RSMN_HUMAN - dbPTM
RSMN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RSMN_HUMAN
UniProt AC P63162
Protein Name Small nuclear ribonucleoprotein-associated protein N
Gene Name SNRPN
Organism Homo sapiens (Human).
Sequence Length 240
Subcellular Localization Nucleus.
Protein Description May be involved in tissue-specific alternative RNA processing events..
Protein Sequence MTVGKSSKMLQHIDYRMRCILQDGRIFIGTFKAFDKHMNLILCDCDEFRKIKPKNAKQPEREEKRVLGLVLLRGENLVSMTVEGPPPKDTGIARVPLAGAAGGPGVGRAAGRGVPAGVPIPQAPAGLAGPVRGVGGPSQQVMTPQGRGTVAAAAVAATASIAGAPTQYPPGRGTPPPPVGRATPPPGIMAPPPGMRPPMGPPIGLPPARGTPIGMPPPGMRPPPPGIRGPPPPGMRPPRP
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
2Phosphorylation------MTVGKSSKM
------CCCCCHHHH
37.6620068231
5Ubiquitination---MTVGKSSKMLQH
---CCCCCHHHHHHH
47.4123000965
6Phosphorylation--MTVGKSSKMLQHI
--CCCCCHHHHHHHH
29.3020068231
7Phosphorylation-MTVGKSSKMLQHID
-CCCCCHHHHHHHHC
26.1029116813
8AcetylationMTVGKSSKMLQHIDY
CCCCCHHHHHHHHCH
51.2022634303
8UbiquitinationMTVGKSSKMLQHIDY
CCCCCHHHHHHHHCH
51.2023000965
9MethylationTVGKSSKMLQHIDYR
CCCCHHHHHHHHCHH
4.74-
9UbiquitinationTVGKSSKMLQHIDYR
CCCCHHHHHHHHCHH
4.74-
12AcetylationKSSKMLQHIDYRMRC
CHHHHHHHHCHHHHH
15.78-
12MethylationKSSKMLQHIDYRMRC
CHHHHHHHHCHHHHH
15.78-
12UbiquitinationKSSKMLQHIDYRMRC
CHHHHHHHHCHHHHH
15.7821890473
12UbiquitinationKSSKMLQHIDYRMRC
CHHHHHHHHCHHHHH
15.7829901268
15PhosphorylationKMLQHIDYRMRCILQ
HHHHHHCHHHHHEEC
13.0029116813
16MethylationMLQHIDYRMRCILQD
HHHHHCHHHHHEECC
11.43-
19 (in isoform 2)Phosphorylation-2.3820068231
24UbiquitinationMRCILQDGRIFIGTF
HHHEECCCCEEEEEC
16.1833845483
26UbiquitinationCILQDGRIFIGTFKA
HEECCCCEEEEECHH
3.45-
28UbiquitinationLQDGRIFIGTFKAFD
ECCCCEEEEECHHHH
4.7732015554
30PhosphorylationDGRIFIGTFKAFDKH
CCCEEEEECHHHHHC
19.6923186163
32UbiquitinationRIFIGTFKAFDKHMN
CEEEEECHHHHHCCC
48.2423000965
32PhosphorylationRIFIGTFKAFDKHMN
CEEEEECHHHHHCCC
48.24-
32AcetylationRIFIGTFKAFDKHMN
CEEEEECHHHHHCCC
48.2488801
36AcetylationGTFKAFDKHMNLILC
EECHHHHHCCCEEEE
38.00-
36UbiquitinationGTFKAFDKHMNLILC
EECHHHHHCCCEEEE
38.0023000965
36UbiquitinationGTFKAFDKHMNLILC
EECHHHHHCCCEEEE
38.0021890473
36AcetylationGTFKAFDKHMNLILC
EECHHHHHCCCEEEE
38.00133787
40UbiquitinationAFDKHMNLILCDCDE
HHHHCCCEEEECHHH
2.16-
40AcetylationAFDKHMNLILCDCDE
HHHHCCCEEEECHHH
2.16-
40UbiquitinationAFDKHMNLILCDCDE
HHHHCCCEEEECHHH
2.1632015554
54UbiquitinationEFRKIKPKNAKQPER
HHHCCCCCCCCCCHH
65.6224816145
64UbiquitinationKQPEREEKRVLGLVL
CCCHHHHHHHHEEEE
42.9524816145
80SulfoxidationRGENLVSMTVEGPPP
CCCCEEEEEEECCCC
3.6628183972
80UbiquitinationRGENLVSMTVEGPPP
CCCCEEEEEEECCCC
3.6633845483
88UbiquitinationTVEGPPPKDTGIARV
EEECCCCCCCCEEEE
73.9423000965
92UbiquitinationPPPKDTGIARVPLAG
CCCCCCCEEEEECCC
2.1021890473
92UbiquitinationPPPKDTGIARVPLAG
CCCCCCCEEEEECCC
2.1033845483
108MethylationAGGPGVGRAAGRGVP
CCCCCHHHCCCCCCC
20.8924390879
108DimethylationAGGPGVGRAAGRGVP
CCCCCHHHCCCCCCC
20.89-
112MethylationGVGRAAGRGVPAGVP
CHHHCCCCCCCCCCC
37.9080702323
112DimethylationGVGRAAGRGVPAGVP
CHHHCCCCCCCCCCC
37.90-
147MethylationQVMTPQGRGTVAAAA
CCCCCCCCHHHHHHH
32.1518600991
147DimethylationQVMTPQGRGTVAAAA
CCCCCCCCHHHHHHH
32.15-
149PhosphorylationMTPQGRGTVAAAAVA
CCCCCCHHHHHHHHH
12.9524260401
158PhosphorylationAAAAVAATASIAGAP
HHHHHHHHHHHCCCC
15.9424260401
160PhosphorylationAAVAATASIAGAPTQ
HHHHHHHHHCCCCCC
14.4924260401
166PhosphorylationASIAGAPTQYPPGRG
HHHCCCCCCCCCCCC
39.9524260401
168PhosphorylationIAGAPTQYPPGRGTP
HCCCCCCCCCCCCCC
17.5524260401
172MethylationPTQYPPGRGTPPPPV
CCCCCCCCCCCCCCC
52.1424129315
181DimethylationTPPPPVGRATPPPGI
CCCCCCCCCCCCCCC
35.21-
181MethylationTPPPPVGRATPPPGI
CCCCCCCCCCCCCCC
35.2182797065
183PhosphorylationPPPVGRATPPPGIMA
CCCCCCCCCCCCCCC
34.6620860994
236DimethylationGPPPPGMRPPRP---
CCCCCCCCCCCC---
43.94-
236MethylationGPPPPGMRPPRP---
CCCCCCCCCCCC---
43.94-
239MethylationPPGMRPPRP------
CCCCCCCCC------
52.85-

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 RSMN_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RSMN_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 RSMN_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LRIF1_HUMANLRIF1physical
16169070
SH3G3_HUMANSH3GL3physical
16169070
P53_HUMANTP53physical
16169070
RENT1_HUMANUPF1physical
18362360
DSRAD_HUMANADARphysical
18362360
RFOX1_HUMANRBFOX1physical
24722188
CTBP1_HUMANCTBP1physical
24722188
RU2A_HUMANSNRPA1physical
28514442
SART3_HUMANSART3physical
28514442
CMTR2_HUMANCMTR2physical
28514442
RBM40_HUMANRNPC3physical
28514442
U2AFM_HUMANZRSR2physical
28514442
ZMAT5_HUMANZMAT5physical
28514442
FARP1_HUMANFARP1physical
28514442
U1SBP_HUMANSNRNP35physical
28514442
PDCD7_HUMANPDCD7physical
28514442
DPP8_HUMANDPP8physical
28514442
SNR48_HUMANSNRNP48physical
28514442
TGS1_HUMANTGS1physical
28514442
ICLN_HUMANCLNS1Aphysical
28514442
RU2B_HUMANSNRPB2physical
28514442
STPAP_HUMANTUT1physical
28514442
LSM11_HUMANLSM11physical
28514442
SMD1_HUMANSNRPD1physical
28514442
NADAP_HUMANSLC4A1APphysical
28514442
SMD2_HUMANSNRPD2physical
28514442
PRPF3_HUMANPRPF3physical
28514442
MEPCE_HUMANMEPCEphysical
28514442
ANM5_HUMANPRMT5physical
28514442
RU17_HUMANSNRNP70physical
28514442
SNR27_HUMANSNRNP27physical
28514442
SNRPA_HUMANSNRPAphysical
28514442
TOE1_HUMANTOE1physical
28514442
SF3A2_HUMANSF3A2physical
28514442
SYF2_HUMANSYF2physical
28514442
PKRI1_HUMANPRKRIP1physical
28514442
PAXB1_HUMANPAXBP1physical
28514442
CSTF1_HUMANCSTF1physical
28514442
EAPP_HUMANEAPPphysical
28514442
WBP4_HUMANWBP4physical
28514442
TFP11_HUMANTFIP11physical
28514442
GEMI8_HUMANGEMIN8physical
28514442
SKAP2_HUMANSKAP2physical
28514442
GEMI5_HUMANGEMIN5physical
28514442
RIOK1_HUMANRIOK1physical
28514442
PRP4_HUMANPRPF4physical
28514442
SF3B1_HUMANSF3B1physical
28514442
HTSF1_HUMANHTATSF1physical
28514442
RU1C_HUMANSNRPCphysical
28514442
DDX23_HUMANDDX23physical
28514442
SF3A3_HUMANSF3A3physical
28514442
U520_HUMANSNRNP200physical
28514442
SYF1_HUMANXAB2physical
28514442
MEP50_HUMANWDR77physical
28514442
SMD3_HUMANSNRPD3physical
28514442
AQR_HUMANAQRphysical
28514442
SPN1_HUMANSNUPNphysical
28514442
SF3A1_HUMANSF3A1physical
28514442
COPRS_HUMANCOPRSphysical
28514442
SF3B2_HUMANSF3B2physical
28514442
PRP6_HUMANPRPF6physical
28514442
PRP8_HUMANPRPF8physical
28514442
CRNL1_HUMANCRNKL1physical
28514442
DHX35_HUMANDHX35physical
28514442
TXN4A_HUMANTXNL4Aphysical
28514442
TSSC4_HUMANTSSC4physical
28514442
AKA7A_HUMANAKAP7physical
28514442
AKA7G_HUMANAKAP7physical
28514442
CRTAP_HUMANCRTAPphysical
28514442
CCD12_HUMANCCDC12physical
28514442
DGC14_HUMANDGCR14physical
28514442
NOL7_HUMANNOL7physical
28514442
PRP17_HUMANCDC40physical
28514442
SF3B4_HUMANSF3B4physical
28514442
LSM6_HUMANLSM6physical
28514442
C19L2_HUMANCWF19L2physical
28514442
LSM8_HUMANLSM8physical
28514442
GPT11_HUMANGPATCH11physical
28514442
PRP31_HUMANPRPF31physical
28514442
GEMI2_HUMANGEMIN2physical
28514442
E41L3_HUMANEPB41L3physical
28514442
LSM4_HUMANLSM4physical
28514442
LSM2_HUMANLSM2physical
28514442
CD2B2_HUMANCD2BP2physical
28514442
WDR83_HUMANWDR83physical
28514442
GPTC1_HUMANGPATCH1physical
28514442
BUD31_HUMANBUD31physical
28514442
RBM42_HUMANRBM42physical
28514442
ISY1_HUMANISY1physical
28514442
NH2L1_HUMANNHP2L1physical
28514442
TRA2A_HUMANTRA2Aphysical
28514442
SF3B5_HUMANSF3B5physical
28514442
U5S1_HUMANEFTUD2physical
28514442
COIL_HUMANCOILphysical
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 RSMN_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-8, AND MASS SPECTROMETRY.

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