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Q6VMQ6 (MCAF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ATF7IP
Synonyms:MCAF, MCAF1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1270 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2 Ref.15

Subunit structure

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. Ref.1 Ref.2 Ref.6 Ref.7 Ref.8 Ref.9 Ref.11 Ref.15

Subcellular location

Nucleus Ref.15.

Tissue specificity

Detected at low levels in breast, lung and stomach; highly up-regulated in the corresponding cancerous tissues (at protein level). Ref.15

Sequence similarities

Belongs to the MCAF family.

Contains 1 fibronectin type-III domain.

Sequence caution

The sequence AAH37312.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AK001001 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AK001001 differs from that shown. Reason: Intron retention.

The sequence BAA91751.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DISC1Q9NRI53EBI-928732,EBI-529989

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6VMQ6-1)

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.
Isoform 2 (identifier: Q6VMQ6-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12701270Activating transcription factor 7-interacting protein 1
PRO_0000281780

Regions

Domain1160 – 1270111Fibronectin type-III
Region562 – 817256Interaction with SETDB1
Region965 – 97511Interaction with SUMO
Region1154 – 1270117Interaction with MBD1
Coiled coil617 – 66549 Potential
Motif553 – 57119Nuclear localization signal By similarity
Compositional bias349 – 580232Glu-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.19
Modified residue571Phosphoserine By similarity
Modified residue1131Phosphoserine Ref.10 Ref.13
Modified residue1181Phosphothreonine Ref.13
Modified residue4731Phosphoserine Ref.13
Modified residue4771Phosphoserine Ref.18
Modified residue4961Phosphoserine Ref.18
Modified residue5591Phosphoserine Ref.18
Modified residue6731Phosphoserine Ref.10 Ref.18
Modified residue8991Phosphoserine Ref.13

Natural variations

Alternative sequence5201Missing in isoform 2.
VSP_024035
Alternative sequence1095 – 110612VTVRV…TTTYV → KRFFLYMAPRYM in isoform 2.
VSP_024038
Alternative sequence1107 – 1270164Missing in isoform 2.
VSP_024039
Natural variant2781E → K.
Corresponds to variant rs2231908 [ dbSNP | Ensembl ].
VAR_031283
Natural variant3481N → I. Ref.2
Corresponds to variant rs2231909 [ dbSNP | Ensembl ].
VAR_031284
Natural variant5301K → R. Ref.1 Ref.4 Ref.5
Corresponds to variant rs3213764 [ dbSNP | Ensembl ].
VAR_031285

Experimental info

Mutagenesis9681D → A: Abolishes the interaction with SUMO. Ref.11
Mutagenesis9691L → A: Abolishes the interaction with SUMO. Ref.11
Mutagenesis12241L → R: Abolishes interaction with MBD1 and subsequent transcriptional repression. Ref.8
Sequence conflict4571L → V in AAH37312. Ref.4
Sequence conflict11821S → G in AAQ92978. Ref.1
Sequence conflict11821S → G in BAA91751. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 11, 2011. Version 3.
Checksum: 96F6E4FBA1D79385

FASTA1,270136,394
        10         20         30         40         50         60 
MDSLEEPQKK VFKARKTMRV SDRQQLEAVY KVKEELLKTD VKLLNGNHEN GDLDPTSPLE 

        70         80         90        100        110        120 
NMDYIKDKEE VNGIEEICFD PEGSKAEWKE TPCILSVNVK NKQDDDLNCE PLSPHNITPE 

       130        140        150        160        170        180 
PVSKLPAEPV SGDPAPGDLD AGDPASGVLA SGDSTSGDPT SSEPSSSDAA SGDATSGDAP 

       190        200        210        220        230        240 
SGDVSPGDAT SGDATADDLS SGDPTSSDPI PGEPVPVEPI SGDCAADDIA SSEITSVDLA 

       250        260        270        280        290        300 
SGAPASTDPA SDDLASGDLS SSELASDDLA TGELASDELT SESTFDRTFE PKSVPVCEPV 

       310        320        330        340        350        360 
PEIDNIEPSS NKDDDFLEKN GADEKLEQIQ SKDSLDEKNK ADNNIDANEE TLETDDTTIC 

       370        380        390        400        410        420 
SDRPPENEKK VEEDIITELA LGEDAISSSM EIDQGEKNED ETSADLVETI NENVIEDNKS 

       430        440        450        460        470        480 
ENILENTDSM ETDEIIPILE KLAPSEDELT CFSKTSLLPI DETNPDLEEK MESSFGSPSK 

       490        500        510        520        530        540 
QESSESLPKE AFLVLSDEED ISGEKDESEV ISQNETCSPA EVESNEKDNK PEEEEQVIHE 

       550        560        570        580        590        600 
DDERPSEKNE FSRRKRSKSE DMDNVQSKRR RYMEEEYEAE FQVKITAKGD INQKLQKVIQ 

       610        620        630        640        650        660 
WLLEEKLCAL QCAVFDKTLA ELKTRVEKIE CNKRHKTVLT ELQAKIARLT KRFEAAKEDL 

       670        680        690        700        710        720 
KKRHEHPPNP PVSPGKTVND VNSNNNMSYR NAGTVRQMLE SKRNVSESAP PSFQTPVNTV 

