SF3A3_HUMAN - dbPTM
SF3A3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SF3A3_HUMAN
UniProt AC Q12874
Protein Name Splicing factor 3A subunit 3
Gene Name SF3A3
Organism Homo sapiens (Human).
Sequence Length 501
Subcellular Localization Nucleus speckle.
Protein Description Subunit of the splicing factor SF3A required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex..
Protein Sequence METILEQQRRYHEEKERLMDVMAKEMLTKKSTLRDQINSDHRTRAMQDRYMEVSGNLRDLYDDKDGLRKEELNAISGPNEFAEFYNRLKQIKEFHRKHPNEICVPMSVEFEELLKARENPSEEAQNLVEFTDEEGYGRYLDLHDCYLKYINLKASEKLDYITYLSIFDQLFDIPKERKNAEYKRYLEMLLEYLQDYTDRVKPLQDQNELFGKIQAEFEKKWENGTFPGWPKETSSALTHAGAHLDLSAFSSWEELASLGLDRLKSALLALGLKCGGTLEERAQRLFSTKGKSLESLDTSLFAKNPKSKGTKRDTERNKDIAFLEAQIYEYVEILGEQRHLTHENVQRKQARTGEEREEEEEEQISESESEDEENEIIYNPKNLPLGWDGKPIPYWLYKLHGLNINYNCEICGNYTYRGPKAFQRHFAEWRHAHGMRCLGIPNTAHFANVTQIEDAVSLWAKLKLQKASERWQPDTEEEYEDSSGNVVNKKTYEDLKRQGLL
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
1Acetylation-------METILEQQ
-------CHHHHHHH		10.4022223895
1Sulfoxidation-------METILEQQ
-------CHHHHHHH		10.4028183972
24UbiquitinationRLMDVMAKEMLTKKS
HHHHHHHHHHHHCHH		26.09-
24AcetylationRLMDVMAKEMLTKKS
HHHHHHHHHHHHCHH		26.0926051181
242-HydroxyisobutyrylationRLMDVMAKEMLTKKS
HHHHHHHHHHHHCHH		26.09-
31PhosphorylationKEMLTKKSTLRDQIN
HHHHHCHHHHHHHHC		33.9428555341
32PhosphorylationEMLTKKSTLRDQINS
HHHHCHHHHHHHHCH		34.3928555341
43PhosphorylationQINSDHRTRAMQDRY
HHCHHHHHHHHHHHH		21.2525278378
49MethylationRTRAMQDRYMEVSGN
HHHHHHHHHHHHCCC		18.79115916589
50PhosphorylationTRAMQDRYMEVSGNL
HHHHHHHHHHHCCCH		13.1023186163
51SulfoxidationRAMQDRYMEVSGNLR
HHHHHHHHHHCCCHH		4.2328183972
54PhosphorylationQDRYMEVSGNLRDLY
HHHHHHHCCCHHHHH		14.5223186163
58MethylationMEVSGNLRDLYDDKD
HHHCCCHHHHHCCCC		35.57115916593
61PhosphorylationSGNLRDLYDDKDGLR
CCCHHHHHCCCCCCC		26.7821406692
64AcetylationLRDLYDDKDGLRKEE
HHHHHCCCCCCCHHH		51.2826051181
642-HydroxyisobutyrylationLRDLYDDKDGLRKEE
HHHHHCCCCCCCHHH		51.28-
64UbiquitinationLRDLYDDKDGLRKEE
HHHHHCCCCCCCHHH		51.28-
69UbiquitinationDDKDGLRKEELNAIS
CCCCCCCHHHHHHCC		61.66-
85PhosphorylationPNEFAEFYNRLKQIK
HHHHHHHHHHHHHHH		7.2927642862
89UbiquitinationAEFYNRLKQIKEFHR
HHHHHHHHHHHHHHH		46.90-
92UbiquitinationYNRLKQIKEFHRKHP
HHHHHHHHHHHHHCC		52.4019608861
92AcetylationYNRLKQIKEFHRKHP
HHHHHHHHHHHHHCC		52.4019608861
97AcetylationQIKEFHRKHPNEICV
HHHHHHHHCCCCCEE		55.6426822725
97UbiquitinationQIKEFHRKHPNEICV
HHHHHHHHCCCCCEE		55.64-
103GlutathionylationRKHPNEICVPMSVEF
HHCCCCCEEECCCCH		1.9822555962
115UbiquitinationVEFEELLKARENPSE
CCHHHHHHHCCCCCH		59.01-
119N-linked_GlycosylationELLKARENPSEEAQN
HHHHHCCCCCHHHHH		39.5819159218
121PhosphorylationLKARENPSEEAQNLV
HHHCCCCCHHHHHHH		60.7025849741
131PhosphorylationAQNLVEFTDEEGYGR
HHHHHHCCCCCCCCC		29.06-
139PhosphorylationDEEGYGRYLDLHDCY
CCCCCCCEECHHHCH		10.5428152594
145GlutathionylationRYLDLHDCYLKYINL
CEECHHHCHHHHCCC		2.7422555962
146PhosphorylationYLDLHDCYLKYINLK
EECHHHCHHHHCCCC		16.5828152594
