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Q9UHB7

- AFF4_HUMAN

UniProt

Q9UHB7 - AFF4_HUMAN

Protein

AF4/FMR2 family member 4

Gene

AFF4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Key component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. In the SEC complex, AFF4 acts as a central scaffold that recruits other factors through direct interactions with ELL proteins (ELL, ELL2 or ELL3) and the P-TEFb complex. In case of infection by HIV-1 virus, the SEC complex is recruited by the viral Tat protein to stimulate viral gene expression.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei350 – 3512Breakpoint for insertion to form KMT2A/MLL1-AFF4 fusion protein

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. sequence-specific DNA binding transcription factor activity Source: ProtInc

    GO - Biological processi

    1. spermatid development Source: Ensembl
    2. transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AF4/FMR2 family member 4
    Alternative name(s):
    ALL1-fused gene from chromosome 5q31 protein
    Short name:
    Protein AF-5q31
    Major CDK9 elongation factor-associated protein
    Gene namesi
    Name:AFF4
    Synonyms:AF5Q31, MCEF
    ORF Names:HSPC092
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:17869. AFF4.

    Subcellular locationi

    Nucleus 1 Publication
    Note: Associates to transcriptionally active chromatin but not at snRNA genes.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving AFF4 is found in acute lymphoblastic leukemia (ALL). Insertion ins(5;11)(q31;q13q23) that forms a KMT2A/MLL1-AFF4 fusion protein.

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA142672641.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11631163AF4/FMR2 family member 4PRO_0000239393Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei387 – 3871Phosphoserine1 Publication
    Modified residuei388 – 3881Phosphoserine1 Publication
    Modified residuei389 – 3891Phosphoserine1 Publication
    Modified residuei392 – 3921Phosphoserine1 Publication
    Modified residuei549 – 5491Phosphoserine2 Publications
    Modified residuei671 – 6711Phosphoserine2 Publications
    Modified residuei674 – 6741Phosphothreonine1 Publication
    Modified residuei694 – 6941Phosphoserine1 Publication
    Modified residuei703 – 7031Phosphoserine2 Publications
    Modified residuei706 – 7061Phosphoserine2 Publications
    Modified residuei712 – 7121Phosphotyrosine1 Publication
    Modified residuei814 – 8141Phosphoserine2 Publications
    Modified residuei822 – 8221N6-acetyllysineBy similarity
    Modified residuei836 – 8361Phosphoserine1 Publication
    Modified residuei1043 – 10431Phosphoserine4 Publications
    Modified residuei1055 – 10551Phosphoserine2 Publications
    Modified residuei1058 – 10581Phosphoserine3 Publications
    Modified residuei1062 – 10621Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UHB7.
    PaxDbiQ9UHB7.
    PeptideAtlasiQ9UHB7.
    PRIDEiQ9UHB7.

    PTM databases

    PhosphoSiteiQ9UHB7.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Strongly expressed in heart, placenta, skeletal muscle, pancreas and to a lower extent in brain.2 Publications

    Developmental stagei

    Expressed in fetal heart, lung, brain and to a lower extent liver.1 Publication

    Gene expression databases

    ArrayExpressiQ9UHB7.
    BgeeiQ9UHB7.
    CleanExiHS_AFF4.
    GenevestigatoriQ9UHB7.

    Organism-specific databases

    HPAiHPA023690.

    Interactioni

    Subunit structurei

    Interacts with ELL3; the interaction is direct By similarity. Interacts with ELL2; the interaction is direct and leads to stabilize ELL2 and prevent ELL2 ubiquitination and degradation. Component of the super elongation complex (SEC), at least composed of EAF1, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Interacts with ELL.By similarity5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCNT1O605635EBI-395282,EBI-2479671
    MLLT1Q031118EBI-395282,EBI-1384215
    MLLT3P425684EBI-395282,EBI-716132
    tatP046084EBI-395282,EBI-6164389From a different organism.

    Protein-protein interaction databases

    BioGridi118016. 22 interactions.
    IntActiQ9UHB7. 16 interactions.
    MINTiMINT-1469196.
    STRINGi9606.ENSP00000265343.

    Structurei

    Secondary structure

    1
    1163
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 1813
    Helixi47 – 5610
    Helixi59 – 624
    Turni63 – 653

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4IMYX-ray2.94G/H/I2-73[»]
    4OGRX-ray3.00C/G/L2-73[»]
    4OR5X-ray2.90E/J32-69[»]
    ProteinModelPortaliQ9UHB7.
    SMRiQ9UHB7. Positions 3-67.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi102 – 461360Ser-richAdd
    BLAST
    Compositional biasi836 – 89964Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the AF4 family.Curated

    Phylogenomic databases

    eggNOGiNOG121636.
    HOVERGENiHBG004189.
    InParanoidiQ9UHB7.
    KOiK15185.
    OMAiKRYNPSS.
    OrthoDBiEOG767390.
    PhylomeDBiQ9UHB7.
    TreeFamiTF326216.

