TSR1_HUMAN - dbPTM
TSR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TSR1_HUMAN
UniProt AC Q2NL82
Protein Name Pre-rRNA-processing protein TSR1 homolog
Gene Name TSR1
Organism Homo sapiens (Human).
Sequence Length 804
Subcellular Localization Nucleus, nucleolus.
Protein Description Required during maturation of the 40S ribosomal subunit in the nucleolus..
Protein Sequence MAAHRPGPLKQQNKAHKGGRHRGRGSAQRDGKGRLALKTLSKKVRKELSRVDQRHRASQLRKQKKEAVLAEKRQLGGKDGPPHQVLVVPLHSRISLPEAMQLLQDRDTGTVHLNELGNTQNFMLLCPRLKHRWFFTSARPGDLHVVLDMAKVADTILFLLDPLEGWDSTGDYCLSCLFAQGLPTYTLAVQGISGLPLKKQIDTRKKLSKAVEKRFPHDKLLLLDTQQEAGMLLRQLANQKQQHLAFRDRRAYLFAHAVDFVPSEENNLVGTLKISGYVRGQTLNVNRLLHIVGYGDFQMKQIDAPGDPFPLNPRGIKPQKDPDMAMEICATDAVDDMEEGLKVLMKADPGRQESLQAEVIPDPMEGEQTWPTEEELSEAKDFLKESSKVVKKVPKGTSSYQAEWILDGGSQSGGEGDEYEYDDMEHEDFMEEESQDESSEEEEEYETMTIGESVHDDLYDKKVDEEAEAKMLEKYKQERLEEMFPDEVDTPRDVAARIRFQKYRGLKSFRTSPWDPKENLPQDYARIFQFQNFTNTRKSIFKEVEEKEVEGAEVGWYVTLHVSEVPVSVVECFRQGTPLIAFSLLPHEQKMSVLNMVVRRDPGNTEPVKAKEELIFHCGFRRFRASPLFSQHTAADKHKLQRFLTADMALVATVYAPITFPPASVLLFKQKSNGMHSLIATGHLMSVDPDRMVIKRVVLSGHPFKIFTKMAVVRYMFFNREDVLWFKPVELRTKWGRRGHIKEPLGTHGHMKCSFDGKLKSQDTVLMNLYKRVFPKWTYDPYVPEPVPWLKSEISSTVPQGGME
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
32UbiquitinationGSAQRDGKGRLALKT
CCCCCCCCCHHHHHH
45.1823000965
32AcetylationGSAQRDGKGRLALKT
CCCCCCCCCHHHHHH
45.1819829891
38AcetylationGKGRLALKTLSKKVR
CCCHHHHHHHHHHHH
41.6425953088
38UbiquitinationGKGRLALKTLSKKVR
CCCHHHHHHHHHHHH
41.6423000965
39PhosphorylationKGRLALKTLSKKVRK
CCHHHHHHHHHHHHH
36.7920873877
41PhosphorylationRLALKTLSKKVRKEL
HHHHHHHHHHHHHHH
35.3420873877
42UbiquitinationLALKTLSKKVRKELS
HHHHHHHHHHHHHHH
59.4023000965
42MethylationLALKTLSKKVRKELS
HHHHHHHHHHHHHHH
59.40116252813
43UbiquitinationALKTLSKKVRKELSR
HHHHHHHHHHHHHHH
43.8523000965
58PhosphorylationVDQRHRASQLRKQKK
HHHHHHHHHHHHHHH
29.6929449344
62UbiquitinationHRASQLRKQKKEAVL
HHHHHHHHHHHHHHH
75.0624816145
722-HydroxyisobutyrylationKEAVLAEKRQLGGKD
HHHHHHHHHHHCCCC
39.58-
72AcetylationKEAVLAEKRQLGGKD
HHHHHHHHHHHCCCC
39.5823749302
72UbiquitinationKEAVLAEKRQLGGKD
HHHHHHHHHHHCCCC
39.5833845483
95PhosphorylationVPLHSRISLPEAMQL
EECCCCCCHHHHHHH
36.4427174698
108PhosphorylationQLLQDRDTGTVHLNE
HHHHCCCCCEEEHHH
35.3327174698
110PhosphorylationLQDRDTGTVHLNELG
HHCCCCCEEEHHHCC
13.5727174698
119PhosphorylationHLNELGNTQNFMLLC
EHHHCCCCCEEEEEC
24.0827174698
205UbiquitinationKKQIDTRKKLSKAVE
HHHHHHHHHHHHHHH
61.2224816145
219UbiquitinationEKRFPHDKLLLLDTQ
HHHCCCCCEEEEEHH
37.6921963094
231SulfoxidationDTQQEAGMLLRQLAN
EHHHHHHHHHHHHHH
4.0321406390
240UbiquitinationLRQLANQKQQHLAFR
HHHHHHHHHHHHHHH
52.3024816145
277PhosphorylationGTLKISGYVRGQTLN
EEEEEECEECCEEEE
4.72-
279MethylationLKISGYVRGQTLNVN
EEEECEECCEEEEHH
24.02115919073
329GlutathionylationPDMAMEICATDAVDD
CCHHHHHHHHHCCCC
1.8122555962
346SumoylationEGLKVLMKADPGRQE
HHHHHHHHCCCCCHH
45.54-
346SumoylationEGLKVLMKADPGRQE
HHHHHHHHCCCCCHH
45.54-
346UbiquitinationEGLKVLMKADPGRQE
HHHHHHHHCCCCCHH
45.5433845483
354PhosphorylationADPGRQESLQAEVIP
CCCCCHHHCEEEECC
19.9027251275
372PhosphorylationEGEQTWPTEEELSEA
CCCCCCCCHHHHHHH
47.8130576142
377PhosphorylationWPTEEELSEAKDFLK
CCCHHHHHHHHHHHH
38.5024850871
384UbiquitinationSEAKDFLKESSKVVK
HHHHHHHHHCHHHEE
56.3933845483
386PhosphorylationAKDFLKESSKVVKKV
HHHHHHHCHHHEEEC
33.5925159151
387PhosphorylationKDFLKESSKVVKKVP
HHHHHHCHHHEEECC
30.4825627689
412PhosphorylationILDGGSQSGGEGDEY
EECCCCCCCCCCCCC
50.9227362937
447PhosphorylationEEEEEYETMTIGESV
HHHHHHHHCCCCHHH
20.7926074081
449PhosphorylationEEEYETMTIGESVHD
HHHHHHCCCCHHHCH
33.0026074081
453PhosphorylationETMTIGESVHDDLYD
HHCCCCHHHCHHHCC
21.3826074081
459PhosphorylationESVHDDLYDKKVDEE
HHHCHHHCCCCCCHH
32.4826074081
470SumoylationVDEEAEAKMLEKYKQ
CCHHHHHHHHHHHHH
35.21-
470UbiquitinationVDEEAEAKMLEKYKQ
CCHHHHHHHHHHHHH
35.2122817900
470SumoylationVDEEAEAKMLEKYKQ
CCHHHHHHHHHHHHH
35.21-
474UbiquitinationAEAKMLEKYKQERLE
HHHHHHHHHHHHHHH
54.5122817900
475PhosphorylationEAKMLEKYKQERLEE
HHHHHHHHHHHHHHH
14.4522817900
476SumoylationAKMLEKYKQERLEEM
HHHHHHHHHHHHHHH
57.67-
483SulfoxidationKQERLEEMFPDEVDT
HHHHHHHHCCCCCCC
4.2821406390
490PhosphorylationMFPDEVDTPRDVAAR
HCCCCCCCHHHHHHH
25.9621815630
502UbiquitinationAARIRFQKYRGLKSF
HHHHHHHHHCCCCCC
33.91-
502AcetylationAARIRFQKYRGLKSF
HHHHHHHHHCCCCCC
33.917664451
508PhosphorylationQKYRGLKSFRTSPWD
HHHCCCCCCCCCCCC
25.6326270265
511PhosphorylationRGLKSFRTSPWDPKE
CCCCCCCCCCCCCCC
36.8125159151
512PhosphorylationGLKSFRTSPWDPKEN
CCCCCCCCCCCCCCC
21.5325159151
517UbiquitinationRTSPWDPKENLPQDY
CCCCCCCCCCCCHHH
57.6829967540
517AcetylationRTSPWDPKENLPQDY
CCCCCCCCCCCCHHH
57.6826051181
534PhosphorylationIFQFQNFTNTRKSIF
HHHHHCCCHHCHHHH
43.14-
539PhosphorylationNFTNTRKSIFKEVEE
CCCHHCHHHHHHHHH
29.9324719451
542UbiquitinationNTRKSIFKEVEEKEV
HHCHHHHHHHHHCCC
60.2129967540
577PhosphorylationVECFRQGTPLIAFSL
HHHHHCCCCEEEEEC
13.44-
605PhosphorylationVRRDPGNTEPVKAKE
EECCCCCCCCCCCHH
47.8020068231
609UbiquitinationPGNTEPVKAKEELIF
CCCCCCCCCHHHEEH
65.54-
611AcetylationNTEPVKAKEELIFHC
CCCCCCCHHHEEHHC
46.1026051181
626PhosphorylationGFRRFRASPLFSQHT
CCCCCCCCCCCCCCC
20.2023312004
630PhosphorylationFRASPLFSQHTAADK
CCCCCCCCCCCCCCH
28.8323312004
633PhosphorylationSPLFSQHTAADKHKL
CCCCCCCCCCCHHHH
18.8623312004
637UbiquitinationSQHTAADKHKLQRFL
CCCCCCCHHHHHHHH
37.60-
637AcetylationSQHTAADKHKLQRFL
CCCCCCCHHHHHHHH
37.6027452117
705AcetylationVLSGHPFKIFTKMAV
ECCCCCCHHHHHHHH
41.1625953088
705UbiquitinationVLSGHPFKIFTKMAV
ECCCCCCHHHHHHHH
41.1622817900
709UbiquitinationHPFKIFTKMAVVRYM
CCCHHHHHHHHHHHH
17.7021963094
709AcetylationHPFKIFTKMAVVRYM
CCCHHHHHHHHHHHH
17.7025953088
727UbiquitinationREDVLWFKPVELRTK
CCCEEEEEEEEEECC
36.25-
742AcetylationWGRRGHIKEPLGTHG
CCCCCCCCCCCCCCC
47.837379993
752AcetylationLGTHGHMKCSFDGKL
CCCCCCCEEECCCCC
22.517380003
758UbiquitinationMKCSFDGKLKSQDTV
CEEECCCCCCCCCCH
55.3629967540
758AcetylationMKCSFDGKLKSQDTV
CEEECCCCCCCCCCH
55.3625953088
760UbiquitinationCSFDGKLKSQDTVLM
EECCCCCCCCCCHHH
49.9429967540
760SumoylationCSFDGKLKSQDTVLM
EECCCCCCCCCCHHH
49.94-
760SumoylationCSFDGKLKSQDTVLM
EECCCCCCCCCCHHH
49.94-
7712-HydroxyisobutyrylationTVLMNLYKRVFPKWT
CHHHHHHHHHCCCCC
45.30-
776UbiquitinationLYKRVFPKWTYDPYV
HHHHHCCCCCCCCCC
40.48-
776SumoylationLYKRVFPKWTYDPYV
HHHHHCCCCCCCCCC
40.48-
776SumoylationLYKRVFPKWTYDPYV
HHHHHCCCCCCCCCC
40.48-
791SumoylationPEPVPWLKSEISSTV
CCCCCCHHHHHCCCC
42.02-
791SumoylationPEPVPWLKSEISSTV
CCCCCCHHHHHCCCC
42.02-
803SulfoxidationSTVPQGGME------
CCCCCCCCC------
7.6521406390

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
490TPhosphorylationKinaseCDK2P24941
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TSR1_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 TSR1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VPS16_HUMANVPS16physical
22939629
UBAC2_HUMANUBAC2physical
22939629
YES_HUMANYES1physical
22939629
SPB1_HUMANFTSJ3physical
24778252
LN28A_HUMANLIN28Aphysical
24778252
TRBP2_HUMANTARBP2physical
24778252
ENPL_HUMANHSP90B1physical
26344197
LTV1_HUMANLTV1physical
26344197
RM02_HUMANMRPL2physical
26344197
RPAC1_HUMANPOLR1Cphysical
26344197
RS7_HUMANRPS7physical
26344197
UCRI_HUMANUQCRFS1physical
26344197
BYST_HUMANBYSLphysical
28514442
LTV1_HUMANLTV1physical
28514442
RS14_HUMANRPS14physical
28514442
KBTB7_HUMANKBTBD7physical
28514442
IMB1_HUMANKPNB1physical
28514442
RS2_HUMANRPS2physical
28514442
PARN_HUMANPARNphysical
28514442
RRP12_HUMANRRP12physical
28514442
NU153_HUMANNUP153physical
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 TSR1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 TYR-475, AND MASSSPECTROMETRY.

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