CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012568
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Splicing factor 3A subunit 1 
Protein Synonyms/Alias
 SF3a120; Spliceosome-associated protein 114; SAP 114 
Gene Name
 SF3A1 
Gene Synonyms/Alias
 SAP114 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
55EVRNIVDKTASFVARacetylation[1]
55EVRNIVDKTASFVARubiquitination[2, 3, 4, 5]
80QNEINNPKFNFLNPNubiquitination[2, 3, 5]
131TQQQLPQKVQAQVIQubiquitination[6, 7]
188FLTQLMQKEQRNYQFubiquitination[2, 5]
223TKILIPPKGLFSKLKubiquitination[2, 3, 5]
251CYRVEWAKFQERERKacetylation[1]
251CYRVEWAKFQERERKubiquitination[2, 5]
399DYDPKASKPLPPAPAubiquitination[6, 7]
419VSPITGEKIPASKMQubiquitination[2, 3, 4, 5, 6, 7, 8]
424GEKIPASKMQEHMRIubiquitination[4]
449RDRSIREKQSDDEVYubiquitination[4, 6]
467LDIESSLKQLAERRTubiquitination[2, 5, 6]
486VEETAIGKKIGEEEIubiquitination[6]
487EETAIGKKIGEEEIQubiquitination[4]
708NKGPVSIKVQVPNMQubiquitination[2, 3, 5]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865] 
Functional 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. 
Sequence Annotation
 REPEAT 52 94 SURP motif 1.
 REPEAT 166 208 SURP motif 2.
 DOMAIN 707 793 Ubiquitin-like.
 MOD_RES 55 55 N6-acetyllysine.
 MOD_RES 320 320 Phosphoserine.
 MOD_RES 329 329 Phosphoserine.
 MOD_RES 359 359 Phosphoserine.
 MOD_RES 413 413 Phosphoserine.
 MOD_RES 451 451 Phosphoserine.
 MOD_RES 456 456 Phosphotyrosine.
 MOD_RES 759 759 Phosphotyrosine.  
Keyword
 3D-structure; Acetylation; Complete proteome; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Spliceosome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 793 AA 
Protein Sequence
MPAGPVQAVP PPPPVPTEPK QPTEEEASSK EDSAPSKPVV GIIYPPPEVR NIVDKTASFV 60
ARNGPEFEAR IRQNEINNPK FNFLNPNDPY HAYYRHKVSE FKEGKAQEPS AAIPKVMQQQ 120
QQTTQQQLPQ KVQAQVIQET IVPKEPPPEF EFIADPPSIS AFDLDVVKLT AQFVARNGRQ 180
FLTQLMQKEQ RNYQFDFLRP QHSLFNYFTK LVEQYTKILI PPKGLFSKLK KEAENPREVL 240
DQVCYRVEWA KFQERERKKE EEEKEKERVA YAQIDWHDFV VVETVDFQPN EQGNFPPPTT 300
PEELGARILI QERYEKFGES EEVEMEVESD EEDDKQEKAE EPPSQLDQDT QVQDMDEGSD 360
DEEEGQKVPP PPETPMPPPL PPTPDQVIVR KDYDPKASKP LPPAPAPDEY LVSPITGEKI 420
PASKMQEHMR IGLLDPRWLE QRDRSIREKQ SDDEVYAPGL DIESSLKQLA ERRTDIFGVE 480
ETAIGKKIGE EEIQKPEEKV TWDGHSGSMA RTQQAAQANI TLQEQIEAIH KAKGLVPEDD 540
TKEKIGPSKP NEIPQQPPPP SSATNIPSSA PPITSVPRPP TMPPPVRTTV VSAVPVMPRP 600
PMASVVRLPP GSVIAPMPPI IHAPRINVVP MPPSAPPIMA PRPPPMIVPT AFVPAPPVAP 660
VPAPAPMPPV HPPPPMEDEP TSKKLKTEDS LMPEEEFLRR NKGPVSIKVQ VPNMQDKTEW 720
KLNGQVLVFT LPLTDQVSVI KVKIHEATGM PAGKQKLQYE GIFIKDSNSL AYYNMANGAV 780
IHLALKERGG RKK 793 
Gene Ontology
 GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005684; C:U2-type spliceosomal complex; IDA:UniProtKB.
 GO:0003723; F:RNA binding; IDA:UniProtKB.
 GO:0000389; P:mRNA 3'-splice site recognition; TAS:HGNC. 
Interpro
 IPR022030; PRP21-like.
 IPR000061; Surp.
 IPR000626; Ubiquitin.
 IPR019955; Ubiquitin_supergroup. 
Pfam
 PF12230; PRP21_like_P
 PF01805; Surp
 PF00240; ubiquitin 
SMART
 SM00648; SWAP
 SM00213; UBQ 
PROSITE
 PS50128; SURP
 PS50053; UBIQUITIN_2 
PRINTS