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Q6VMQ6

- MCAF1_HUMAN

UniProt

Q6VMQ6 - MCAF1_HUMAN

Protein

Activating transcription factor 7-interacting protein 1

Gene

ATF7IP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Recruiter that couples transcriptional factors to general transcription apparatus and thereby modulates transcription regulation and chromatin formation. Can both act as an activator or a repressor depending on the context. Mediates MBD1-dependent transcriptional repression, probably by recruiting complexes containing SETDB1. Required to stimulate histone methyltransferase activity of SETDB1 and facilitate the conversion of dimethylated to trimethylated H3 'Lys-9' (H3K9me3). The complex formed with MBD1 and SETDB1 represses transcription and couples DNA methylation and histone H3 'Lys-9' trimethylation (H3K9me3). Facilitates telomerase TERT and TERC gene expression by SP1 in cancer cells.3 Publications

    GO - Molecular functioni

    1. ATPase activity Source: Ensembl
    2. protein binding Source: UniProtKB
    3. transcription corepressor activity Source: Ensembl

    GO - Biological processi

    1. DNA methylation Source: UniProtKB
    2. negative regulation of transcription, DNA-templated Source: UniProtKB
    3. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    4. positive regulation of transcription, DNA-templated Source: UniProtKB
    5. regulation of RNA polymerase II transcriptional preinitiation complex assembly Source: UniProtKB
    6. transcription, DNA-templated Source: UniProtKB-KW
    7. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Host-virus interaction, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Activating transcription factor 7-interacting protein 1
    Alternative name(s):
    ATF-interacting protein
    Short name:
    ATF-IP
    ATF7-interacting protein
    ATFa-associated modulator
    Short name:
    hAM
    MBD1-containing chromatin-associated factor 1
    P621
    Gene namesi
    Name:ATF7IP
    Synonyms:MCAF, MCAF1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:20092. ATF7IP.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: UniProtKB
    2. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi968 – 9681D → A: Abolishes the interaction with SUMO. 1 Publication
    Mutagenesisi969 – 9691L → A: Abolishes the interaction with SUMO. 1 Publication
    Mutagenesisi1224 – 12241L → R: Abolishes interaction with MBD1 and subsequent transcriptional repression. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12701270Activating transcription factor 7-interacting protein 1PRO_0000281780Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei57 – 571PhosphoserineBy similarity
    Modified residuei113 – 1131Phosphoserine2 Publications
    Modified residuei118 – 1181Phosphothreonine1 Publication
    Modified residuei473 – 4731Phosphoserine1 Publication
    Modified residuei477 – 4771Phosphoserine1 Publication
    Modified residuei496 – 4961Phosphoserine1 Publication
    Modified residuei559 – 5591Phosphoserine1 Publication
    Modified residuei673 – 6731Phosphoserine2 Publications
    Modified residuei899 – 8991Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ6VMQ6.
    PaxDbiQ6VMQ6.
    PRIDEiQ6VMQ6.

    PTM databases

    PhosphoSiteiQ6VMQ6.

    Expressioni

    Tissue specificityi

    Detected at low levels in breast, lung and stomach; highly up-regulated in the corresponding cancerous tissues (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ6VMQ6.
    BgeeiQ6VMQ6.
    CleanExiHS_ATF7IP.
    GenevestigatoriQ6VMQ6.

    Organism-specific databases

    HPAiHPA016578.
    HPA023505.

    Interactioni

    Subunit structurei

    Interacts with MBD1; the interaction is enhanced when MBD1 is sumoylated. Probably forms a complex with SETDB1 and MBD1. Interacts with SUMO ubiquitin-like proteins (SUMO1, SUNO2 and SUMO3), with a preference for SUMO2 and SUMO3. Interacts with SP1, ATF7 and ZHX1. Interacts with the general transcription machinery, including ERCC2, ERCC3, GTF2E1, GTF2E2 and POLR2A. Interacts with Epstein-Barr virus BRLF1/Rta protein, leading to promote and regulate host genes in Epstein-Barr virus-infected cells.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DISC1Q9NRI53EBI-928732,EBI-529989

