SF3B3_HUMAN - dbPTM
SF3B3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SF3B3_HUMAN
UniProt AC Q15393
Protein Name Splicing factor 3B subunit 3
Gene Name SF3B3
Organism Homo sapiens (Human).
Sequence Length 1217
Subcellular Localization Nucleus .
Protein Description Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex, a constituent of the spliceosome. [PubMed: 10490618]
Protein Sequence MFLYNLTLQRATGISFAIHGNFSGTKQQEIVVSRGKILELLRPDPNTGKVHTLLTVEVFGVIRSLMAFRLTGGTKDYIVVGSDSGRIVILEYQPSKNMFEKIHQETFGKSGCRRIVPGQFLAVDPKGRAVMISAIEKQKLVYILNRDAAARLTISSPLEAHKANTLVYHVVGVDVGFENPMFACLEMDYEEADNDPTGEAAANTQQTLTFYELDLGLNHVVRKYSEPLEEHGNFLITVPGGSDGPSGVLICSENYITYKNFGDQPDIRCPIPRRRNDLDDPERGMIFVCSATHKTKSMFFFLAQTEQGDIFKITLETDEDMVTEIRLKYFDTVPVAAAMCVLKTGFLFVASEFGNHYLYQIAHLGDDDEEPEFSSAMPLEEGDTFFFQPRPLKNLVLVDELDSLSPILFCQIADLANEDTPQLYVACGRGPRSSLRVLRHGLEVSEMAVSELPGNPNAVWTVRRHIEDEFDAYIIVSFVNATLVLSIGETVEEVTDSGFLGTTPTLSCSLLGDDALVQVYPDGIRHIRADKRVNEWKTPGKKTIVKCAVNQRQVVIALTGGELVYFEMDPSGQLNEYTERKEMSADVVCMSLANVPPGEQRSRFLAVGLVDNTVRIISLDPSDCLQPLSMQALPAQPESLCIVEMGGTEKQDELGERGSIGFLYLNIGLQNGVLLRTVLDPVTGDLSDTRTRYLGSRPVKLFRVRMQGQEAVLAMSSRSWLSYSYQSRFHLTPLSYETLEFASGFASEQCPEGIVAISTNTLRILALEKLGAVFNQVAFPLQYTPRKFVIHPESNNLIIIETDHNAYTEATKAQRKQQMAEEMVEAAGEDERELAAEMAAAFLNENLPESIFGAPKAGNGQWASVIRVMNPIQGNTLDLVQLEQNEAAFSVAVCRFSNTGEDWYVLVGVAKDLILNPRSVAGGFVYTYKLVNNGEKLEFLHKTPVEEVPAAIAPFQGRVLIGVGKLLRVYDLGKKKLLRKCENKHIANYISGIQTIGHRVIVSDVQESFIWVRYKRNENQLIIFADDTYPRWVTTASLLDYDTVAGADKFGNICVVRLPPNTNDEVDEDPTGNKALWDRGLLNGASQKAEVIMNYHVGETVLSLQKTTLIPGGSESLVYTTLSGGIGILVPFTSHEDHDFFQHVEMHLRSEHPPLCGRDHLSFRSYYFPVKNVIDGDLCEQFNSMEPNKQKNVSEELDRTPPEVSKKLEDIRTRYAF
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
1Sulfoxidation-------MFLYNLTL
-------CCEEEEEE		25.3328183972
12PhosphorylationNLTLQRATGISFAIH
EEEEEECCCCEEEEE		36.9221406692
15PhosphorylationLQRATGISFAIHGNF
EEECCCCEEEEECCC		15.2321406692
23PhosphorylationFAIHGNFSGTKQQEI
EEEECCCCCCCCEEE		49.9421406692
25PhosphorylationIHGNFSGTKQQEIVV
EECCCCCCCCEEEEE		25.2021406692
26UbiquitinationHGNFSGTKQQEIVVS
ECCCCCCCCEEEEEE		54.21-
33PhosphorylationKQQEIVVSRGKILEL
CCEEEEEECCCCHHH		25.1524719451
36UbiquitinationEIVVSRGKILELLRP
EEEEECCCCHHHCCC		42.90-
64PhosphorylationEVFGVIRSLMAFRLT
HHHHHHHHHHCHHCC		16.0427251275
71PhosphorylationSLMAFRLTGGTKDYI
HHHCHHCCCCCCEEE		29.3427362937
75AcetylationFRLTGGTKDYIVVGS
HHCCCCCCEEEEEEC		52.3826051181
75UbiquitinationFRLTGGTKDYIVVGS
HHCCCCCCEEEEEEC		52.3821906983
75 (in isoform 1)Ubiquitination-52.3821890473
75 (in isoform 2)Ubiquitination-52.3821890473
77PhosphorylationLTGGTKDYIVVGSDS
CCCCCCEEEEEECCC		9.3630631047
82PhosphorylationKDYIVVGSDSGRIVI
CEEEEEECCCCEEEE		19.5921712546
