SNUT2_HUMAN - dbPTM
SNUT2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNUT2_HUMAN
UniProt AC Q53GS9
Protein Name U4/U6.U5 tri-snRNP-associated protein 2
Gene Name USP39
Organism Homo sapiens (Human).
Sequence Length 565
Subcellular Localization Nucleus .
Protein Description Plays a role in pre-mRNA splicing as a component of the U4/U6-U5 tri-snRNP, one of the building blocks of the spliceosome. Regulates AURKB mRNA levels, and thereby plays a role in cytokinesis and in the spindle checkpoint. Does not have ubiquitin-specific peptidase activity, but could be a competitor of ubiquitin C-terminal hydrolases (UCHs)..
Protein Sequence MSGRSKRESRGSTRGKRESESRGSSGRVKRERDREREPEAASSRGSPVRVKREFEPASAREAPASVVPFVRVKREREVDEDSEPEREVRAKNGRVDSEDRRSRHCPYLDTINRSVLDFDFEKLCSISLSHINAYACLVCGKYFQGRGLKSHAYIHSVQFSHHVFLNLHTLKFYCLPDNYEIIDSSLEDITYVLKPTFTKQQIANLDKQAKLSRAYDGTTYLPGIVGLNNIKANDYANAVLQALSNVPPLRNYFLEEDNYKNIKRPPGDIMFLLVQRFGELMRKLWNPRNFKAHVSPHEMLQAVVLCSKKTFQITKQGDGVDFLSWFLNALHSALGGTKKKKKTIVTDVFQGSMRIFTKKLPHPDLPAEEKEQLLHNDEYQETMVESTFMYLTLDLPTAPLYKDEKEQLIIPQVPLFNILAKFNGITEKEYKTYKENFLKRFQLTKLPPYLIFCIKRFTKNNFFVEKNPTIVNFPITNVDLREYLSEEVQAVHKNTTYDLIANIVHDGKPSEGSYRIHVLHHGTGKWYELQDLQVTDILPQMITLSEAYIQIWKRRDNDETNQQGA
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
3 (in isoform 2)Phosphorylation-36.2630206219
7 (in isoform 2)Phosphorylation-48.6630206219
11 (in isoform 2)Phosphorylation-42.5230206219
42PhosphorylationEREPEAASSRGSPVR
HCCHHHHHCCCCCCE		27.8423401153
43PhosphorylationREPEAASSRGSPVRV
CCHHHHHCCCCCCEE		35.6123401153
46PhosphorylationEAASSRGSPVRVKRE
HHHHCCCCCCEEEEE		21.0720201521
51SumoylationRGSPVRVKREFEPAS
CCCCCEEEEECCCCC		35.3328112733
58PhosphorylationKREFEPASAREAPAS
EEECCCCCCCCCCCC		38.2826074081
65PhosphorylationSAREAPASVVPFVRV
CCCCCCCCCCCEEEE		23.6920068231
73SumoylationVVPFVRVKREREVDE
CCCEEEEEEEECCCC		37.67-
82PhosphorylationEREVDEDSEPEREVR
EECCCCCCCCHHHHH		53.6729255136
97PhosphorylationAKNGRVDSEDRRSRH
HHCCCCCCHHHHHCC		38.2420068231
102PhosphorylationVDSEDRRSRHCPYLD
CCCHHHHHCCCCCHH		27.5428555341
207UbiquitinationQQIANLDKQAKLSRA
HHHCCHHHHHHHHHC		56.15-
207AcetylationQQIANLDKQAKLSRA
HHHCCHHHHHHHHHC		56.1525953088
210UbiquitinationANLDKQAKLSRAYDG
CCHHHHHHHHHCCCC		44.49-
259PhosphorylationYFLEEDNYKNIKRPP
HCCCCCCCCCCCCCC		20.10-
260UbiquitinationFLEEDNYKNIKRPPG
CCCCCCCCCCCCCCC		59.45-
283UbiquitinationRFGELMRKLWNPRNF
HHHHHHHHHHCCCCC		43.84-
291MethylationLWNPRNFKAHVSPHE
HHCCCCCCCCCCHHH		40.92115978891
308UbiquitinationQAVVLCSKKTFQITK
HHHHHHCCCEEEEEE		55.63-
325AcetylationDGVDFLSWFLNALHS
CCHHHHHHHHHHHHH		12.1419608861
343PhosphorylationGTKKKKKTIVTDVFQ
CCCCCCCEEEEECCC		29.5620068231
346PhosphorylationKKKKTIVTDVFQGSM
CCCCEEEEECCCCCE		23.6920068231
352PhosphorylationVTDVFQGSMRIFTKK
EEECCCCCEEHHCCC		8.2920068231
353SulfoxidationTDVFQGSMRIFTKKL
EECCCCCEEHHCCCC		4.9421406390
357PhosphorylationQGSMRIFTKKLPHPD
CCCEEHHCCCCCCCC		25.5420068231
426PhosphorylationLAKFNGITEKEYKTY
HHHHCCCCHHHHHHH		42.2628509920
428AcetylationKFNGITEKEYKTYKE
HHCCCCHHHHHHHHH		58.6623749302
428UbiquitinationKFNGITEKEYKTYKE
HHCCCCHHHHHHHHH		58.6619608861
430PhosphorylationNGITEKEYKTYKENF
CCCCHHHHHHHHHHH		21.5028509920
432PhosphorylationITEKEYKTYKENFLK
CCHHHHHHHHHHHHH		38.6328509920
432O-linked_GlycosylationITEKEYKTYKENFLK
CCHHHHHHHHHHHHH		38.6330379171
433PhosphorylationTEKEYKTYKENFLKR
CHHHHHHHHHHHHHH		16.5028509920
4342-HydroxyisobutyrylationEKEYKTYKENFLKRF
HHHHHHHHHHHHHHH		51.95-
434AcetylationEKEYKTYKENFLKRF
HHHHHHHHHHHHHHH		51.9526822725
434UbiquitinationEKEYKTYKENFLKRF
HHHHHHHHHHHHHHH		51.95-
439AcetylationTYKENFLKRFQLTKL
HHHHHHHHHHCCCCC		47.2125953088
445UbiquitinationLKRFQLTKLPPYLIF
HHHHCCCCCCCCHHE		68.53-
455AcetylationPYLIFCIKRFTKNNF
CCHHEEEEECCCCCC		42.5126051181
459AcetylationFCIKRFTKNNFFVEK
EEEEECCCCCCEECC		47.3725953088
466AcetylationKNNFFVEKNPTIVNF
CCCCEECCCCEEEEC		64.0326051181
466UbiquitinationKNNFFVEKNPTIVNF
CCCCEECCCCEEEEC		64.03-
481MethylationPITNVDLREYLSEEV
CCCCCCHHHHHHHHH		26.50115919629
508UbiquitinationANIVHDGKPSEGSYR
EEEEECCCCCCCEEE		51.97-
510PhosphorylationIVHDGKPSEGSYRIH
EEECCCCCCCEEEEE		59.0624300666
513PhosphorylationDGKPSEGSYRIHVLH
CCCCCCCEEEEEEEE		13.7424300666
514PhosphorylationGKPSEGSYRIHVLHH
CCCCCCEEEEEEEEC		25.1724300666
523PhosphorylationIHVLHHGTGKWYELQ
EEEEECCCCCEEEEC		31.0924300666
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 SNUT2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNUT2_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 SNUT2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PA2G4_HUMANPA2G4physical
19615732
P53_HUMANTP53physical
19615732
PRP4B_HUMANPRPF4Bphysical
19615732
SNUT1_HUMANSART1physical
19615732
PRP4_HUMANPRPF4physical
19615732
PRPF3_HUMANPRPF3physical
19615732
U5S1_HUMANEFTUD2physical
19615732
ZRAB2_HUMANZRANB2physical
19615732
SNR40_HUMANSNRNP40physical
19615732
DDX23_HUMANDDX23physical
19615732
PRP16_HUMANDHX38physical
19615732
CD2B2_HUMANCD2BP2physical
19615732
PRP8_HUMANPRPF8physical
19615732
TXN4A_HUMANTXNL4Aphysical
19615732
SNR27_HUMANSNRNP27physical
19615732
U520_HUMANSNRNP200physical
19615732
RRP8_HUMANRRP8physical
19615732
PRP6_HUMANPRPF6physical
19615732
PRP31_HUMANPRPF31physical
19615732
LSM8_HUMANLSM8physical
19615732
GAR1_HUMANGAR1physical
19615732
MRRP1_HUMANTRMT10Cphysical
19615732
MRM3_HUMANRNMTL1physical
19615732
COPRS_HUMANCOPRSphysical
19615732
DDX24_HUMANDDX24physical
19615732
NOC3L_HUMANNOC3Lphysical
19615732
TSR2_HUMANTSR2physical
19615732
RL22L_HUMANRPL22L1physical
19615732
A4_HUMANAPPphysical
21832049
SON_HUMANSONphysical
22939629
TF3C1_HUMANGTF3C1physical
22939629
TPBG_HUMANTPBGphysical
22939629
TRI55_HUMANTRIM55physical
22939629
ZCH18_HUMANZC3H18physical
22939629
VTNC_HUMANVTNphysical
22939629
SP16H_HUMANSUPT16Hphysical
22939629
TRAF6_HUMANTRAF6physical
23105109
TRI25_HUMANTRIM25physical
23105109
TRI26_HUMANTRIM26physical
23105109
TRI39_HUMANTRIM39physical
23105109
TRIM8_HUMANTRIM8physical
23105109
TRIM5_HUMANTRIM5physical
23105109
RED1_HUMANADARB1physical
26344197
KC1E_HUMANCSNK1Ephysical
26344197
LEG9_HUMANLGALS9physical
26344197
NSUN2_HUMANNSUN2physical
26344197
PCNA_HUMANPCNAphysical
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 SNUT2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-428, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND MASSSPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-46 AND SER-82,AND MASS SPECTROMETRY.
"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-46 AND SER-82, AND MASSSPECTROMETRY.

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