SNRPA_HUMAN - dbPTM
SNRPA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SNRPA_HUMAN
UniProt AC P09012
Protein Name U1 small nuclear ribonucleoprotein A
Gene Name SNRPA
Organism Homo sapiens (Human).
Sequence Length 282
Subcellular Localization Nucleus.
Protein Description Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. U1 snRNP is the first snRNP to interact with pre-mRNA. This interaction is required for the subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP. SNRPA binds stem loop II of U1 snRNA. In a snRNP-free form (SF-A) may be involved in coupled pre-mRNA splicing and polyadenylation process. May bind preferentially to the 5'-UGCAC-3' motif on RNAs..
Protein Sequence MAVPETRPNHTIYINNLNEKIKKDELKKSLYAIFSQFGQILDILVSRSLKMRGQAFVIFKEVSSATNALRSMQGFPFYDKPMRIQYAKTDSDIIAKMKGTFVERDRKREKRKPKSQETPATKKAVQGGGATPVVGAVQGPVPGMPPMTQAPRIMHHMPGQPPYMPPPGMIPPPGLAPGQIPPGAMPPQQLMPGQMPPAQPLSENPPNHILFLTNLPEETNELMLSMLFNQFPGFKEVRLVPGRHDIAFVEFDNEVQAGAARDALQGFKITQNNAMKISFAKK
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------MAVPETRPN
------CCCCCCCCC		26.1019413330
202-HydroxyisobutyrylationYINNLNEKIKKDELK
EECCCCHHHCHHHHH		59.77-
20UbiquitinationYINNLNEKIKKDELK
EECCCCHHHCHHHHH		59.7721906983
22UbiquitinationNNLNEKIKKDELKKS
CCCCHHHCHHHHHHH		66.3022817900
23UbiquitinationNLNEKIKKDELKKSL
CCCHHHCHHHHHHHH		60.9722817900
31PhosphorylationDELKKSLYAIFSQFG
HHHHHHHHHHHHHHH		12.54-
35PhosphorylationKSLYAIFSQFGQILD
HHHHHHHHHHHHHHH		20.6322210691
60AcetylationGQAFVIFKEVSSATN
CCEEEEEEEHHHHHH		46.1919608861
60UbiquitinationGQAFVIFKEVSSATN
CCEEEEEEEHHHHHH		46.1922817900
63PhosphorylationFVIFKEVSSATNALR
EEEEEEHHHHHHHHH		18.4928348404
64PhosphorylationVIFKEVSSATNALRS
EEEEEHHHHHHHHHH		44.2620068231
66PhosphorylationFKEVSSATNALRSMQ
EEEHHHHHHHHHHCC		23.9920068231
71PhosphorylationSATNALRSMQGFPFY
HHHHHHHHCCCCCCC		19.1325690035
78PhosphorylationSMQGFPFYDKPMRIQ
HCCCCCCCCCCCEEE		24.2429759185
802-HydroxyisobutyrylationQGFPFYDKPMRIQYA
CCCCCCCCCCEEEEE		29.36-
80UbiquitinationQGFPFYDKPMRIQYA
CCCCCCCCCCEEEEE		29.3624816145
80AcetylationQGFPFYDKPMRIQYA
CCCCCCCCCCEEEEE		29.3625825284
86PhosphorylationDKPMRIQYAKTDSDI
CCCCEEEEEECCHHH		14.0129759185
882-HydroxyisobutyrylationPMRIQYAKTDSDIIA
CCEEEEEECCHHHHH		48.18-
88AcetylationPMRIQYAKTDSDIIA
CCEEEEEECCHHHHH		48.1823236377
88UbiquitinationPMRIQYAKTDSDIIA
CCEEEEEECCHHHHH		48.1827667366
91PhosphorylationIQYAKTDSDIIAKMK
EEEEECCHHHHHHHH		35.6221712546
96AcetylationTDSDIIAKMKGTFVE
CCHHHHHHHHCCHHH		30.6423236377
96UbiquitinationTDSDIIAKMKGTFVE
CCHHHHHHHHCCHHH		30.6421906983
982-HydroxyisobutyrylationSDIIAKMKGTFVERD
HHHHHHHHCCHHHHH		54.84-
98UbiquitinationSDIIAKMKGTFVERD
HHHHHHHHCCHHHHH		54.8421906983
112UbiquitinationDRKREKRKPKSQETP
HHHHHHCCCCCCCCH		68.7929967540
114UbiquitinationKREKRKPKSQETPAT
HHHHCCCCCCCCHHH		68.7429967540