84PhosphorylationYIVVGSDSGRIVILE
EEEEECCCCEEEEEE		31.5027362937
92PhosphorylationGRIVILEYQPSKNMF
CEEEEEEEECCCCHH		23.4428152594
95PhosphorylationVILEYQPSKNMFEKI
EEEEEECCCCHHHHH		22.5728152594
96AcetylationILEYQPSKNMFEKIH
EEEEECCCCHHHHHH		60.1426051181
96UbiquitinationILEYQPSKNMFEKIH
EEEEECCCCHHHHHH		60.1421890473
96 (in isoform 1)Ubiquitination-60.1421890473
96 (in isoform 2)Ubiquitination-60.1421890473
101AcetylationPSKNMFEKIHQETFG
CCCCHHHHHHHHHHC		33.9327452117
101UbiquitinationPSKNMFEKIHQETFG
CCCCHHHHHHHHHHC		33.93-
1092-HydroxyisobutyrylationIHQETFGKSGCRRIV
HHHHHHCCCCCCEEC		39.21-
109AcetylationIHQETFGKSGCRRIV
HHHHHHCCCCCCEEC		39.2119608861
109UbiquitinationIHQETFGKSGCRRIV
HHHHHHCCCCCCEEC		39.2122053931
110PhosphorylationHQETFGKSGCRRIVP
HHHHHCCCCCCEECC		43.4330631047
118 (in isoform 3)Ubiquitination-21.7021890473
124 (in isoform 3)Ubiquitination-33.3221890473
1262-HydroxyisobutyrylationQFLAVDPKGRAVMIS
CEEEECCCCCEEEEE		57.47-
126AcetylationQFLAVDPKGRAVMIS
CEEEECCCCCEEEEE		57.4719608861
126UbiquitinationQFLAVDPKGRAVMIS
CEEEECCCCCEEEEE		57.4719608861
133O-linked_GlycosylationKGRAVMISAIEKQKL
CCCEEEEEEEHHCCE		12.7123301498
133PhosphorylationKGRAVMISAIEKQKL
CCCEEEEEEEHHCCE		12.7120068231
1372-HydroxyisobutyrylationVMISAIEKQKLVYIL
EEEEEEHHCCEEEEE		46.77-
137AcetylationVMISAIEKQKLVYIL
EEEEEEHHCCEEEEE		46.7723236377
137UbiquitinationVMISAIEKQKLVYIL
EEEEEEHHCCEEEEE		46.77-
139UbiquitinationISAIEKQKLVYILNR
EEEEHHCCEEEEECC		51.4921890473
139 (in isoform 1)Ubiquitination-51.4921890473
139 (in isoform 2)Ubiquitination-51.4921890473
142PhosphorylationIEKQKLVYILNRDAA
EHHCCEEEEECCCHH		15.3228152594
147 (in isoform 3)Ubiquitination-39.2121890473
153PhosphorylationRDAAARLTISSPLEA
CCHHHHCCCCCCHHH		17.1723312004
155PhosphorylationAAARLTISSPLEAHK
HHHHCCCCCCHHHHH		22.2229978859
156PhosphorylationAARLTISSPLEAHKA
HHHCCCCCCHHHHHC		29.6525159151
237O-linked_GlycosylationEHGNFLITVPGGSDG
HHCCEEEEECCCCCC		23.8523301498
256 (in isoform 3)Ubiquitination-5.2421890473
268MethylationFGDQPDIRCPIPRRR
CCCCCCCCCCCCCCC		27.78115916661
296UbiquitinationCSATHKTKSMFFFLA
EECCCCCCEEEEEEE		44.73-
314PhosphorylationQGDIFKITLETDEDM
CCCEEEEEEECCCCC		21.0927251275
321SulfoxidationTLETDEDMVTEIRLK
EEECCCCCEEEHHHH		3.6521406390
328AcetylationMVTEIRLKYFDTVPV
CEEEHHHHHCCHHHH		33.7426051181
328UbiquitinationMVTEIRLKYFDTVPV
CEEEHHHHHCCHHHH		33.74-
373 (in isoform 3)Ubiquitination-11.6321890473
388 (in isoform 3)Ubiquitination-28.1221890473
434PhosphorylationCGRGPRSSLRVLRHG
CCCCCHHHHHHHHHC		22.83-
537UbiquitinationDKRVNEWKTPGKKTI
CCCCCCCCCCCCCEE		38.37-
5462-HydroxyisobutyrylationPGKKTIVKCAVNQRQ
CCCCEEEEEEECCCE		16.78-