    Family and domain databases

    InterProiIPR007797. TF_AF4/FMR2.
    [Graphical view]
    PANTHERiPTHR10528. PTHR10528. 1 hit.
    PfamiPF05110. AF-4. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UHB7-1) [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

    MNREDRNVLR MKERERRNQE IQQGEDAFPP SSPLFAEPYK VTSKEDKLSS     50
    RIQSMLGNYD EMKDFIGDRS IPKLVAIPKP TVPPSADEKS NPNFFEQRHG 100
    GSHQSSKWTP VGPAPSTSQS QKRSSGLQSG HSSQRTSAGS SSGTNSSGQR 150
    HDRESYNNSG SSSRKKGQHG SEHSKSRSSS PGKPQAVSSL NSSHSRSHGN 200
    DHHSKEHQRS KSPRDPDANW DSPSRVPFSS GQHSTQSFPP SLMSKSNSML 250
    QKPTAYVRPM DGQESMEPKL SSEHYSSQSH GNSMTELKPS SKAHLTKLKI 300
    PSQPLDASAS GDVSCVDEIL KEMTHSWPPP LTAIHTPCKT EPSKFPFPTK 350
    ESQQSNFGTG EQKRYNPSKT SNGHQSKSML KDDLKLSSSE DSDGEQDCDK 400
    TMPRSTPGSN SEPSHHNSEG ADNSRDDSSS HSGSESSSGS DSESESSSSD 450
    SEANEPSQSA SPEPEPPPTN KWQLDNWLNK VNPHKVSPAS SVDSNIPSSQ 500
    GYKKEGREQG TGNSYTDTSG PKETSSATPG RDSKTIQKGS ESGRGRQKSP 550
    AQSDSTTQRR TVGKKQPKKA EKAAAEEPRG GLKIESETPV DLASSMPSSR 600
    HKAATKGSRK PNIKKESKSS PRPTAEKKKY KSTSKSSQKS REIIETDTSS 650
    SDSDESESLP PSSQTPKYPE SNRTPVKPSS VEEEDSFFRQ RMFSPMEEKE 700
    LLSPLSEPDD RYPLIVKIDL NLLTRIPGKP YKETEPPKGE KKNVPEKHTR 750
    EAQKQASEKV SNKGKRKHKN EDDNRASESK KPKTEDKNSA GHKPSSNRES 800
    SKQSAAKEKD LLPSPAGPVP SKDPKTEHGS RKRTISQSSS LKSSSNSNKE 850
    TSGSSKNSSS TSKQKKTEGK TSSSSKEVKE KAPSSSSNCP PSAPTLDSSK 900
    PRRTKLVFDD RNYSADHYLQ EAKKLKHNAD ALSDRFEKAV YYLDAVVSFI 950
    ECGNALEKNA QESKSPFPMY SETVDLIKYT MKLKNYLAPD ATAADKRLTV 1000
    LCLRCESLLY LRLFKLKKEN ALKYSKTLTE HLKNSYNNSQ APSPGLGSKA 1050
    VGMPSPVSPK LSPGNSGNYS SGASSASASG SSVTIPQKIH QMAASYVQVT 1100
    SNFLYATEIW DQAEQLSKEQ KEFFAELDKV MGPLIFNASI MTDLVRYTRQ 1150
    GLHWLRQDAK LIS 1163
    Length:1,163
    Mass (Da):127,459
    Last modified:May 1, 2000 - v1
    Checksum:i474E1906B8832AC1
    GO
    Isoform 2 (identifier: Q9UHB7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         880-900: EKAPSSSSNCPPSAPTLDSSK → VKCWGPGAFENHSTCHVTFPG
         901-1163: Missing.

    Show »
    Length:900
    Mass (Da):98,205
    Checksum:iA7C5BAE4A45086AE
    GO
    Isoform 3 (identifier: Q9UHB7-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         351-353: ESQ → VSK
         354-1163: Missing.

