Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q15637

- SF01_HUMAN

UniProt

Q15637 - SF01_HUMAN

Protein

Splicing factor 1

Gene

SF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri277 – 29620CCHC-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. RNA binding Source: UniProtKB
    3. transcription corepressor activity Source: ProtInc
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. Leydig cell differentiation Source: Ensembl
    2. male sex determination Source: Ensembl
    3. mRNA 3'-splice site recognition Source: HGNC
    4. mRNA splicing, via spliceosome Source: HGNC
    5. negative regulation of smooth muscle cell proliferation Source: Ensembl
    6. regulation of steroid biosynthetic process Source: Ensembl
    7. regulation of transcription, DNA-templated Source: UniProtKB-KW
    8. spliceosomal complex assembly Source: UniProtKB
    9. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    mRNA processing, mRNA splicing, Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, RNA-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:SF1
    Synonyms:ZFM1, ZNF162
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:12950. SF1.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: UniProtKB
    2. ribosome Source: UniProtKB
    3. spliceosomal complex Source: HGNC

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi15 – 173KKR → EED: Abolishes interaction with U2AF2.
    Mutagenesisi16 – 183KRK → EDE: Abolishes interaction with U2AF2.
    Mutagenesisi20 – 201S → A: Strongly decreases interaction with U2AF2 and spliceosome assembly. 1 Publication
    Mutagenesisi20 – 201S → T: Decreases interaction with U2AF2. 1 Publication
    Mutagenesisi21 – 211R → A: Decreases interaction with U2AF2 and spliceosome assembly. 1 Publication
    Mutagenesisi21 – 211R → K: No effect. 1 Publication
    Mutagenesisi22 – 221W → A: Abolishes interaction with U2AF2. 1 Publication
    Mutagenesisi22 – 221W → F: No effect. 1 Publication
    Mutagenesisi151 – 1511N → A: Decreases RNA-binding. 1 Publication
    Mutagenesisi160 – 1601R → A: Strongly reduces RNA-binding. 1 Publication
    Mutagenesisi184 – 1841K → A: Abolishes RNA-binding. 1 Publication
    Mutagenesisi244 – 2441L → A: Decreases RNA-binding. 1 Publication
    Mutagenesisi247 – 2471L → A: Decreases RNA-binding. 1 Publication
    Mutagenesisi254 – 2541L → A: Slightly decreases RNA-binding. 1 Publication
    Mutagenesisi255 – 2551R → A: Slightly decreases RNA-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA37533.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 639638Splicing factor 1PRO_0000050129Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine4 Publications
    Modified residuei20 – 201Phosphoserine; by PKG1 Publication
    Modified residuei80 – 801Phosphoserine4 Publications
    Modified residuei82 – 821Phosphoserine4 Publications
    Modified residuei87 – 871PhosphotyrosineBy similarity

    Post-translational modificationi

    Phosphorylation on Ser-20 interferes with U2AF2 binding and spliceosome assembly. Isoform 6 is phosphorylated on Ser-463.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15637.
    PaxDbiQ15637.
    PRIDEiQ15637.

    Expressioni

    Tissue specificityi

    Detected in lung, ovary, adrenal gland, colon, kidney, muscle, pancreas, thyroid, placenta, brain, liver and heart.1 Publication

    Gene expression databases

    ArrayExpressiQ15637.
    BgeeiQ15637.
    CleanExiHS_SF1.
    GenevestigatoriQ15637.

    Organism-specific databases

    HPAiHPA018883.

    Interactioni

    Subunit structurei

    Binds U2AF2. Interacts with U1 snRNA. Binds EWSR1, FUS and TAF15. Interacts with RBM17.7 Publications

    Protein-protein interaction databases

    BioGridi113368. 93 interactions.
    DIPiDIP-29410N.
    IntActiQ15637. 31 interactions.
    MINTiMINT-1582417.

    Structurei

    Secondary structure

    1
    639
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi15 – 173
    Helixi46 – 6722
    Helixi76 – 794
    Beta strandi93 – 953
    Helixi97 – 11519
    Helixi116 – 1183
    Beta strandi136 – 1416
    Turni144 – 1463
    Helixi150 – 1578
    Beta strandi159 – 1613
    Helixi162 – 1709
    Beta strandi174 – 19017
    Beta strandi203 – 2119
    Helixi212 – 22615
    Turni227 – 2304
    Helixi238 – 2447
    Helixi245 – 2484
    Turni249 – 2524

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K1GNMR-A133-260[»]
    1O0PNMR-B13-25[»]
    1OPINMR-B13-25[»]
    2M09NMR-A27-145[»]
    2M0GNMR-A1-145[»]
    4FXWX-ray2.29B/D14-132[»]
    4FXXX-ray2.48A/B/C/D26-132[»]
    ProteinModelPortaliQ15637.
    SMRiQ15637. Positions 1-255.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15637.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini141 – 22282KHPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi15 – 195Nuclear localization signalSequence Analysis

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi324 – 637314Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the BBP/SF1 family.Curated
    Contains 1 CCHC-type zinc finger.PROSITE-ProRule annotation
    Contains 1 KH domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri277 – 29620CCHC-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5176.
    HOVERGENiHBG063318.
    KOiK13095.
    OrthoDBiEOG7K0ZC4.
    PhylomeDBiQ15637.
    TreeFamiTF319159.

    Family and domain databases

    Gene3Di3.30.1370.10. 1 hit.
    InterProiIPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    IPR001878. Znf_CCHC.
    [Graphical view]
    PfamiPF00013. KH_1. 1 hit.
    PF00098. zf-CCHC. 1 hit.
    [Graphical view]
    SMARTiSM00322. KH. 1 hit.
    SM00343. ZnF_C2HC. 1 hit.
    [Graphical view]
    SUPFAMiSSF54791. SSF54791. 1 hit.
    PROSITEiPS50084. KH_TYPE_1. 1 hit.
    PS50158. ZF_CCHC. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q15637-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MATGANATPL DFPSKKRKRS RWNQDTMEQK TVIPGMPTVI PPGLTREQER    50
    AYIVQLQIED LTRKLRTGDL GIPPNPEDRS PSPEPIYNSE GKRLNTREFR 100
    TRKKLEEERH NLITEMVALN PDFKPPADYK PPATRVSDKV MIPQDEYPEI 150
    NFVGLLIGPR GNTLKNIEKE CNAKIMIRGK GSVKEGKVGR KDGQMLPGED 200
    EPLHALVTAN TMENVKKAVE QIRNILKQGI ETPEDQNDLR KMQLRELARL 250
    NGTLREDDNR ILRPWQSSET RSITNTTVCT KCGGAGHIAS DCKFQRPGDP 300
    QSAQDKARMD KEYLSLMAEL GEAPVPASVG STSGPATTPL ASAPRPAAPA 350
    NNPPPPSLMS TTQSRPPWMN SGPSESRPYH GMHGGGPGGP GGGPHSFPHP 400
    LPSLTGGHGG HPMQHNPNGP PPPWMQPPPP PMNQGPHPPG HHGPPPMDQY 450
    LGSTPVGSGV YRLHQGKGMM PPPPMGMMPP PPPPPSGQPP PPPSGPLPPW 500
    QQQQQQPPPP PPPSSSMASS TPLPWQQNTT TTTTSAGTGS IPPWQQQQAA 550
    AAASPGAPQM QGNPTMVPLP PGVQPPLPPG APPPPPPPPP GSAGMMYAPP 600
    PPPPPPMDPS NFVTMMGMGV AGMPPFGMPP APPPPPPQN 639
    Length:639
    Mass (Da):68,330
    Last modified:January 23, 2007 - v4
    Checksum:iEEBC6A02B29DAE4D
    GO
    Isoform 2 (identifier: Q15637-2) [UniParc]FASTAAdd to Basket

    Also known as: SF1-Bo, Bone

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

    Show »
    Length:638
    Mass (Da):68,633
    Checksum:i06044F670EDC10C9
    GO
    Isoform 3 (identifier: Q15637-3) [UniParc]FASTAAdd to Basket

    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

    Show »
    Length:623
    Mass (Da):67,277
    Checksum:iC07C74BBDC4093B7
    GO
    Isoform 4 (identifier: Q15637-4) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:548
    Mass (Da):59,712
    Checksum:iDDB42B66ABA2AD18
    GO
    Isoform 5 (identifier: Q15637-5) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:673
    Mass (Da):71,752
    Checksum:i8F39B77A4DAE9FBD
    GO
    Isoform 6 (identifier: Q15637-6) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:571
    Mass (Da):61,889
    Checksum:i5DA04D16D93EBDD5
    GO
    Isoform 7 (identifier: Q15637-7) [UniParc]FASTAAdd to Basket

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

    Note: No experimental confirmation available.

    Show »
    Length:613
    Mass (Da):65,371
    Checksum:iC1EBBE4FC3AA66BF
    GO

    Sequence cautioni

    The sequence AAH00773.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti269 – 2691E → G in BAA05116. (PubMed:7912130)Curated
    Sequence conflicti269 – 2691E → G in BAA05117. (PubMed:7912130)Curated
    Sequence conflicti348 – 3481A → R in AAB03514. (PubMed:9192847)Curated
    Sequence conflicti348 – 3481A → R in AAB04033. (PubMed:9192847)Curated
    Sequence conflicti377 – 3771R → W in BAA05116. (PubMed:7912130)Curated
    Sequence conflicti377 – 3771R → W in BAA05117. (PubMed:7912130)Curated
    Sequence conflicti570 – 5701P → L in BAH11587. (PubMed:14702039)Curated
    Sequence conflicti591 – 5911G → V in AAB04033. (PubMed:9192847)Curated
    Sequence conflicti623 – 6231M → I in AAB04033. (PubMed:9192847)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti357 – 3571S → T.1 Publication
    VAR_017196

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2626Missing in isoform 7. 1 PublicationVSP_045274Add
    BLAST
    Alternative sequencei10 – 101L → LGKLGPPGLPPLPGPKGGFE PGPPPAPGPGAGLLAPGPPP PPPVGSMGALTAAFPFAALP PPPPPPPPPPPQQPPPPPPP PSPGASYPPPQPPPPPPLYQ RVSPPQPPPPQPPRKDQQPG PAGGGG in isoform 5. 1 PublicationVSP_008833
    Alternative sequencei448 – 548101DQYLG…WQQQQ → GKSVPGKYACGLWGLSPASR KRYDAATTYGHDA in isoform 6. 1 PublicationVSP_008834Add
    BLAST
    Alternative sequencei528 – 54821NTTTT…WQQQQ → RSLPAAAMARAMRVRTFRAH W in isoform 4 and isoform 5. 2 PublicationsVSP_008835Add
    BLAST
    Alternative sequencei549 – 63991Missing in isoform 4 and isoform 5. 2 PublicationsVSP_008836Add
    BLAST
    Alternative sequencei555 – 63985PGAPQ…PPPQN → QWAAPTPSLWSSSPMATTAA AASATPSAQQQYGFQYPLAM AAKIPPRGGDGPSHESEDFP RPLVTLPGRQPQQRPWWTGW FGKAA in isoform 6. 1 PublicationVSP_008837Add
    BLAST
    Alternative sequencei587 – 63953PPPPG…PPPQN → RSIECLLCLLSLLTQLPLPL PKPGRQDPSPRRRWPEP in isoform 3. 1 PublicationVSP_008838Add
    BLAST
    Alternative sequencei597 – 63943YAPPP…PPPQN → IPPRGGDGPSHESEDFPRPL VTLPGRQPQQRPWWTGWFGK AA in isoform 2. 1 PublicationVSP_008839Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS31599.1. [Q15637-1]
    CCDS44642.2. [Q15637-6]
    CCDS53660.1. [Q15637-7]
    CCDS53661.1. [Q15637-5]
    CCDS8080.1. [Q15637-2]
    CCDS8081.1. [Q15637-4]
    PIRiG02919.
    RefSeqiNP_001171501.1. NM_001178030.1. [Q15637-5]
    NP_001171502.1. NM_001178031.1. [Q15637-7]
    NP_004621.2. NM_004630.3. [Q15637-1]
    NP_973724.1. NM_201995.2. [Q15637-2]
    NP_973727.1. NM_201998.2. [Q15637-4]
    UniGeneiHs.502829.

    Genome annotation databases

    EnsembliENST00000227503; ENSP00000227503; ENSG00000168066. [Q15637-4]
    ENST00000334944; ENSP00000334414; ENSG00000168066. [Q15637-2]
    ENST00000377387; ENSP00000366604; ENSG00000168066. [Q15637-5]
    ENST00000377390; ENSP00000366607; ENSG00000168066. [Q15637-1]
    ENST00000377394; ENSP00000366611; ENSG00000168066. [Q15637-6]
    ENST00000433274; ENSP00000396793; ENSG00000168066. [Q15637-7]
    GeneIDi7536.
    KEGGihsa:7536.
    UCSCiuc001oaz.2. human. [Q15637-5]
    uc001oba.2. human. [Q15637-2]
    uc001obb.2. human. [Q15637-1]
    uc001obc.2. human. [Q15637-4]
    uc001obd.2. human. [Q15637-6]

