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P51825

- AFF1_HUMAN

UniProt

P51825 - AFF1_HUMAN

Protein

AF4/FMR2 family member 1

Gene

AFF1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

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

    GO - Biological processi

    1. positive regulation of transcription, DNA-templated Source: Ensembl

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AF4/FMR2 family member 1
    Alternative name(s):
    ALL1-fused gene from chromosome 4 protein
    Short name:
    Protein AF-4
    Protein FEL
    Proto-oncogene AF4
    Gene namesi
    Name:AFF1
    Synonyms:AF4, FEL, MLLT2, PBM1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:7135. AFF1.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving AFF1 is associated with acute leukemias. Translocation t(4;11)(q21;q23) with KMT2A/MLL1. The result is a rogue activator protein.

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    Orphaneti99860. Precursor B-cell acute lymphoblastic leukemia.
    PharmGKBiPA30851.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12101210AF4/FMR2 family member 1PRO_0000215910Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei206 – 2061Phosphoserine5 Publications
    Modified residuei212 – 2121Phosphoserine3 Publications
    Modified residuei220 – 2201Phosphothreonine1 Publication
    Modified residuei588 – 5881Phosphoserine1 Publication
    Modified residuei681 – 6811N6-acetyllysine1 Publication
    Modified residuei697 – 6971Phosphothreonine2 Publications
    Modified residuei750 – 7501Phosphoserine3 Publications
    Modified residuei755 – 7551Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP51825.
    PaxDbiP51825.
    PRIDEiP51825.

    PTM databases

    PhosphoSiteiP51825.

    Expressioni

    Gene expression databases

    ArrayExpressiP51825.
    BgeeiP51825.
    CleanExiHS_AFF1.
    GenevestigatoriP51825.

    Interactioni

    Subunit structurei

    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).2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    tatP046083EBI-2610180,EBI-6164389From a different organism.

    Protein-protein interaction databases

    BioGridi110445. 28 interactions.
    DIPiDIP-56407N.
    IntActiP51825. 15 interactions.
    MINTiMINT-1198004.
    STRINGi9606.ENSP00000305689.

    Structurei

    Secondary structure

    1
    1210
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni768 – 7703

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LM0NMR-A738-779[»]
    ProteinModelPortaliP51825.
    SMRiP51825. Positions 10-71, 738-779.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi483 – 49210Poly-Ser
    Compositional biasi835 – 8439Poly-Ser
    Compositional biasi866 – 8694Poly-Pro
    Compositional biasi871 – 8744Poly-Ser

    Sequence similaritiesi

    Belongs to the AF4 family.Curated

    Phylogenomic databases

    eggNOGiNOG120323.
    HOVERGENiHBG004189.
    KOiK15184.
    OMAiEPYKTAK.
    OrthoDBiEOG767390.
    PhylomeDBiP51825.
    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: P51825-1) [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