    Show »
    Length:353
    Mass (Da):38,823
    Checksum:iF7811E19E60C9A92
    GO

    Sequence cautioni

    The sequence AAI00288.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence BAD92784.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti264 – 2641E → G in AAM00184. (PubMed:12065898)Curated
    Sequence conflicti359 – 3591T → I in AAM00184. (PubMed:12065898)Curated
    Sequence conflicti383 – 3831D → G in AAM00184. (PubMed:12065898)Curated
    Sequence conflicti445 – 4451E → G in AAM00184. (PubMed:12065898)Curated
    Sequence conflicti870 – 8701K → R in AAF28915. (PubMed:11042152)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti136 – 1361T → P.
    Corresponds to variant rs34527550 [ dbSNP | Ensembl ].
    VAR_053003
    Natural varianti757 – 7571S → T Found in a clear cell renal carcinoma case; somatic mutation. 1 Publication
    VAR_064693

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei351 – 3533ESQ → VSK in isoform 3. 1 PublicationVSP_019218
    Alternative sequencei354 – 1163810Missing in isoform 3. 1 PublicationVSP_019219Add
    BLAST
    Alternative sequencei880 – 90021EKAPS…LDSSK → VKCWGPGAFENHSTCHVTFP G in isoform 2. 2 PublicationsVSP_019220Add
    BLAST
    Alternative sequencei901 – 1163263Missing in isoform 2. 2 PublicationsVSP_019221Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF197927 mRNA. Translation: AAF18981.1.
    AF213987 mRNA. Translation: AAM00184.2.
    AB209547 mRNA. Translation: BAD92784.1. Different initiation.
    AC004500 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW62305.1.
    BC063007 mRNA. Translation: AAH63007.1.
    BC100287 mRNA. Translation: AAI00288.1. Sequence problems.
    BC137226 mRNA. Translation: AAI37227.1.
    AF161355 mRNA. Translation: AAF28915.1.
    CCDSiCCDS4164.1. [Q9UHB7-1]
    RefSeqiNP_055238.1. NM_014423.3. [Q9UHB7-1]
    XP_005272020.1. XM_005271963.2. [Q9UHB7-1]
    UniGeneiHs.519313.
    Hs.664840.

    Genome annotation databases

    EnsembliENST00000265343; ENSP00000265343; ENSG00000072364. [Q9UHB7-1]
    ENST00000378595; ENSP00000367858; ENSG00000072364. [Q9UHB7-2]
    GeneIDi27125.
    KEGGihsa:27125.
    UCSCiuc003kyd.3. human. [Q9UHB7-1]
    uc003kye.1. human. [Q9UHB7-2]
    uc003kyf.4. human. [Q9UHB7-3]

    Polymorphism databases

    DMDMi74720814.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF197927 mRNA. Translation: AAF18981.1 .
    AF213987 mRNA. Translation: AAM00184.2 .
    AB209547 mRNA. Translation: BAD92784.1 . Different initiation.
    AC004500 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW62305.1 .
    BC063007 mRNA. Translation: AAH63007.1 .
    BC100287 mRNA. Translation: AAI00288.1 . Sequence problems.
    BC137226 mRNA. Translation: AAI37227.1 .
    AF161355 mRNA. Translation: AAF28915.1 .
    CCDSi CCDS4164.1. [Q9UHB7-1 ]
    RefSeqi NP_055238.1. NM_014423.3. [Q9UHB7-1 ]
    XP_005272020.1. XM_005271963.2. [Q9UHB7-1 ]
    UniGenei Hs.519313.
    Hs.664840.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4IMY X-ray 2.94 G/H/I 2-73 [» ]
    4OGR X-ray 3.00 C/G/L 2-73 [» ]
    4OR5 X-ray 2.90 E/J 32-69 [» ]
    ProteinModelPortali Q9UHB7.
    SMRi Q9UHB7. Positions 3-67.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118016. 22 interactions.
    IntActi Q9UHB7. 16 interactions.
    MINTi MINT-1469196.
    STRINGi 9606.ENSP00000265343.

    PTM databases

    PhosphoSitei Q9UHB7.

    Polymorphism databases

    DMDMi 74720814.

    Proteomic databases

    MaxQBi Q9UHB7.
    PaxDbi Q9UHB7.
    PeptideAtlasi Q9UHB7.
    PRIDEi Q9UHB7.

    Protocols and materials databases

    DNASUi 27125.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265343 ; ENSP00000265343 ; ENSG00000072364 . [Q9UHB7-1 ]
    ENST00000378595 ; ENSP00000367858 ; ENSG00000072364 . [Q9UHB7-2 ]
    GeneIDi 27125.
    KEGGi hsa:27125.
    UCSCi uc003kyd.3. human. [Q9UHB7-1 ]
    uc003kye.1. human. [Q9UHB7-2 ]
    uc003kyf.4. human. [Q9UHB7-3 ]

    Organism-specific databases

    CTDi 27125.
    GeneCardsi GC05M132211.
    HGNCi HGNC:17869. AFF4.
    HPAi HPA023690.
    MIMi 604417. gene.
    neXtProti NX_Q9UHB7.
    PharmGKBi PA142672641.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG121636.
    HOVERGENi HBG004189.
    InParanoidi Q9UHB7.
    KOi K15185.
    OMAi KRYNPSS.
    OrthoDBi EOG767390.
    PhylomeDBi Q9UHB7.
    TreeFami TF326216.

    Miscellaneous databases

    ChiTaRSi AFF4. human.
    GenomeRNAii 27125.
    NextBioi 49830.
    PROi Q9UHB7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UHB7.
    Bgeei Q9UHB7.
    CleanExi HS_AFF4.
    Genevestigatori Q9UHB7.

    Family and domain databases

    InterProi IPR007797. TF_AF4/FMR2.
    [Graphical view ]
    PANTHERi PTHR10528. PTHR10528. 1 hit.
    Pfami PF05110. AF-4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "AF5q31, a newly identified AF4-related gene, is fused to MLL in infant acute lymphoblastic leukemia with ins(5;11)(q31;q13q23)."
      Taki T., Kano H., Taniwaki M., Sako M., Yanagisawa M., Hayashi Y.
      Proc. Natl. Acad. Sci. U.S.A. 96:14535-14540(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Tissue: Placenta.
    2. "MCEF, the newest member of the AF4 family of transcription factors involved in leukemia, is a positive transcription elongation factor-b-associated protein."
      Estable M.C., Naghavi M.H., Kato H., Xiao H., Qin J., Vahlne A., Roeder R.G.
      J. Biomed. Sci. 9:234-245(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 111-122, IDENTIFICATION IN P-TEFB COMPLEX, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
      Tissue: Fetal brain.
    3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    4. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-363 (ISOFORMS 1/2).
      Tissue: Blood, Brain and Skin.
    7. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 788-1163 (ISOFORM 2).
      Tissue: Umbilical cord blood.
    8. "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-703 AND SER-706, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    11. "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 THR-674, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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-549; SER-814; SER-1043 AND SER-1055, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387; SER-388; SER-389; SER-392; SER-671; SER-694; SER-703; SER-706; TYR-712; SER-1043; SER-1055; SER-1058 AND SER-1062, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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].
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-549; SER-671; SER-1043 AND SER-1058, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1058, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "HIV-1 Tat and host AFF4 recruit two transcription elongation factors into a bifunctional complex for coordinated activation of HIV-1 transcription."
      He N., Liu M., Hsu J., Xue Y., Chou S., Burlingame A., Krogan N.J., Alber T., Zhou Q.
      Mol. Cell 38:428-438(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE SEC COMPLEX.
    18. "AFF4, a component of the ELL/P-TEFb elongation complex and a shared subunit of MLL chimeras, can link transcription elongation to leukemia."
      Lin C., Smith E.R., Takahashi H., Lai K.C., Martin-Brown S., Florens L., Washburn M.P., Conaway J.W., Conaway R.C., Shilatifard A.
      Mol. Cell 37:429-437(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE SEC COMPLEX.
    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-814; SER-836 AND SER-1043, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: IDENTIFICATION IN THE SEC COMPLEX.
    22. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "The ubiquitin ligase Siah1 controls ELL2 stability and formation of super elongation complexes to modulate gene transcription."
      Liu M., Hsu J., Chan C., Li Z., Zhou Q.
      Mol. Cell 46:325-334(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ELL2.
    24. "The super elongation complex (SEC) family in transcriptional control."
      Luo Z., Lin C., Shilatifard A.
      Nat. Rev. Mol. Cell Biol. 13:543-547(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON THE SUPER ELONGATION COMPLEX.
    25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "HIV-1 Tat recruits transcription elongation factors dispersed along a flexible AFF4 scaffold."
      Chou S., Upton H., Bao K., Schulze-Gahmen U., Samelson A.J., He N., Nowak A., Lu H., Krogan N.J., Zhou Q., Alber T.
      Proc. Natl. Acad. Sci. U.S.A. 110:E123-E131(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    27. Cited for: VARIANT THR-757.

    Entry informationi

    Entry nameiAFF4_HUMAN
    AccessioniPrimary (citable) accession number: Q9UHB7
    Secondary accession number(s): B2RP19
    , B7WPD2, Q498B2, Q59FB3, Q6P592, Q8TDR1, Q9P0E4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 13, 2006
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 109 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

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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