SF3A1_MOUSE - dbPTM
SF3A1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SF3A1_MOUSE
UniProt AC Q8K4Z5
Protein Name Splicing factor 3A subunit 1
Gene Name Sf3a1
Organism Mus musculus (Mouse).
Sequence Length 791
Subcellular Localization Nucleus.
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 (By similarity)..
Protein Sequence MQAGPVQAVPPPPPVATESKQPIEEEASSKEDPTPSKPVVGIIYPPPEVRNIVDKTASFVARNGPEFEARIRQNEINNPKFNFLNPNDPYHAYYRHKVSEFKEGKAQEPSAAIPKVMQQQQQATQQQLPQKVQAQVIQETIVPKEPPPEFEFIADPPSISAFDLDVVKLTAQFVARNGRQFLTQLMQKEQRNYQFDFLRPQHSLFNYFTKLVEQYTKILIPPKGLFSKLKKEAENPREVLDQVCYRVEWAKFQERERKKEEEEKEKERVAYAQIDWHDFVVVETVDFQPNEQGNFPPPTTPEELGARILIQERYEKFGESEEVEMEVESDEEDQEKAEETPSQLDQDTQVQDMDEGSDDEEEGQKVPPPPETPMPPPLPPTPDQVIVRKDYDPKASKPLPPAPAPDEYLVSPITGEKIPASKMQEHMRIGLLDPRWLEQRDRSIREKQSDDEVYAPGLDIESSLKQLAERRTDIFGVEETAIGKKIGEEEIQKPEEKVTWDGHSGSMARTQQAAQANITLQEQIEAIHKAKGLVPEDDTKEKIGPSKPNEIPQQPPPPSSATNIPSSAPPITSVPRPPAMPPPVRTTVVSAVPVMPRPPMASVVRLPPGSVIAPMPPIIHAPRINVVPMPPAAPPIMAPRPPPMIVPTAFVPAPPVAPVPAPAPMPPVHPPPPMEDEPPSKKLKTEDSLMPEEEFLRRNKGPVSIKVQVPNMQDKTEWKLNGQGLVFTLPLTDQVSVIKVKIHEATGMPAGKQKLQYEGIFIKDSNSLAYYNMASGAVIHLALKERGGRKK
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
34PhosphorylationASSKEDPTPSKPVVG
HHCCCCCCCCCCEEE		53.1427180971
36PhosphorylationSKEDPTPSKPVVGII
CCCCCCCCCCEEEEE		52.6627180971
55MalonylationEVRNIVDKTASFVAR
HHHHHHHHHHHHHHH		34.7926320211
55AcetylationEVRNIVDKTASFVAR
HHHHHHHHHHHHHHH		34.7923806337
80UbiquitinationQNEINNPKFNFLNPN
HCCCCCCCCCCCCCC		55.87-
188UbiquitinationFLTQLMQKEQRNYQF
HHHHHHHHHHHHCCC		41.68-
188AcetylationFLTQLMQKEQRNYQF
HHHHHHHHHHHHCCC		41.6822826441
223UbiquitinationTKILIPPKGLFSKLK
HHHHCCCCCHHHHHH		63.99-
251AcetylationCYRVEWAKFQERERK
HHHHHHHHHHHHHHH		48.9622826441
320PhosphorylationRYEKFGESEEVEMEV
HHHHHCCCCEEEEEE		39.1625619855
329PhosphorylationEVEMEVESDEEDQEK
EEEEEECCCHHHHHH		56.3425521595
340PhosphorylationDQEKAEETPSQLDQD
HHHHHHHCHHHCCCC		21.5323649490
342PhosphorylationEKAEETPSQLDQDTQ
HHHHHCHHHCCCCCC		51.2825619855
348PhosphorylationPSQLDQDTQVQDMDE
HHHCCCCCCCCCCCC		25.6325619855
357PhosphorylationVQDMDEGSDDEEEGQ
CCCCCCCCCCHHCCC		39.5825521595
408PhosphorylationPAPAPDEYLVSPITG
CCCCCCCEEECCCCC		21.5625159016
411PhosphorylationAPDEYLVSPITGEKI
CCCCEEECCCCCCCC		14.1625159016
417UbiquitinationVSPITGEKIPASKMQ
ECCCCCCCCCHHHHH		56.16-
422UbiquitinationGEKIPASKMQEHMRI
CCCCCHHHHHHHHHH		46.86-
443PhosphorylationWLEQRDRSIREKQSD
HHHHHHHHHHHHCCC		30.2226745281
447UbiquitinationRDRSIREKQSDDEVY
HHHHHHHHCCCCCCC		45.30-
449PhosphorylationRSIREKQSDDEVYAP
HHHHHHCCCCCCCCC		59.0821082442
454PhosphorylationKQSDDEVYAPGLDIE
HCCCCCCCCCCCCHH		12.6725619855
465UbiquitinationLDIESSLKQLAERRT
CCHHHHHHHHHHHCC		45.26-
484AcetylationVEETAIGKKIGEEEI
CCHHHHCCHHCHHHC		34.7923236377
506PhosphorylationTWDGHSGSMARTQQA
CCCCCCHHHHHHHHH		16.57-
529UbiquitinationEQIEAIHKAKGLVPE
HHHHHHHHHCCCCCC		45.76-
752MalonylationATGMPAGKQKLQYEG
HHCCCCCCCEEEEEE		46.4926320211
754MalonylationGMPAGKQKLQYEGIF
CCCCCCCEEEEEEEE		40.8326320211
757PhosphorylationAGKQKLQYEGIFIKD
CCCCEEEEEEEEECC		26.93-
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 SF3A1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SF3A1_MOUSE !!
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 SF3A1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SF3A1_HUMANSF3A1physical
20360068
SPF45_HUMANRBM17physical
20360068
TTC33_HUMANTTC33physical
20360068
SF3A2_HUMANSF3A2physical
20360068
GPT11_HUMANGPATCH11physical
20360068
DHX15_HUMANDHX15physical
20360068
CCD97_HUMANCCDC97physical
20360068
DDX42_HUMANDDX42physical
20360068
SMD1_HUMANSNRPD1physical
20360068
SF3B1_HUMANSF3B1physical
20360068
RUXE_HUMANSNRPEphysical
20360068
RSMB_HUMANSNRPBphysical
20360068
SF3B2_HUMANSF3B2physical
20360068
SMD2_HUMANSNRPD2physical
20360068
DNJC8_HUMANDNAJC8physical
20360068
RU2A_HUMANSNRPA1physical
20360068
SF3A3_HUMANSF3A3physical
20360068
SF3B6_HUMANSF3B6physical
20360068
P3H1_HUMANP3H1physical
20360068
RUXG_HUMANSNRPGphysical
20360068
RUXF_HUMANSNRPFphysical
20360068
PHF5A_HUMANPHF5Aphysical
20360068
RU2B_HUMANSNRPB2physical
20360068
SF3B3_HUMANSF3B3physical
20360068
SF3B4_HUMANSF3B4physical
20360068
SR140_HUMANU2SURPphysical
20360068
SMD3_HUMANSNRPD3physical
20360068
HTSF1_HUMANHTATSF1physical
20360068
RBM39_HUMANRBM39physical
20360068
DDX46_HUMANDDX46physical
20360068
CRTAP_HUMANCRTAPphysical
20360068
SF3B5_HUMANSF3B5physical
20360068
WDR61_HUMANWDR61physical
20360068
CHERP_HUMANCHERPphysical
20360068
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SF3A1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329, AND MASSSPECTROMETRY.

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