Q6VMQ6 (MCAF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ATF7IP
Synonyms:	MCAF, MCAF1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1270 AA.
Sequence status	Complete.
Protein existence	Evidence 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.14
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.14
Subcellular location	Nucleus Ref.14.
Tissue specificity	Detected at low levels in breast, lung and stomach; highly up-regulated in the corresponding cancerous tissues (at protein level). Ref.14
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.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil
Molecular function	Activator Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA methylation Inferred from direct assay Ref.2. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent Inferred from direct assay Ref.2. Source: UniProtKB positive regulation of transcription, DNA-dependent Inferred from direct assay Ref.2. Source: UniProtKB regulation of RNA polymerase II transcriptional preinitiation complex assembly Inferred from direct assay Ref.2. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from direct assay Ref.2. Source: UniProtKB transcription factor complex Inferred from electronic annotation. Source: Compara
Molecular_function	ATPase activity Inferred from electronic annotation. Source: Compara transcription corepressor activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DISC1	Q9NRI5	3	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1270	1270	Activating transcription factor 7-interacting protein 1		PRO_0000281780
Regions
	Domain	1157 – 1261	105	Fibronectin type-III
	Region	562 – 817	256	Interaction with SETDB1
	Region	965 – 975	11	Interaction with SUMO
	Region	1154 – 1270	117	Interaction with MBD1
	Coiled coil	617 – 665	49	Potential
	Motif	553 – 571	19	Nuclear localization signal By similarity
	Compositional bias	349 – 580	232	Glu-rich
Amino acid modifications
	Modified residue	113	1	Phosphoserine Ref.10 Ref.13
	Modified residue	118	1	Phosphothreonine Ref.13
	Modified residue	473	1	Phosphoserine Ref.13
	Modified residue	477	1	Phosphoserine Ref.17
	Modified residue	496	1	Phosphoserine Ref.17
	Modified residue	559	1	Phosphoserine Ref.17
	Modified residue	673	1	Phosphoserine Ref.10 Ref.17
	Modified residue	899	1	Phosphoserine Ref.13
Natural variations
	Alternative sequence	520	1	Missing in isoform 2.		VSP_024035
	Alternative sequence	1095 – 1106	12	VTVRV…TTTYV → KRFFLYMAPRYM in isoform 2.		VSP_024038
	Alternative sequence	1107 – 1270	164	Missing in isoform 2.		VSP_024039
	Natural variant	278	1	E → K. Corresponds to variant rs2231908 [ dbSNP | Ensembl ].		VAR_031283
	Natural variant	348	1	N → I. Ref.2 Corresponds to variant rs2231909 [ dbSNP | Ensembl ].		VAR_031284
	Natural variant	530	1	K → R. Ref.1 Ref.4 Ref.5 Corresponds to variant rs3213764 [ dbSNP | Ensembl ].		VAR_031285
Experimental info
	Mutagenesis	968	1	D → A: Abolishes the interaction with SUMO. Ref.11
	Mutagenesis	969	1	L → A: Abolishes the interaction with SUMO. Ref.11
	Mutagenesis	1224	1	L → R: Abolishes interaction with MBD1 and subsequent transcriptional repression. Ref.8
	Sequence conflict	457	1	L → V in AAH37312. Ref.4
	Sequence conflict	1182	1	S → G in AAQ92978. Ref.1
	Sequence conflict	1182	1	S → G in BAA91751. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 11, 2011. Version 3. Checksum: 96F6E4FBA1D79385	FASTA	1,270	136,394
	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
	Isoform 2 [UniParc]. Checksum: 4B84876A207DDC12	FASTA	1,105	118,654
	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 ISQNETCSPE VESNEKDNKP EEEEQVIHED 550 560 570 580 590 600 DERPSEKNEF SRRKRSKSED MDNVQSKRRR YMEEEYEAEF QVKITAKGDI NQKLQKVIQW 610 620 630 640 650 660 LLEEKLCALQ CAVFDKTLAE LKTRVEKIEC NKRHKTVLTE LQAKIARLTK RFEAAKEDLK 670 680 690 700 710 720 KRHEHPPNPP VSPGKTVNDV NSNNNMSYRN AGTVRQMLES KRNVSESAPP SFQTPVNTVS 730 740 750 760 770 780 STNLVTPPAV VSSQPKLQTP VTSGSLTATS VLPAPNTATV VATTQVPSGN PQPTISLQPL 790 800 810 820 830 840 PVILHVPVAV SSQPQLLQSH PGTLVTNQPS GNVEFISVQS PPTVSGLTKN PVSLPSLPNP 850 860 870 880 890 900 TKPNNVPSVP SPSIQRNPTA SAAPLGTTLA VQAVPTAHSI VQATRTSLPT VGPSGLYSPS 910 920 930 940 950 960 TNRGPIQMKI PISAFSTSSA AEQNSNTTPR IENQTNKTID ASVSKKAADS TSQCGKATGS 970 980 990 1000 1010 1020 DSSGVIDLTM DDEESGASQD PKKLNHTPVS TMSSSQPVSR PLQPIQPAPP LQPSGVPTSG 1030 1040 1050 1060 1070 1080 PSQTTIHLLP TAPTTVNVTH RPVTQVTTRL PVPRAPANHQ VVYTTLPAPP AQAPLRGTVM 1090 1100 QAPAVRQVNP QNSKRFFLYM APRYM

