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 | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
32 | Ubiquitination | GSAQRDGKGRLALKT CCCCCCCCCHHHHHH | 45.18 | 23000965 | |
32 | Acetylation | GSAQRDGKGRLALKT CCCCCCCCCHHHHHH | 45.18 | 19829891 | |
38 | Acetylation | GKGRLALKTLSKKVR CCCHHHHHHHHHHHH | 41.64 | 25953088 | |
38 | Ubiquitination | GKGRLALKTLSKKVR CCCHHHHHHHHHHHH | 41.64 | 23000965 | |
39 | Phosphorylation | KGRLALKTLSKKVRK CCHHHHHHHHHHHHH | 36.79 | 20873877 | |
41 | Phosphorylation | RLALKTLSKKVRKEL HHHHHHHHHHHHHHH | 35.34 | 20873877 | |
42 | Ubiquitination | LALKTLSKKVRKELS HHHHHHHHHHHHHHH | 59.40 | 23000965 | |
42 | Methylation | LALKTLSKKVRKELS HHHHHHHHHHHHHHH | 59.40 | 116252813 | |
43 | Ubiquitination | ALKTLSKKVRKELSR HHHHHHHHHHHHHHH | 43.85 | 23000965 | |
58 | Phosphorylation | VDQRHRASQLRKQKK HHHHHHHHHHHHHHH | 29.69 | 29449344 | |
62 | Ubiquitination | HRASQLRKQKKEAVL HHHHHHHHHHHHHHH | 75.06 | 24816145 | |
72 | 2-Hydroxyisobutyrylation | KEAVLAEKRQLGGKD HHHHHHHHHHHCCCC | 39.58 | - | |
72 | Acetylation | KEAVLAEKRQLGGKD HHHHHHHHHHHCCCC | 39.58 | 23749302 | |
72 | Ubiquitination | KEAVLAEKRQLGGKD HHHHHHHHHHHCCCC | 39.58 | 33845483 | |
95 | Phosphorylation | VPLHSRISLPEAMQL EECCCCCCHHHHHHH | 36.44 | 27174698 | |
108 | Phosphorylation | QLLQDRDTGTVHLNE HHHHCCCCCEEEHHH | 35.33 | 27174698 | |
110 | Phosphorylation | LQDRDTGTVHLNELG HHCCCCCEEEHHHCC | 13.57 | 27174698 | |
119 | Phosphorylation | HLNELGNTQNFMLLC EHHHCCCCCEEEEEC | 24.08 | 27174698 | |
205 | Ubiquitination | KKQIDTRKKLSKAVE HHHHHHHHHHHHHHH | 61.22 | 24816145 | |
219 | Ubiquitination | EKRFPHDKLLLLDTQ HHHCCCCCEEEEEHH | 37.69 | 21963094 | |
231 | Sulfoxidation | DTQQEAGMLLRQLAN EHHHHHHHHHHHHHH | 4.03 | 21406390 | |
240 | Ubiquitination | LRQLANQKQQHLAFR HHHHHHHHHHHHHHH | 52.30 | 24816145 | |
277 | Phosphorylation | GTLKISGYVRGQTLN EEEEEECEECCEEEE | 4.72 | - | |
279 | Methylation | LKISGYVRGQTLNVN EEEECEECCEEEEHH | 24.02 | 115919073 | |
329 | Glutathionylation | PDMAMEICATDAVDD CCHHHHHHHHHCCCC | 1.81 | 22555962 | |
346 | Sumoylation | EGLKVLMKADPGRQE HHHHHHHHCCCCCHH | 45.54 | - | |
346 | Sumoylation | EGLKVLMKADPGRQE HHHHHHHHCCCCCHH | 45.54 | - | |
346 | Ubiquitination | EGLKVLMKADPGRQE HHHHHHHHCCCCCHH | 45.54 | 33845483 | |
354 | Phosphorylation | ADPGRQESLQAEVIP CCCCCHHHCEEEECC | 19.90 | 27251275 | |
372 | Phosphorylation | EGEQTWPTEEELSEA CCCCCCCCHHHHHHH | 47.81 | 30576142 | |
377 | Phosphorylation | WPTEEELSEAKDFLK CCCHHHHHHHHHHHH | 38.50 | 24850871 | |
384 | Ubiquitination | SEAKDFLKESSKVVK HHHHHHHHHCHHHEE | 56.39 | 33845483 | |
386 | Phosphorylation | AKDFLKESSKVVKKV HHHHHHHCHHHEEEC | 33.59 | 25159151 | |
387 | Phosphorylation | KDFLKESSKVVKKVP HHHHHHCHHHEEECC | 30.48 | 25627689 | |
412 | Phosphorylation | ILDGGSQSGGEGDEY EECCCCCCCCCCCCC | 50.92 | 27362937 | |
447 | Phosphorylation | EEEEEYETMTIGESV HHHHHHHHCCCCHHH | 20.79 | 26074081 | |
449 | Phosphorylation | EEEYETMTIGESVHD HHHHHHCCCCHHHCH | 33.00 | 26074081 | |
453 | Phosphorylation | ETMTIGESVHDDLYD HHCCCCHHHCHHHCC | 21.38 | 26074081 | |
459 | Phosphorylation | ESVHDDLYDKKVDEE HHHCHHHCCCCCCHH | 32.48 | 26074081 | |
470 | Sumoylation | VDEEAEAKMLEKYKQ CCHHHHHHHHHHHHH | 35.21 | - | |
470 | Ubiquitination | VDEEAEAKMLEKYKQ CCHHHHHHHHHHHHH | 35.21 | 22817900 | |
470 | Sumoylation | VDEEAEAKMLEKYKQ CCHHHHHHHHHHHHH | 35.21 | - | |
474 | Ubiquitination | AEAKMLEKYKQERLE HHHHHHHHHHHHHHH | 54.51 | 22817900 | |
475 | Phosphorylation | EAKMLEKYKQERLEE HHHHHHHHHHHHHHH | 14.45 | 22817900 | |
476 | Sumoylation | AKMLEKYKQERLEEM HHHHHHHHHHHHHHH | 57.67 | - | |
483 | Sulfoxidation | KQERLEEMFPDEVDT HHHHHHHHCCCCCCC | 4.28 | 21406390 | |
490 | Phosphorylation | MFPDEVDTPRDVAAR HCCCCCCCHHHHHHH | 25.96 | 21815630 | |
502 | Ubiquitination | AARIRFQKYRGLKSF HHHHHHHHHCCCCCC | 33.91 | - | |
502 | Acetylation | AARIRFQKYRGLKSF HHHHHHHHHCCCCCC | 33.91 | 7664451 | |
508 | Phosphorylation | QKYRGLKSFRTSPWD HHHCCCCCCCCCCCC | 25.63 | 26270265 | |
511 | Phosphorylation | RGLKSFRTSPWDPKE CCCCCCCCCCCCCCC | 36.81 | 25159151 | |
512 | Phosphorylation | GLKSFRTSPWDPKEN CCCCCCCCCCCCCCC | 21.53 | 25159151 | |
517 | Ubiquitination | RTSPWDPKENLPQDY CCCCCCCCCCCCHHH | 57.68 | 29967540 | |
517 | Acetylation | RTSPWDPKENLPQDY CCCCCCCCCCCCHHH | 57.68 | 26051181 | |
534 | Phosphorylation | IFQFQNFTNTRKSIF HHHHHCCCHHCHHHH | 43.14 | - | |
539 | Phosphorylation | NFTNTRKSIFKEVEE CCCHHCHHHHHHHHH | 29.93 | 24719451 | |
542 | Ubiquitination | NTRKSIFKEVEEKEV HHCHHHHHHHHHCCC | 60.21 | 29967540 | |
577 | Phosphorylation | VECFRQGTPLIAFSL HHHHHCCCCEEEEEC | 13.44 | - | |
605 | Phosphorylation | VRRDPGNTEPVKAKE EECCCCCCCCCCCHH | 47.80 | 20068231 | |
609 | Ubiquitination | PGNTEPVKAKEELIF CCCCCCCCCHHHEEH | 65.54 | - | |
611 | Acetylation | NTEPVKAKEELIFHC CCCCCCCHHHEEHHC | 46.10 | 26051181 | |
626 | Phosphorylation | GFRRFRASPLFSQHT CCCCCCCCCCCCCCC | 20.20 | 23312004 | |
630 | Phosphorylation | FRASPLFSQHTAADK CCCCCCCCCCCCCCH | 28.83 | 23312004 | |
633 | Phosphorylation | SPLFSQHTAADKHKL CCCCCCCCCCCHHHH | 18.86 | 23312004 | |
637 | Ubiquitination | SQHTAADKHKLQRFL CCCCCCCHHHHHHHH | 37.60 | - | |
637 | Acetylation | SQHTAADKHKLQRFL CCCCCCCHHHHHHHH | 37.60 | 27452117 | |
705 | Acetylation | VLSGHPFKIFTKMAV ECCCCCCHHHHHHHH | 41.16 | 25953088 | |
