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Q99590

- SCAFB_HUMAN

UniProt

Q99590 - SCAFB_HUMAN

Protein

Protein SCAF11

Gene

SCAF11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (07 Jul 2009)
      Previous versions | rss
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    Functioni

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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri41 – 8242RING-type; degeneratePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. mRNA processing Source: ProtInc
    2. RNA splicing Source: UniProtKB
    3. RNA splicing, via transesterification reactions Source: UniProtKB
    4. spliceosomal complex assembly Source: UniProtKB

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein SCAF11
    Alternative name(s):
    CTD-associated SR protein 11
    Renal carcinoma antigen NY-REN-40
    SC35-interacting protein 1
    SR-related and CTD-associated factor 11
    SRSF2-interacting protein
    Serine/arginine-rich splicing factor 2-interacting protein
    Splicing factor, arginine/serine-rich 2-interacting protein
    Splicing regulatory protein 129
    Short name:
    SRrp129
    Gene namesi
    Name:SCAF11
    Synonyms:CASP11, SFRS2IP, SIP1, SRSF2IP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:10784. SCAF11.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleolus Source: HPA
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35700.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14631463Protein SCAF11PRO_0000076314Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei338 – 3381Phosphoserine1 Publication
    Modified residuei341 – 3411Phosphoserine1 Publication
    Modified residuei344 – 3441Phosphoserine1 Publication
    Modified residuei400 – 4001Phosphoserine1 Publication
    Modified residuei401 – 4011Phosphoserine1 Publication
    Modified residuei402 – 4021Phosphoserine1 Publication
    Modified residuei405 – 4051Phosphoserine5 Publications
    Modified residuei410 – 4101Phosphothreonine1 Publication
    Modified residuei413 – 4131Phosphoserine1 Publication
    Modified residuei533 – 5331Phosphoserine1 Publication
    Modified residuei608 – 6081Phosphoserine4 Publications
    Modified residuei614 – 6141Phosphoserine2 Publications
    Modified residuei680 – 6801Phosphoserine2 Publications
    Modified residuei687 – 6871Phosphoserine1 Publication
    Modified residuei723 – 7231Phosphoserine1 Publication
    Modified residuei726 – 7261Phosphoserine1 Publication
    Modified residuei769 – 7691Phosphothreonine1 Publication
    Modified residuei771 – 7711Phosphoserine1 Publication
    Modified residuei776 – 7761Phosphoserine2 Publications
    Modified residuei796 – 7961Phosphoserine4 Publications
    Modified residuei798 – 7981Phosphoserine1 Publication
    Modified residuei802 – 8021Phosphoserine3 Publications
    Modified residuei807 – 8071Phosphothreonine1 Publication
    Modified residuei963 – 9631Phosphoserine1 Publication
    Modified residuei1127 – 11271Phosphoserine2 Publications
    Modified residuei1169 – 11691Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ99590.
    PaxDbiQ99590.
    PRIDEiQ99590.

    PTM databases

    PhosphoSiteiQ99590.

    Miscellaneous databases

    PMAP-CutDBQ99590.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ99590.
    BgeeiQ99590.
    CleanExiHS_SFRS2IP.
    HS_SIP1.
    GenevestigatoriQ99590.

    Organism-specific databases

    HPAiHPA038862.
    HPA045456.
    HPA046345.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi114610. 14 interactions.
    IntActiQ99590. 2 interactions.
    MINTiMINT-2866162.
    STRINGi9606.ENSP00000358374.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99590.
    SMRiQ99590. Positions 37-80.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi841 – 985145Arg-richAdd
    BLAST
    Compositional biasi1225 – 128561Pro-richAdd
    BLAST

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri41 – 8242RING-type; degeneratePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG300312.
    HOVERGENiHBG101126.
    InParanoidiQ99590.
    OMAiLELSWFP.
    OrthoDBiEOG7F24SX.
    PhylomeDBiQ99590.
    TreeFamiTF332183.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF13639. zf-RING_2. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]
    PROSITEiPS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q99590-1) [UniParc]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

    MKKKTVCTLN MGDKKYEDME GEENGDNTIS TGLLYSEADR CPICLNCLLE     50
    KEVGFPESCN HVFCMTCILK WAETLASCPI DRKPFQAVFK FSALEGYVKV 100
    QVKKQLRETK DKKNENSFEK QVSCHENSKS CIRRKAIVRE DLLSAKVCDL 150
    KWIHRNSLYS ETGGKKNAAI KINKPQRSNW STNQCFRNFF SNMFSSVSHS 200
    GESSFTYRAY CTEFIEASEI SALIRQKRHE LELSWFPDTL PGIGRIGFIP 250
    WNVETEVLPL ISSVLPRTIF PTSTISFEHF GTSCKGYALA HTQEGEEKKQ 300
    TSGTSNTRGS RRKPAMTTPT RRSTRNTRAE TASQSQRSPI SDNSGCDAPG 350
    NSNPSLSVPS SAESEKQTRQ APKRKSVRRG RKPPLLKKKL RSSVAAPEKS 400
    SSNDSVDEET AESDTSPVLE KEHQPDVDSS NICTVQTHVE NQSANCLKSC 450
    NEQIEESEKH TANYDTEERV GSSSSESCAQ DLPVLVGEEG EVKKLENTGI 500
    EANVLCLESE ISENILEKGG DPLEKQDQIS GLSQSEVKTD VCTVHLPNDF 550
    PTCLTSESKV YQPVSCPLSD LSENVESVVN EEKITESSLV EITEHKDFTL 600
    KTEELIESPK LESSEGEIIQ TVDRQSVKSP EVQLLGHVET EDVEIIATCD 650
    TFGNEDFNNI QDSENNLLKN NLLNTKLEKS LEEKNESLTE HPRSTELPKT 700
    HIEQIQKHFS EDNNEMIPME CDSFCSDQNE SEVEPSVNAD LKQMNENSVT 750
    HCSENNMPSS DLADEKVETV SQPSESPKDT IDKTKKPRTR RSRFHSPSTT 800
    WSPNKDTPQE KKRPQSPSPR RETGKESRKS QSPSPKNESA RGRKKSRSQS 850
    PKKDIARERR QSQSRSPKRD TTRESRRSES LSPRRETSRE NKRSQPRVKD 900
    SSPGEKSRSQ SRERESDRDG QRRERERRTR KWSRSRSHSR SPSRCRTKSK 950
    SSSFGRIDRD SYSPRWKGRW ANDGWRCPRG NDRYRKNDPE KQNENTRKEK 1000
    NDIHLDADDP NSADKHRNDC PNWITEKINS GPDPRTRNPE KLKESHWEEN 1050
    RNENSGNSWN KNFGSGWVSN RGRGRGNRGR GTYRSSFAYK DQNENRWQNR 1100
    KPLSGNSNSS GSESFKFVEQ QSYKRKSEQE FSFDTPADRS GWTSASSWAV 1150
    RKTLPADVQN YYSRRGRNSS GPQSGWMKQE EETSGQDSSL KDQTNQQVDG 1200
    SQLPINMMQP QMNVMQQQMN AQHQPMNIFP YPVGVHAPLM NIQRNPFNIH 1250
    PQLPLHLHTG VPLMQVATPT SVSQGLPPPP PPPPPSQQVN YIASQPDGKQ 1300
    LQGIPSSSHV SNNMSTPVLP APTAAPGNTG MVQGPSSGNT SSSSHSKASN 1350
    AAVKLAESKV SVAVEASADS SKTDKKLQIQ EKAAQEVKLA IKPFYQNKDI 1400
    TKEEYKEIVR KAVDKVCHSK SGEVNSTKVA NLVKAYVDKY KYSRKGSQKK 1450
    TLEEPVSTEK NIG 1463
    Length:1,463
    Mass (Da):164,652
    Last modified:July 7, 2009 - v2
    Checksum:i7170B88544BAF7D4
    GO
    Isoform 2 (identifier: Q99590-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,148
    Mass (Da):128,875
    Checksum:iB57FD40EE5E4C48C
    GO

    Sequence cautioni

    The sequence AAH40951.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAC39565.1 differs from that shown. Reason: Frameshift at position 62.
    The sequence AAC39565.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH40951.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti584 – 5841I → M in AAH40951. (PubMed:15489334)Curated
    Sequence conflicti623 – 6231D → G in AAH40951. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti657 – 6571F → Y.
    Corresponds to variant rs7315731 [ dbSNP | Ensembl ].
    VAR_059722
    Natural varianti1261 – 12611V → L.
    Corresponds to variant rs11574973 [ dbSNP | Ensembl ].
    VAR_059723

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 315315Missing in isoform 2. 1 PublicationVSP_037665Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11251 mRNA. Translation: CAA72121.1.
    AF030234 mRNA. Translation: AAC39565.1. Sequence problems.
    AC000015 Genomic DNA. No translation available.
    CH471111 Genomic DNA. Translation: EAW57892.1.
    CH471111 Genomic DNA. Translation: EAW57894.1.
    BC040951 mRNA. Translation: AAH40951.1. Sequence problems.
    CCDSiCCDS8748.2. [Q99590-1]
    PIRiT09073.
    RefSeqiNP_004710.2. NM_004719.2. [Q99590-1]
    UniGeneiHs.210367.

    Genome annotation databases

    EnsembliENST00000369367; ENSP00000358374; ENSG00000139218. [Q99590-1]
    ENST00000465950; ENSP00000449812; ENSG00000139218. [Q99590-2]
    GeneIDi9169.
    KEGGihsa:9169.
    UCSCiuc001row.3. human. [Q99590-1]

    Polymorphism databases

    DMDMi251757337.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

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

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi 114610. 14 interactions.
    IntActi Q99590. 2 interactions.
    MINTi MINT-2866162.
    STRINGi 9606.ENSP00000358374.

    PTM databases

    PhosphoSitei Q99590.

    Polymorphism databases

    DMDMi 251757337.

    Proteomic databases

    MaxQBi Q99590.
    PaxDbi Q99590.
    PRIDEi Q99590.

    Protocols and materials databases

    DNASUi 9169.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

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

    Organism-specific databases

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

    Phylogenomic databases

    eggNOGi NOG300312.
    HOVERGENi HBG101126.
    InParanoidi Q99590.
    OMAi LELSWFP.
    OrthoDBi EOG7F24SX.
    PhylomeDBi Q99590.
    TreeFami TF332183.

    Miscellaneous databases

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

    Gene expression databases

    ArrayExpressi Q99590.
    Bgeei Q99590.
    CleanExi HS_SFRS2IP.
    HS_SIP1.
    Genevestigatori Q99590.

    Family and domain databases

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

    Publicationsi

    1. "A novel SR-related protein specifically interacts with the carboxy-terminal domain (CTD) of RNA polymerase II through a conserved interaction domain."
      Tanner S., Stagljar I., Georgiev O., Schaffner W., Bourquin J.-P.
      Biol. Chem. 378:565-571(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
      Tissue: Lymphocyte.
    2. "Sip1, a novel RS domain-containing protein essential for pre-mRNA splicing."
      Zhang W.-J., Wu J.Y.
      Mol. Cell. Biol. 18:676-684(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH SRSF2; U2AF2 AND SNRNP70, SUBCELLULAR LOCATION.
      Tissue: Cervix carcinoma.
    3. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 212-669 (ISOFORM 1).
      Tissue: Prostate.
    6. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
      Tissue: Renal cell carcinoma.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-723 AND SER-726, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    9. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-338; SER-341; SER-344; SER-405; THR-410; SER-533; SER-608; SER-614; SER-680; SER-796; SER-802; THR-807; SER-963 AND SER-1127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-413; SER-608; SER-796; SER-798 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-608; SER-614; SER-680; SER-687; SER-771; SER-776; SER-796; SER-1127 AND SER-1169, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-400; SER-401; SER-402; SER-405; THR-769; SER-776; SER-796 AND SER-802, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSCAFB_HUMAN
    AccessioniPrimary (citable) accession number: Q99590
    Secondary accession number(s): A6NEU9, A6NLW5, Q8IW59
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 7, 2006
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    This is version 106 of the entry and version 2 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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