    MAAQSSLYND DRNLLRIREK ERRNQEAHQE KEAFPEKIPL FGEPYKTAKG     50
    DELSSRIQNM LGNYEEVKEF LSTKSHTHRL DASENRLGKP KYPLIPDKGS 100
    SIPSSSFHTS VHHQSIHTPA SGPLSVGNIS HNPKMAQPRT EPMPSLHAKS 150
    CGPPDSQHLT QDRLGQEGFG SSHHKKGDRR ADGDHCASVT DSAPERELSP 200
    LISLPSPVPP LSPIHSNQQT LPRTQGSSKV HGSSNNSKGY CPAKSPKDLA 250
    VKVHDKETPQ DSLVAPAQPP SQTFPPPSLP SKSVAMQQKP TAYVRPMDGQ 300
    DQAPSESPEL KPLPEDYRQQ TFEKTDLKVP AKAKLTKLKM PSQSVEQTYS 350
    NEVHCVEEIL KEMTHSWPPP LTAIHTPSTA EPSKFPFPTK DSQHVSSVTQ 400
    NQKQYDTSSK THSNSQQGTS SMLEDDLQLS DSEDSDSEQT PEKPPSSSAP 450
    PSAPQSLPEP VASAHSSSAE SESTSDSDSS SDSESESSSS DSEENEPLET 500
    PAPEPEPPTT NKWQLDNWLT KVSQPAAPPE GPRSTEPPRR HPESKGSSDS 550
    ATSQEHSESK DPPPKSSSKA PRAPPEAPHP GKRSCQKSPA QQEPPQRQTV 600
    GTKQPKKPVK ASARAGSRTS LQGEREPGLL PYGSRDQTSK DKPKVKTKGR 650
    PRAAASNEPK PAVPPSSEKK KHKSSLPAPS KALSGPEPAK DNVEDRTPEH 700
    FALVPLTESQ GPPHSGSGSR TSGCRQAVVV QEDSRKDRLP LPLRDTKLLS 750
    PLRDTPPPQS LMVKITLDLL SRIPQPPGKG SRQRKAEDKQ PPAGKKHSSE 800
    KRSSDSSSKL AKKRKGEAER DCDNKKIRLE KEIKSQSSSS SSSHKESSKT 850
    KPSRPSSQSS KKEMLPPPPV SSSSQKPAKP ALKRSRREAD TCGQDPPKSA 900
    SSTKSNHKDS SIPKQRRVEG KGSRSSSEHK GSSGDTANPF PVPSLPNGNS 950
    KPGKPQVKFD KQQADLHMRE AKKMKQKAEL MTDRVGKAFK YLEAVLSFIE 1000
    CGIATESESQ SSKSAYSVYS ETVDLIKFIM SLKSFSDATA PTQEKIFAVL 1050
    CMRCQSILNM AMFRCKKDIA IKYSRTLNKH FESSSKVAQA PSPCIASTGT 1100
    PSPLSPMPSP ASSVGSQSSA GSVGSSGVAA TISTPVTIQN MTSSYVTITS 1150
    HVLTAFDLWE QAEALTRKNK EFFARLSTNV CTLALNSSLV DLVHYTRQGF 1200
    QQLQELTKTP 1210
    Length:1,210
    Mass (Da):131,422
    Last modified:October 1, 1996 - v1
    Checksum:iF0E334DF8FC2FF04
    GO
    Isoform 2 (identifier: P51825-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-5: MAAQS → MAFTERVNSSGN
         1096-1096: A → AR

    Note: No experimental confirmation available.

    Show »
    Length:1,218
    Mass (Da):132,384
    Checksum:i8C9DCE41FF2EA841
    GO
    Isoform 3 (identifier: P51825-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1096-1096: A → AR

    Show »
    Length:1,211
    Mass (Da):131,578
    Checksum:iFD08BE7A2BE38BFC
    GO

    Sequence cautioni

    The sequence AAA36642.1 differs from that shown. Reason: Frameshift at positions 897, 905 and 1178.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 461K → R in AAA36642. (PubMed:8443374)Curated
    Sequence conflicti624 – 6241E → G in AAA36642. (PubMed:8443374)Curated
    Sequence conflicti762 – 7621M → V in BAG62103. (PubMed:14702039)Curated
    Sequence conflicti820 – 8201R → G in BAG62103. (PubMed:14702039)Curated
    Sequence conflicti899 – 9057SASSTKS → VPAVPRV in AAA36642. (PubMed:8443374)Curated
    Sequence conflicti928 – 9292EH → AD in AAA36642. (PubMed:8443374)Curated
    Sequence conflicti999 – 9991I → N in AAA36642. (PubMed:8443374)Curated
    Sequence conflicti1140 – 11401N → I in AAA36642. (PubMed:8443374)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti209 – 2091P → A.
    Corresponds to variant rs3733378 [ dbSNP | Ensembl ].
    VAR_020370
    Natural varianti1204 – 12041Q → K in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036130

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 55MAAQS → MAFTERVNSSGN in isoform 2. 1 PublicationVSP_046095
    Alternative sequencei1096 – 10961A → AR in isoform 2 and isoform 3. 2 PublicationsVSP_046096

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L13773 mRNA. Translation: AAA58360.1.
    L25050 mRNA. Translation: AAA36642.1. Frameshift.
    AK300364 mRNA. Translation: BAG62103.1.
    AC092658 Genomic DNA. No translation available.
    AC093779 Genomic DNA. No translation available.
    AC093827 Genomic DNA. No translation available.
    CCDSiCCDS3616.1. [P51825-1]
    CCDS54775.1. [P51825-2]
    PIRiA58198.
    I39410.
    RefSeqiNP_001160165.1. NM_001166693.1. [P51825-2]
    NP_005926.1. NM_005935.2. [P51825-1]
    XP_005263064.1. XM_005263007.1. [P51825-2]
    XP_005263065.1. XM_005263008.2. [P51825-2]
    UniGeneiHs.480190.

    Genome annotation databases

    EnsembliENST00000307808; ENSP00000305689; ENSG00000172493. [P51825-1]
    ENST00000395146; ENSP00000378578; ENSG00000172493. [P51825-2]
    GeneIDi4299.
    KEGGihsa:4299.
    UCSCiuc003hqj.4. human. [P51825-1]

    Polymorphism databases

    DMDMi1703194.

    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
    L13773 mRNA. Translation: AAA58360.1 .
    L25050 mRNA. Translation: AAA36642.1 . Frameshift.
    AK300364 mRNA. Translation: BAG62103.1 .
    AC092658 Genomic DNA. No translation available.
    AC093779 Genomic DNA. No translation available.
    AC093827 Genomic DNA. No translation available.
    CCDSi CCDS3616.1. [P51825-1 ]
    CCDS54775.1. [P51825-2 ]
    PIRi A58198.
    I39410.
    RefSeqi NP_001160165.1. NM_001166693.1. [P51825-2 ]
    NP_005926.1. NM_005935.2. [P51825-1 ]
    XP_005263064.1. XM_005263007.1. [P51825-2 ]
    XP_005263065.1. XM_005263008.2. [P51825-2 ]
    UniGenei Hs.480190.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LM0 NMR - A 738-779 [» ]
    ProteinModelPortali P51825.
    SMRi P51825. Positions 10-71, 738-779.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110445. 28 interactions.
    DIPi DIP-56407N.
    IntActi P51825. 15 interactions.
    MINTi MINT-1198004.
    STRINGi 9606.ENSP00000305689.

    PTM databases

    PhosphoSitei P51825.

    Polymorphism databases

    DMDMi 1703194.

    Proteomic databases

    MaxQBi P51825.
    PaxDbi P51825.
    PRIDEi P51825.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000307808 ; ENSP00000305689 ; ENSG00000172493 . [P51825-1 ]
    ENST00000395146 ; ENSP00000378578 ; ENSG00000172493 . [P51825-2 ]
    GeneIDi 4299.
    KEGGi hsa:4299.
    UCSCi uc003hqj.4. human. [P51825-1 ]

    Organism-specific databases

    CTDi 4299.
    GeneCardsi GC04P087856.
    HGNCi HGNC:7135. AFF1.
    MIMi 159557. gene.
    neXtProti NX_P51825.
    Orphaneti 99860. Precursor B-cell acute lymphoblastic leukemia.
    PharmGKBi PA30851.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG120323.
    HOVERGENi HBG004189.
    KOi K15184.
    OMAi EPYKTAK.
    OrthoDBi EOG767390.
    PhylomeDBi P51825.
    TreeFami TF326216.

    Miscellaneous databases

    ChiTaRSi AFF1. human.
    GeneWikii AFF1.
    GenomeRNAii 4299.
    NextBioi 16923.
    PROi P51825.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51825.
    Bgeei P51825.
    CleanExi HS_AFF1.
    Genevestigatori P51825.

    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. "Genes on chromosomes 4, 9, and 19 involved in 11q23 abnormalities in acute leukemia share sequence homology and/or common motifs."
      Nakamura T., Alder H., Gu Y., Prasad R., Canaani O., Kamada N., Gale R.P., Lange B., Crist W.M., Nowell P.C., Croce C.M., Canaani E.
      Proc. Natl. Acad. Sci. U.S.A. 90:4631-4635(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "A serine/proline-rich protein is fused to HRX in t(4;11) acute leukemias."
      Morrissey J., Tkachuk D.C., Milatovich A., Francke U., Link M., Cleary M.L.
      Blood 81:1124-1131(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), CHROMOSOMAL TRANSLOCATION WITH KMT2A.
    3. "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 2).
      Tissue: Placenta.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The t(4;11) chromosome translocation of human acute leukemias fuses the ALL-1 gene, related to Drosophila trithorax, to the AF-4 gene."
      Gu Y., Nakamura T., Alder H., Prasad R., Canaani O., Cimino G., Croce C.M., Canaani E.
      Cell 71:701-708(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL TRANSLOCATION WITH KMT2A.
    6. "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-206; SER-212 AND THR-697, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-212; THR-220; SER-750 AND THR-755, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-212; SER-588 AND SER-750, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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-206 AND SER-750, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-681, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION IN THE SEC COMPLEX.
    13. "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 THR-697, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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.
    15. "Leukemia fusion target AF9 is an intrinsically disordered transcriptional regulator that recruits multiple partners via coupled folding and binding."
      Leach B.I., Kuntimaddi A., Schmidt C.R., Cierpicki T., Johnson S.A., Bushweller J.H.
      Structure 21:176-183(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 738-779 IN COMPLEX WITH MLLT3.
    16. Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-1204.

    Entry informationi

    Entry nameiAFF1_HUMAN
    AccessioniPrimary (citable) accession number: P51825
    Secondary accession number(s): B4DTU1, E9PBM3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 118 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, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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