Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q15637 (SF01_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length639 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processmRNA processing
mRNA splicing
Transcription
Transcription regulation
   Cellular componentNucleus
Spliceosome
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandMetal-binding
RNA-binding
Zinc
   Molecular functionRepressor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processLeydig cell differentiation

Inferred from electronic annotation. Source: Ensembl

mRNA 3'-splice site recognition

Traceable author statement PubMed 15647371. Source: HGNC

mRNA splicing, via spliceosome

Inferred by curator PubMed 9731529. Source: HGNC

male sex determination

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of steroid biosynthetic process

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

spliceosomal complex assembly

Non-traceable author statement Ref.1. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleus

Non-traceable author statement Ref.3. Source: UniProtKB

ribosome

Non-traceable author statement Ref.1. Source: UniProtKB

spliceosomal complex

Inferred from direct assay PubMed 9731529. Source: HGNC

   Molecular_functionRNA binding

Traceable author statement Ref.1. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. 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
     549-639: Missing.
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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 639638Splicing factor 1
PRO_0000050129

Regions

Domain141 – 22282KH
Zinc finger277 – 29620CCHC-type
Motif15 – 195Nuclear localization signal Potential
Compositional bias324 – 637314Pro-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.16 Ref.21 Ref.22
Modified residue201Phosphoserine; by PKG Ref.9
Modified residue801Phosphoserine Ref.15 Ref.17 Ref.18 Ref.20
Modified residue821Phosphoserine Ref.15 Ref.17 Ref.18 Ref.20
Modified residue871Phosphotyrosine By similarity

Natural variations

Alternative sequence1 – 2626Missing in isoform 7.
VSP_045274
Alternative sequence101L → LGKLGPPGLPPLPGPKGGFE PGPPPAPGPGAGLLAPGPPP PPPVGSMGALTAAFPFAALP PPPPPPPPPPPQQPPPPPPP PSPGASYPPPQPPPPPPLYQ RVSPPQPPPPQPPRKDQQPG PAGGGG in isoform 5.
VSP_008833
Alternative sequence448 – 548101DQYLG…WQQQQ → GKSVPGKYACGLWGLSPASR KRYDAATTYGHDA in isoform 6.
VSP_008834
Alternative sequence528 – 54821NTTTT…WQQQQ → RSLPAAAMARAMRVRTFRAH W in isoform 4 and isoform 5.
VSP_008835
Alternative sequence549 – 63991Missing in isoform 4 and isoform 5.
VSP_008836
Alternative sequence555 – 63985PGAPQ…PPPQN → QWAAPTPSLWSSSPMATTAA AASATPSAQQQYGFQYPLAM AAKIPPRGGDGPSHESEDFP RPLVTLPGRQPQQRPWWTGW FGKAA in isoform 6.
VSP_008837
Alternative sequence587 – 63953PPPPG…PPPQN → RSIECLLCLLSLLTQLPLPL PKPGRQDPSPRRRWPEP in isoform 3.
VSP_008838
Alternative sequence597 – 63943YAPPP…PPPQN → IPPRGGDGPSHESEDFPRPL VTLPGRQPQQRPWWTGWFGK AA in isoform 2.
VSP_008839
Natural variant3571S → T. Ref.1
VAR_017196

Experimental info

Mutagenesis15 – 173KKR → EED: Abolishes interaction with U2AF2.
Mutagenesis16 – 183KRK → EDE: Abolishes interaction with U2AF2. Ref.24
Mutagenesis201S → A: Strongly decreases interaction with U2AF2 and spliceosome assembly. Ref.9
Mutagenesis201S → T: Decreases interaction with U2AF2. Ref.9
Mutagenesis211R → A: Decreases interaction with U2AF2 and spliceosome assembly. Ref.24
Mutagenesis211R → K: No effect. Ref.24
Mutagenesis221W → A: Abolishes interaction with U2AF2. Ref.24
Mutagenesis221W → F: No effect. Ref.24
Mutagenesis1511N → A: Decreases RNA-binding. Ref.23
Mutagenesis1601R → A: Strongly reduces RNA-binding. Ref.23
Mutagenesis1841K → A: Abolishes RNA-binding. Ref.23
Mutagenesis2441L → A: Decreases RNA-binding. Ref.23
Mutagenesis2471L → A: Decreases RNA-binding. Ref.23
Mutagenesis2541L → A: Slightly decreases RNA-binding. Ref.23
Mutagenesis2551R → A: Slightly decreases RNA-binding. Ref.23
Sequence conflict2691E → G in BAA05116. Ref.3
Sequence conflict2691E → G in BAA05117. Ref.3
Sequence conflict3481A → R in AAB03514. Ref.2
Sequence conflict3481A → R in AAB04033. Ref.2
Sequence conflict3771R → W in BAA05116. Ref.3
Sequence conflict3771R → W in BAA05117. Ref.3
Sequence conflict5701P → L in BAH11587. Ref.4
Sequence conflict5911G → V in AAB04033. Ref.2
Sequence conflict6231M → I in AAB04033. Ref.2

Secondary structure

............................... 639
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SF1-HL1) [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: EEBC6A02B29DAE4D

FASTA63968,330
        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 

« Hide

Isoform 2 (SF1-Bo) (Bone) [UniParc].

