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Q6VMQ6

- MCAF1_HUMAN

UniProt

Q6VMQ6 - MCAF1_HUMAN

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Protein

Activating transcription factor 7-interacting protein 1

Gene
ATF7IP, MCAF, MCAF1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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 – 571Phosphoserine By 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.8 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.

Miscellaneous databases

EvolutionaryTraceiQ6VMQ6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1160 – 1270111Fibronectin type-IIIAdd
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 – 66549 Reviewed predictionAdd
BLAST

Motif

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

Compositional bias

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

Sequence similaritiesi

Belongs to the MCAF family.

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.

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. VSP_055912
Alternative sequencei520 – 5201Missing in isoform 2 and isoform 4. VSP_024035
Alternative sequencei1095 – 110612VTVRV…TTTYV → KRFFLYMAPRYM in isoform 2. VSP_024038Add
BLAST
Alternative sequencei1107 – 1270164Missing in isoform 2. VSP_024039Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti457 – 4571L → V in AAH37312. 1 Publication
Sequence conflicti1182 – 11821S → G in AAQ92978. 1 Publication
Sequence conflicti1182 – 11821S → G in BAA91751. 1 Publication

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.
ENST00000540793; ENSP00000444589; ENSG00000171681. [Q6VMQ6-1]
ENST00000543189; ENSP00000443179; ENSG00000171681. [Q6VMQ6-2]
ENST00000544627; ENSP00000440440; ENSG00000171681.
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 .
ENST00000540793 ; ENSP00000444589 ; ENSG00000171681 . [Q6VMQ6-1 ]
ENST00000543189 ; ENSP00000443179 ; ENSG00000171681 . [Q6VMQ6-2 ]
ENST00000544627 ; ENSP00000440440 ; ENSG00000171681 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 106 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

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