705 | Ubiquitination | VLSGHPFKIFTKMAV ECCCCCCHHHHHHHH | 41.16 | 22817900 | |
709 | Ubiquitination | HPFKIFTKMAVVRYM CCCHHHHHHHHHHHH | 17.70 | 21963094 | |
709 | Acetylation | HPFKIFTKMAVVRYM CCCHHHHHHHHHHHH | 17.70 | 25953088 | |
727 | Ubiquitination | REDVLWFKPVELRTK CCCEEEEEEEEEECC | 36.25 | - | |
742 | Acetylation | WGRRGHIKEPLGTHG CCCCCCCCCCCCCCC | 47.83 | 7379993 | |
752 | Acetylation | LGTHGHMKCSFDGKL CCCCCCCEEECCCCC | 22.51 | 7380003 | |
758 | Ubiquitination | MKCSFDGKLKSQDTV CEEECCCCCCCCCCH | 55.36 | 29967540 | |
758 | Acetylation | MKCSFDGKLKSQDTV CEEECCCCCCCCCCH | 55.36 | 25953088 | |
760 | Ubiquitination | CSFDGKLKSQDTVLM EECCCCCCCCCCHHH | 49.94 | 29967540 | |
760 | Sumoylation | CSFDGKLKSQDTVLM EECCCCCCCCCCHHH | 49.94 | - | |
760 | Sumoylation | CSFDGKLKSQDTVLM EECCCCCCCCCCHHH | 49.94 | - | |
771 | 2-Hydroxyisobutyrylation | TVLMNLYKRVFPKWT CHHHHHHHHHCCCCC | 45.30 | - | |
776 | Ubiquitination | LYKRVFPKWTYDPYV HHHHHCCCCCCCCCC | 40.48 | - | |
776 | Sumoylation | LYKRVFPKWTYDPYV HHHHHCCCCCCCCCC | 40.48 | - | |
776 | Sumoylation | LYKRVFPKWTYDPYV HHHHHCCCCCCCCCC | 40.48 | - | |
791 | Sumoylation | PEPVPWLKSEISSTV CCCCCCHHHHHCCCC | 42.02 | - | |
791 | Sumoylation | PEPVPWLKSEISSTV CCCCCCHHHHHCCCC | 42.02 | - | |
803 | Sulfoxidation | STVPQGGME------ CCCCCCCCC------ | 7.65 | 21406390 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
490 | T | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TSR1_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
VPS16_HUMAN | VPS16 | physical | 22939629 | |
UBAC2_HUMAN | UBAC2 | physical | 22939629 | |
YES_HUMAN | YES1 | physical | 22939629 | |
SPB1_HUMAN | FTSJ3 | physical | 24778252 | |
LN28A_HUMAN | LIN28A | physical | 24778252 | |
TRBP2_HUMAN | TARBP2 | physical | 24778252 | |
ENPL_HUMAN | HSP90B1 | physical | 26344197 | |
LTV1_HUMAN | LTV1 | physical | 26344197 | |
RM02_HUMAN | MRPL2 | physical | 26344197 | |
RPAC1_HUMAN | POLR1C | physical | 26344197 | |
RS7_HUMAN | RPS7 | physical | 26344197 | |
UCRI_HUMAN | UQCRFS1 | physical | 26344197 | |
BYST_HUMAN | BYSL | physical | 28514442 | |
LTV1_HUMAN | LTV1 | physical | 28514442 | |
RS14_HUMAN | RPS14 | physical | 28514442 | |
KBTB7_HUMAN | KBTBD7 | physical | 28514442 | |
IMB1_HUMAN | KPNB1 | physical | 28514442 | |
RS2_HUMAN | RPS2 | physical | 28514442 | |
PARN_HUMAN | PARN | physical | 28514442 | |
RRP12_HUMAN | RRP12 | physical | 28514442 | |
NU153_HUMAN | NUP153 | physical | 28514442 |
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. |
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Phosphorylation | |
Reference | PubMed |
"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. |