    Polymorphism databases

    DMDMi38258418.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS31599.1. [Q15637-1 ]
    CCDS44642.2. [Q15637-6 ]
    CCDS53660.1. [Q15637-7 ]
    CCDS53661.1. [Q15637-5 ]
    CCDS8080.1. [Q15637-2 ]
    CCDS8081.1. [Q15637-4 ]
    PIRi G02919.
    RefSeqi NP_001171501.1. NM_001178030.1. [Q15637-5 ]
    NP_001171502.1. NM_001178031.1. [Q15637-7 ]
    NP_004621.2. NM_004630.3. [Q15637-1 ]
    NP_973724.1. NM_201995.2. [Q15637-2 ]
    NP_973727.1. NM_201998.2. [Q15637-4 ]
    UniGenei Hs.502829.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K1G NMR - A 133-260 [» ]
    1O0P NMR - B 13-25 [» ]
    1OPI NMR - B 13-25 [» ]
    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 [» ]
    ProteinModelPortali Q15637.
    SMRi Q15637. Positions 1-255.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113368. 93 interactions.
    DIPi DIP-29410N.
    IntActi Q15637. 31 interactions.
    MINTi MINT-1582417.

    Polymorphism databases

    DMDMi 38258418.

    Proteomic databases

    MaxQBi Q15637.
    PaxDbi Q15637.
    PRIDEi Q15637.

    Protocols and materials databases

    DNASUi 7536.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000227503 ; ENSP00000227503 ; ENSG00000168066 . [Q15637-4 ]
    ENST00000334944 ; ENSP00000334414 ; ENSG00000168066 . [Q15637-2 ]
    ENST00000377387 ; ENSP00000366604 ; ENSG00000168066 . [Q15637-5 ]
    ENST00000377390 ; ENSP00000366607 ; ENSG00000168066 . [Q15637-1 ]
    ENST00000377394 ; ENSP00000366611 ; ENSG00000168066 . [Q15637-6 ]
    ENST00000433274 ; ENSP00000396793 ; ENSG00000168066 . [Q15637-7 ]
    GeneIDi 7536.
    KEGGi hsa:7536.
    UCSCi uc001oaz.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

    CTDi 7536.
    GeneCardsi GC11M064532.
    HGNCi HGNC:12950. SF1.
    HPAi HPA018883.
    MIMi 601516. gene.
    neXtProti NX_Q15637.
    PharmGKBi PA37533.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5176.
    HOVERGENi HBG063318.
    KOi K13095.
    OrthoDBi EOG7K0ZC4.
    PhylomeDBi Q15637.
    TreeFami TF319159.

    Miscellaneous databases

    ChiTaRSi SF1. human.
    EvolutionaryTracei Q15637.
    GeneWikii SF1_(gene).
    GenomeRNAii 7536.
    NextBioi 29487.
    PROi Q15637.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15637.
    Bgeei Q15637.
    CleanExi HS_SF1.
    Genevestigatori Q15637.

    Family and domain databases

    Gene3Di 3.30.1370.10. 1 hit.
    InterProi IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    IPR001878. Znf_CCHC.
    [Graphical view ]
    Pfami PF00013. KH_1. 1 hit.
    PF00098. zf-CCHC. 1 hit.
    [Graphical view ]
    SMARTi SM00322. KH. 1 hit.
    SM00343. ZnF_C2HC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54791. SSF54791. 1 hit.
    PROSITEi PS50084. KH_TYPE_1. 1 hit.
    PS50158. ZF_CCHC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. "U2AF-homology motif interactions are required for alternative splicing regulation by SPF45."
      Corsini L., Bonnal S., Basquin J., Hothorn M., Scheffzek K., Valcarcel J., Sattler M.
      Nat. Struct. Mol. Biol. 14:620-629(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBM17.
    15. "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.
    16. 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.
    17. "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].
    18. "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.
    19. "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.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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].
    22. "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].
    23. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "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.
    25. "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.

    Entry informationi

    Entry nameiSF01_HUMAN
    AccessioniPrimary (citable) accession number: Q15637
    Secondary accession number(s): B7Z1Q1
    , C9JJE2, Q14818, Q14819, Q15913, Q8IY00, Q92744, Q92745, Q969H7, Q9BW01, Q9UEI0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 7, 2003
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 154 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3