       730        740        750        760        770        780 
SSTNLVTPPA VVSSQPKLQT PVTSGSLTAT SVLPAPNTAT VVATTQVPSG NPQPTISLQP 

       790        800        810        820        830        840 
LPVILHVPVA VSSQPQLLQS HPGTLVTNQP SGNVEFISVQ SPPTVSGLTK NPVSLPSLPN 

       850        860        870        880        890        900 
PTKPNNVPSV PSPSIQRNPT ASAAPLGTTL AVQAVPTAHS IVQATRTSLP TVGPSGLYSP 

       910        920        930        940        950        960 
STNRGPIQMK IPISAFSTSS AAEQNSNTTP RIENQTNKTI DASVSKKAAD STSQCGKATG 

       970        980        990       1000       1010       1020 
SDSSGVIDLT MDDEESGASQ DPKKLNHTPV STMSSSQPVS RPLQPIQPAP PLQPSGVPTS 

      1030       1040       1050       1060       1070       1080 
GPSQTTIHLL PTAPTTVNVT HRPVTQVTTR LPVPRAPANH QVVYTTLPAP PAQAPLRGTV 

      1090       1100       1110       1120       1130       1140 
MQAPAVRQVN PQNSVTVRVP QTTTYVVNNG LTLGSTGPQL TVHHRPPQVH TEPPRPVHPA 

      1150       1160       1170       1180       1190       1200 
PLPEAPQPQR LPPEAASTSL PQKPHLKLAR VQSQNGIVLS WSVLEVDRSC ATVDSYHLYA 

      1210       1220       1230       1240       1250       1260 
YHEEPSATVP SQWKKIGEVK ALPLPMACTL TQFVSGSKYY FAVRAKDIYG RFGPFCDPQS 

      1270 
TDVISSTQSS 

« Hide

Isoform 2 [UniParc].

Checksum: 4B84876A207DDC12
Show »

FASTA1,105118,654

References

« Hide 'large scale' references
[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]"MCAF mediates MBD1-dependent transcriptional repression."
Fujita N., Watanabe S., Ichimura T., Ohkuma Y., Chiba T., Saya H., Nakao M.
Mol. Cell. Biol. 23:2834-2843(2003) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"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.
[5]"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. expand/collapse author list , 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.
[6]"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.
[7]"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.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
[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]"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.
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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].
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY337596 mRNA. Translation: AAQ92978.1.
AF425650 mRNA. Translation: AAO91864.1.
AC007782 Genomic DNA. No translation available.
AC008814 Genomic DNA. No translation available.
AC124892 Genomic DNA. No translation available.
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.
RefSeqNP_001273444.1. NM_001286515.1.
NP_060649.3. NM_018179.4.
NP_851997.1. NM_181352.1.
UniGeneHs.504856.
Hs.591151.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RPQNMR-B938-981[»]
ProteinModelPortalQ6VMQ6.
SMRQ6VMQ6. Positions 1165-1259.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120849. 19 interactions.
IntActQ6VMQ6. 51 interactions.
MINTMINT-1179935.
STRING9606.ENSP00000261168.

PTM databases

PhosphoSiteQ6VMQ6.

Polymorphism databases

DMDM317373420.

Proteomic databases

PaxDbQ6VMQ6.
PRIDEQ6VMQ6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261168; ENSP00000261168; ENSG00000171681. [Q6VMQ6-1]
ENST00000540793; ENSP00000444589; ENSG00000171681. [Q6VMQ6-1]
ENST00000543189; ENSP00000443179; ENSG00000171681. [Q6VMQ6-2]
GeneID55729.
KEGGhsa:55729.
UCSCuc001rbu.3. human. [Q6VMQ6-1]
uc001rbv.1. human. [Q6VMQ6-2]

Organism-specific databases

CTD55729.
GeneCardsGC12P014468.
H-InvDBHIX0010453.
HGNCHGNC:20092. ATF7IP.
HPAHPA016578.
HPA023505.
MIM613644. gene.
neXtProtNX_Q6VMQ6.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG82478.
HOVERGENHBG087180.
InParanoidQ6VMQ6.
OrthoDBEOG7KH9K1.
PhylomeDBQ6VMQ6.
TreeFamTF329427.

Gene expression databases

ArrayExpressQ6VMQ6.
BgeeQ6VMQ6.
CleanExHS_ATF7IP.
GenevestigatorQ6VMQ6.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR026085. ATF7-int.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
[Graphical view]
PANTHERPTHR23210. PTHR23210. 1 hit.
SUPFAMSSF49265. SSF49265. 1 hit.
PROSITEPS50853. FN3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATF7IP. human.
EvolutionaryTraceQ6VMQ6.
GeneWikiATF7IP.
GenomeRNAi55729.
NextBio60648.
PROQ6VMQ6.
SOURCESearch...

Entry information

Entry nameMCAF1_HUMAN
AccessionPrimary (citable) accession number: Q6VMQ6
Secondary accession number(s): Q4G0T9 expand/collapse secondary AC list , Q6P3T3, Q86XW5, Q9NVJ9, Q9NWC2, Q9Y4X8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 102 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM