SF3A2_HUMAN - dbPTM
SF3A2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SF3A2_HUMAN
UniProt AC Q15428
Protein Name Splicing factor 3A subunit 2
Gene Name SF3A2
Organism Homo sapiens (Human).
Sequence Length 464
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..
Protein Sequence MDFQHRPGGKTGSGGVASSSESNRDRRERLRQLALETIDINKDPYFMKNHLGSYECKLCLTLHNNEGSYLAHTQGKKHQTNLARRAAKEAKEAPAQPAPEKVKVEVKKFVKIGRPGYKVTKQRDSEMGQQSLLFQIDYPEIAEGIMPRHRFMSAYEQRIEPPDRRWQYLLMAAEPYETIAFKVPSREIDKAEGKFWTHWNRETKQFFLQFHFKMEKPPAPPSLPAGPPGVKRPPPPLMNGLPPRPPLPESLPPPPPGGLPLPPMPPTGPAPSGPPGPPQLPPPAPGVHPPAPVVHPPASGVHPPAPGVHPPAPGVHPPAPGVHPPTSGVHPPAPGVHPPAPGVHPPAPGVHPPAPGVHPPAPGVHPPPSAGVHPQAPGVHPAAPAVHPQAPGVHPPAPGMHPQAPGVHPQPPGVHPSAPGVHPQPPGVHPSNPGVHPPTPMPPMLRPPLPSEGPGNIPPPPPTN
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-------MDFQHRPG
-------CCCCCCCC
11.98-
10UbiquitinationFQHRPGGKTGSGGVA
CCCCCCCCCCCCCCC
56.48-
10MalonylationFQHRPGGKTGSGGVA
CCCCCCCCCCCCCCC
56.4826320211
11PhosphorylationQHRPGGKTGSGGVAS
CCCCCCCCCCCCCCC
39.5927794612
13PhosphorylationRPGGKTGSGGVASSS
CCCCCCCCCCCCCCC
37.2925159151
18PhosphorylationTGSGGVASSSESNRD
CCCCCCCCCCCCHHH
31.8029396449
19PhosphorylationGSGGVASSSESNRDR
CCCCCCCCCCCHHHH
28.5227794612
20PhosphorylationSGGVASSSESNRDRR
CCCCCCCCCCHHHHH
42.4227794612
37PhosphorylationLRQLALETIDINKDP
HHHHHHHHCCCCCCC
25.4628555341
42AcetylationLETIDINKDPYFMKN
HHHCCCCCCCHHHHH
61.4926051181
42UbiquitinationLETIDINKDPYFMKN
HHHCCCCCCCHHHHH
61.4921890473
48UbiquitinationNKDPYFMKNHLGSYE
CCCCHHHHHCCCCEE
31.1721890473
54NitrationMKNHLGSYECKLCLT
HHHCCCCEEEEEEEE
24.45-
57AcetylationHLGSYECKLCLTLHN
CCCCEEEEEEEEECC
30.2326051181
61PhosphorylationYECKLCLTLHNNEGS
EEEEEEEEECCCCCC
25.6028152594
68PhosphorylationTLHNNEGSYLAHTQG
EECCCCCCEEEECCC
15.7028152594
69PhosphorylationLHNNEGSYLAHTQGK
ECCCCCCEEEECCCH
20.8228152594
73PhosphorylationEGSYLAHTQGKKHQT
CCCEEEECCCHHHHH
33.1528152594
762-HydroxyisobutyrylationYLAHTQGKKHQTNLA
EEEECCCHHHHHHHH
36.95-
76AcetylationYLAHTQGKKHQTNLA
EEEECCCHHHHHHHH
36.9525953088
77UbiquitinationLAHTQGKKHQTNLAR
EEECCCHHHHHHHHH
48.01-
77AcetylationLAHTQGKKHQTNLAR
EEECCCHHHHHHHHH
48.0111922691
88AcetylationNLARRAAKEAKEAPA
HHHHHHHHHHHHCCC
58.1618527857
91AcetylationRRAAKEAKEAPAQPA
HHHHHHHHHCCCCCC
56.3426051181
91UbiquitinationRRAAKEAKEAPAQPA
HHHHHHHHHCCCCCC
56.34-
101AcetylationPAQPAPEKVKVEVKK
CCCCCCCCEEEEEEE
46.4223749302
101UbiquitinationPAQPAPEKVKVEVKK
CCCCCCCCEEEEEEE
46.42-
103UbiquitinationQPAPEKVKVEVKKFV
CCCCCCEEEEEEEEE
43.69-
103SumoylationQPAPEKVKVEVKKFV
CCCCCCEEEEEEEEE
43.69-
103SumoylationQPAPEKVKVEVKKFV
CCCCCCEEEEEEEEE
43.69-
111UbiquitinationVEVKKFVKIGRPGYK
EEEEEEEEECCCCCE
42.44-
118UbiquitinationKIGRPGYKVTKQRDS
EECCCCCEEEEHHCC
49.71-
150MethylationEGIMPRHRFMSAYEQ
CCCCCHHHHHHHHHH
30.18115916581
153PhosphorylationMPRHRFMSAYEQRIE
CCHHHHHHHHHHHCC
25.6125850435
155PhosphorylationRHRFMSAYEQRIEPP
HHHHHHHHHHHCCCC
12.8023186163
155NitrationRHRFMSAYEQRIEPP
HHHHHHHHHHHCCCC
12.80-
176PhosphorylationLLMAAEPYETIAFKV
HHHHCCCCCEEEEEC
19.74-
194UbiquitinationEIDKAEGKFWTHWNR
HHHHHCCCEECCCCH
29.2721890473
194AcetylationEIDKAEGKFWTHWNR
HHHHHCCCEECCCCH
29.2727452117
197PhosphorylationKAEGKFWTHWNRETK
