SYF2_HUMAN - dbPTM
SYF2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYF2_HUMAN
UniProt AC O95926
Protein Name Pre-mRNA-splicing factor SYF2
Gene Name SYF2
Organism Homo sapiens (Human).
Sequence Length 243
Subcellular Localization Nucleus .
Protein Description Involved in pre-mRNA splicing as component of the spliceosome. [PubMed: 11991638]
Protein Sequence MAAIAASEVLVDSAEEGSLAAAAELAAQKREQRLRKFRELHLMRNEARKLNHQEVVEEDKRLKLPANWEAKKARLEWELKEEEKKKECAARGEDYEKVKLLEISAEDAERWERKKKRKNPDLGFSDYAAAQLRQYHRLTKQIKPDMETYERLREKHGEEFFPTSNSLLHGTHVPSTEEIDRMVIDLEKQIEKRDKYSRRRPYNDDADIDYINERNAKFNKKAERFYGKYTAEIKQNLERGTAV
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------MAAIAASEV
------CCCHHHCCE		13.9422814378
7Phosphorylation-MAAIAASEVLVDSA
-CCCHHHCCEECCCC		21.1521406692
13PhosphorylationASEVLVDSAEEGSLA
HCCEECCCCHHCHHH		30.0528464451
18PhosphorylationVDSAEEGSLAAAAEL
CCCCHHCHHHHHHHH		20.3628464451
60UbiquitinationQEVVEEDKRLKLPAN
HHHHHHHHCCCCCCC		64.0124816145
95PhosphorylationCAARGEDYEKVKLLE
HHHCCCCHHHHEEEE		17.2228796482
104PhosphorylationKVKLLEISAEDAERW
HHEEEEECHHHHHHH		19.0721815630
113UbiquitinationEDAERWERKKKRKNP
HHHHHHHHHHHHCCC		49.4829967540
127PhosphorylationPDLGFSDYAAAQLRQ
CCCCCCHHHHHHHHH		9.2828674419
143AcetylationHRLTKQIKPDMETYE
HHHHHHCCCCHHHHH		32.2526051181
143SumoylationHRLTKQIKPDMETYE
HHHHHHCCCCHHHHH		32.2528112733
143SumoylationHRLTKQIKPDMETYE
HHHHHHCCCCHHHHH		32.25-
146UbiquitinationTKQIKPDMETYERLR
HHHCCCCHHHHHHHH		5.8624816145
148PhosphorylationQIKPDMETYERLREK
HCCCCHHHHHHHHHH		24.8424043423
149PhosphorylationIKPDMETYERLREKH
CCCCHHHHHHHHHHH		5.9224043423
155UbiquitinationTYERLREKHGEEFFP
HHHHHHHHHCCCCCC		50.9429967540
164PhosphorylationGEEFFPTSNSLLHGT
CCCCCCCCCCCCCCC		25.3427251275
166PhosphorylationEFFPTSNSLLHGTHV
CCCCCCCCCCCCCCC		31.8827251275
171PhosphorylationSNSLLHGTHVPSTEE
CCCCCCCCCCCCHHH		14.6728555341
175PhosphorylationLHGTHVPSTEEIDRM
CCCCCCCCHHHHHHH		47.5728348404
175UbiquitinationLHGTHVPSTEEIDRM
CCCCCCCCHHHHHHH		47.5724816145
176PhosphorylationHGTHVPSTEEIDRMV
CCCCCCCHHHHHHHH		31.4128348404
188UbiquitinationRMVIDLEKQIEKRDK
HHHHCHHHHHHHHHH		64.9724816145
192UbiquitinationDLEKQIEKRDKYSRR
CHHHHHHHHHHCCCC		68.4729967540
196PhosphorylationQIEKRDKYSRRRPYN
HHHHHHHCCCCCCCC		16.23-
210PhosphorylationNDDADIDYINERNAK
CCCCCCHHHHHHCHH		13.1428796482
217UbiquitinationYINERNAKFNKKAER
HHHHHCHHHHHHHHH		53.6824816145
226PhosphorylationNKKAERFYGKYTAEI
HHHHHHHHCHHHHHH		20.9422817900
228AcetylationKAERFYGKYTAEIKQ
HHHHHHCHHHHHHHH		28.2225953088
229PhosphorylationAERFYGKYTAEIKQN
HHHHHCHHHHHHHHH		13.5622817900
234UbiquitinationGKYTAEIKQNLERGT
CHHHHHHHHHHHCCC		25.3329967540
234SumoylationGKYTAEIKQNLERGT
CHHHHHHHHHHHCCC		25.3328112733
234SumoylationGKYTAEIKQNLERGT
CHHHHHHHHHHHCCC		25.33-
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 SYF2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYF2_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 SYF2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MCM3_HUMANMCM3physical
16951160
CCDB1_HUMANCCNDBP1physical
16951160
A4_HUMANAPPphysical
21832049
GPTC1_HUMANGPATCH1physical
28514442
PPIE_HUMANPPIEphysical
28514442
WDR83_HUMANWDR83physical
28514442
C19L2_HUMANCWF19L2physical
28514442
DHX35_HUMANDHX35physical
28514442
PRP17_HUMANCDC40physical
28514442
AQR_HUMANAQRphysical
28514442
CRNL1_HUMANCRNKL1physical
28514442
SYF1_HUMANXAB2physical
28514442
GCFC2_HUMANGCFC2physical
28514442
ISY1_HUMANISY1physical
28514442
PRP19_HUMANPRPF19physical
28514442
SNW1_HUMANSNW1physical
28514442
RU2A_HUMANSNRPA1physical
28514442
CCD12_HUMANCCDC12physical
28514442
RBM22_HUMANRBM22physical
28514442
BUD31_HUMANBUD31physical
28514442
DGC14_HUMANDGCR14physical
28514442
PLRG1_HUMANPLRG1physical
28514442
CDC5L_HUMANCDC5Lphysical
28514442
C19L1_HUMANCWF19L1physical
28514442
BTBD1_HUMANBTBD1physical
28514442
SPF27_HUMANBCAS2physical
28514442
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 SYF2_HUMAN

loading...

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.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory