCC		40.1330266825
11AcetylationPSLERPEKGAGKSEF
CCCCCCCCCCCHHHH		57.6625953088
15UbiquitinationRPEKGAGKSEFRNQK
CCCCCCCHHHHHCCC		46.4024816145
15AcetylationRPEKGAGKSEFRNQK
CCCCCCCHHHHHCCC		46.4026051181
16PhosphorylationPEKGAGKSEFRNQKP
CCCCCCHHHHHCCCC		40.8426074081
22UbiquitinationKSEFRNQKPKPENQD
HHHHHCCCCCCCCCC		59.5722817900
22AcetylationKSEFRNQKPKPENQD
HHHHHCCCCCCCCCC		59.5726051181
24SumoylationEFRNQKPKPENQDES
HHHCCCCCCCCCCHH		72.5028112733
24SumoylationEFRNQKPKPENQDES
HHHCCCCCCCCCCHH		72.50-
24UbiquitinationEFRNQKPKPENQDES
HHHCCCCCCCCCCHH		72.5021906983
31PhosphorylationKPENQDESELLTVPD
CCCCCCHHHCEECCC		41.6625159151
41AcetylationLTVPDGWKEPAFSKE
EECCCCCCCCCCCCC		60.3926051181
41UbiquitinationLTVPDGWKEPAFSKE
EECCCCCCCCCCCCC		60.3921906983
47AcetylationWKEPAFSKEDNPRGL
CCCCCCCCCCCCCHH		63.7326051181
47UbiquitinationWKEPAFSKEDNPRGL
CCCCCCCCCCCCCHH		63.7327667366
66UbiquitinationSFATLFPKYREAYLK
CHHHHCHHHHHHHHH		49.9929967540
73AcetylationKYREAYLKECWPLVQ
HHHHHHHHHHHHHHH		37.8426051181
105AcetylationSMTVCTTKKTFDPYI
CEEEECCCCCCCCEE		31.5026051181
105UbiquitinationSMTVCTTKKTFDPYI
CEEEECCCCCCCCEE		31.5023000965
106UbiquitinationMTVCTTKKTFDPYII
EEEECCCCCCCCEEE		52.9423000965
106AcetylationMTVCTTKKTFDPYII
EEEECCCCCCCCEEE		52.9426051181
106MalonylationMTVCTTKKTFDPYII
EEEECCCCCCCCEEE		52.9426320211
106UbiquitinationMTVCTTKKTFDPYII
EEEECCCCCCCCEEE		52.9421890473
106UbiquitinationMTVCTTKKTFDPYII
EEEECCCCCCCCEEE		52.9421890473
106UbiquitinationMTVCTTKKTFDPYII
EEEECCCCCCCCEEE		52.9421890473
111PhosphorylationTKKTFDPYIIIRARD
CCCCCCCEEEEEHHH		13.4428152594
121AcetylationIRARDLIKLLARSVS
EEHHHHHHHHHHCCC		44.7526051181
1212-HydroxyisobutyrylationIRARDLIKLLARSVS
EEHHHHHHHHHHCCC		44.75-
121UbiquitinationIRARDLIKLLARSVS
EEHHHHHHHHHHCCC		44.7521890473
121UbiquitinationIRARDLIKLLARSVS
EEHHHHHHHHHHCCC		44.7521890473
121UbiquitinationIRARDLIKLLARSVS
EEHHHHHHHHHHCCC		44.7521890473
121UbiquitinationIRARDLIKLLARSVS
EEHHHHHHHHHHCCC		44.7521906983
142GlutathionylationILQDDVACDIIKIGS
HHHCCHHCCEEHHCH		3.7622555962
146UbiquitinationDVACDIIKIGSLVRN
CHHCCEEHHCHHHHC		41.15-
149PhosphorylationCDIIKIGSLVRNKER
CCEEHHCHHHHCHHH		27.4523186163
168UbiquitinationRQRLIGPKGSTLKAL
HHHHHCCCCHHHHHH		61.3521890473
168UbiquitinationRQRLIGPKGSTLKAL
HHHHHCCCCHHHHHH		61.3521906983
168UbiquitinationRQRLIGPKGSTLKAL
HHHHHCCCCHHHHHH		61.3521890473
173UbiquitinationGPKGSTLKALELLTN
CCCCHHHHHHHHHHC		51.5222817900
211UbiquitinationKVVLDTMKNIHPIYN
HHHHHHHCCCCCCCC		55.6429967540
217PhosphorylationMKNIHPIYNIKSLMI
HCCCCCCCCHHHHHH		18.4520071362
220UbiquitinationIHPIYNIKSLMIKRE
CCCCCCHHHHHHHHH		33.6221906983
220AcetylationIHPIYNIKSLMIKRE
CCCCCCHHHHHHHHH		33.6226051181
220UbiquitinationIHPIYNIKSLMIKRE
CCCCCCHHHHHHHHH		33.6221890473
220UbiquitinationIHPIYNIKSLMIKRE
CCCCCCHHHHHHHHH		33.6221890473
225SumoylationNIKSLMIKRELAKDS
CHHHHHHHHHHHCCH		26.34-
225UbiquitinationNIKSLMIKRELAKDS
CHHHHHHHHHHHCCH		26.3422817900
230UbiquitinationMIKRELAKDSELRSQ
HHHHHHHCCHHHHHH		74.5324816145
235MethylationLAKDSELRSQSWERF
HHCCHHHHHHHHHHH		28.71115481433
238PhosphorylationDSELRSQSWERFLPQ
CHHHHHHHHHHHHHH		31.9525627689
247UbiquitinationERFLPQFKHKNVNKR
HHHHHHHHCCCCCCC		48.7133845483
247MethylationERFLPQFKHKNVNKR
HHHHHHHHCCCCCCC		48.71115972215
264UbiquitinationPKKKTVKKEYTPFPP
CCCCCCCCCCCCCCC		52.1729967540
266PhosphorylationKKTVKKEYTPFPPPQ
CCCCCCCCCCCCCCC		28.7022199227
267PhosphorylationKTVKKEYTPFPPPQP