    Protein-protein interaction databases

    BioGridi120849. 20 interactions.
    IntActiQ6VMQ6. 51 interactions.
    MINTiMINT-1179935.
    STRINGi9606.ENSP00000261168.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RPQNMR-B938-981[»]
    ProteinModelPortaliQ6VMQ6.
    SMRiQ6VMQ6. Positions 1165-1259.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ6VMQ6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1160 – 1270111Fibronectin type-IIIPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni562 – 817256Interaction with SETDB1Add
    BLAST
    Regioni965 – 97511Interaction with SUMOAdd
    BLAST
    Regioni1154 – 1270117Interaction with MBD1Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili617 – 66549Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi553 – 57119Nuclear localization signalBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi349 – 580232Glu-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the MCAF family.Curated
    Contains 1 fibronectin type-III domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG82478.
    HOVERGENiHBG087180.
    InParanoidiQ6VMQ6.
    OrthoDBiEOG7KH9K1.
    PhylomeDBiQ6VMQ6.
    TreeFamiTF329427.

    Family and domain databases

    Gene3Di2.60.40.10. 1 hit.
    InterProiIPR026085. ATF7-int.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    [Graphical view]
    PANTHERiPTHR23210. PTHR23210. 1 hit.
    SUPFAMiSSF49265. SSF49265. 1 hit.
    PROSITEiPS50853. FN3. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6VMQ6-1) [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

    MDSLEEPQKK VFKARKTMRV SDRQQLEAVY KVKEELLKTD VKLLNGNHEN     50
    GDLDPTSPLE NMDYIKDKEE VNGIEEICFD PEGSKAEWKE TPCILSVNVK 100
    NKQDDDLNCE PLSPHNITPE PVSKLPAEPV SGDPAPGDLD AGDPASGVLA 150
    SGDSTSGDPT SSEPSSSDAA SGDATSGDAP SGDVSPGDAT SGDATADDLS 200
    SGDPTSSDPI PGEPVPVEPI SGDCAADDIA SSEITSVDLA SGAPASTDPA 250
    SDDLASGDLS SSELASDDLA TGELASDELT SESTFDRTFE PKSVPVCEPV 300
    PEIDNIEPSS NKDDDFLEKN GADEKLEQIQ SKDSLDEKNK ADNNIDANEE 350
    TLETDDTTIC SDRPPENEKK VEEDIITELA LGEDAISSSM EIDQGEKNED 400
    ETSADLVETI NENVIEDNKS ENILENTDSM ETDEIIPILE KLAPSEDELT 450
    CFSKTSLLPI DETNPDLEEK MESSFGSPSK QESSESLPKE AFLVLSDEED 500
    ISGEKDESEV ISQNETCSPA EVESNEKDNK PEEEEQVIHE DDERPSEKNE 550
    FSRRKRSKSE DMDNVQSKRR RYMEEEYEAE FQVKITAKGD INQKLQKVIQ 600
    WLLEEKLCAL QCAVFDKTLA ELKTRVEKIE CNKRHKTVLT ELQAKIARLT 650
    KRFEAAKEDL KKRHEHPPNP PVSPGKTVND VNSNNNMSYR NAGTVRQMLE 700
    SKRNVSESAP PSFQTPVNTV SSTNLVTPPA VVSSQPKLQT PVTSGSLTAT 750
    SVLPAPNTAT VVATTQVPSG NPQPTISLQP LPVILHVPVA VSSQPQLLQS 800
    HPGTLVTNQP SGNVEFISVQ SPPTVSGLTK NPVSLPSLPN PTKPNNVPSV 850
    PSPSIQRNPT ASAAPLGTTL AVQAVPTAHS IVQATRTSLP TVGPSGLYSP 900
    STNRGPIQMK IPISAFSTSS AAEQNSNTTP RIENQTNKTI DASVSKKAAD 950
    STSQCGKATG SDSSGVIDLT MDDEESGASQ DPKKLNHTPV STMSSSQPVS 1000
    RPLQPIQPAP PLQPSGVPTS GPSQTTIHLL PTAPTTVNVT HRPVTQVTTR 1050
    LPVPRAPANH QVVYTTLPAP PAQAPLRGTV MQAPAVRQVN PQNSVTVRVP 1100
    QTTTYVVNNG LTLGSTGPQL TVHHRPPQVH TEPPRPVHPA PLPEAPQPQR 1150
    LPPEAASTSL PQKPHLKLAR VQSQNGIVLS WSVLEVDRSC ATVDSYHLYA 1200
    YHEEPSATVP SQWKKIGEVK ALPLPMACTL TQFVSGSKYY FAVRAKDIYG 1250
    RFGPFCDPQS TDVISSTQSS 1270
    Length:1,270
    Mass (Da):136,394
    Last modified:January 11, 2011 - v3
    Checksum:i96F6E4FBA1D79385
    GO
    Isoform 2 (identifier: Q6VMQ6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         520-520: Missing.
         1095-1106: VTVRVPQTTTYV → KRFFLYMAPRYM
         1107-1270: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,105
    Mass (Da):118,654
    Checksum:i4B84876A207DDC12
    GO
    Isoform 3 (identifier: Q6VMQ6-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MHQDQRFRM

    Note: No experimental confirmation available. Gene prediction based on EST data.

    Show »
    Length:1,278
    Mass (Da):137,493
    Checksum:i3775C6DF7DC731BD
    GO
    Isoform 4 (identifier: Q6VMQ6-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         520-520: Missing.

    Note: No experimental confirmation available. Gene prediction based on EST data.

    Show »
    Length:1,269
    Mass (Da):136,323
    Checksum:i220BCFBC8E0AB7A7
    GO

    Sequence cautioni

    The sequence AAH37312.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AK001001 differs from that shown. Reason: Intron retention.
    The sequence AK001001 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA91751.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti457 – 4571L → V in AAH37312. (PubMed:15489334)Curated
    Sequence conflicti1182 – 11821S → G in AAQ92978. (PubMed:14536086)Curated
    Sequence conflicti1182 – 11821S → G in BAA91751. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti278 – 2781E → K.
    Corresponds to variant rs2231908 [ dbSNP | Ensembl ].
    VAR_031283
    Natural varianti348 – 3481N → I.1 Publication
    Corresponds to variant rs2231909 [ dbSNP | Ensembl ].
    VAR_031284
    Natural varianti530 – 5301K → R.3 Publications
    Corresponds to variant rs3213764 [ dbSNP | Ensembl ].
    VAR_031285

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MHQDQRFRM in isoform 3. CuratedVSP_055912
    Alternative sequencei520 – 5201Missing in isoform 2 and isoform 4. 1 PublicationVSP_024035
    Alternative sequencei1095 – 110612VTVRV…TTTYV → KRFFLYMAPRYM in isoform 2. 1 PublicationVSP_024038Add
    BLAST
    Alternative sequencei1107 – 1270164Missing in isoform 2. 1 PublicationVSP_024039Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY337596 mRNA. Translation: AAQ92978.1.
    AF425650 mRNA. Translation: AAO91864.1.
    AC007782 Genomic DNA. No translation available.
    AC008114 Genomic DNA. No translation available.
    AC008814 Genomic DNA. No translation available.
    AC124892 Genomic DNA. No translation available.
    CH471094 Genomic DNA. Translation: EAW96320.1.
    BC037312 mRNA. Translation: AAH37312.1. Sequence problems.
    BC063855 mRNA. Translation: AAH63855.1.
    AK001001 mRNA. No translation available.
    AK001550 mRNA. Translation: BAA91751.1. Different initiation.
    AJ242978 mRNA. Translation: CAB45135.1.
    CCDSiCCDS8663.1. [Q6VMQ6-1]
    RefSeqiNP_001273444.1. NM_001286515.1. [Q6VMQ6-2]
    NP_060649.3. NM_018179.4. [Q6VMQ6-1]
    NP_851997.1. NM_181352.1.
    XP_006719171.1. XM_006719108.1. [Q6VMQ6-1]
    XP_006719172.1. XM_006719109.1. [Q6VMQ6-1]
    UniGeneiHs.504856.
    Hs.591151.

    Genome annotation databases

    EnsembliENST00000261168; ENSP00000261168; ENSG00000171681. [Q6VMQ6-1]
    ENST00000536444; ENSP00000445955; ENSG00000171681. [Q6VMQ6-5]
    ENST00000540793; ENSP00000444589; ENSG00000171681. [Q6VMQ6-1]
    ENST00000543189; ENSP00000443179; ENSG00000171681. [Q6VMQ6-2]
    ENST00000544627; ENSP00000440440; ENSG00000171681. [Q6VMQ6-4]
    GeneIDi55729.
    KEGGihsa:55729.
    UCSCiuc001rbu.3. human. [Q6VMQ6-1]
    uc001rbv.1. human. [Q6VMQ6-2]

    Polymorphism databases

    DMDMi317373420.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY337596 mRNA. Translation: AAQ92978.1 .
    AF425650 mRNA. Translation: AAO91864.1 .
    AC007782 Genomic DNA. No translation available.
    AC008114 Genomic DNA. No translation available.
    AC008814 Genomic DNA. No translation available.
    AC124892 Genomic DNA. No translation available.
    CH471094 Genomic DNA. Translation: EAW96320.1 .
    BC037312 mRNA. Translation: AAH37312.1 . Sequence problems.
    BC063855 mRNA. Translation: AAH63855.1 .
    AK001001 mRNA. No translation available.
    AK001550 mRNA. Translation: BAA91751.1 . Different initiation.
    AJ242978 mRNA. Translation: CAB45135.1 .
    CCDSi CCDS8663.1. [Q6VMQ6-1 ]
    RefSeqi NP_001273444.1. NM_001286515.1. [Q6VMQ6-2 ]
    NP_060649.3. NM_018179.4. [Q6VMQ6-1 ]
    NP_851997.1. NM_181352.1.
    XP_006719171.1. XM_006719108.1. [Q6VMQ6-1 ]
    XP_006719172.1. XM_006719109.1. [Q6VMQ6-1 ]
    UniGenei Hs.504856.
    Hs.591151.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RPQ NMR - B 938-981 [» ]
    ProteinModelPortali Q6VMQ6.
    SMRi Q6VMQ6. Positions 1165-1259.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120849. 20 interactions.
    IntActi Q6VMQ6. 51 interactions.
    MINTi MINT-1179935.
    STRINGi 9606.ENSP00000261168.

    PTM databases

    PhosphoSitei Q6VMQ6.

    Polymorphism databases

    DMDMi 317373420.

    Proteomic databases

    MaxQBi Q6VMQ6.
    PaxDbi Q6VMQ6.
    PRIDEi Q6VMQ6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261168 ; ENSP00000261168 ; ENSG00000171681 . [Q6VMQ6-1 ]
    ENST00000536444 ; ENSP00000445955 ; ENSG00000171681 . [Q6VMQ6-5 ]
    ENST00000540793 ; ENSP00000444589 ; ENSG00000171681 . [Q6VMQ6-1 ]
    ENST00000543189 ; ENSP00000443179 ; ENSG00000171681 . [Q6VMQ6-2 ]
    ENST00000544627 ; ENSP00000440440 ; ENSG00000171681 . [Q6VMQ6-4 ]
    GeneIDi 55729.
    KEGGi hsa:55729.
    UCSCi uc001rbu.3. human. [Q6VMQ6-1 ]
    uc001rbv.1. human. [Q6VMQ6-2 ]

    Organism-specific databases

    CTDi 55729.
    GeneCardsi GC12P014468.
    H-InvDB HIX0010453.
    HGNCi HGNC:20092. ATF7IP.
    HPAi HPA016578.
    HPA023505.
    MIMi 613644. gene.
    neXtProti NX_Q6VMQ6.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG82478.
    HOVERGENi HBG087180.
    InParanoidi Q6VMQ6.
    OrthoDBi EOG7KH9K1.
    PhylomeDBi Q6VMQ6.
    TreeFami TF329427.

    Miscellaneous databases

    ChiTaRSi ATF7IP. human.
    EvolutionaryTracei Q6VMQ6.
    GeneWikii ATF7IP.
    GenomeRNAii 55729.
    NextBioi 60648.
    PROi Q6VMQ6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6VMQ6.
    Bgeei Q6VMQ6.
    CleanExi HS_ATF7IP.
    Genevestigatori Q6VMQ6.

    Family and domain databases

    Gene3Di 2.60.40.10. 1 hit.
    InterProi IPR026085. ATF7-int.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    [Graphical view ]
    PANTHERi PTHR23210. PTHR23210. 1 hit.
    SUPFAMi SSF49265. SSF49265. 1 hit.
    PROSITEi PS50853. FN3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "mAM facilitates conversion by ESET of dimethyl to trimethyl lysine 9 of histone H3 to cause transcriptional repression."
      Wang H., An W., Cao R., Xia L., Erdjument-Bromage H., Chatton B., Tempst P., Roeder R.G., Zhang Y.
      Mol. Cell 12:475-487(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH SETDB1, VARIANT ARG-530.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH MBD1, VARIANT ILE-348.
    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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-513, VARIANT ARG-530.
      Tissue: Brain and PNS.
    6. "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] OF 479-1270 AND 479-1270 (ISOFORM 1), VARIANT ARG-530.
      Tissue: Embryo and Teratocarcinoma.
    7. "A set of proteins interacting with transcription factor Sp1 identified in a two-hybrid screening."
      Gunther M., Laithier M., Brison O.
      Mol. Cell. Biochem. 210:131-142(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 545-1058 (ISOFORM 1), INTERACTION WITH SP1.
      Tissue: Colon.
    8. "Analysis of zinc-fingers and homeoboxes (ZHX)-1-interacting proteins: molecular cloning and characterization of a member of the ZHX family, ZHX3."
      Yamada K., Kawata H., Shou Z., Hirano S., Mizutani T., Yazawa T., Sekiguchi T., Yoshino M., Kajitani T., Miyamoto K.
      Biochem. J. 373:167-178(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZHX1.
    9. "Transcriptional repression and heterochromatin formation by MBD1 and MCAF/AM family proteins."
      Ichimura T., Watanabe S., Sakamoto Y., Aoto T., Fujita N., Nakao M.
      J. Biol. Chem. 280:13928-13935(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SETDB1; MBD1 AND SP1, MUTAGENESIS OF LEU-1224.
    10. "Activation of Sp1-mediated transcription by Rta of Epstein-Barr virus via an interaction with MCAF1."
      Chang L.-K., Chung J.-Y., Hong Y.-R., Ichimura T., Nakao M., Liu S.-T.
      Nucleic Acids Res. 33:6528-6539(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EBV VIRUS BRLF1.
    11. "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-113 AND SER-673, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Involvement of SUMO modification in MBD1- and MCAF1-mediated heterochromatin formation."
      Uchimura Y., Ichimura T., Uwada J., Tachibana T., Sugahara S., Nakao M., Saitoh H.
      J. Biol. Chem. 281:23180-23190(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SUMO AND MBD1, MUTAGENESIS OF ASP-968 AND LEU-969.
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; THR-118; SER-473 AND SER-899, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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].
    16. "MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated telomerase activity."
      Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S., Watanabe S., Saitoh N., Ito T., Nakao M.
      J. Biol. Chem. 284:5165-5174(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ERCC2; ERCC3; GTF2E1; GTF2E2; POLR2A AND SP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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-477; SER-496; SER-559 AND SER-673, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Structure of the small ubiquitin-like modifier (SUMO)-interacting motif of MBD1-containing chromatin-associated factor 1 bound to SUMO-3."
      Sekiyama N., Ikegami T., Yamane T., Ikeguchi M., Uchimura Y., Baba D., Ariyoshi M., Tochio H., Saitoh H., Shirakawa M.
      J. Biol. Chem. 283:35966-35975(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 938-981 IN COMPLEX WITH SUMO3.

    Entry informationi

    Entry nameiMCAF1_HUMAN
    AccessioniPrimary (citable) accession number: Q6VMQ6
    Secondary accession number(s): F5GX74
    , G3V1U0, Q4G0T9, Q6P3T3, Q86XW5, Q9NVJ9, Q9NWC2, Q9Y4X8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 107 of the entry and version 3 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 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3