SF3B4_HUMAN - dbPTM
SF3B4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SF3B4_HUMAN
UniProt AC Q15427
Protein Name Splicing factor 3B subunit 4
Gene Name SF3B4
Organism Homo sapiens (Human).
Sequence Length 424
Subcellular Localization Nucleus .
Protein Description Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex. [PubMed: 27720643 SF3B complex is 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]
Protein Sequence MAAGPISERNQDATVYVGGLDEKVSEPLLWELFLQAGPVVNTHMPKDRVTGQHQGYGFVEFLSEEDADYAIKIMNMIKLYGKPIRVNKASAHNKNLDVGANIFIGNLDPEIDEKLLYDTFSAFGVILQTPKIMRDPDTGNSKGYAFINFASFDASDAAIEAMNGQYLCNRPITVSYAFKKDSKGERHGSAAERLLAAQNPLSQADRPHQLFADAPPPPSAPNPVVSSLGSGLPPPGMPPPGSFPPPVPPPGALPPGIPPAMPPPPMPPGAAGHGPPSAGTPGAGHPGHGHSHPHPFPPGGMPHPGMSQMQLAHHGPHGLGHPHAGPPGSGGQPPPRPPPGMPHPGPPPMGMPPRGPPFGSPMGHPGPMPPHGMRGPPPLMPPHGYTGPPRPPPYGYQRGPLPPPRPTPRPPVPPRGPLRGPLPQ
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
2Acetylation------MAAGPISER
------CCCCCCCCC		22.5622223895
7Phosphorylation-MAAGPISERNQDAT
-CCCCCCCCCCCCCE		33.3722210691
14PhosphorylationSERNQDATVYVGGLD
CCCCCCCEEEECCCC		22.2128152594
16NitrationRNQDATVYVGGLDEK
CCCCCEEEECCCCHH		6.77-
16PhosphorylationRNQDATVYVGGLDEK
CCCCCEEEECCCCHH		6.7721082442
42PhosphorylationQAGPVVNTHMPKDRV
HHCCEEECCCCCCCC		14.1324719451
56PhosphorylationVTGQHQGYGFVEFLS
CCCCCCCCEEEEECC		10.7922817900
63PhosphorylationYGFVEFLSEEDADYA
CEEEEECCHHCHHHH		44.24-
69PhosphorylationLSEEDADYAIKIMNM
CCHHCHHHHHHHHHH		16.37-
78AcetylationIKIMNMIKLYGKPIR
HHHHHHHHHHCCCEE		25.5325953088
78UbiquitinationIKIMNMIKLYGKPIR
HHHHHHHHHHCCCEE		25.53-
80PhosphorylationIMNMIKLYGKPIRVN
HHHHHHHHCCCEEEC		20.3628152594
82AcetylationNMIKLYGKPIRVNKA
HHHHHHCCCEEECHH		24.5826051181
82UbiquitinationNMIKLYGKPIRVNKA
HHHHHHCCCEEECHH		24.58-
117PhosphorylationEIDEKLLYDTFSAFG
HHCHHHHHHHHHHHH		24.3120068231
119PhosphorylationDEKLLYDTFSAFGVI
CHHHHHHHHHHHHHH		13.1120068231
121PhosphorylationKLLYDTFSAFGVILQ
HHHHHHHHHHHHHHC		25.4420068231
129PhosphorylationAFGVILQTPKIMRDP
HHHHHHCCCCCCCCC		24.0924719451
138PhosphorylationKIMRDPDTGNSKGYA
CCCCCCCCCCCCCEE		43.5820068231
141PhosphorylationRDPDTGNSKGYAFIN
CCCCCCCCCCEEEEE		28.8920068231
390DimethylationHGYTGPPRPPPYGYQ
CCCCCCCCCCCCCCC		60.53-
390MethylationHGYTGPPRPPPYGYQ
CCCCCCCCCCCCCCC		60.5352718107
398MethylationPPPYGYQRGPLPPPR
CCCCCCCCCCCCCCC		39.9730763133
398DimethylationPPPYGYQRGPLPPPR
CCCCCCCCCCCCCCC		39.97-
409MethylationPPPRPTPRPPVPPRG
CCCCCCCCCCCCCCC		51.1130763139
409DimethylationPPPRPTPRPPVPPRG
CCCCCCCCCCCCCCC		51.11-
415MethylationPRPPVPPRGPLRGPL
CCCCCCCCCCCCCCC		53.9830763145
415DimethylationPRPPVPPRGPLRGPL
CCCCCCCCCCCCCCC		53.98-
419MethylationVPPRGPLRGPLPQ--
CCCCCCCCCCCCC--		48.0624395699
419DimethylationVPPRGPLRGPLPQ--
CCCCCCCCCCCCC--		48.06-
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 SF3B4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SF3B4_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 SF3B4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CREST_HUMANSS18L1physical
16189514
SF3B2_HUMANSF3B2physical
16189514
BMR1A_HUMANBMPR1Aphysical
15351706
SF3B2_HUMANSF3B2physical
7958871
SMD2_HUMANSNRPD2physical
22939629
SF3B5_HUMANSF3B5physical
22939629
THOC4_HUMANALYREFphysical
22939629
SRRM2_HUMANSRRM2physical
22939629
MPLKI_HUMANMPLKIPphysical
22939629
UBC9_HUMANUBE2Iphysical
22939629
SRPRB_HUMANSRPRBphysical
22939629
VAPA_HUMANVAPAphysical
22939629
TBL2_HUMANTBL2physical
22939629
THIM_HUMANACAA2physical
22939629
RIDA_HUMANHRSP12physical
22939629
YTHD1_HUMANYTHDF1physical
22939629
STOM_HUMANSTOMphysical
22939629
THIK_HUMANACAA1physical
22939629
TIAR_HUMANTIAL1physical
22939629
UBE4B_HUMANUBE4Bphysical
22939629
SSBP_HUMANSSBP1physical
22939629
ZC11A_HUMANZC3H11Aphysical
22939629
TIM13_HUMANTIMM13physical
22939629
VDAC3_HUMANVDAC3physical
22939629
SLIRP_HUMANSLIRPphysical
22939629
SF3B2_HUMANSF3B2physical
22365833
CHERP_HUMANCHERPphysical
22365833
RBM10_HUMANRBM10physical
22365833
SF01_HUMANSF1physical
22365833
ILF3_HUMANILF3physical
22365833
SRSF6_HUMANSRSF6physical
22365833
PRP8_HUMANPRPF8physical
22365833
U5S1_HUMANEFTUD2physical
22365833
SPF27_HUMANBCAS2physical
22365833
WDR83_HUMANWDR83physical
22365833
DDX42_HUMANDDX42physical
22365833
DDX17_HUMANDDX17physical
22365833
HNRL1_HUMANHNRNPUL1physical
22365833
RBM4_HUMANRBM4physical
22365833
MEP50_HUMANWDR77physical
22365833
HNRPD_HUMANHNRNPDphysical
22365833
HNRPF_HUMANHNRNPFphysical
22365833
HNRH1_HUMANHNRNPH1physical
22365833
BAIP2_HUMANBAIAP2physical
25416956
SF3B2_HUMANSF3B2physical
25416956
HNRL1_HUMANHNRNPUL1physical
25416956
CREST_HUMANSS18L1physical
25416956
PP16B_HUMANPPP1R16Bphysical
25416956
HSPB7_HUMANHSPB7physical
25416956
NUB1_HUMANNUB1physical
25416956
UBS3A_HUMANUBASH3Aphysical
25416956
ZCH10_HUMANZCCHC10physical
25416956
MET17_HUMANMETTL17physical
25416956
C19L2_HUMANCWF19L2physical
25416956
SF3A1_HUMANSF3A1physical
26344197
SF3A2_HUMANSF3A2physical
26344197
SF3B3_HUMANSF3B3physical
26344197
FRK_HUMANFRKphysical
21516116
TCAF1_HUMANFAM115Aphysical
21516116
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
154400Acrofacial dysostosis 1, Nager type (AFD1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SF3B4_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 ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-16, AND MASSSPECTROMETRY.
"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-56, AND MASSSPECTROMETRY.

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