CCCCCCCCCCCCCCC		21.3921815630
276PhosphorylationFPPPQPESQIDKELA
CCCCCCHHHHCHHHH		38.84-
280UbiquitinationQPESQIDKELASGEY
CCHHHHCHHHHHCHH		57.1422817900
284PhosphorylationQIDKELASGEYFLKA
HHCHHHHHCHHHHHH		44.7921815630
287PhosphorylationKELASGEYFLKANQK
HHHHHCHHHHHHHHH		20.10-
290SumoylationASGEYFLKANQKKRQ
HHCHHHHHHHHHHHH		35.08-
290UbiquitinationASGEYFLKANQKKRQ
HHCHHHHHHHHHHHH		35.0827667366
290SumoylationASGEYFLKANQKKRQ
HHCHHHHHHHHHHHH		35.08-
305UbiquitinationKMEAIKAKQAEAISK
HHHHHHHHHHHHHHH		45.0727667366
311PhosphorylationAKQAEAISKRQEERN
HHHHHHHHHHHHHHH		28.9120860994
312AcetylationKQAEAISKRQEERNK
HHHHHHHHHHHHHHH		52.5725953088
327UbiquitinationAFIPPKEKPIVKPKE
CCCCCCCCCCCCCCC		46.2827667366
336PhosphorylationIVKPKEASTETKIDV
CCCCCCCCCCCCCCH		28.0622817900
337PhosphorylationVKPKEASTETKIDVA
CCCCCCCCCCCCCHH		55.5122817900
339PhosphorylationPKEASTETKIDVASI
CCCCCCCCCCCHHHH		33.1322817900
340UbiquitinationKEASTETKIDVASIK
CCCCCCCCCCHHHHH		30.58-
340SumoylationKEASTETKIDVASIK
CCCCCCCCCCHHHHH		30.5828112733
340SumoylationKEASTETKIDVASIK
CCCCCCCCCCHHHHH		30.58-
345PhosphorylationETKIDVASIKEKVKK
CCCCCHHHHHHHHHH		33.7621815630
347UbiquitinationKIDVASIKEKVKKAK
CCCHHHHHHHHHHHH		49.3333845483
3572-HydroxyisobutyrylationVKKAKNKKLGALTAE
HHHHHCCCCCCCCHH		62.64-
357UbiquitinationVKKAKNKKLGALTAE
HHHHHCCCCCCCCHH		62.6429967540
369SumoylationTAEEIALKMEADEKK
CHHHHHHHHHHHHHH		26.1828112733
369SumoylationTAEEIALKMEADEKK
CHHHHHHHHHHHHHH		26.18-
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
-KUbiquitinationE3 ubiquitin ligaseBIRC3Q13489
PMID:18570872
-KUbiquitinationE3 ubiquitin ligaseTANKQ92844
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseTRAF2Q12933
PMID:15175328
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KRR1_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 KRR1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AATF_HUMANAATFphysical
26344197
ABT1_HUMANABT1physical
26344197
DDX18_HUMANDDX18physical
26344197
DDX27_HUMANDDX27physical
26344197
DDX52_HUMANDDX52physical
26344197
DDX56_HUMANDDX56physical
26344197
DKC1_HUMANDKC1physical
26344197
EBP2_HUMANEBNA1BP2physical
26344197
GNL1_HUMANGNL1physical
26344197
GNL3_HUMANGNL3physical
26344197
PUM3_HUMANKIAA0020physical
26344197
MRT4_HUMANMRTO4physical
26344197
MK67I_HUMANNIFKphysical
26344197
NOP2_HUMANNOP2physical
26344197
RBM34_HUMANRBM34physical
26344197
RPF2_HUMANRPF2physical
26344197
RL11_HUMANRPL11physical
26344197
RS18_HUMANRPS18physical
26344197
RS3_HUMANRPS3physical
26344197
RS3A_HUMANRPS3Aphysical
26344197
RS4X_HUMANRPS4Xphysical
26344197
RS7_HUMANRPS7physical
26344197
TBL3_HUMANTBL3physical
26344197
UTP15_HUMANUTP15physical
26344197
WDR36_HUMANWDR36physical
26344197
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 KRR1_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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-3 AND SER-5, AND MASS SPECTROMETRY.
Phosphorylation
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 ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-3 AND SER-5, AND MASS SPECTROMETRY.
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336; THR-337 ANDTHR-339, AND MASS SPECTROMETRY.
"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-3 AND SER-5, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, AND MASSSPECTROMETRY.

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