SCAF11

Functionⁱ

Plays a role in pre-mRNA alternative splicing by regulating spliceosome assembly.1 Publication

Regions

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Zinc fingerⁱ	41 – 82	42	RING-type; degeneratePROSITE-ProRule annotation Manual assertion according to rulesⁱ PROSITE-ProRule:PRU00175			Add BLAST

GO - Molecular functionⁱ

poly(A) RNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 22658674
- 22681889
zinc ion binding Source: InterPro

GO - Biological processⁱ

mRNA processing
Source: ProtInc
Traceable author statementⁱ
- 9447963
RNA splicing
Source: UniProtKB
Inferred from direct assayⁱ
- 9447963
RNA splicing, via transesterification reactions
Source: UniProtKB
Inferred from direct assayⁱ
- 9447963
spliceosomal complex assembly
Source: UniProtKB
Inferred from direct assayⁱ
- 9447963

Complete GO annotation...

Keywords - Biological processⁱ

mRNA processing, mRNA splicing

Keywords - Ligandⁱ

Metal-binding, Zinc

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Protein SCAF11 Alternative name(s): CTD-associated SR protein 11 Renal carcinoma antigen NY-REN-40 SC35-interacting protein 1 SR-related and CTD-associated factor 11 SRSF2-interacting protein Serine/arginine-rich splicing factor 2-interacting protein Splicing factor, arginine/serine-rich 2-interacting protein Splicing regulatory protein 129 Short name: SRrp129
Gene namesⁱ	Name:SCAF11 Synonyms:CASP11, SFRS2IP, SIP1, SRSF2IP
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640: Chromosome 12

Organism-specific databases

HGNCⁱ	HGNC:10784. SCAF11.

HGNCⁱ

HGNC:10784. SCAF11.

Subcellular locationⁱ

Nucleus 1 Publication

GO - Cellular componentⁱ

nucleolus Source: HPA
nucleoplasm Source: HPA
nucleus Source: HPA

Complete GO annotation...

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Organism-specific databases

PharmGKBⁱ	PA35700.

PharmGKBⁱ

PA35700.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Chainⁱ	1 – 1463	1463	Protein SCAF11		PRO_0000076314	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description
Modified residueⁱ	338 – 338	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.10 "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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-341; SER-344; SER-405; THR-410; SER-533; SER-608; SER-614; SER-680; SER-796; SER-802; THR-807; SER-963 AND SER-1127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	341 – 341	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.10 "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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-341; SER-344; SER-405; THR-410; SER-533; SER-608; SER-614; SER-680; SER-796; SER-802; THR-807; SER-963 AND SER-1127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	344 – 344	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.10 "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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-341; SER-344; SER-405; THR-410; SER-533; SER-608; SER-614; SER-680; SER-796; SER-802; THR-807; SER-963 AND SER-1127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	400 – 400	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.15 "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400; SER-401; SER-402; SER-405; THR-769; SER-776; SER-796 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	401 – 401	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.15 "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400; SER-401; SER-402; SER-405; THR-769; SER-776; SER-796 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	402 – 402	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.15 "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400; SER-401; SER-402; SER-405; THR-769; SER-776; SER-796 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	405 – 405	1	Phosphoserine5 Publications Manual assertion based on experiment inⁱ Ref.7 "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-723 AND SER-726, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.10 "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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-341; SER-344; SER-405; THR-410; SER-533; SER-608; SER-614; SER-680; SER-796; SER-802; THR-807; SER-963 AND SER-1127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.12 "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-413; SER-608; SER-796; SER-798 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.13 "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-608; SER-614; SER-680; SER-687; SER-771; SER-776; SER-796; SER-1127 AND SER-1169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.15 "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400; SER-401; SER-402; SER-405; THR-769; SER-776; SER-796 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	410 – 410	1	Phosphothreonine1 Publication Manual assertion based on experiment inⁱ Ref.10 "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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-341; SER-344; SER-405; THR-410; SER-533; SER-608; SER-614; SER-680; SER-796; SER-802; THR-807; SER-963 AND SER-1127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	413 – 413	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.12 "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-413; SER-608; SER-796; SER-798 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	533 – 533	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.10 "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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-341; SER-344; SER-405; THR-410; SER-533; SER-608; SER-614; SER-680; SER-796; SER-802; THR-807; SER-963 AND SER-1127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	608 – 608	1	Phosphoserine4 Publications Manual assertion based on experiment inⁱ Ref.9 "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.10 "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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-341; SER-344; SER-405; THR-410; SER-533; SER-608; SER-614; SER-680; SER-796; SER-802; THR-807; SER-963 AND SER-1127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.12 "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-413; SER-608; SER-796; SER-798 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.13 "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-608; SER-614; SER-680; SER-687; SER-771; SER-776; SER-796; SER-1127 AND SER-1169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	614 – 614	1	Phosphoserine2 Publications Manual assertion based on experiment inⁱ Ref.10 "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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-341; SER-344; SER-405; THR-410; SER-533; SER-608; SER-614; SER-680; SER-796; SER-802; THR-807; SER-963 AND SER-1127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.13 "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-608; SER-614; SER-680; SER-687; SER-771; SER-776; SER-796; SER-1127 AND SER-1169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	680 – 680	1	Phosphoserine2 Publications Manual assertion based on experiment inⁱ Ref.10 "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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-341; SER-344; SER-405; THR-410; SER-533; SER-608; SER-614; SER-680; SER-796; SER-802; THR-807; SER-963 AND SER-1127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.13 "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-608; SER-614; SER-680; SER-687; SER-771; SER-776; SER-796; SER-1127 AND SER-1169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	687 – 687	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.13 "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-608; SER-614; SER-680; SER-687; SER-771; SER-776; SER-796; SER-1127 AND SER-1169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	723 – 723	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.7 "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-723 AND SER-726, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	726 – 726	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.7 "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-723 AND SER-726, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	769 – 769	1	Phosphothreonine1 Publication Manual assertion based on experiment inⁱ Ref.15 "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400; SER-401; SER-402; SER-405; THR-769; SER-776; SER-796 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	771 – 771	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.13 "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-608; SER-614; SER-680; SER-687; SER-771; SER-776; SER-796; SER-1127 AND SER-1169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	776 – 776	1	Phosphoserine2 Publications Manual assertion based on experiment inⁱ Ref.13 "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-608; SER-614; SER-680; SER-687; SER-771; SER-776; SER-796; SER-1127 AND SER-1169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.15 "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400; SER-401; SER-402; SER-405; THR-769; SER-776; SER-796 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	796 – 796	1	Phosphoserine4 Publications Manual assertion based on experiment inⁱ Ref.10 "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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-341; SER-344; SER-405; THR-410; SER-533; SER-608; SER-614; SER-680; SER-796; SER-802; THR-807; SER-963 AND SER-1127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.12 "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-413; SER-608; SER-796; SER-798 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.13 "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-608; SER-614; SER-680; SER-687; SER-771; SER-776; SER-796; SER-1127 AND SER-1169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.15 "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400; SER-401; SER-402; SER-405; THR-769; SER-776; SER-796 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	798 – 798	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.12 "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-413; SER-608; SER-796; SER-798 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	802 – 802	1	Phosphoserine3 Publications Manual assertion based on experiment inⁱ Ref.10 "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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-341; SER-344; SER-405; THR-410; SER-533; SER-608; SER-614; SER-680; SER-796; SER-802; THR-807; SER-963 AND SER-1127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.12 "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-413; SER-608; SER-796; SER-798 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.15 "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400; SER-401; SER-402; SER-405; THR-769; SER-776; SER-796 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	807 – 807	1	Phosphothreonine1 Publication Manual assertion based on experiment inⁱ Ref.10 "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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-341; SER-344; SER-405; THR-410; SER-533; SER-608; SER-614; SER-680; SER-796; SER-802; THR-807; SER-963 AND SER-1127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	963 – 963	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.10 "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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-341; SER-344; SER-405; THR-410; SER-533; SER-608; SER-614; SER-680; SER-796; SER-802; THR-807; SER-963 AND SER-1127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1127 – 1127	1	Phosphoserine2 Publications Manual assertion based on experiment inⁱ Ref.10 "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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-341; SER-344; SER-405; THR-410; SER-533; SER-608; SER-614; SER-680; SER-796; SER-802; THR-807; SER-963 AND SER-1127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.13 "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-608; SER-614; SER-680; SER-687; SER-771; SER-776; SER-796; SER-1127 AND SER-1169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1169 – 1169	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.13 "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-608; SER-614; SER-680; SER-687; SER-771; SER-776; SER-796; SER-1127 AND SER-1169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

MaxQBⁱ	Q99590.
PaxDbⁱ	Q99590.
PRIDEⁱ	Q99590.

PTM databases

PhosphoSiteⁱ	Q99590.

PhosphoSiteⁱ

Q99590.

Miscellaneous databases

PMAP-CutDB	Q99590.

PMAP-CutDB

Q99590.

Expressionⁱ

Tissue specificityⁱ

Widely expressed.1 Publication

Gene expression databases

Bgeeⁱ	Q99590.
CleanExⁱ	HS_SFRS2IP. HS_SIP1.
ExpressionAtlasⁱ	Q99590. baseline and differential.
Genevestigatorⁱ	Q99590.

Organism-specific databases

HPAⁱ	HPA038862. HPA045456. HPA046345.

Interactionⁱ

Subunit structureⁱ

Interacts with SRSF2/SFRS2, U2AF2 and SNRNP70.1 Publication

Protein-protein interaction databases

BioGridⁱ	114610. 15 interactions.
IntActⁱ	Q99590. 2 interactions.
MINTⁱ	MINT-2866162.
STRINGⁱ	9606.ENSP00000358374.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q99590.
SMRⁱ	Q99590. Positions 37-80.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Compositional bias

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Compositional biasⁱ	841 – 985	145	Arg-rich			Add BLAST
Compositional biasⁱ	1225 – 1285	61	Pro-rich			Add BLAST

Sequence similaritiesⁱ

Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Zinc fingerⁱ	41 – 82	42	RING-type; degeneratePROSITE-ProRule annotation Manual assertion according to rulesⁱ PROSITE-ProRule:PRU00175			Add BLAST

Keywords - Domainⁱ

Zinc-finger

Phylogenomic databases

eggNOGⁱ	NOG300312.
GeneTreeⁱ	ENSGT00530000063661.
HOVERGENⁱ	HBG101126.
InParanoidⁱ	Q99590.
OMAⁱ	YCTEFIE.
OrthoDBⁱ	EOG7F24SX.
PhylomeDBⁱ	Q99590.
TreeFamⁱ	TF332183.

Family and domain databases

Gene3Dⁱ	3.30.40.10. 1 hit.
InterProⁱ	IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR017907. Znf_RING_CS. [Graphical view]
Pfamⁱ	PF13639. zf-RING_2. 1 hit. [Graphical view]
SMARTⁱ	SM00184. RING. 1 hit. [Graphical view]
PROSITEⁱ	PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. [Graphical view]

Sequences (2)ⁱ

Sequence statusⁱ: Complete.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align

Isoform 1 (identifier: Q99590-1) [UniParc]FASTA Add to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKKKTVCTLN MGDKKYEDME GEENGDNTIS TGLLYSEADR CPICLNCLLE 
        60         70         80         90        100
KEVGFPESCN HVFCMTCILK WAETLASCPI DRKPFQAVFK FSALEGYVKV 
       110        120        130        140        150
QVKKQLRETK DKKNENSFEK QVSCHENSKS CIRRKAIVRE DLLSAKVCDL 
       160        170        180        190        200
KWIHRNSLYS ETGGKKNAAI KINKPQRSNW STNQCFRNFF SNMFSSVSHS 
       210        220        230        240        250
GESSFTYRAY CTEFIEASEI SALIRQKRHE LELSWFPDTL PGIGRIGFIP 
       260        270        280        290        300
WNVETEVLPL ISSVLPRTIF PTSTISFEHF GTSCKGYALA HTQEGEEKKQ 
       310        320        330        340        350
TSGTSNTRGS RRKPAMTTPT RRSTRNTRAE TASQSQRSPI SDNSGCDAPG 
       360        370        380        390        400
NSNPSLSVPS SAESEKQTRQ APKRKSVRRG RKPPLLKKKL RSSVAAPEKS 
       410        420        430        440        450
SSNDSVDEET AESDTSPVLE KEHQPDVDSS NICTVQTHVE NQSANCLKSC 
       460        470        480        490        500
NEQIEESEKH TANYDTEERV GSSSSESCAQ DLPVLVGEEG EVKKLENTGI 
       510        520        530        540        550
EANVLCLESE ISENILEKGG DPLEKQDQIS GLSQSEVKTD VCTVHLPNDF 
       560        570        580        590        600
PTCLTSESKV YQPVSCPLSD LSENVESVVN EEKITESSLV EITEHKDFTL 
       610        620        630        640        650
KTEELIESPK LESSEGEIIQ TVDRQSVKSP EVQLLGHVET EDVEIIATCD 
       660        670        680        690        700
TFGNEDFNNI QDSENNLLKN NLLNTKLEKS LEEKNESLTE HPRSTELPKT 
       710        720        730        740        750
HIEQIQKHFS EDNNEMIPME CDSFCSDQNE SEVEPSVNAD LKQMNENSVT 
       760        770        780        790        800
HCSENNMPSS DLADEKVETV SQPSESPKDT IDKTKKPRTR RSRFHSPSTT 
       810        820        830        840        850
WSPNKDTPQE KKRPQSPSPR RETGKESRKS QSPSPKNESA RGRKKSRSQS 
       860        870        880        890        900
PKKDIARERR QSQSRSPKRD TTRESRRSES LSPRRETSRE NKRSQPRVKD 
       910        920        930        940        950
SSPGEKSRSQ SRERESDRDG QRRERERRTR KWSRSRSHSR SPSRCRTKSK 
       960        970        980        990       1000
SSSFGRIDRD SYSPRWKGRW ANDGWRCPRG NDRYRKNDPE KQNENTRKEK 
      1010       1020       1030       1040       1050
NDIHLDADDP NSADKHRNDC PNWITEKINS GPDPRTRNPE KLKESHWEEN 
      1060       1070       1080       1090       1100
RNENSGNSWN KNFGSGWVSN RGRGRGNRGR GTYRSSFAYK DQNENRWQNR 
      1110       1120       1130       1140       1150
KPLSGNSNSS GSESFKFVEQ QSYKRKSEQE FSFDTPADRS GWTSASSWAV 
      1160       1170       1180       1190       1200
RKTLPADVQN YYSRRGRNSS GPQSGWMKQE EETSGQDSSL KDQTNQQVDG 
      1210       1220       1230       1240       1250
SQLPINMMQP QMNVMQQQMN AQHQPMNIFP YPVGVHAPLM NIQRNPFNIH 
      1260       1270       1280       1290       1300
PQLPLHLHTG VPLMQVATPT SVSQGLPPPP PPPPPSQQVN YIASQPDGKQ 
      1310       1320       1330       1340       1350
LQGIPSSSHV SNNMSTPVLP APTAAPGNTG MVQGPSSGNT SSSSHSKASN 
      1360       1370       1380       1390       1400
AAVKLAESKV SVAVEASADS SKTDKKLQIQ EKAAQEVKLA IKPFYQNKDI 
      1410       1420       1430       1440       1450
TKEEYKEIVR KAVDKVCHSK SGEVNSTKVA NLVKAYVDKY KYSRKGSQKK 
      1460 
TLEEPVSTEK NIG

Length:1,463

Mass (Da):164,652

Last modified:July 7, 2009 - v2

Checksum:ⁱ7170B88544BAF7D4

GO

Isoform 2 (identifier: Q99590-2) [UniParc]FASTA Add to Basket

The sequence of this isoform differs from the canonical sequence as follows:
1-315: Missing.

« Hide

        10         20         30         40         50
MTTPTRRSTR NTRAETASQS QRSPISDNSG CDAPGNSNPS LSVPSSAESE 
        60         70         80         90        100
KQTRQAPKRK SVRRGRKPPL LKKKLRSSVA APEKSSSNDS VDEETAESDT 
       110        120        130        140        150
SPVLEKEHQP DVDSSNICTV QTHVENQSAN CLKSCNEQIE ESEKHTANYD 
       160        170        180        190        200
TEERVGSSSS ESCAQDLPVL VGEEGEVKKL ENTGIEANVL CLESEISENI 
       210        220        230        240        250
LEKGGDPLEK QDQISGLSQS EVKTDVCTVH LPNDFPTCLT SESKVYQPVS 
       260        270        280        290        300
CPLSDLSENV ESVVNEEKIT ESSLVEITEH KDFTLKTEEL IESPKLESSE 
       310        320        330        340        350
GEIIQTVDRQ SVKSPEVQLL GHVETEDVEI IATCDTFGNE DFNNIQDSEN 
       360        370        380        390        400
NLLKNNLLNT KLEKSLEEKN ESLTEHPRST ELPKTHIEQI QKHFSEDNNE 
       410        420        430        440        450
MIPMECDSFC SDQNESEVEP SVNADLKQMN ENSVTHCSEN NMPSSDLADE 
       460        470        480        490        500
KVETVSQPSE SPKDTIDKTK KPRTRRSRFH SPSTTWSPNK DTPQEKKRPQ 
       510        520        530        540        550
SPSPRRETGK ESRKSQSPSP KNESARGRKK SRSQSPKKDI ARERRQSQSR 
       560        570        580        590        600
SPKRDTTRES RRSESLSPRR ETSRENKRSQ PRVKDSSPGE KSRSQSRERE 
       610        620        630        640        650
SDRDGQRRER ERRTRKWSRS RSHSRSPSRC RTKSKSSSFG RIDRDSYSPR 
       660        670        680        690        700
WKGRWANDGW RCPRGNDRYR KNDPEKQNEN TRKEKNDIHL DADDPNSADK 
       710        720        730        740        750
HRNDCPNWIT EKINSGPDPR TRNPEKLKES HWEENRNENS GNSWNKNFGS 
       760        770        780        790        800
GWVSNRGRGR GNRGRGTYRS SFAYKDQNEN RWQNRKPLSG NSNSSGSESF 
       810        820        830        840        850
KFVEQQSYKR KSEQEFSFDT PADRSGWTSA SSWAVRKTLP ADVQNYYSRR 
       860        870        880        890        900
GRNSSGPQSG WMKQEEETSG QDSSLKDQTN QQVDGSQLPI NMMQPQMNVM 
       910        920        930        940        950
QQQMNAQHQP MNIFPYPVGV HAPLMNIQRN PFNIHPQLPL HLHTGVPLMQ 
       960        970        980        990       1000
VATPTSVSQG LPPPPPPPPP SQQVNYIASQ PDGKQLQGIP SSSHVSNNMS 
      1010       1020       1030       1040       1050
TPVLPAPTAA PGNTGMVQGP SSGNTSSSSH SKASNAAVKL AESKVSVAVE 
      1060       1070       1080       1090       1100
ASADSSKTDK KLQIQEKAAQ EVKLAIKPFY QNKDITKEEY KEIVRKAVDK 
      1110       1120       1130       1140 
VCHSKSGEVN STKVANLVKA YVDKYKYSRK GSQKKTLEEP VSTEKNIG

Show »

Length:1,148

Mass (Da):128,875

Checksum:ⁱB57FD40EE5E4C48C

GO

Sequence cautionⁱ

The sequence AAC39565.1 differs from that shown. Reason: Frameshift at position 62. Curated

The sequence AAC39565.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

The sequence AAH40951.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated

The sequence AAH40951.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Sequence conflictⁱ	584 – 584	1	I → M in AAH40951. (PubMed:15489334)Curated
Sequence conflictⁱ	623 – 623	1	D → G in AAH40951. (PubMed:15489334)Curated

Natural variant

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Natural variantⁱ	657 – 657	1	F → Y. Corresponds to variant rs7315731 [ dbSNP \| Ensembl ].		VAR_059722
Natural variantⁱ	1261 – 1261	1	V → L. Corresponds to variant rs11574973 [ dbSNP \| Ensembl ].		VAR_059723

Alternative sequence

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Alternative sequenceⁱ	1 – 315	315	Missing in isoform 2. 1 Publication Manual assertion based on opinion inⁱ Ref.1 "A novel SR-related protein specifically interacts with the carboxy-terminal domain (CTD) of RNA polymerase II through a conserved interaction domain." Tanner S., Stagljar I., Georgiev O., Schaffner W., Bourquin J.-P. Biol. Chem. 378:565-571(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.		VSP_037665	Add BLAST

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	Y11251 mRNA. Translation: CAA72121.1. AF030234 mRNA. Translation: AAC39565.1. Sequence problems. AC000015 Genomic DNA. No translation available. CH471111 Genomic DNA. Translation: EAW57892.1. CH471111 Genomic DNA. Translation: EAW57894.1. BC040951 mRNA. Translation: AAH40951.1. Sequence problems.
CCDSⁱ	CCDS8748.2. [Q99590-1]
PIRⁱ	T09073.
RefSeqⁱ	NP_004710.2. NM_004719.2. [Q99590-1]
UniGeneⁱ	Hs.210367.

Genome annotation databases

Ensemblⁱ	ENST00000369367; ENSP00000358374; ENSG00000139218. [Q99590-1] ENST00000465950; ENSP00000449812; ENSG00000139218. [Q99590-2]
GeneIDⁱ	9169.
KEGGⁱ	hsa:9169.
UCSCⁱ	uc001row.3. human. [Q99590-1]

Polymorphism databases

DMDMⁱ	251757337.

DMDMⁱ

251757337.

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	Y11251 mRNA. Translation: CAA72121.1. AF030234 mRNA. Translation: AAC39565.1. Sequence problems. AC000015 Genomic DNA. No translation available. CH471111 Genomic DNA. Translation: EAW57892.1. CH471111 Genomic DNA. Translation: EAW57894.1. BC040951 mRNA. Translation: AAH40951.1. Sequence problems.
CCDSⁱ	CCDS8748.2. [Q99590-1]
PIRⁱ	T09073.
RefSeqⁱ	NP_004710.2. NM_004719.2. [Q99590-1]
UniGeneⁱ	Hs.210367.

3D structure databases

ProteinModelPortalⁱ	Q99590.
SMRⁱ	Q99590. Positions 37-80.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	114610. 15 interactions.
IntActⁱ	Q99590. 2 interactions.
MINTⁱ	MINT-2866162.
STRINGⁱ	9606.ENSP00000358374.

PTM databases

PhosphoSiteⁱ	Q99590.

PhosphoSiteⁱ

Q99590.

Polymorphism databases

DMDMⁱ	251757337.

DMDMⁱ

251757337.

Proteomic databases

MaxQBⁱ	Q99590.
PaxDbⁱ	Q99590.
PRIDEⁱ	Q99590.

Protocols and materials databases

DNASUⁱ	9169.
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000369367; ENSP00000358374; ENSG00000139218. [Q99590-1] ENST00000465950; ENSP00000449812; ENSG00000139218. [Q99590-2]
GeneIDⁱ	9169.
KEGGⁱ	hsa:9169.
UCSCⁱ	uc001row.3. human. [Q99590-1]

Organism-specific databases

CTDⁱ	9169.
GeneCardsⁱ	GC12M046313.
H-InvDB	HIX0010567.
HGNCⁱ	HGNC:10784. SCAF11.
HPAⁱ	HPA038862. HPA045456. HPA046345.
MIMⁱ	603668. gene.
neXtProtⁱ	NX_Q99590.
PharmGKBⁱ	PA35700.
GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	NOG300312.
GeneTreeⁱ	ENSGT00530000063661.
HOVERGENⁱ	HBG101126.
InParanoidⁱ	Q99590.
OMAⁱ	YCTEFIE.
OrthoDBⁱ	EOG7F24SX.
PhylomeDBⁱ	Q99590.
TreeFamⁱ	TF332183.

Miscellaneous databases

ChiTaRSⁱ	SCAF11. human.
GeneWikiⁱ	SFRS2IP.
GenomeRNAiⁱ	9169.
NextBioⁱ	34387.
PMAP-CutDB	Q99590.
PROⁱ	Q99590.
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	Q99590.
CleanExⁱ	HS_SFRS2IP. HS_SIP1.
ExpressionAtlasⁱ	Q99590. baseline and differential.
Genevestigatorⁱ	Q99590.

Family and domain databases

Gene3Dⁱ	3.30.40.10. 1 hit.
InterProⁱ	IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR017907. Znf_RING_CS. [Graphical view]
Pfamⁱ	PF13639. zf-RING_2. 1 hit. [Graphical view]
SMARTⁱ	SM00184. RING. 1 hit. [Graphical view]
PROSITEⁱ	PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNetⁱ	Search...

Publicationsⁱ

« Hide 'large scale' publications

"A novel SR-related protein specifically interacts with the carboxy-terminal domain (CTD) of RNA polymerase II through a conserved interaction domain."
Tanner S., Stagljar I., Georgiev O., Schaffner W., Bourquin J.-P.
Biol. Chem. 378:565-571(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
Tissue: Lymphocyte.
"Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing."
Zhang W.-J., Wu J.Y.
Mol. Cell. Biol. 18:676-684(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH SRSF2; U2AF2 AND SNRNP70, SUBCELLULAR LOCATION.
Tissue: Cervix carcinoma.
"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R.
Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 212-669 (ISOFORM 1).
Tissue: Prostate.
"Antigens recognized by autologous antibody in patients with renal-cell carcinoma."
Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H., Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T., Old L.J.
Int. J. Cancer 83:456-464(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
Tissue: Renal cell carcinoma.
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-723 AND SER-726, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
"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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-341; SER-344; SER-405; THR-410; SER-533; SER-608; SER-614; SER-680; SER-796; SER-802; THR-807; SER-963 AND SER-1127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-413; SER-608; SER-796; SER-798 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-608; SER-614; SER-680; SER-687; SER-771; SER-776; SER-796; SER-1127 AND SER-1169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400; SER-401; SER-402; SER-405; THR-769; SER-776; SER-796 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

+Additional computationally mapped references.

Entry informationⁱ

Entry nameⁱ

SCAFB_HUMAN

Accessionⁱ

Primary (citable) accession number: Q99590
Secondary accession number(s): A6NEU9, A6NLW5, Q8IW59

Entry historyⁱ

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	July 7, 2009
Last modified:	February 4, 2015
This is version 109 of the entry and version 2 of the sequence. [Complete history]

Entry statusⁱ

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

Human chromosome 12
Human chromosome 12: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
SIMILARITY comments
Index of protein domains and families

External Data

Dasty 3

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

UniProtKB

Proteomes

UniRef

Supporting data

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Q99590 - SCAFB_HUMAN

UniProt

Q99590 - SCAFB_HUMAN

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Protein SCAF11

Select a section on the left to see content.

<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functioni

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>Provides information on the disease(s) and phenotype(s) associated with the deficiency of a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

Miscellaneous databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>Provides information on the tertiary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Compositional bias

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>Reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.</p><p><a href='../manual/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Polymorphism databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Contains the literature citations that are the sources of data used to annotate the entry. Each reference is numbered and contains several subsections allowing a precise description of a given citation.</p><p><a href='../manual/publications_section' target='_top'>More...</a></p>Publicationsi

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

External Data

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequences (2)ⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Publicationsⁱ

Entry informationⁱ

Miscellaneousⁱ