1482-HydroxyisobutyrylationDLHDCYLKYINLKAS
CHHHCHHHHCCCCHH		20.01-
148UbiquitinationDLHDCYLKYINLKAS
CHHHCHHHHCCCCHH		20.01-
148AcetylationDLHDCYLKYINLKAS
CHHHCHHHHCCCCHH		20.0126051181
1532-HydroxyisobutyrylationYLKYINLKASEKLDY
HHHHCCCCHHHCCCH		45.43-
153UbiquitinationYLKYINLKASEKLDY
HHHHCCCCHHHCCCH		45.43-
153AcetylationYLKYINLKASEKLDY
HHHHCCCCHHHCCCH		45.4325953088
188SulfoxidationEYKRYLEMLLEYLQD
HHHHHHHHHHHHHHH		4.8328183972
201AcetylationQDYTDRVKPLQDQNE
HHHHHCCCCCCCHHH		40.6926051181
201UbiquitinationQDYTDRVKPLQDQNE
HHHHHCCCCCCCHHH		40.6921890473
212AcetylationDQNELFGKIQAEFEK
CHHHHHHHHHHHHHH		25.0626051181
212UbiquitinationDQNELFGKIQAEFEK
CHHHHHHHHHHHHHH		25.06-
2192-HydroxyisobutyrylationKIQAEFEKKWENGTF
HHHHHHHHHHCCCCC		69.38-
219AcetylationKIQAEFEKKWENGTF
HHHHHHHHHHCCCCC		69.3823749302
225PhosphorylationEKKWENGTFPGWPKE
HHHHCCCCCCCCCCH		37.9322985185
2642-HydroxyisobutyrylationSLGLDRLKSALLALG
HCCHHHHHHHHHHHC		34.28-
265PhosphorylationLGLDRLKSALLALGL
CCHHHHHHHHHHHCC		28.8321712546
273UbiquitinationALLALGLKCGGTLEE
HHHHHCCCCCCCHHH		29.09-
277PhosphorylationLGLKCGGTLEERAQR
HCCCCCCCHHHHHHH		19.1122817900
2892-HydroxyisobutyrylationAQRLFSTKGKSLESL
HHHHHCCCCCCHHHH		64.24-
291UbiquitinationRLFSTKGKSLESLDT
HHHCCCCCCHHHHCH		54.12-
291AcetylationRLFSTKGKSLESLDT
HHHCCCCCCHHHHCH		54.1226051181
292PhosphorylationLFSTKGKSLESLDTS
HHCCCCCCHHHHCHH		46.1428464451
295PhosphorylationTKGKSLESLDTSLFA
CCCCCHHHHCHHHHC		36.5219664994
298PhosphorylationKSLESLDTSLFAKNP
CCHHHHCHHHHCCCC		32.4025159151
299PhosphorylationSLESLDTSLFAKNPK
CHHHHCHHHHCCCCC		22.5825159151
303UbiquitinationLDTSLFAKNPKSKGT
HCHHHHCCCCCCCCC		67.46-
303AcetylationLDTSLFAKNPKSKGT
HCHHHHCCCCCCCCC		67.4625953088
306UbiquitinationSLFAKNPKSKGTKRD
HHHCCCCCCCCCCCC		74.35-
307PhosphorylationLFAKNPKSKGTKRDT
HHCCCCCCCCCCCCC		37.2626074081
310PhosphorylationKNPKSKGTKRDTERN
CCCCCCCCCCCCHHH		27.0026074081
314PhosphorylationSKGTKRDTERNKDIA
CCCCCCCCHHHHHHH		40.6626074081
352PhosphorylationVQRKQARTGEEREEE
HHHHHHHCCCHHHHH		52.5428176443
365PhosphorylationEEEEEQISESESEDE
HHHHHHHCCCCCCHH		34.4621955146
367PhosphorylationEEEQISESESEDEEN
HHHHHCCCCCCHHCC		39.3621955146
369PhosphorylationEQISESESEDEENEI
HHHCCCCCCHHCCCC		60.6821955146
378PhosphorylationDEENEIIYNPKNLPL
HHCCCCCCCCCCCCC		30.9528176443
390UbiquitinationLPLGWDGKPIPYWLY
CCCCCCCCCCCHHHH		36.9821890473
390AcetylationLPLGWDGKPIPYWLY
CCCCCCCCCCCHHHH		36.9826051181
406PhosphorylationLHGLNINYNCEICGN
HHCCCCCCCEEECCC		19.8628152594
414PhosphorylationNCEICGNYTYRGPKA
CEEECCCEEECCCHH		7.1628152594
415PhosphorylationCEICGNYTYRGPKAF
EEECCCEEECCCHHH		15.6728152594
416PhosphorylationEICGNYTYRGPKAFQ
EECCCEEECCCHHHH		11.8328152594
420UbiquitinationNYTYRGPKAFQRHFA
CEEECCCHHHHHHHH		65.73-
4662-HydroxyisobutyrylationWAKLKLQKASERWQP
HHHHHHHHHHHHCCC		65.40-
466UbiquitinationWAKLKLQKASERWQP
HHHHHHHHHHHHCCC		65.40-
468PhosphorylationKLKLQKASERWQPDT
HHHHHHHHHHCCCCC		34.4326074081
470MethylationKLQKASERWQPDTEE
HHHHHHHHCCCCCHH		34.53115916585
475PhosphorylationSERWQPDTEEEYEDS
HHHCCCCCHHHCCCC		52.5623401153
479PhosphorylationQPDTEEEYEDSSGNV
CCCCHHHCCCCCCCC		28.4623927012
482PhosphorylationTEEEYEDSSGNVVNK
CHHHCCCCCCCCCCH		28.3623927012
483PhosphorylationEEEYEDSSGNVVNKK
HHHCCCCCCCCCCHH		46.8623403867
489AcetylationSSGNVVNKKTYEDLK
CCCCCCCHHHHHHHH		34.5825953088
489UbiquitinationSSGNVVNKKTYEDLK
CCCCCCCHHHHHHHH		34.5821890473
491PhosphorylationGNVVNKKTYEDLKRQ
CCCCCHHHHHHHHHC		33.4828796482
492PhosphorylationNVVNKKTYEDLKRQG
CCCCHHHHHHHHHCC		19.1428796482
496UbiquitinationKKTYEDLKRQGLL--
HHHHHHHHHCCCC--		55.80-
496MethylationKKTYEDLKRQGLL--
HHHHHHHHHCCCC--		55.80115981409
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 SF3A3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SF3A3_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 SF3A3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CC85B_HUMANCCDC85Bphysical
16189514
A4_HUMANAPPphysical
21832049
SF3B1_HUMANSF3B1physical
22939629
SF3B3_HUMANSF3B3physical
22939629
SF3B4_HUMANSF3B4physical
22939629
SNRPA_HUMANSNRPAphysical
22939629
SRSF9_HUMANSRSF9physical
22939629
T2FA_HUMANGTF2F1physical
22939629
SNUT1_HUMANSART1physical
22939629
SRPK1_HUMANSRPK1physical
22939629
TRPM8_HUMANTRPM8physical
22939629
VASP_HUMANVASPphysical
22939629
TOX4_HUMANTOX4physical
22939629
TSKS_HUMANTSKSphysical
22939629
TTC4_HUMANTTC4physical
22939629
SF3A1_HUMANSF3A1physical
22365833
ANM5_HUMANPRMT5physical
22365833
HGS_HUMANHGSphysical
22863883
TRI69_HUMANTRIM69physical
25416956
ACTZ_HUMANACTR1Aphysical
26344197
CSN3_HUMANCOPS3physical
26344197
DCTN1_HUMANDCTN1physical
26344197
ISY1_HUMANISY1physical
26344197
PLRG1_HUMANPLRG1physical
26344197
PRP19_HUMANPRPF19physical
26344197
PRP31_HUMANPRPF31physical
26344197
PRP4_HUMANPRPF4physical
26344197
PR40B_HUMANPRPF40Bphysical
26344197
PSME3_HUMANPSME3physical
26344197
SF3A1_HUMANSF3A1physical
26344197
SF3A2_HUMANSF3A2physical
26344197
SF3B3_HUMANSF3B3physical
26344197
RU17_HUMANSNRNP70physical
26344197
SYF1_HUMANXAB2physical
26344197
ZN830_HUMANZNF830physical
26344197
TRI69_HUMANTRIM69physical
21516116
TAD2A_HUMANTADA2Aphysical
21516116
SRP68_HUMANSRP68physical
27173435
TRAP1_HUMANTRAP1physical
27173435
SND1_HUMANSND1physical
27173435
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 SF3A3_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 MET-1, 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-92, AND MASS SPECTROMETRY.
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-119, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-299; SER-365;SER-367 AND SER-369, AND MASS SPECTROMETRY.
"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-365; SER-367 ANDSER-369, 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 THR-277; SER-365; SER-367AND SER-369, AND MASS SPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-414, AND MASSSPECTROMETRY.

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