546AcetylationPGKKTIVKCAVNQRQ
CCCCEEEEEEECCCE		16.7825953088
546UbiquitinationPGKKTIVKCAVNQRQ
CCCCEEEEEEECCCE		16.78-
571PhosphorylationVYFEMDPSGQLNEYT
EEEEECCCCCCCHHH		34.6021406692
577PhosphorylationPSGQLNEYTERKEMS
CCCCCCHHHHCCCCC		16.9021406692
578PhosphorylationSGQLNEYTERKEMSA
CCCCCHHHHCCCCCC		24.1221406692
618PhosphorylationDNTVRIISLDPSDCL
CCEEEEEEECHHHCC		25.0928176443
622PhosphorylationRIISLDPSDCLQPLS
EEEEECHHHCCCCCC		40.3928176443
629PhosphorylationSDCLQPLSMQALPAQ
HHCCCCCCCCCCCCC		18.6128176443
639PhosphorylationALPAQPESLCIVEMG
CCCCCCCCEEEEECC		34.9128176443
648PhosphorylationCIVEMGGTEKQDELG
EEEECCCCCCCCCHH		33.9928176443
687PhosphorylationDPVTGDLSDTRTRYL
CCCCCCCCCCCHHCC		41.49-
693PhosphorylationLSDTRTRYLGSRPVK
CCCCCHHCCCCCCEE		18.1428152594
696PhosphorylationTRTRYLGSRPVKLFR
CCHHCCCCCCEEEEE		30.7128348404
700UbiquitinationYLGSRPVKLFRVRMQ
CCCCCCEEEEEEEEC		44.5921890473
700 (in isoform 1)Ubiquitination-44.5921890473
706SulfoxidationVKLFRVRMQGQEAVL
EEEEEEEECCCCEEE		4.8621406390
727PhosphorylationWLSYSYQSRFHLTPL
HHHCCCCCCCEECCC		28.7824719451
769UbiquitinationLRILALEKLGAVFNQ
HHHHHHHHHHHHHHH		53.74-
784PhosphorylationVAFPLQYTPRKFVIH
CCCCCCCCCCCEEEC		12.0327067055
787AcetylationPLQYTPRKFVIHPES
CCCCCCCCEEECCCC		45.2326051181
787UbiquitinationPLQYTPRKFVIHPES
CCCCCCCCEEECCCC		45.23-
807PhosphorylationIETDHNAYTEATKAQ
EECCCHHHHHHHHHH		15.49-
812UbiquitinationNAYTEATKAQRKQQM
HHHHHHHHHHHHHHH		49.96-
816UbiquitinationEATKAQRKQQMAEEM
HHHHHHHHHHHHHHH		32.57-
904PhosphorylationSNTGEDWYVLVGVAK
CCCCCCEEEEEEEEE		9.02-
919PhosphorylationDLILNPRSVAGGFVY
CEECCCCCCCCEEEE		19.9921406692
926PhosphorylationSVAGGFVYTYKLVNN
CCCCEEEEEEEECCC		11.3321406692
927PhosphorylationVAGGFVYTYKLVNNG
CCCEEEEEEEECCCC		14.6321406692
928PhosphorylationAGGFVYTYKLVNNGE
CCEEEEEEEECCCCC		5.6621406692
929AcetylationGGFVYTYKLVNNGEK
CEEEEEEEECCCCCE		37.8526051181
936AcetylationKLVNNGEKLEFLHKT
EECCCCCEEEEEECC		55.5019608861
936UbiquitinationKLVNNGEKLEFLHKT
EECCCCCEEEEEECC		55.5021890473
936 (in isoform 1)Ubiquitination-55.5021890473
942AcetylationEKLEFLHKTPVEEVP
CEEEEEECCCHHHCC		57.5826051181
942UbiquitinationEKLEFLHKTPVEEVP
CEEEEEECCCHHHCC		57.5821906983
942 (in isoform 1)Ubiquitination-57.5821890473
9652-HydroxyisobutyrylationRVLIGVGKLLRVYDL
EEEEECHHHHHHEEC		41.77-
965AcetylationRVLIGVGKLLRVYDL
EEEEECHHHHHHEEC		41.7725953088
965UbiquitinationRVLIGVGKLLRVYDL
EEEEECHHHHHHEEC		41.7721890473
965 (in isoform 1)Ubiquitination-41.7721890473
968MethylationIGVGKLLRVYDLGKK
EECHHHHHHEECCHH		35.07115916665
9742-HydroxyisobutyrylationLRVYDLGKKKLLRKC
HHHEECCHHHHHHHH		54.77-
974AcetylationLRVYDLGKKKLLRKC
HHHEECCHHHHHHHH		54.7726051181