HHCCCEECCCCHHHH
21.8329523821
216UbiquitinationQFHFKMEKPPAPPSL
EEEEECCCCCCCCCC
53.45-
216AcetylationQFHFKMEKPPAPPSL
EEEEECCCCCCCCCC
53.4526051181
222PhosphorylationEKPPAPPSLPAGPPG
CCCCCCCCCCCCCCC
46.0225159151

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 SF3A2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SF3A2_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 SF3A2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SF3B1_HUMANSF3B1physical
12234937
SF3B2_HUMANSF3B2physical
12234937
SF3B3_HUMANSF3B3physical
12234937
SF3B4_HUMANSF3B4physical
12234937
PHF5A_HUMANPHF5Aphysical
12234937
SF3B5_HUMANSF3B5physical
12234937
SF3A1_HUMANSF3A1physical
12234937
SF3A3_HUMANSF3A3physical
12234937
SR140_HUMANU2SURPphysical
12234937
DHX15_HUMANDHX15physical
12234937
TRAP1_HUMANTRAP1physical
12234937
CH60_HUMANHSPD1physical
12234937
SPF45_HUMANRBM17physical
12234937
CHERP_HUMANCHERPphysical
12234937
DDX46_HUMANDDX46physical
12234937
U2AF2_HUMANU2AF2physical
12234937
U2AF1_HUMANU2AF1physical
12234937
HM20B_HUMANHMG20Bphysical
12234937
DNJC8_HUMANDNAJC8physical
12234937
SRSF1_HUMANSRSF1physical
12234937
SF3B6_HUMANSF3B6physical
12234937
SPF30_HUMANSMNDC1physical
12234937
PUF60_HUMANPUF60physical
12234937
RU2A_HUMANSNRPA1physical
12234937
RU2B_HUMANSNRPB2physical
12234937
RSMB_HUMANSNRPBphysical
12234937
SMD3_HUMANSNRPD3physical
12234937
SMD2_HUMANSNRPD2physical
12234937
SMD1_HUMANSNRPD1physical
12234937
RUXE_HUMANSNRPEphysical
12234937
RUXG_HUMANSNRPGphysical
12234937
RUXF_HUMANSNRPFphysical
12234937
DDX42_HUMANDDX42physical
12234937
RU1C_HUMANSNRPCphysical
17332742
RSMB_HUMANSNRPBphysical
17332742
SMD1_HUMANSNRPD1physical
17332742
SMD2_HUMANSNRPD2physical
17332742
SMD3_HUMANSNRPD3physical
17332742
RUXE_HUMANSNRPEphysical
17332742
RUXF_HUMANSNRPFphysical
17332742
RUXG_HUMANSNRPGphysical
17332742
RU17_HUMANSNRNP70physical
17332742
SNRPA_HUMANSNRPAphysical
17332742
PR40A_HUMANPRPF40Aphysical
17332742
RU2A_HUMANSNRPA1physical
17332742
RU2B_HUMANSNRPB2physical
17332742
SF3A1_HUMANSF3A1physical
17332742
SF3A3_HUMANSF3A3physical
17332742
SF3B1_HUMANSF3B1physical
17332742
SF3B2_HUMANSF3B2physical
17332742
SF3B3_HUMANSF3B3physical
17332742
SF3B4_HUMANSF3B4physical
17332742
SF3B6_HUMANSF3B6physical
17332742
PHF5A_HUMANPHF5Aphysical
17332742
SF3B5_HUMANSF3B5physical
17332742
DHX15_HUMANDHX15physical
17332742
SPF45_HUMANRBM17physical
17332742
SPF30_HUMANSMNDC1physical
17332742
U2AF2_HUMANU2AF2physical
17332742
U2AF1_HUMANU2AF1physical
17332742
DNJC8_HUMANDNAJC8physical
17332742
DDX46_HUMANDDX46physical
17332742
SR140_HUMANU2SURPphysical
17332742
CHERP_HUMANCHERPphysical
17332742
PUF60_HUMANPUF60physical
17332742
DDX42_HUMANDDX42physical
17332742
PRP8_HUMANPRPF8physical
17332742
U520_HUMANSNRNP200physical
17332742
U5S1_HUMANEFTUD2physical
17332742
PRP6_HUMANPRPF6physical
17332742
DDX23_HUMANDDX23physical
17332742
CD2B2_HUMANCD2BP2physical
17332742
PRPF3_HUMANPRPF3physical
17332742
SNUT1_HUMANSART1physical
17332742
SRSF1_HUMANSRSF1physical
17332742
SRSF7_HUMANSRSF7physical
17332742
SRSF3_HUMANSRSF3physical
17332742
SRSF9_HUMANSRSF9physical
17332742
SRSF5_HUMANSRSF5physical
17332742
SRSF6_HUMANSRSF6physical
17332742
SRSF4_HUMANSRSF4physical
17332742
SRSF2_HUMANSRSF2physical
17332742
TRA2B_HUMANTRA2Bphysical
17332742
ARGL1_HUMANARGLU1physical
17332742
SRRM1_HUMANSRRM1physical
17332742
SRRM2_HUMANSRRM2physical
17332742
ROA1_HUMANHNRNPA1physical
17332742
ROA3_HUMANHNRNPA3physical
17332742
ROAA_HUMANHNRNPABphysical
17332742
ROA2_HUMANHNRNPA2B1physical
17332742
HNRPC_HUMANHNRNPCphysical
17332742
RBMX_HUMANRBMXphysical
17332742
HNRPK_HUMANHNRNPKphysical
17332742
HNRPQ_HUMANSYNCRIPphysical
17332742
HNRPR_HUMANHNRNPRphysical
17332742
HNRPU_HUMANHNRNPUphysical
17332742
PCBP1_HUMANPCBP1physical
17332742
HNRL1_HUMANHNRNPUL1physical
17332742
NCBP2_HUMANNCBP2physical
17332742
NCBP1_HUMANNCBP1physical
17332742
PRP19_HUMANPRPF19physical
17332742
CDC5L_HUMANCDC5Lphysical
17332742
SPF27_HUMANBCAS2physical
17332742
PLRG1_HUMANPLRG1physical
17332742
HSP7C_HUMANHSPA8physical
17332742
CWC15_HUMANCWC15physical
17332742
CTBL1_HUMANCTNNBL1physical
17332742
WBP11_HUMANWBP11physical
17332742
PQBP1_HUMANPQBP1physical
17332742
PRCC_HUMANPRCCphysical
17332742
RBM5_HUMANRBM5physical
17332742
CCAR1_HUMANCCAR1physical
17332742
SRRT_HUMANSRRTphysical
17332742
DDX5_HUMANDDX5physical
17332742
SUGP1_HUMANSUGP1physical
17332742
RBM39_HUMANRBM39physical
17332742
FUS_HUMANFUSphysical
17332742
ELAV1_HUMANELAVL1physical
17332742
YBOX1_HUMANYBX1physical
17332742
ILF3_HUMANILF3physical
17332742
DHX9_HUMANDHX9physical
17332742
SF01_HUMANSF1physical
17332742
HTSF1_HUMANHTATSF1physical
17332742
CS043_HUMANC19orf43physical
17332742
RBM10_HUMANRBM10physical
17332742
ZN207_HUMANZNF207physical
17332742
BUB3_HUMANBUB3physical
17332742
TCRG1_HUMANTCERG1physical
17332742
NRIP2_HUMANNRIP2physical
17332742
ZCH18_HUMANZC3H18physical
17332742
PP1R8_HUMANPPP1R8physical
17332742
S30BP_HUMANSAP30BPphysical
17332742
PP1A_HUMANPPP1CAphysical
17332742
ILF2_HUMANILF2physical
17332742
DDX17_HUMANDDX17physical
17332742
ACINU_HUMANACIN1physical
17332742
PININ_HUMANPNNphysical
17332742
RNPS1_HUMANRNPS1physical
17332742
CCAR2_HUMANCCAR2physical
17332742
SC31B_HUMANSEC31Bphysical
17332742
AGGF1_HUMANAGGF1physical
17332742
CIRBP_HUMANCIRBPphysical
17332742
CFA20_HUMANCFAP20physical
17332742
SF3A3_HUMANSF3A3physical
22939629
SF3B3_HUMANSF3B3physical
22939629
SF3B1_HUMANSF3B1physical
22939629
SF3B2_HUMANSF3B2physical
22939629
SNUT1_HUMANSART1physical
22939629
TPM3_HUMANTPM3physical
22939629
SF3A1_HUMANSF3A1physical
22365833
AQR_HUMANAQRphysical
26344197
BUD31_HUMANBUD31physical
26344197
DDX46_HUMANDDX46physical
26344197
IF4G1_HUMANEIF4G1physical
26344197
ISY1_HUMANISY1physical
26344197
PRP19_HUMANPRPF19physical
26344197
PRP31_HUMANPRPF31physical
26344197
PRP4_HUMANPRPF4physical
26344197
PSMD3_HUMANPSMD3physical
26344197
SF3A1_HUMANSF3A1physical
26344197
SMC1A_HUMANSMC1Aphysical
26344197
U520_HUMANSNRNP200physical
26344197
RU2A_HUMANSNRPA1physical
26344197
RU1C_HUMANSNRPCphysical
26344197
SMD2_HUMANSNRPD2physical
26344197
ZN830_HUMANZNF830physical
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 SF3A2_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.

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