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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.
[15]	"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.
[16]	"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].
[17]	"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, MASS SPECTROMETRY.
[18]	"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.

IPI

IPI00795654.
IPI00796928.

RefSeq

NP_060649.3. NM_018179.3.

UniGene

Hs.591151.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2RPQ	NMR	-	B	938-981	[»]

ProteinModelPortal

Q6VMQ6.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q6VMQ6. 3 interactions.

MINT

MINT-1179935.

STRING

9606.ENSP00000261168.

PTM databases

PhosphoSite

Q6VMQ6.

Polymorphism databases

DMDM

215274101.

Proteomic databases

PaxDb

Q6VMQ6.

PRIDE

Q6VMQ6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000261168; ENSP00000261168; ENSG00000171681.
ENST00000540793; ENSP00000444589; ENSG00000171681.
ENST00000543189; ENSP00000443179; ENSG00000171681.

GeneID

55729.

KEGG

hsa:55729.

UCSC

uc001rbu.3. human.
uc001rbv.1. human.

Organism-specific databases

CTD

55729.

GeneCards

GC12P014468.

H-InvDB

HIX0010453.

HGNC

HGNC:20092. ATF7IP.

HPA

HPA016578.
HPA023505.

MIM

613644. gene.

neXtProt

NX_Q6VMQ6.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG82478.

HOVERGEN

HBG087180.

InParanoid

Q6VMQ6.

OrthoDB

EOG4G7BXM.

PhylomeDB

Q6VMQ6.

Gene expression databases

ArrayExpress

Q6VMQ6.

Bgee

Q6VMQ6.

CleanEx

HS_ATF7IP.

Genevestigator

Q6VMQ6.

Family and domain databases

Gene3D

2.60.40.10. 1 hit.

InterPro

IPR026085. ATF7-int.
IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
[Graphical view]

PANTHER

PTHR23210. PTHR23210. 1 hit.

SUPFAM

SSF49265. FN_III-like. 1 hit.

PROSITE

PS50853. FN3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ATF7IP. human.

EvolutionaryTrace

Q6VMQ6.

GenomeRNAi

55729.

NextBio

60648.

SOURCE

Search...

Entry information

Entry name

MCAF1_HUMAN

Accession

Primary (citable) accession number: Q6VMQ6
Secondary accession number(s): Q4G0T9 , Q6P3T3, Q86XW5, Q9NVJ9, Q9NWC2, Q9Y4X8

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 3, 2007
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.