SFR15_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SFR15_HUMAN
• UniProt AC: O95104
• Protein Name: Splicing factor, arginine/serine-rich 15
• Gene Name: SCAF4
• Organism: Homo sapiens (Human).
• Sequence Length: 1147
• Subcellular Localization: Nucleus.
• Protein Description: May act to physically and functionally link transcription and pre-mRNA processing..
• Protein Sequence: MDAVNAFNQELFSLMDMKPPISRAKMILITKAAIKAIKLYKHVVQIVEKFIKKCKPEYKVPGLYVIDSIVRQSRHQFGTDKDVFGPRFSKNITATFQYLYLCPSEDKSKIVRVLNLWQKNGVFKIEIIQPLLDMAAGTSNAAPVAENVTNNEGSPPPPVKVSSEPPTQATPNSVPAVPQLPSSDAFAAVAQLFQTTQGQQLQQILQTFQQPPKPQSPALDNAVMAQVQAITAQLKTTPTQPSEQKAAFPPPEQKTAFDKKLLDRFDYDDEPEAVEESKKEDTTAVTTTAPAAAVPPAPTATVPAAAAPAAASPPPPQAPFGFPGDGMQQPAYTQHQNMDQFQPRMMGIQQDPMHHQVPLPPNGQMPGFGLLPTPPFPPMAQPVIPPTPPVQQPFQASFQAQNEPLTQKPHQQEMEVEQPCIQEVKRHMSDNRKSRSRSASRSPKRRRSRSGSRSRRSRHRRSRSRSRDRRRHSPRSRSQERRDREKERERRQKGLPQVKPETASVCSTTLWVGQLDKRTTQQDVASLLEEFGPIESINMIPPRGCAYIVMVHRQDAYRALQKLSRGNYKVNQKSIKIAWALNKGIKADYKQYWDVELGVTYIPWDKVKPEELESFCEGGMLDSDTLNPDWKGIPKKPENEVAQNGGAETSHTEPVSPIPKPLPVPVPPIPVPAPITVPPPQVPPHQPGPPVVGALQPPAFTPPLGIPPPGFGPGVPPPPPPPPFLRPGFNPMHLPPGFLPPGPPPPITPPVSIPPPHTPPISIPNSTIAGINEDTTKDLSIGNPIPTVVSGARGNAESGDSVKMYGSAVPPAAPTNLPTPPVTQPVSLLGTQGVAPGPVIGLQAPSTGLLGARPGLIPLQRPPGMPPPHLQRFPLMPPRPMPPHMMHRGPPPGPGGFAMPPPHGMKGPFPPHGPFVRPGGMPGLGGPGPGPGGPEDRDGRQQPPQQPQQQPQPQAPQQPQQQQQQQPPPSQQPPPTQQQPQQFRNDNRQQFNSGRDQERFGRRSFGNRVENDRERYGNRNDDRDNSNRDRREWGRRSPDRDRHRDLEERNRRSSGHRDRERDSRDRESRREKEEARGKEKPEVTDRAGGNKTVEPPISQVGNVDTASELEKGVSEAAVLKPSEELPAEATSSVEPEKDSGSAAEAPR

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
41	Acetylation	IKAIKLYKHVVQIVE HHHHHHHHHHHHHHH	40.12	26051181
104	Ubiquitination	QYLYLCPSEDKSKIV EEEEECCCCCHHHHH	58.38	21890473
119	Acetylation	RVLNLWQKNGVFKIE HHHHHHHHCCEEEEE	44.05	25953088
119 (in isoform 1)	Ubiquitination	-	44.05	21890473
119 (in isoform 2)	Ubiquitination	-	44.05	21890473
517	Acetylation	LWVGQLDKRTTQQDV EEEECCCCCCCHHHH	61.30	26051181
562	Acetylation	DAYRALQKLSRGNYK HHHHHHHHHHCCCCC	49.64	25953088
568	Ubiquitination	QKLSRGNYKVNQKSI HHHHCCCCCCCHHHH	21.09	21890473
576	Acetylation	KVNQKSIKIAWALNK CCCHHHHHHHHHHHC	33.20	25953088
583 (in isoform 1)	Ubiquitination	-	63.96	21890473
583 (in isoform 2)	Ubiquitination	-	63.96	21890473
616	Glutathionylation	PEELESFCEGGMLDS HHHHHHHHHCCCCCC	7.08	22555962
1078	Acetylation	EKEEARGKEKPEVTD HHHHHCCCCCCCCCC	57.94	26051181
1080	Acetylation	EEARGKEKPEVTDRA HHHCCCCCCCCCCCC	50.38	25953088
1091	Acetylation	TDRAGGNKTVEPPIS CCCCCCCCCCCCCHH	58.17	26051181

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SFR15_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SFR15_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SFR15_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SH3L1_HUMAN	SH3BGRL	physical	22939629
SVIL_HUMAN	SVIL	physical	22939629
UCRI_HUMAN	UQCRFS1	physical	22939629
TXD17_HUMAN	TXNDC17	physical	22939629
VINC_HUMAN	VCL	physical	22939629
VMA21_HUMAN	VMA21	physical	22939629
SUCB2_HUMAN	SUCLG2	physical	22939629
UPAR_HUMAN	PLAUR	physical	22939629
SPT2_HUMAN	SPTY2D1	physical	22939629
VAPB_HUMAN	VAPB	physical	22939629
CDK12_HUMAN	CDK12	physical	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.

Related Literatures of Post-Translational Modification

Acetylation

"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-49, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND MASSSPECTROMETRY.
PubMed: 19690332

"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND MASSSPECTROMETRY.
PubMed: 19413330

"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-154, AND MASSSPECTROMETRY.
PubMed: 18669648

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-656 AND SER-1037, ANDMASS SPECTROMETRY.
PubMed: 17081983

"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154 AND THR-237, ANDMASS SPECTROMETRY.
PubMed: 15302935