974UbiquitinationLRVYDLGKKKLLRKC
HHHEECCHHHHHHHH		54.77-
975UbiquitinationRVYDLGKKKLLRKCE
HHEECCHHHHHHHHC		47.02-
980UbiquitinationGKKKLLRKCENKHIA
CHHHHHHHHCCHHHH		45.96-
984AcetylationLLRKCENKHIANYIS
HHHHHCCHHHHHHHH		17.6926051181
984UbiquitinationLLRKCENKHIANYIS
HHHHHCCHHHHHHHH		17.69-
989PhosphorylationENKHIANYISGIQTI
CCHHHHHHHHCCCCC		6.3528152594
991PhosphorylationKHIANYISGIQTIGH
HHHHHHHHCCCCCCE		21.3428152594
1029NitrationIIFADDTYPRWVTTA
EEEECCCCCCCEEHH		9.59-
1029PhosphorylationIIFADDTYPRWVTTA
EEEECCCCCCCEEHH		9.5925147952
1041PhosphorylationTTASLLDYDTVAGAD
EHHHHCCCCCCCCCC		17.3025147952
1043PhosphorylationASLLDYDTVAGADKF
HHHCCCCCCCCCCCC		13.16-
1049UbiquitinationDTVAGADKFGNICVV
CCCCCCCCCCCEEEE		55.4220972266
1054GlutathionylationADKFGNICVVRLPPN
CCCCCCEEEEECCCC		2.4122555962
1062PhosphorylationVVRLPPNTNDEVDED
EEECCCCCCCCCCCC		50.2326714015
1074AcetylationDEDPTGNKALWDRGL
CCCCCCCHHHHHHCC		46.3226051181
1074UbiquitinationDEDPTGNKALWDRGL
CCCCCCCHHHHHHCC		46.3222053931
1074 (in isoform 1)Ubiquitination-46.3221890473
1079MethylationGNKALWDRGLLNGAS
CCHHHHHHCCCCCHH		26.52115916653
1088UbiquitinationLLNGASQKAEVIMNY
CCCCHHCCEEEEEEC		43.98-
1103PhosphorylationHVGETVLSLQKTTLI
CCCCEEEEEEEEEEE		25.1524719451
1164MethylationGRDHLSFRSYYFPVK
CCCCCCCHHEEEEEC		22.00115916657
1165PhosphorylationRDHLSFRSYYFPVKN
CCCCCCHHEEEEECC		23.3628152594
1166PhosphorylationDHLSFRSYYFPVKNV
CCCCCHHEEEEECCE		12.6028152594
1167PhosphorylationHLSFRSYYFPVKNVI
CCCCHHEEEEECCEE		11.5828152594
1171UbiquitinationRSYYFPVKNVIDGDL
HHEEEEECCEECCHH		45.81-
1179GlutathionylationNVIDGDLCEQFNSME
CEECCHHHHHHHCCC		4.6122555962
1189AcetylationFNSMEPNKQKNVSEE
HHCCCCCCCCCCCHH		73.6626051181
1189UbiquitinationFNSMEPNKQKNVSEE
HHCCCCCCCCCCCHH		73.66-
1191AcetylationSMEPNKQKNVSEELD
CCCCCCCCCCCHHHH		62.0126051181
1191UbiquitinationSMEPNKQKNVSEELD
CCCCCCCCCCCHHHH		62.0121906983
1191 (in isoform 1)Ubiquitination-62.0121890473
1194PhosphorylationPNKQKNVSEELDRTP
CCCCCCCCHHHHCCC		34.4428176443
1200PhosphorylationVSEELDRTPPEVSKK
CCHHHHCCCHHHHHH		42.7523401153
1205PhosphorylationDRTPPEVSKKLEDIR
HCCCHHHHHHHHHHH		23.5528176443
12062-HydroxyisobutyrylationRTPPEVSKKLEDIRT
CCCHHHHHHHHHHHH		67.56-
1206AcetylationRTPPEVSKKLEDIRT
CCCHHHHHHHHHHHH		67.5625953088
1206UbiquitinationRTPPEVSKKLEDIRT
CCCHHHHHHHHHHHH		67.562190698
1206 (in isoform 1)Ubiquitination-67.5621890473
1207UbiquitinationTPPEVSKKLEDIRTR
CCHHHHHHHHHHHHH		49.99-
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 SF3B3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SF3B3_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 SF3B3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RUFY2_HUMANRUFY2physical
21900206
RAD9A_HUMANRAD9Aphysical
21900206
ZN579_HUMANZNF579physical
21900206
SMD1_HUMANSNRPD1physical
22939629
SMD2_HUMANSNRPD2physical
22939629
SF3B4_HUMANSF3B4physical
22939629
SF3B5_HUMANSF3B5physical
22939629
U520_HUMANSNRNP200physical
22939629
SRSF1_HUMANSRSF1physical
22939629
TCRG1_HUMANTCERG1physical
22939629
U5S1_HUMANEFTUD2physical
22939629
YBOX1_HUMANYBX1physical
22939629
SNRPA_HUMANSNRPAphysical
22939629
SRSF7_HUMANSRSF7physical
22939629
U2AF1_HUMANU2AF1physical
22939629
U2AF2_HUMANU2AF2physical
22939629
SRSF2_HUMANSRSF2physical
22939629
SRRM2_HUMANSRRM2physical
22939629
SFPQ_HUMANSFPQphysical
22939629
SMC1A_HUMANSMC1Aphysical
22939629
SNUT1_HUMANSART1physical
22939629
SMU1_HUMANSMU1physical
22939629
TBB5_HUMANTUBBphysical
22939629
WDR18_HUMANWDR18physical
22939629
STML2_HUMANSTOML2physical
22939629
TCPB_HUMANCCT2physical
22939629
TPBG_HUMANTPBGphysical
22939629
TRA2A_HUMANTRA2Aphysical
22939629
TRXR1_HUMANTXNRD1physical
22939629
ZCH18_HUMANZC3H18physical
22939629
TJAP1_HUMANTJAP1physical
22939629
UBE3A_HUMANUBE3Aphysical
22939629
SPDLY_HUMANSPDL1physical
22939629
UT14A_HUMANUTP14Aphysical
22939629
VTNC_HUMANVTNphysical
22939629
VP33B_HUMANVPS33Bphysical
22939629
SPEB_HUMANAGMATphysical
22939629
TR150_HUMANTHRAP3physical
22939629
TMOD2_HUMANTMOD2physical
22939629
STOM_HUMANSTOMphysical
22939629
TRI55_HUMANTRIM55physical
22939629
SSRG_HUMANSSR3physical
22939629
U5S1_HUMANEFTUD2physical
22365833
PPIL1_HUMANPPIL1physical
22365833
HSPB1_HUMANHSPB1physical
22365833
TOE1_HUMANTOE1physical
22365833
CUL1_HUMANCUL1physical
23951410
SKP1_HUMANSKP1physical
23951410
SKP2_HUMANSKP2physical
23951410
SPF27_HUMANBCAS2physical
26344197
CCAR1_HUMANCCAR1physical
26344197
CCAR2_HUMANCCAR2physical
26344197
DCTN1_HUMANDCTN1physical
26344197
ISY1_HUMANISY1physical
26344197
LUC7L_HUMANLUC7Lphysical
26344197
PHF5A_HUMANPHF5Aphysical
26344197
PRP19_HUMANPRPF19physical
26344197
PRPF3_HUMANPRPF3physical
26344197
PRP31_HUMANPRPF31physical
26344197
PRP4_HUMANPRPF4physical
26344197
SF3A1_HUMANSF3A1physical
26344197
SF3A2_HUMANSF3A2physical
26344197
SF3B5_HUMANSF3B5physical
26344197
SF3B6_HUMANSF3B6physical
26344197
SMC1A_HUMANSMC1Aphysical
26344197
SMC3_HUMANSMC3physical
26344197
SMD3_HUMANSNRPD3physical
26344197
SPTN1_HUMANSPTAN1physical
26344197
SSA27_HUMANSSSCA1physical
26344197
HNRPQ_HUMANSYNCRIPphysical
26344197
PLK1_HUMANPLK1physical
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 SF3B3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-109 AND LYS-126, AND MASSSPECTROMETRY.

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