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Q9NQ55

- SSF1_HUMAN

UniProt

Q9NQ55 - SSF1_HUMAN

Protein

Suppressor of SWI4 1 homolog

Gene

PPAN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    May have a role in cell growth.

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. RNA splicing Source: ProtInc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Suppressor of SWI4 1 homolog
    Short name:
    Ssf-1
    Alternative name(s):
    Brix domain-containing protein 3
    Peter Pan homolog
    Gene namesi
    Name:PPAN
    Synonyms:BXDC3, SSF1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:9227. PPAN.

    Subcellular locationi

    Nucleusnucleolus 1 Publication

    GO - Cellular componenti

    1. nucleolus Source: UniProtKB-SubCell
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162399971.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 473473Suppressor of SWI4 1 homologPRO_0000120257Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei238 – 2381Phosphoserine4 Publications
    Modified residuei240 – 2401Phosphoserine4 Publications
    Modified residuei359 – 3591Phosphoserine8 Publications
    Modified residuei438 – 4381N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9NQ55.
    PaxDbiQ9NQ55.
    PRIDEiQ9NQ55.

    2D gel databases

    SWISS-2DPAGEQ9NQ55.

    PTM databases

    PhosphoSiteiQ9NQ55.

    Expressioni

    Tissue specificityi

    Widely expressed.2 Publications

    Gene expression databases

    ArrayExpressiQ9NQ55.
    BgeeiQ9NQ55.
    CleanExiHS_PPAN.
    GenevestigatoriQ9NQ55.

    Organism-specific databases

    HPAiHPA043265.

    Interactioni

    Protein-protein interaction databases

    BioGridi121141. 14 interactions.
    593098. 2 interactions.
    IntActiQ9NQ55. 7 interactions.
    MINTiMINT-3072003.
    STRINGi9606.ENSP00000253107.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NQ55.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 292264BrixPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 Brix domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG272199.
    HOGENOMiHOG000210038.
    HOVERGENiHBG026954.
    InParanoidiQ9NQ55.
    KOiK14859.
    OMAiLGVTHLM.
    PhylomeDBiQ9NQ55.
    TreeFamiTF318923.

    Family and domain databases

    InterProiIPR007109. Brix.
    [Graphical view]
    PfamiPF04427. Brix. 1 hit.
    [Graphical view]
    SMARTiSM00879. Brix. 1 hit.
    [Graphical view]
    PROSITEiPS50833. BRIX. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NQ55-1) [UniParc]FASTAAdd 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

    MGQSGRSRHQ KRARAQAQLR NLEAYAANPH SFVFTRGCTG RNIRQLSLDV    50
    RRVMEPLTAS RLQVRKKNSL KDCVAVAGPL GVTHFLILSK TETNVYFKLM 100
    RLPGGPTLTF QVKKYSLVRD VVSSLRRHRM HEQQFAHPPL LVLNSFGPHG 150
    MHVKLMATMF QNLFPSINVH KVNLNTIKRC LLIDYNPDSQ ELDFRHYSIK 200
    VVPVGASRGM KKLLQEKFPN MSRLQDISEL LATGAGLSES EAEPDGDHNI 250
    TELPQAVAGR GNMRAQQSAV RLTEIGPRMT LQLIKVQEGV GEGKVMFHSF 300
    VSKTEEELQA ILEAKEKKLR LKAQRQAQQA QNVQRKQEQR EAHRKKSLEG 350
    MKKARVGGSD EEASGIPSRT ASLELGEDDD EQEDDDIEYF CQAVGEAPSE 400
    DLFPEAKQKR LAKSPGRKRK RWEMDRGRGR LCDQKFPKTK DKSQGAQARR 450
    GPRGASRDGG RGRGRGRPGK RVA 473
    Length:473
    Mass (Da):53,194
    Last modified:October 1, 2000 - v1
    Checksum:i9FF7B7201BD37BEC
    GO
    Isoform 2 (identifier: Q9NQ55-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         444-456: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:460
    Mass (Da):51,900
    Checksum:iDEDA8FEF86C6575D
    GO
    Isoform 3 (identifier: Q9NQ55-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         448-473: ARRGPRGASRDGGRGRGRGRPGKRVA → VPSPALPTSW...SWQSATCSAP

    Note: No experimental confirmation available.Curated

    Show »
    Length:520
    Mass (Da):58,199
    Checksum:iB5EE1A65E9E13B5E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Isoform 3 (identifier: Q9NQ55-3)
    Sequence conflicti520 – 5201P → L in BC171852. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti358 – 3581G → V.
    Corresponds to variant rs2305793 [ dbSNP | Ensembl ].
    VAR_022157
    Natural varianti408 – 4081Q → R.
    Corresponds to variant rs11559188 [ dbSNP | Ensembl ].
    VAR_048422

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei444 – 45613Missing in isoform 2. 1 PublicationVSP_003973Add
    BLAST
    Alternative sequencei448 – 47326ARRGP…GKRVA → VPSPALPTSWQLPTTNSVGS RGTSCGPYWWLSSWWPWPAM AWPCTASASGSSAHGTPPWS SLSSWQSATCSAP in isoform 3. 1 PublicationVSP_046377Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ292529 mRNA. Translation: CAB99252.1.
    AC020931 Genomic DNA. No translation available.
    BC000535 mRNA. Translation: AAH00535.2.
    BC009833 mRNA. Translation: AAH09833.1.
    BC033202 mRNA. Translation: AAH33202.1.
    BC171852 mRNA. No translation available.
    AJ300588 mRNA. Translation: CAC18877.1. Different termination.
    CCDSiCCDS12225.1. [Q9NQ55-1]
    PIRiJC7359.
    RefSeqiNP_001035754.1. NM_001040664.2.
    NP_001185619.1. NM_001198690.1. [Q9NQ55-3]
    NP_064615.3. NM_020230.5. [Q9NQ55-1]
    UniGeneiHs.14468.

    Genome annotation databases

    EnsembliENST00000253107; ENSP00000253107; ENSG00000130810. [Q9NQ55-1]
    GeneIDi56342.
    692312.
    KEGGihsa:56342.
    hsa:692312.
    UCSCiuc002mmz.2. human. [Q9NQ55-1]

    Polymorphism databases

    DMDMi21264056.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ292529 mRNA. Translation: CAB99252.1 .
    AC020931 Genomic DNA. No translation available.
    BC000535 mRNA. Translation: AAH00535.2 .
    BC009833 mRNA. Translation: AAH09833.1 .
    BC033202 mRNA. Translation: AAH33202.1 .
    BC171852 mRNA. No translation available.
    AJ300588 mRNA. Translation: CAC18877.1 . Different termination.
    CCDSi CCDS12225.1. [Q9NQ55-1 ]
    PIRi JC7359.
    RefSeqi NP_001035754.1. NM_001040664.2.
    NP_001185619.1. NM_001198690.1. [Q9NQ55-3 ]
    NP_064615.3. NM_020230.5. [Q9NQ55-1 ]
    UniGenei Hs.14468.

    3D structure databases

    ProteinModelPortali Q9NQ55.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121141. 14 interactions.
    593098. 2 interactions.
    IntActi Q9NQ55. 7 interactions.
    MINTi MINT-3072003.
    STRINGi 9606.ENSP00000253107.

    PTM databases

    PhosphoSitei Q9NQ55.

    Polymorphism databases

    DMDMi 21264056.

    2D gel databases

    SWISS-2DPAGE Q9NQ55.

    Proteomic databases

    MaxQBi Q9NQ55.
    PaxDbi Q9NQ55.
    PRIDEi Q9NQ55.

    Protocols and materials databases

    DNASUi 56342.
    692312.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000253107 ; ENSP00000253107 ; ENSG00000130810 . [Q9NQ55-1 ]
    GeneIDi 56342.
    692312.
    KEGGi hsa:56342.
    hsa:692312.
    UCSCi uc002mmz.2. human. [Q9NQ55-1 ]

    Organism-specific databases

    CTDi 56342.
    692312.
    GeneCardsi GC19P010216.
    GC19P010217.
    HGNCi HGNC:9227. PPAN.
    HPAi HPA043265.
    MIMi 607793. gene.
    neXtProti NX_Q9NQ55.
    PharmGKBi PA162399971.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG272199.
    HOGENOMi HOG000210038.
    HOVERGENi HBG026954.
    InParanoidi Q9NQ55.
    KOi K14859.
    OMAi LGVTHLM.
    PhylomeDBi Q9NQ55.
    TreeFami TF318923.

    Miscellaneous databases

    ChiTaRSi PPAN. human.
    GeneWikii PPAN.
    NextBioi 124574.
    PROi Q9NQ55.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NQ55.
    Bgeei Q9NQ55.
    CleanExi HS_PPAN.
    Genevestigatori Q9NQ55.

    Family and domain databases

    InterProi IPR007109. Brix.
    [Graphical view ]
    Pfami PF04427. Brix. 1 hit.
    [Graphical view ]
    SMARTi SM00879. Brix. 1 hit.
    [Graphical view ]
    PROSITEi PS50833. BRIX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, genomic organization, and tissue distribution of human Ssf-1."
      Suarez-Huerta N., Boeynaems J.-M., Communi D.
      Biochem. Biophys. Res. Commun. 275:37-42(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Placenta.
    2. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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; 2 AND 3).
      Tissue: Brain, Placenta and Skin.
    4. "Cotranscription and intergenic splicing of human P2Y11 and SSF1 genes."
      Communi D., Suarez-Huerta N., Dussossoy D., Savi P., Boeynaems J.-M.
      J. Biol. Chem. 276:16561-16566(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-427, TISSUE SPECIFICITY, TRANS-SPLICING.
      Tissue: Placenta.
    5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "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-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238; SER-240 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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].
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-238; SER-240 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "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-238; SER-240 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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-238; SER-240 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSSF1_HUMAN
    AccessioniPrimary (citable) accession number: Q9NQ55
    Secondary accession number(s): C9J3F9, Q9BW97, Q9H170
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 27, 2002
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 125 of the entry and version 1 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

    Miscellaneous

    A chimeric transcript, characterized by the first third of PPAN exon 12 joined to P2RY11 exon 2, has been detected. It is possibly produced by trans-splicing. The chimeric transcript is widely expressed and can be induced by retinoic acid during the granulocytic differentiation of the HL-60 cell line. The resulting chimeric protein shows a much lower activity than the non-chimeric P2RY11 gene product, but qualitatively indistinguishable (PubMed:11278528).1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3