P55197 (AF10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein AF-10

Alternative name(s):
ALL1-fused gene from chromosome 10 protein

Gene names

Name:	MLLT10
Synonyms:	AF10

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	1027 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probably involved in transcriptional regulation. In vitro or as fusion protein with MLL has transactivation activity. Binds to cruciform DNA. Ref.9
Subunit structure	Self-associates. Interacts with FSTL3 isoform 2; the interaction enhances MLLT10 in vitro transcriptional activity and self-association. Interacts with YEATS4. Interacts with SS18. Interacts with DOT1L. Ref.5 Ref.6 Ref.8 Ref.9
Subcellular location	Nucleus Ref.4.
Tissue specificity	Expressed abundantly in testis.
Involvement in disease	A chromosomal aberration involving MLLT10 is associated with acute leukemias. Translocation t(10;11)(p12;q23) with MLL/HRX. The result is a rogue activator protein. A chromosomal aberration involving MLLT10 is associated with diffuse histiocytic lymphomas. Translocation t(10;11)(p13;q14) with PICALM.
Sequence similarities	Contains 2 PHD-type zinc fingers.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement
Disease	Proto-oncogene
Domain	Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.9. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW sequence-specific DNA binding transcription factor activity Non-traceable author statement Ref.1. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P55197-1)

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: P55197-2)

The sequence of this isoform differs from the canonical sequence as follows:
     81-126: RCELCPHKDG...VSTMEPIVLQ → AESRSVAQAK...GMQFLLVSLI
     127-1027: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: P55197-3)

The sequence of this isoform differs from the canonical sequence as follows:
     81-179: RCELCPHKDG...CAQFAGLLCE → MVCNSCWLAS...VIWRFKKERW
     180-1027: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1027	1027	Protein AF-10		PRO_0000215935
Regions
	Zinc finger	22 – 74	53	PHD-type 1
	Zinc finger	68 – 85	18	C4-type
	Zinc finger	134 – 197	64	PHD-type 2
	Region	80 – 287	208	Self-association
	Region	141 – 233	93	Interaction with FSTL3
	Region	311 – 690	380	DNA-binding
	Region	719 – 800	82	Transactivation domain
	Region	766 – 794	29	Leucine-zipper
	Compositional bias	229 – 240	12	Glu/Lys-rich
	Compositional bias	856 – 861	6	Poly-Ser
Sites
	Site	266	1	MLL fusion point (in acute myeloid leukemia patient B)
	Site	643	1	MLL fusion point (in acute myeloid leukemia patient C)
	Site	680	1	MLL fusion point (in acute myeloid leukemia patient A)
Amino acid modifications
	Modified residue	700	1	Phosphoserine Ref.11
	Modified residue	702	1	Phosphoserine Ref.11
Natural variations
	Alternative sequence	81 – 179	99	RCELC…GLLCE → MVCNSCWLASSENVTPGYIE HHCACASPHPRCLVSNVPPV SGALMHCFWACLTTAAFFGP QSFTTCHMSFLVSRDILFYI YGFMPFISVVIWRFKKERW in isoform 3.		VSP_044552
	Alternative sequence	81 – 126	46	RCELC…PIVLQ → AESRSVAQAKVQWCDLSPLQ PLLPGFKRFSCLSLPNGMQF LLVSLI in isoform 2.		VSP_043044
	Alternative sequence	127 – 1027	901	Missing in isoform 2.		VSP_043045
	Alternative sequence	180 – 1027	848	Missing in isoform 3.		VSP_044553

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 7C7C0059DDD46589	FASTA	1,027	109,026
	10 20 30 40 50 60 MVSSDRPVSL EDEVSHSMKE MIGGCCVCSD ERGWAENPLV YCDGHGCSVA VHQACYGIVQ 70 80 90 100 110 120 VPTGPWFCRK CESQERAARV RCELCPHKDG ALKRTDNGGW AHVVCALYIP EVQFANVSTM 130 140 150 160 170 180 EPIVLQSVPH DRYNKTCYIC DEQGRESKAA TGACMTCNKH GCRQAFHVTC AQFAGLLCEE 190 200 210 220 230 240 EGNGADNVQY CGYCKYHFSK LKKSKRGSNR SYDQSLSDSS SHSQDKHHEK EKKKYKEKDK 250 260 270 280 290 300 HKQKHKKQPE PSPALVPSLT VTTEKTYTST SNNSISGSLK RLEDTTARFT NANFQEVSAH 310 320 330 340 350 360 TSSGKDVSET RGSEGKGKKS SAHSSGQRGR KPGGGRNPGT TVSAASPFPQ GSFSGTPGSV 370 380 390 400 410 420 KSSSGSSVQS PQDFLSFTDS DLRNDSYSHS QQSSATKDVH KGESGSQEGG VNSFSTLIGL 430 440 450 460 470 480 PSTSAVTSQP KSFENSPGDL GNSSLPTAGY KRAQTSGIEE ETVKEKKRKG NKQSKHGPGR 490 500 510 520 530 540 PKGNKNQENV SHLSVSSASP TSSVASAAGS ITSSSLQKSP TLLRNGSLQS LSVGSSPVGS 550 560 570 580 590 600 EISMQYRHDG ACPTTTFSEL LNAIHNDRGD SSTLTKQELK FIGIYNSNDV AVSFPNVVSG 610 620 630 640 650 660 SGSSTPVSSS HLPQQSSGHL QQVGALSPSA VSSAAPAVAT TQANTLSGSS LSQAPSHMYG 670 680 690 700 710 720 NRSNSSMAAL IAQSENNQTD QDLGDNSRNL VGRGSSPRGS LSPRSPVSSL QIRYDQPGNS 730 740 750 760 770 780 SLENLPPVAA SIEQLLERQW SEGQQFLLEQ GTPSDILGML KSLHQLQVEN RRLEEQIKNL 790 800 810 820 830 840 TAKKERLQLL NAQLSVPFPT ITANPSPSHQ IHTFSAQTAP TTDSLNSSKS PHIGNSFLPD 850 860 870 880 890 900 NSLPVLNQDL TSSGQSTSSS SALSTPPPAG QSPAQQGSGV SGVQQVNGVT VGALASGMQP 910 920 930 940 950 960 VTSTIPAVSA VGGIIGALPG NQLAINGIVG ALNGVMQTPV TMSQNPTPLT HTTVPPNATH 970 980 990 1000 1010 1020 PMPATLTNSA SGLGLLSDQQ RQILIHQQQF QQLLNSQQLT PVHRHPHFTQ LPPTHFSPSM EIMQVRK
	Isoform 2 [UniParc]. Checksum: B8E45EC6C2BA9FA8	FASTA	126	13,851
	10 20 30 40 50 60 MVSSDRPVSL EDEVSHSMKE MIGGCCVCSD ERGWAENPLV YCDGHGCSVA VHQACYGIVQ 70 80 90 100 110 120 VPTGPWFCRK CESQERAARV AESRSVAQAK VQWCDLSPLQ PLLPGFKRFS CLSLPNGMQF LLVSLI
	Isoform 3 [UniParc]. Checksum: E522FE1E4B1ED346	FASTA	179	20,047
	10 20 30 40 50 60 MVSSDRPVSL EDEVSHSMKE MIGGCCVCSD ERGWAENPLV YCDGHGCSVA VHQACYGIVQ 70 80 90 100 110 120 VPTGPWFCRK CESQERAARV MVCNSCWLAS SENVTPGYIE HHCACASPHP RCLVSNVPPV 130 140 150 160 170 SGALMHCFWA CLTTAAFFGP QSFTTCHMSF LVSRDILFYI YGFMPFISVV IWRFKKERW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel class of zinc finger/leucine zipper genes identified from the molecular cloning of the t(10;11) translocation in acute leukemia." Chaplin T., Ayton P., Bernard O.A., Saha V., Della Valle V., Hillion J., Gregorini A., Lillington D., Berger R., Young B.D. Blood 85:1435-1441(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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] (ISOFORMS 2 AND 3). Tissue: Ovary and Prostate.
[4]	"Biochemical analyses of the AF10 protein: the extended LAP/PHD-finger mediates oligomerisation." Linder B., Newman R., Jones L.K., Debernardi S., Young B.D., Freemont P., Verrijzer C.P., Saha V. J. Mol. Biol. 299:369-378(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SELF-ASSOCIATION, SUBCELLULAR LOCATION, DNA-BINDING.
[5]	"The synovial sarcoma associated protein SYT interacts with the acute leukemia associated protein AF10." de Bruijn D.R., dos Santos N.R., Thijssen J., Balemans M., Debernardi S., Linder B., Young B.D., Geurts van Kessel A. Oncogene 20:3281-3289(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SS18.
[6]	"The MLL fusion partner AF10 binds GAS41, a protein that interacts with the human SWI/SNF complex." Debernardi S., Bassini A., Jones L.K., Chaplin T., Linder B., de Bruijn D.R.H., Meese E., Young B.D. Blood 99:275-281(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH YEATS4.
[7]	"The AF10 leucine zipper is required for leukemic transformation of myeloid progenitors by MLL-AF10." DiMartino J.F., Ayton P.M., Chen E.H., Naftzger C.C., Young B.D., Cleary M.L. Blood 99:3780-3785(2002) [PubMed] [Europe PMC] [Abstract] Cited for: TRANSACTIVATION DOMAIN.
[8]	"hDOT1L links histone methylation to leukemogenesis." Okada Y., Feng Q., Lin Y., Jiang Q., Li Y., Coffield V.M., Su L., Xu G., Zhang Y. Cell 121:167-178(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DOT1L.
[9]	"AF10-dependent transcription is enhanced by its interaction with FLRG." Forissier S., Razanajaona D., Ay A.S., Martel S., Bartholin L., Rimokh R. Biol. Cell 99:563-571(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SELF-ASSOCIATION, INTERACTION WITH FSTL3.
[10]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[11]	"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-700 AND SER-702, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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.
[13]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	U13948 mRNA. Translation: AAA79972.1. AL161799 , AL358780, AL359697, AL357372 Genomic DNA. Translation: CAI39663.1. AL358780 , AL161799, AL357372, AL359697 Genomic DNA. Translation: CAI13979.1. AL358780 Genomic DNA. Translation: CAI13982.1. AL358780 Genomic DNA. Translation: CAI13983.1. AL359697 , AL357372, AL358780, AL161799 Genomic DNA. Translation: CAH73410.1. AL357372 , AL359697, AL358780, AL161799 Genomic DNA. Translation: CAI41348.1. BC080577 mRNA. Translation: AAH80577.1. BC094844 mRNA. No translation available.
IPI	IPI00023464. IPI00470780. IPI00514978.
PIR	I38759.
RefSeq	NP_001182556.1. NM_001195627.1. NP_001182557.1. NM_001195628.1. NP_001182559.1. NM_001195630.1. NP_004632.1. NM_004641.3.
UniGene	Hs.30385.
3D structure databases
ProteinModelPortal	P55197.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-37633N.
IntAct	P55197. 1 interaction.
STRING	9606.ENSP00000366272.
PTM databases
PhosphoSite	P55197.
Polymorphism databases
DMDM	1703190.
Proteomic databases
PaxDb	P55197.
PRIDE	P55197.
Protocols and materials databases
DNASU	8028.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000377072; ENSP00000366272; ENSG00000078403. ENST00000377091; ENSP00000366295; ENSG00000078403. ENST00000377100; ENSP00000366304; ENSG00000078403.
GeneID	8028.
KEGG	hsa:8028.
UCSC	uc001iqs.3. human.
Organism-specific databases
CTD	8028.
GeneCards	GC10P021825.
HGNC	HGNC:16063. MLLT10.
HPA	HPA005747.
MIM	602409. gene.
neXtProt	NX_P55197.
PharmGKB	PA30849.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5141.
HOGENOM	HOG000033831.
HOVERGEN	HBG004186.
OrthoDB	EOG4XD3QG.
PhylomeDB	P55197.
Gene expression databases
ArrayExpress	P55197.
Bgee	P55197.
CleanEx	HS_MLLT10.
Genevestigator	P55197.
GermOnline	ENSG00000078403. Homo sapiens.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR019786. Zinc_finger_PHD-type_CS. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR013083. Znf_RING/FYVE/PHD. [Graphical view]
SMART	SM00249. PHD. 2 hits. [Graphical view]
SUPFAM	SSF57903. FYVE_PHD_ZnF. 1 hit.
PROSITE	PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MLLT10. human.
GenomeRNAi	8028.
NextBio	30601.
SOURCE	Search...

Entry information

Entry name

AF10_HUMAN

Accession

Primary (citable) accession number: P55197
Secondary accession number(s): B1ANA8, Q5JT37, Q66K63

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 1, 2013
This is version 113 of the entry and version 1 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.