SYF1_HUMAN - dbPTM
SYF1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYF1_HUMAN
UniProt AC Q9HCS7
Protein Name Pre-mRNA-splicing factor SYF1
Gene Name XAB2
Organism Homo sapiens (Human).
Sequence Length 855
Subcellular Localization Nucleus . Detected in the splicing complex carrying pre-mRNA.
Protein Description Involved in pre-mRNA splicing as component of the spliceosome. [PubMed: 11991638]
Protein Sequence MVVMARLSRPERPDLVFEEEDLPYEEEIMRNQFSVKCWLRYIEFKQGAPKPRLNQLYERALKLLPCSYKLWYRYLKARRAQVKHRCVTDPAYEDVNNCHERAFVFMHKMPRLWLDYCQFLMDQGRVTHTRRTFDRALRALPITQHSRIWPLYLRFLRSHPLPETAVRGYRRFLKLSPESAEEYIEYLKSSDRLDEAAQRLATVVNDERFVSKAGKSNYQLWHELCDLISQNPDKVQSLNVDAIIRGGLTRFTDQLGKLWCSLADYYIRSGHFEKARDVYEEAIRTVMTVRDFTQVFDSYAQFEESMIAAKMETASELGREEEDDVDLELRLARFEQLISRRPLLLNSVLLRQNPHHVHEWHKRVALHQGRPREIINTYTEAVQTVDPFKATGKPHTLWVAFAKFYEDNGQLDDARVILEKATKVNFKQVDDLASVWCQCGELELRHENYDEALRLLRKATALPARRAEYFDGSEPVQNRVYKSLKVWSMLADLEESLGTFQSTKAVYDRILDLRIATPQIVINYAMFLEEHKYFEESFKAYERGISLFKWPNVSDIWSTYLTKFIARYGGRKLERARDLFEQALDGCPPKYAKTLYLLYAQLEEEWGLARHAMAVYERATRAVEPAQQYDMFNIYIKRAAEIYGVTHTRGIYQKAIEVLSDEHAREMCLRFADMECKLGEIDRARAIYSFCSQICDPRTTGAFWQTWKDFEVRHGNEDTIKEMLRIRRSVQATYNTQVNFMASQMLKVSGSATGTVSDLAPGQSGMDDMKLLEQRAEQLAAEAERDQPLRAQSKILFVRSDASREELAELAQQVNPEEIQLGEDEDEDEMDLEPNEVRLEQQSVPAAVFGSLKED
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
8PhosphorylationMVVMARLSRPERPDL
CCEEECCCCCCCCCC		39.9925159151
36UbiquitinationMRNQFSVKCWLRYIE
HHCCCHHHHHHHHHH		20.63-
36AcetylationMRNQFSVKCWLRYIE
HHCCCHHHHHHHHHH		20.6326051181
45UbiquitinationWLRYIEFKQGAPKPR
HHHHHHHHCCCCCCC		34.7224816145
62UbiquitinationQLYERALKLLPCSYK
HHHHHHHHHHCCCHH		47.1727667366
62AcetylationQLYERALKLLPCSYK
HHHHHHHHHHCCCHH		47.1725953088
66S-nitrosylationRALKLLPCSYKLWYR
HHHHHHCCCHHHHHH		7.5724105792
68PhosphorylationLKLLPCSYKLWYRYL
HHHHCCCHHHHHHHH		19.4729759185
69AcetylationKLLPCSYKLWYRYLK
HHHCCCHHHHHHHHH		19.0926051181
69UbiquitinationKLLPCSYKLWYRYLK
HHHCCCHHHHHHHHH		19.09-
72PhosphorylationPCSYKLWYRYLKARR
CCCHHHHHHHHHHHH		10.3829759185
174UbiquitinationRGYRRFLKLSPESAE
HHHHHHHHCCHHHHH		44.1821906983
176PhosphorylationYRRFLKLSPESAEEY
HHHHHHCCHHHHHHH		25.6528348404
183PhosphorylationSPESAEEYIEYLKSS
CHHHHHHHHHHHHCC		7.20-
188UbiquitinationEEYIEYLKSSDRLDE
HHHHHHHHCCCCHHH		47.1921906983
212UbiquitinationNDERFVSKAGKSNYQ
CCHHHHHCCCCCHHH		56.7227667366
215UbiquitinationRFVSKAGKSNYQLWH
HHHHCCCCCHHHHHH		40.1529967540
279PhosphorylationFEKARDVYEEAIRTV
HHHHHHHHHHHHHHH		16.6120860994
285PhosphorylationVYEEAIRTVMTVRDF
HHHHHHHHHHCHHHH		14.4428270605
288PhosphorylationEAIRTVMTVRDFTQV
HHHHHHHCHHHHHHH		14.1928270605
293PhosphorylationVMTVRDFTQVFDSYA
HHCHHHHHHHHHHHH		28.2828270605
298PhosphorylationDFTQVFDSYAQFEES
HHHHHHHHHHHHHHH		15.7628270605
299PhosphorylationFTQVFDSYAQFEESM
HHHHHHHHHHHHHHH		13.2828270605
305PhosphorylationSYAQFEESMIAAKME
HHHHHHHHHHHHHHH		14.3228270605
313PhosphorylationMIAAKMETASELGRE
HHHHHHHHHHHHCCC		31.8029523821
315PhosphorylationAAKMETASELGREEE
HHHHHHHHHHCCCCC		40.5529523821
389UbiquitinationVQTVDPFKATGKPHT
HHHCCCCCCCCCCCE		50.8829967540
393UbiquitinationDPFKATGKPHTLWVA
CCCCCCCCCCEEEEE		29.30-
420AcetylationDARVILEKATKVNFK
CHHHHHHHCCCCCCC		58.8919608861
420UbiquitinationDARVILEKATKVNFK
CHHHHHHHCCCCCCC		58.8921906983
423UbiquitinationVILEKATKVNFKQVD
HHHHHCCCCCCCCHH		39.7922817900
458UbiquitinationEALRLLRKATALPAR
HHHHHHHHHHCCCCH		50.4827667366
460PhosphorylationLRLLRKATALPARRA
HHHHHHHHCCCCHHH		31.5924719451
469PhosphorylationLPARRAEYFDGSEPV
CCCHHHHHCCCCCCC		13.1427642862
479MethylationGSEPVQNRVYKSLKV
CCCCCHHHHHHHHHH		18.95115920109
482UbiquitinationPVQNRVYKSLKVWSM
CCHHHHHHHHHHHHH		46.59-
496PhosphorylationMLADLEESLGTFQST
HHHHHHHHHCCCHHH		23.79-
499PhosphorylationDLEESLGTFQSTKAV
HHHHHHCCCHHHHHH		24.6418491316
539UbiquitinationKYFEESFKAYERGIS
HHHHHHHHHHHHCCC		60.3821906983
546PhosphorylationKAYERGISLFKWPNV
HHHHHCCCCCCCCCH		30.4924719451
590UbiquitinationALDGCPPKYAKTLYL
HHCCCCHHHHHHHHH		42.8729967540
590AcetylationALDGCPPKYAKTLYL
HHCCCCHHHHHHHHH		42.8726051181
593UbiquitinationGCPPKYAKTLYLLYA
CCCHHHHHHHHHHHH		35.65-
620PhosphorylationMAVYERATRAVEPAQ
HHHHHHHHCCCCHHH		25.94-
637UbiquitinationDMFNIYIKRAAEIYG
CCHHHHHHHHHHHHC		21.0021906983
654UbiquitinationHTRGIYQKAIEVLSD
CCCCHHHHHHHHHCH		34.0721906983
677UbiquitinationRFADMECKLGEIDRA
HHHCCCCCCCCHHHH		46.3421906983
6772-HydroxyisobutyrylationRFADMECKLGEIDRA
HHHCCCCCCCCHHHH		46.34-
692PhosphorylationRAIYSFCSQICDPRT
HHHHHHHHHHCCCCC		22.1423532336
706PhosphorylationTTGAFWQTWKDFEVR
CCCHHHHHHHHEEHH		25.69-
708UbiquitinationGAFWQTWKDFEVRHG
CHHHHHHHHEEHHHC		56.7922817900
721UbiquitinationHGNEDTIKEMLRIRR
HCCHHHHHHHHHHHH		38.8821906983
733PhosphorylationIRRSVQATYNTQVNF
HHHHHHCHHHHHHHH		10.5429116813
734PhosphorylationRRSVQATYNTQVNFM
HHHHHCHHHHHHHHH		21.1629116813
736PhosphorylationSVQATYNTQVNFMAS
HHHCHHHHHHHHHHH		24.3929116813
743PhosphorylationTQVNFMASQMLKVSG
HHHHHHHHHHHEECC		12.3429978859
749PhosphorylationASQMLKVSGSATGTV
HHHHHEECCCCCCCH		25.9925627689
751PhosphorylationQMLKVSGSATGTVSD
HHHEECCCCCCCHHH		18.3625627689
753PhosphorylationLKVSGSATGTVSDLA
HEECCCCCCCHHHCC		34.7725627689
755PhosphorylationVSGSATGTVSDLAPG
ECCCCCCCHHHCCCC		16.6928555341
770UbiquitinationQSGMDDMKLLEQRAE
CCCCCHHHHHHHHHH		57.8421906983
793PhosphorylationDQPLRAQSKILFVRS
CCCCHHHCEEEEECC		22.2228555341
794AcetylationQPLRAQSKILFVRSD
CCCHHHCEEEEECCC		31.2025953088
794UbiquitinationQPLRAQSKILFVRSD
CCCHHHCEEEEECCC		31.2023000965
800PhosphorylationSKILFVRSDASREEL
CEEEEECCCCCHHHH		32.0222210691
803PhosphorylationLFVRSDASREELAEL
EEECCCCCHHHHHHH		45.2622210691
843PhosphorylationEVRLEQQSVPAAVFG
CHHHHHHCCCHHHHC		29.7528555341
851PhosphorylationVPAAVFGSLKED---
CCHHHHCCCCCC---		25.4630266825
853UbiquitinationAAVFGSLKED-----
HHHHCCCCCC-----		62.6321906983
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 SYF1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYF1_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 SYF1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERCC8_HUMANERCC8physical
10944529
RPB1_HUMANPOLR2Aphysical
10944529
ERCC6_HUMANERCC6physical
10944529
SF3B2_HUMANSF3B2physical
22365833
ILF3_HUMANILF3physical
22365833
ISY1_HUMANISY1physical
22365833
SNW1_HUMANSNW1physical
22365833
PPIE_HUMANPPIEphysical
22365833
RED_HUMANIKphysical
22365833
DHX16_HUMANDHX16physical
22365833
AQR_HUMANAQRphysical
26344197
PRP17_HUMANCDC40physical
26344197
CRNL1_HUMANCRNKL1physical
26344197
DDX23_HUMANDDX23physical
26344197
DHX15_HUMANDHX15physical
26344197
U5S1_HUMANEFTUD2physical
26344197
ISY1_HUMANISY1physical
26344197
PLRG1_HUMANPLRG1physical
26344197
PRP19_HUMANPRPF19physical
26344197
PRPF3_HUMANPRPF3physical
26344197
PRP31_HUMANPRPF31physical
26344197
SF3A1_HUMANSF3A1physical
26344197
SF3B3_HUMANSF3B3physical
26344197
U520_HUMANSNRNP200physical
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 SYF1_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-420, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-851, AND MASSSPECTROMETRY.

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