Q15637 (SF01_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Splicing factor 1

Alternative name(s):
Mammalian branch point-binding protein
Short name=BBP
Short name=mBBP
Transcription factor ZFM1
Zinc finger gene in MEN1 locus
Zinc finger protein 162

Gene names

Name:	SF1
Synonyms:	ZFM1, ZNF162

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	639 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Necessary for the ATP-dependent first step of spliceosome assembly. Binds to the intron branch point sequence (BPS) 5'-UACUAAC-3' of the pre-mRNA. May act as transcription repressor. Ref.1 Ref.9 Ref.11
Subunit structure	Binds U2AF2. Interacts with U1 snRNA. Binds EWSR1, FUS and TAF15. Ref.1 Ref.9 Ref.10 Ref.11
Subcellular location	Nucleus.
Tissue specificity	Detected in lung, ovary, adrenal gland, colon, kidney, muscle, pancreas, thyroid, placenta, brain, liver and heart. Ref.3
Post-translational modification	Phosphorylation on Ser-20 interferes with U2AF2 binding and spliceosome assembly. Isoform 6 is phosphorylated on Ser-463. Ref.9
Sequence similarities	Belongs to the BBP/SF1 family. Contains 1 CCHC-type zinc finger. Contains 1 KH domain.
Sequence caution	The sequence AAH00773.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding RNA-binding Zinc
Molecular function	Repressor
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Leydig cell differentiation Inferred from electronic annotation. Source: Compara cell cycle process Inferred from electronic annotation. Source: Compara mRNA 3'-splice site recognition Traceable author statement PubMed 15647371. Source: HGNC male sex determination Inferred from electronic annotation. Source: Compara regulation of steroid biosynthetic process Inferred from electronic annotation. Source: Compara regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	ribosome Non-traceable author statement Ref.1. Source: UniProtKB spliceosomal complex Inferred from direct assay PubMed 9731529. Source: HGNC
Molecular_function	RNA binding Traceable author statement Ref.1. Source: UniProtKB transcription corepressor activity Traceable author statement Ref.11. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 7 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: Q15637-1)

Also known as: SF1-HL1;

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.

Isoform 2 (identifier: Q15637-2)

Also known as: SF1-Bo; Bone;

The sequence of this isoform differs from the canonical sequence as follows:
     597-639: YAPPPPPPPP...PAPPPPPPQN → IPPRGGDGPS...WWTGWFGKAA

Isoform 3 (identifier: Q15637-3)

Also known as: ZFM1-A; ZFM1-ABCDEF;

The sequence of this isoform differs from the canonical sequence as follows:
     587-639: PPPPGSAGMM...PAPPPPPPQN → RSIECLLCLL...PSPRRRWPEP

Isoform 4 (identifier: Q15637-4)

Also known as: ZFM1-B; ZFM1-ABCDF;

The sequence of this isoform differs from the canonical sequence as follows:
     528-548: NTTTTTTSAGTGSIPPWQQQQ → RSLPAAAMARAMRVRTFRAHW
     549-639: Missing.

Isoform 5 (identifier: Q15637-5)

The sequence of this isoform differs from the canonical sequence as follows:
     10-10: L → LGKLGPPGLP...QQPGPAGGGG
     528-548: NTTTTTTSAGTGSIPPWQQQQ → RSLPAAAMARAMRVRTFRAHW

Note: No experimental confirmation available.

Isoform 6 (identifier: Q15637-6)

Also known as: ZFM1-D; B6;

The sequence of this isoform differs from the canonical sequence as follows:
     448-548: DQYLGSTPVG...GSIPPWQQQQ → GKSVPGKYACGLWGLSPASRKRYDAATTYGHDA
     555-639: PGAPQMQGNP...PAPPPPPPQN → QWAAPTPSLW...WWTGWFGKAA

Note: Contains a phosphoserine at position 463.

Isoform 7 (identifier: Q15637-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 639

638

Splicing factor 1

PRO_0000050129

Regions

Domain

141 – 222

82

KH

Zinc finger

277 – 296

20

CCHC-type

Motif

15 – 19

5

Nuclear localization signal Potential

Compositional bias

324 – 637

314

Pro-rich

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.8

Modified residue

20

1

Phosphoserine; by PKG Ref.9

Modified residue

80

1

Phosphoserine Ref.15 Ref.16 Ref.17 Ref.19

Modified residue

82

1

Phosphoserine Ref.15 Ref.16 Ref.17 Ref.19

Natural variations

Alternative sequence

1 – 26

26

Missing in isoform 7.

VSP_045274

Alternative sequence

10

1

L → LGKLGPPGLPPLPGPKGGFE PGPPPAPGPGAGLLAPGPPP PPPVGSMGALTAAFPFAALP PPPPPPPPPPPQQPPPPPPP PSPGASYPPPQPPPPPPLYQ RVSPPQPPPPQPPRKDQQPG PAGGGG in isoform 5.

VSP_008833

Alternative sequence

448 – 548

101

DQYLG…WQQQQ → GKSVPGKYACGLWGLSPASR KRYDAATTYGHDA in isoform 6.

VSP_008834

Alternative sequence

528 – 548

21

NTTTT…WQQQQ → RSLPAAAMARAMRVRTFRAH W in isoform 4 and isoform 5.

VSP_008835

Alternative sequence

549 – 639

91

Missing in isoform 4.

VSP_008836

Alternative sequence

555 – 639

85

PGAPQ…PPPQN → QWAAPTPSLWSSSPMATTAA AASATPSAQQQYGFQYPLAM AAKIPPRGGDGPSHESEDFP RPLVTLPGRQPQQRPWWTGW FGKAA in isoform 6.

VSP_008837

Alternative sequence

587 – 639

53

PPPPG…PPPQN → RSIECLLCLLSLLTQLPLPL PKPGRQDPSPRRRWPEP in isoform 3.

VSP_008838

Alternative sequence

597 – 639

43

YAPPP…PPPQN → IPPRGGDGPSHESEDFPRPL VTLPGRQPQQRPWWTGWFGK AA in isoform 2.

VSP_008839

Natural variant

357

1

S → T. Ref.1

VAR_017196

Experimental info

Mutagenesis

15 – 17

3

KKR → EED: Abolishes interaction with U2AF2.

Mutagenesis

16 – 18

3

KRK → EDE: Abolishes interaction with U2AF2. Ref.21

Mutagenesis

20

1

S → A: Strongly decreases interaction with U2AF2 and spliceosome assembly. Ref.9

Mutagenesis

20

1

S → T: Decreases interaction with U2AF2. Ref.9

Mutagenesis

21

1

R → A: Decreases interaction with U2AF2 and spliceosome assembly. Ref.21

Mutagenesis

21

1

R → K: No effect. Ref.21

Mutagenesis

22

1

W → A: Abolishes interaction with U2AF2. Ref.21

Mutagenesis

22

1

W → F: No effect. Ref.21

Mutagenesis

151

1

N → A: Decreases RNA-binding. Ref.20

Mutagenesis

160

1

R → A: Strongly reduces RNA-binding. Ref.20

Mutagenesis

184

1

K → A: Abolishes RNA-binding. Ref.20

Mutagenesis

244

1

L → A: Decreases RNA-binding. Ref.20

Mutagenesis

247

1

L → A: Decreases RNA-binding. Ref.20

Mutagenesis

254

1

L → A: Slightly decreases RNA-binding. Ref.20

Mutagenesis

255

1

R → A: Slightly decreases RNA-binding. Ref.20

Sequence conflict

269

1

E → G in BAA05116. Ref.3

Sequence conflict

269

1

E → G in BAA05117. Ref.3

Sequence conflict

348

1

A → R in AAB03514. Ref.2

Sequence conflict

348

1

A → R in AAB04033. Ref.2

Sequence conflict

377

1

R → W in BAA05116. Ref.3

Sequence conflict

377

1

R → W in BAA05117. Ref.3

Sequence conflict

570

1

P → L in BAH11587. Ref.4

Sequence conflict

591

1

G → V in AAB04033. Ref.2

Sequence conflict

623

1

M → I in AAB04033. Ref.2

Secondary structure

1

.

.

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.

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.

.

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.

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.

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.

.

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.

639

Helix Strand Turn

Details...

Beta strand

16 – 19

4

Helix

46 – 67

22

Helix

76 – 79

4

Beta strand

93 – 95

3

Helix

97 – 115

19

Helix

116 – 118

3

Beta strand

136 – 141

6

Turn

144 – 146

3

Helix

150 – 157

8

Beta strand

159 – 161

3

Helix

162 – 170

9

Beta strand

174 – 190

17

Beta strand

203 – 211

9

Helix

212 – 226

15

Turn

227 – 230

4

Helix

238 – 244

7

Helix

245 – 248

4

Turn

249 – 252

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (SF1-HL1) [UniParc]. Last modified January 23, 2007. Version 4. Checksum: EEBC6A02B29DAE4D	FASTA	639	68,330
	10 20 30 40 50 60 MATGANATPL DFPSKKRKRS RWNQDTMEQK TVIPGMPTVI PPGLTREQER AYIVQLQIED 70 80 90 100 110 120 LTRKLRTGDL GIPPNPEDRS PSPEPIYNSE GKRLNTREFR TRKKLEEERH NLITEMVALN 130 140 150 160 170 180 PDFKPPADYK PPATRVSDKV MIPQDEYPEI NFVGLLIGPR GNTLKNIEKE CNAKIMIRGK 190 200 210 220 230 240 GSVKEGKVGR KDGQMLPGED EPLHALVTAN TMENVKKAVE QIRNILKQGI ETPEDQNDLR 250 260 270 280 290 300 KMQLRELARL NGTLREDDNR ILRPWQSSET RSITNTTVCT KCGGAGHIAS DCKFQRPGDP 310 320 330 340 350 360 QSAQDKARMD KEYLSLMAEL GEAPVPASVG STSGPATTPL ASAPRPAAPA NNPPPPSLMS 370 380 390 400 410 420 TTQSRPPWMN SGPSESRPYH GMHGGGPGGP GGGPHSFPHP LPSLTGGHGG HPMQHNPNGP 430 440 450 460 470 480 PPPWMQPPPP PMNQGPHPPG HHGPPPMDQY LGSTPVGSGV YRLHQGKGMM PPPPMGMMPP 490 500 510 520 530 540 PPPPPSGQPP PPPSGPLPPW QQQQQQPPPP PPPSSSMASS TPLPWQQNTT TTTTSAGTGS 550 560 570 580 590 600 IPPWQQQQAA AAASPGAPQM QGNPTMVPLP PGVQPPLPPG APPPPPPPPP GSAGMMYAPP 610 620 630 PPPPPPMDPS NFVTMMGMGV AGMPPFGMPP APPPPPPQN
	Isoform 2 (SF1-Bo) (Bone) [UniParc]. Checksum: 06044F670EDC10C9	FASTA	638	68,633
	10 20 30 40 50 60 MATGANATPL DFPSKKRKRS RWNQDTMEQK TVIPGMPTVI PPGLTREQER AYIVQLQIED 70 80 90 100 110 120 LTRKLRTGDL GIPPNPEDRS PSPEPIYNSE GKRLNTREFR TRKKLEEERH NLITEMVALN 130 140 150 160 170 180 PDFKPPADYK PPATRVSDKV MIPQDEYPEI NFVGLLIGPR GNTLKNIEKE CNAKIMIRGK 190 200 210 220 230 240 GSVKEGKVGR KDGQMLPGED EPLHALVTAN TMENVKKAVE QIRNILKQGI ETPEDQNDLR 250 260 270 280 290 300 KMQLRELARL NGTLREDDNR ILRPWQSSET RSITNTTVCT KCGGAGHIAS DCKFQRPGDP 310 320 330 340 350 360 QSAQDKARMD KEYLSLMAEL GEAPVPASVG STSGPATTPL ASAPRPAAPA NNPPPPSLMS 370 380 390 400 410 420 TTQSRPPWMN SGPSESRPYH GMHGGGPGGP GGGPHSFPHP LPSLTGGHGG HPMQHNPNGP 430 440 450 460 470 480 PPPWMQPPPP PMNQGPHPPG HHGPPPMDQY LGSTPVGSGV YRLHQGKGMM PPPPMGMMPP 490 500 510 520 530 540 PPPPPSGQPP PPPSGPLPPW QQQQQQPPPP PPPSSSMASS TPLPWQQNTT TTTTSAGTGS 550 560 570 580 590 600 IPPWQQQQAA AAASPGAPQM QGNPTMVPLP PGVQPPLPPG APPPPPPPPP GSAGMMIPPR 610 620 630 GGDGPSHESE DFPRPLVTLP GRQPQQRPWW TGWFGKAA
	Isoform 3 (ZFM1-A) (ZFM1-ABCDEF) [UniParc]. Checksum: C07C74BBDC4093B7	FASTA	623	67,277
	10 20 30 40 50 60 MATGANATPL DFPSKKRKRS RWNQDTMEQK TVIPGMPTVI PPGLTREQER AYIVQLQIED 70 80 90 100 110 120 LTRKLRTGDL GIPPNPEDRS PSPEPIYNSE GKRLNTREFR TRKKLEEERH NLITEMVALN 130 140 150 160 170 180 PDFKPPADYK PPATRVSDKV MIPQDEYPEI NFVGLLIGPR GNTLKNIEKE CNAKIMIRGK 190 200 210 220 230 240 GSVKEGKVGR KDGQMLPGED EPLHALVTAN TMENVKKAVE QIRNILKQGI ETPEDQNDLR 250 260 270 280 290 300 KMQLRELARL NGTLREDDNR ILRPWQSSET RSITNTTVCT KCGGAGHIAS DCKFQRPGDP 310 320 330 340 350 360 QSAQDKARMD KEYLSLMAEL GEAPVPASVG STSGPATTPL ASAPRPAAPA NNPPPPSLMS 370 380 390 400 410 420 TTQSRPPWMN SGPSESRPYH GMHGGGPGGP GGGPHSFPHP LPSLTGGHGG HPMQHNPNGP 430 440 450 460 470 480 PPPWMQPPPP PMNQGPHPPG HHGPPPMDQY LGSTPVGSGV YRLHQGKGMM PPPPMGMMPP 490 500 510 520 530 540 PPPPPSGQPP PPPSGPLPPW QQQQQQPPPP PPPSSSMASS TPLPWQQNTT TTTTSAGTGS 550 560 570 580 590 600 IPPWQQQQAA AAASPGAPQM QGNPTMVPLP PGVQPPLPPG APPPPPRSIE CLLCLLSLLT 610 620 QLPLPLPKPG RQDPSPRRRW PEP
	Isoform 4 (ZFM1-B) (ZFM1-ABCDF) [UniParc]. Checksum: DDB42B66ABA2AD18	FASTA	548	59,712
	10 20 30 40 50 60 MATGANATPL DFPSKKRKRS RWNQDTMEQK TVIPGMPTVI PPGLTREQER AYIVQLQIED 70 80 90 100 110 120 LTRKLRTGDL GIPPNPEDRS PSPEPIYNSE GKRLNTREFR TRKKLEEERH NLITEMVALN 130 140 150 160 170 180 PDFKPPADYK PPATRVSDKV MIPQDEYPEI NFVGLLIGPR GNTLKNIEKE CNAKIMIRGK 190 200 210 220 230 240 GSVKEGKVGR KDGQMLPGED EPLHALVTAN TMENVKKAVE QIRNILKQGI ETPEDQNDLR 250 260 270 280 290 300 KMQLRELARL NGTLREDDNR ILRPWQSSET RSITNTTVCT KCGGAGHIAS DCKFQRPGDP 310 320 330 340 350 360 QSAQDKARMD KEYLSLMAEL GEAPVPASVG STSGPATTPL ASAPRPAAPA NNPPPPSLMS 370 380 390 400 410 420 TTQSRPPWMN SGPSESRPYH GMHGGGPGGP GGGPHSFPHP LPSLTGGHGG HPMQHNPNGP 430 440 450 460 470 480 PPPWMQPPPP PMNQGPHPPG HHGPPPMDQY LGSTPVGSGV YRLHQGKGMM PPPPMGMMPP 490 500 510 520 530 540 PPPPPSGQPP PPPSGPLPPW QQQQQQPPPP PPPSSSMASS TPLPWQQRSL PAAAMARAMR VRTFRAHW
	Isoform 5 [UniParc]. Checksum: 379C21D0B513F706	FASTA	764	80,620
	10 20 30 40 50 60 MATGANATPL GKLGPPGLPP LPGPKGGFEP GPPPAPGPGA GLLAPGPPPP PPVGSMGALT 70 80 90 100 110 120 AAFPFAALPP PPPPPPPPPP QQPPPPPPPP SPGASYPPPQ PPPPPPLYQR VSPPQPPPPQ 130 140 150 160 170 180 PPRKDQQPGP AGGGGDFPSK KRKRSRWNQD TMEQKTVIPG MPTVIPPGLT REQERAYIVQ 190 200 210 220 230 240 LQIEDLTRKL RTGDLGIPPN PEDRSPSPEP IYNSEGKRLN TREFRTRKKL EEERHNLITE 250 260 270 280 290 300 MVALNPDFKP PADYKPPATR VSDKVMIPQD EYPEINFVGL LIGPRGNTLK NIEKECNAKI 310 320 330 340 350 360 MIRGKGSVKE GKVGRKDGQM LPGEDEPLHA LVTANTMENV KKAVEQIRNI LKQGIETPED 370 380 390 400 410 420 QNDLRKMQLR ELARLNGTLR EDDNRILRPW QSSETRSITN TTVCTKCGGA GHIASDCKFQ 430 440 450 460 470 480 RPGDPQSAQD KARMDKEYLS LMAELGEAPV PASVGSTSGP ATTPLASAPR PAAPANNPPP 490 500 510 520 530 540 PSLMSTTQSR PPWMNSGPSE SRPYHGMHGG GPGGPGGGPH SFPHPLPSLT GGHGGHPMQH 550 560 570 580 590 600 NPNGPPPPWM QPPPPPMNQG PHPPGHHGPP PMDQYLGSTP VGSGVYRLHQ GKGMMPPPPM 610 620 630 640 650 660 GMMPPPPPPP SGQPPPPPSG PLPPWQQQQQ QPPPPPPPSS SMASSTPLPW QQRSLPAAAM 670 680 690 700 710 720 ARAMRVRTFR AHWAAAAASP GAPQMQGNPT MVPLPPGVQP PLPPGAPPPP PPPPPGSAGM 730 740 750 760 MYAPPPPPPP PMDPSNFVTM MGMGVAGMPP FGMPPAPPPP PPQN
	Isoform 6 (ZFM1-D) (B6) [UniParc]. Checksum: 5DA04D16D93EBDD5	FASTA	571	61,889
	10 20 30 40 50 60 MATGANATPL DFPSKKRKRS RWNQDTMEQK TVIPGMPTVI PPGLTREQER AYIVQLQIED 70 80 90 100 110 120 LTRKLRTGDL GIPPNPEDRS PSPEPIYNSE GKRLNTREFR TRKKLEEERH NLITEMVALN 130 140 150 160 170 180 PDFKPPADYK PPATRVSDKV MIPQDEYPEI NFVGLLIGPR GNTLKNIEKE CNAKIMIRGK 190 200 210 220 230 240 GSVKEGKVGR KDGQMLPGED EPLHALVTAN TMENVKKAVE QIRNILKQGI ETPEDQNDLR 250 260 270 280 290 300 KMQLRELARL NGTLREDDNR ILRPWQSSET RSITNTTVCT KCGGAGHIAS DCKFQRPGDP 310 320 330 340 350 360 QSAQDKARMD KEYLSLMAEL GEAPVPASVG STSGPATTPL ASAPRPAAPA NNPPPPSLMS 370 380 390 400 410 420 TTQSRPPWMN SGPSESRPYH GMHGGGPGGP GGGPHSFPHP LPSLTGGHGG HPMQHNPNGP 430 440 450 460 470 480 PPPWMQPPPP PMNQGPHPPG HHGPPPMGKS VPGKYACGLW GLSPASRKRY DAATTYGHDA 490 500 510 520 530 540 AAAAASQWAA PTPSLWSSSP MATTAAAASA TPSAQQQYGF QYPLAMAAKI PPRGGDGPSH 550 560 570 ESEDFPRPLV TLPGRQPQQR PWWTGWFGKA A
	Isoform 7 [UniParc]. Checksum: C1EBBE4FC3AA66BF	FASTA	613	65,371
	10 20 30 40 50 60 MEQKTVIPGM PTVIPPGLTR EQERAYIVQL QIEDLTRKLR TGDLGIPPNP EDRSPSPEPI 70 80 90 100 110 120 YNSEGKRLNT REFRTRKKLE EERHNLITEM VALNPDFKPP ADYKPPATRV SDKVMIPQDE 130 140 150 160 170 180 YPEINFVGLL IGPRGNTLKN IEKECNAKIM IRGKGSVKEG KVGRKDGQML PGEDEPLHAL 190 200 210 220 230 240 VTANTMENVK KAVEQIRNIL KQGIETPEDQ NDLRKMQLRE LARLNGTLRE DDNRILRPWQ 250 260 270 280 290 300 SSETRSITNT TVCTKCGGAG HIASDCKFQR PGDPQSAQDK ARMDKEYLSL MAELGEAPVP 310 320 330 340 350 360 ASVGSTSGPA TTPLASAPRP AAPANNPPPP SLMSTTQSRP PWMNSGPSES RPYHGMHGGG 370 380 390 400 410 420 PGGPGGGPHS FPHPLPSLTG GHGGHPMQHN PNGPPPPWMQ PPPPPMNQGP HPPGHHGPPP 430 440 450 460 470 480 MDQYLGSTPV GSGVYRLHQG KGMMPPPPMG MMPPPPPPPS GQPPPPPSGP LPPWQQQQQQ 490 500 510 520 530 540 PPPPPPPSSS MASSTPLPWQ QNTTTTTTSA GTGSIPPWQQ QQAAAAASPG APQMQGNPTM 550 560 570 580 590 600 VPLPPGVQPP LPPGAPPPPP PPPPGSAGMM YAPPPPPPPP MDPSNFVTMM GMGVAGMPPF 610 GMPPAPPPPP PQN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Mammalian splicing factor SF1 is encoded by variant cDNAs and binds to RNA." Arning S., Grueter P., Bilbe G., Kraemer A. RNA 2:794-810(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 20-30 AND 136-150, VARIANT THR-357, FUNCTION, INTERACTION WITH U1 SNRNA, RNA-BINDING. Tissue: Bone and Cervix carcinoma.
[2]	"Identification of two novel isoforms of the ZNF162 gene: a growing family of signal transduction and activator of RNA proteins." Caslini C., Spinelli O., Cazzaniga G., Golay J., De Gioia L., Pedretti A., Breviario F., Amaru R., Barbui T., Biondi A., Introna M., Rambaldi A. Genomics 42:268-277(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6). Tissue: Myeloid leukemia cell.
[3]	"Isolation and characterization of a novel gene encoding nuclear protein at a locus (D11S636) tightly linked to multiple endocrine neoplasia type 1 (MEN1)." Toda T., Iida A., Miwa T., Nakamura Y., Imai T. Hum. Mol. Genet. 3:465-470(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY. Tissue: Brain cortex, Cerebellum and Fetal liver.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7). Tissue: Cerebellum.
[5]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORMS 1; 4 AND 5). Tissue: Brain, Eye, Kidney, Muscle and Skin.
[7]	"Diverse modes of alternative splicing of human splicing factor SF1 deduced from the exon-intron structure of the gene." Kraemer A., Quentin M., Mulhauser F. Gene 211:29-37(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-295.
[8]	Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M. Submitted (MAY-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-15, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: T-cell.
[9]	"Phosphorylation of splicing factor SF1 on Ser20 by cGMP-dependent protein kinase regulates spliceosome assembly." Wang X., Bruderer S., Rafi Z., Xue J., Milburn P.J., Kraemer A., Robinson P.J. EMBO J. 18:4549-4559(1999) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 19-28; 94-103; 228-239 AND 298-308, FUNCTION, INTERACTION WITH U2AF2, MUTAGENESIS OF SER-20, PHOSPHORYLATION AT SER-20.
[10]	"Large-scale proteomic analysis of the human spliceosome." Rappsilber J., Ryder U., Lamond A.I., Mann M. Genome Res. 12:1231-1245(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 110-135, MASS SPECTROMETRY, INTERACTION WITH THE SPLICEOSOME.
[11]	"The transcriptional repressor ZFM1 interacts with and modulates the ability of EWS to activate transcription." Zhang D., Paley A.J., Childs G. J. Biol. Chem. 273:18086-18091(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH EWSR1; FUS AND TAF15.
[12]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[13]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463 (ISOFORM 6), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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-463 (ISOFORM 6), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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-80 AND SER-82, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463 (ISOFORM 6), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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-80 AND SER-82, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"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-80 AND SER-82, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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].
[19]	"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-80 AND SER-82, MASS SPECTROMETRY.
[20]	"Structural basis for recognition of the intron branch site RNA by splicing factor 1." Liu Z., Luyten I., Bottomley M.J., Messias A.C., Houngninou-Molango S., Sprangers R., Zanier K., Kraemer A., Sattler M. Science 294:1098-1102(2001) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 133-255 IN COMPLEX WITH THE BRANCH SITE SEQUENCE 5'-UAUACUAACAA-3', MUTAGENESIS OF ASN-151; ARG-160; LYS-184; LEU-244; LEU-247; LEU-254 AND ARG-255.
[21]	"Structural basis for the molecular recognition between human splicing factors U2AF65 and SF1/mBBP." Selenko P., Gregorovic G., Sprangers R., Stier G., Rhani Z., Kraemer A., Sattler M. Mol. Cell 11:965-976(2003) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 13-25 IN COMPLEX WITH U2AF2, MUTAGENESIS OF 16-LYS--ARG-18; 17-LYS-LYS-18; ARG-21 AND TRP-22.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Y08765 mRNA. Translation: CAA70018.1.
Y08766 mRNA. Translation: CAA70019.1.
L49345 mRNA. Translation: AAB03514.1.
L49380 mRNA. Translation: AAB04033.1.
D26120 mRNA. Translation: BAA05116.1.
D26120 mRNA. Translation: BAA05117.1.
AK293753 mRNA. Translation: BAH11587.1.
AP001462 Genomic DNA. No translation available.
BC000773 mRNA. Translation: AAH00773.1. Different initiation.
BC008080 mRNA. Translation: AAH08080.1.
BC008724 mRNA. Translation: AAH08724.1.
BC011657 mRNA. No translation available.
BC020217 mRNA. Translation: AAH20217.1.
BC038446 mRNA. Translation: AAH38446.1.
AJ000051, AJ000052 Genomic DNA. Translation: CAA03883.1.

IPI

IPI00294627.
IPI00386114.
IPI00386117.
IPI00386119.
IPI00386120.
IPI00852591.
IPI00941553.

PIR

G02919.

RefSeq

NP_001171501.1. NM_001178030.1.
NP_001171502.1. NM_001178031.1.
NP_004621.2. NM_004630.3.
NP_973724.1. NM_201995.2.
NP_973726.2. NM_201997.2.
NP_973727.1. NM_201998.2.

UniGene

Hs.502829.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K1G	NMR	-	A	133-260	[»]
2M09	NMR	-	A	27-145	[»]
2M0G	NMR	-	A	1-145	[»]
4FXW	X-ray	2.29	B/D	14-132	[»]
4FXX	X-ray	2.48	A/B/C/D	26-132	[»]

ProteinModelPortal

Q15637.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29410N.

IntAct

Q15637. 14 interactions.

MINT

MINT-1582417.

Polymorphism databases

DMDM

38258418.

Proteomic databases

PaxDb

Q15637.

PRIDE

Q15637.

Protocols and materials databases

DNASU

7536.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000227503; ENSP00000227503; ENSG00000168066.
ENST00000334944; ENSP00000334414; ENSG00000168066.
ENST00000377387; ENSP00000366604; ENSG00000168066.
ENST00000377390; ENSP00000366607; ENSG00000168066.
ENST00000377394; ENSP00000366611; ENSG00000168066.
ENST00000433274; ENSP00000396793; ENSG00000168066.

GeneID

7536.

KEGG

hsa:7536.

UCSC

uc001oaz.2. human.
uc001oba.2. human.
uc001obb.2. human.
uc001obc.2. human.
uc001obd.2. human.

Organism-specific databases

CTD

7536.

GeneCards

GC11M064532.

HGNC

HGNC:12950. SF1.

HPA

HPA018883.

MIM

601516. gene.

neXtProt

NX_Q15637.

PharmGKB

PA37533.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5176.

HOVERGEN

HBG063318.

KO

K13095.

Gene expression databases

ArrayExpress

Q15637.

Bgee

Q15637.

CleanEx

HS_SF1.

Genevestigator

Q15637.

GermOnline

ENSG00000168066. Homo sapiens.

Family and domain databases

InterPro

IPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR001878. Znf_CCHC.
[Graphical view]

Pfam

PF00013. KH_1. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view]

SMART

SM00322. KH. 1 hit.
SM00343. ZnF_C2HC. 1 hit.
[Graphical view]

PROSITE

PS50084. KH_TYPE_1. 1 hit.
PS50158. ZF_CCHC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SF1. human.

EvolutionaryTrace

Q15637.

GenomeRNAi

7536.

NextBio

29487.

SOURCE

Search...

Entry information

Entry name

SF01_HUMAN

Accession

Primary (citable) accession number: Q15637
Secondary accession number(s): B7Z1Q1 , C9JJE2, Q14818, Q14819, Q15913, Q8IY00, Q92744, Q92745, Q969H7, Q9BW01, Q9UEI0

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 7, 2003
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 141 of the entry and version 4 of the sequence. [Complete history]

Entry status

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.