115PhosphorylationREKRKPKSQETPATK
HHHCCCCCCCCHHHH		41.6028985074
118PhosphorylationRKPKSQETPATKKAV
CCCCCCCCHHHHHHH		15.5824719451
122UbiquitinationSQETPATKKAVQGGG
CCCCHHHHHHHCCCC		40.6233845483
122AcetylationSQETPATKKAVQGGG
CCCCHHHHHHHCCCC		40.6225953088
123UbiquitinationQETPATKKAVQGGGA
CCCHHHHHHHCCCCC		49.8124816145
131PhosphorylationAVQGGGATPVVGAVQ
HHCCCCCCCCEECCC		21.6425159151
131O-linked_GlycosylationAVQGGGATPVVGAVQ
HHCCCCCCCCEECCC		21.6430059200
144SulfoxidationVQGPVPGMPPMTQAP
CCCCCCCCCCCCCCC		2.4928183972
147SulfoxidationPVPGMPPMTQAPRIM
CCCCCCCCCCCCCHH		3.4128183972
148PhosphorylationVPGMPPMTQAPRIMH
CCCCCCCCCCCCHHH		27.6128555341
148O-linked_GlycosylationVPGMPPMTQAPRIMH
CCCCCCCCCCCCHHH		27.6130059200
152MethylationPPMTQAPRIMHHMPG
CCCCCCCCHHHCCCC		41.7124129315
268UbiquitinationRDALQGFKITQNNAM
HHHHCCCEEECCCEE		52.2322817900
276UbiquitinationITQNNAMKISFAKK-
EECCCEEEEEEECC-		32.5622817900
276MalonylationITQNNAMKISFAKK-
EECCCEEEEEEECC-		32.5626320211
281UbiquitinationAMKISFAKK------
EEEEEEECC------		57.9422817900
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 SNRPA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SNRPA_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 SNRPA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNRPA_HUMANSNRPAphysical
10688667
CS043_HUMANC19orf43physical
16189514
SNRPA_HUMANSNRPAphysical
16189514
T2FA_HUMANGTF2F1physical
22939629
THTR_HUMANTSTphysical
22939629
TIF1A_HUMANTRIM24physical
22939629
SPEB_HUMANAGMATphysical
22939629
TIM13_HUMANTIMM13physical
22939629
TNPO1_HUMANTNPO1physical
22939629
RU2A_HUMANSNRPA1physical
22365833
U2AF2_HUMANU2AF2physical
22365833
CS043_HUMANC19orf43physical
22365833
HNRPK_HUMANHNRNPKphysical
22365833
RBM42_HUMANRBM42physical
22365833
PTBP1_HUMANPTBP1physical
22365833
PTBP2_HUMANPTBP2physical
22365833
IL7RA_HUMANIL7Rphysical
23151878
PRKDC_HUMANPRKDCphysical
22863883
PTBP1_HUMANPTBP1physical
17507659
SFPQ_HUMANSFPQphysical
17507659
SNRPA_HUMANSNRPAphysical
25416956
RU2A_HUMANSNRPA1physical
25416956
QKI_HUMANQKIphysical
25416956
ENOX2_HUMANENOX2physical
25416956
U2AF2_HUMANU2AF2physical
25416956
MTUS2_HUMANMTUS2physical
25416956
NDUF3_HUMANNDUFAF3physical
25416956
RBMX_HUMANRBMXphysical
25416956
MET13_HUMANMETTL13physical
25416956
LENG8_HUMANLENG8physical
25416956
UBC_HUMANUBCphysical
19373254
PRP6_HUMANPRPF6physical
26344197
SF3A2_HUMANSF3A2physical
26344197
SF3A3_HUMANSF3A3physical
26344197
SF3B1_HUMANSF3B1physical
26344197
SYYC_HUMANYARSphysical
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 SNRPA_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, AND MASS SPECTROMETRY.
"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-60, 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 THR-131, AND MASSSPECTROMETRY.

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