Checksum: 06044F670EDC10C9
Show »

FASTA63868,633
Isoform 3 (ZFM1-A) (ZFM1-ABCDEF) [UniParc].

Checksum: C07C74BBDC4093B7
Show »

FASTA62367,277
Isoform 4 (ZFM1-B) (ZFM1-ABCDF) [UniParc].

Checksum: DDB42B66ABA2AD18
Show »

FASTA54859,712
Isoform 5 [UniParc].

Checksum: 8F39B77A4DAE9FBD
Show »

FASTA67371,752
Isoform 6 (ZFM1-D) (B6) [UniParc].

Checksum: 5DA04D16D93EBDD5
Show »

FASTA57161,889
Isoform 7 [UniParc].

Checksum: C1EBBE4FC3AA66BF
Show »

FASTA61365,371

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[18]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"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].
[20]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"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.
[24]"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.
PIRG02919.
RefSeqNP_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.
UniGeneHs.502829.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K1GNMR-A133-260[»]
1OPINMR-B13-25[»]
2M09NMR-A27-145[»]
2M0GNMR-A1-145[»]
4FXWX-ray2.29B/D14-132[»]
4FXXX-ray2.48A/B/C/D26-132[»]
ProteinModelPortalQ15637.
SMRQ15637. Positions 1-255.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113368. 90 interactions.
DIPDIP-29410N.
IntActQ15637. 31 interactions.
MINTMINT-1582417.

Polymorphism databases

DMDM38258418.

Proteomic databases

PaxDbQ15637.
PRIDEQ15637.

Protocols and materials databases

DNASU7536.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000227503; ENSP00000227503; ENSG00000168066. [Q15637-4]
ENST00000334944; ENSP00000334414; ENSG00000168066. [Q15637-2]
ENST00000377387; ENSP00000366604; ENSG00000168066.
ENST00000377390; ENSP00000366607; ENSG00000168066. [Q15637-1]
ENST00000377394; ENSP00000366611; ENSG00000168066. [Q15637-6]
ENST00000433274; ENSP00000396793; ENSG00000168066. [Q15637-7]
GeneID7536.
KEGGhsa:7536.
UCSCuc001oaz.2. human. [Q15637-5]
uc001oba.2. human. [Q15637-2]
uc001obb.2. human. [Q15637-1]
uc001obc.2. human. [Q15637-4]
uc001obd.2. human. [Q15637-6]

Organism-specific databases

CTD7536.
GeneCardsGC11M064532.
HGNCHGNC:12950. SF1.
HPAHPA018883.
MIM601516. gene.
neXtProtNX_Q15637.
PharmGKBPA37533.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5176.
HOVERGENHBG063318.
KOK13095.
OrthoDBEOG7K0ZC4.
PhylomeDBQ15637.
TreeFamTF319159.

Gene expression databases

ArrayExpressQ15637.
BgeeQ15637.
CleanExHS_SF1.
GenevestigatorQ15637.

Family and domain databases

Gene3D3.30.1370.10. 1 hit.
InterProIPR004087. KH_dom.
IPR004088. KH_dom_type_1.
IPR001878. Znf_CCHC.
[Graphical view]
PfamPF00013. KH_1. 1 hit.
PF00098. zf-CCHC. 1 hit.
[Graphical view]
SMARTSM00322. KH. 1 hit.
SM00343. ZnF_C2HC. 1 hit.
[Graphical view]
SUPFAMSSF54791. SSF54791. 1 hit.
PROSITEPS50084. KH_TYPE_1. 1 hit.
PS50158. ZF_CCHC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSF1. human.
EvolutionaryTraceQ15637.
GeneWikiSF1_(gene).
GenomeRNAi7536.
NextBio29487.
PROQ15637.
SOURCESearch...

Entry information

Entry nameSF01_HUMAN
AccessionPrimary (citable) accession number: Q15637
Secondary accession number(s): B7Z1Q1 expand/collapse secondary AC list , 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: April 16, 2014
This is version 149 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM