Q9UHB7 (AFF4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
AF4/FMR2 family member 4

Alternative name(s):
ALL1-fused gene from chromosome 5q31 protein
Short name=Protein AF-5q31
Major CDK9 elongation factor-associated protein

Gene names

Name:	AFF4
Synonyms:	AF5Q31, MCEF
ORF Names:	HSPC092

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1163 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play a role in transcriptional regulation By similarity.
Subunit structure	Component of the cyclin-dependent kinase pair (CDK9/cyclin-T1) complex, also called positive transcription elongation factor b (P-TEFb).
Subcellular location	Nucleus Ref.2.
Tissue specificity	Ubiquitously expressed. Strongly expressed in heart, placenta, skeletal muscle, pancreas and to a lower extent in brain. Ref.1 Ref.2
Developmental stage	Expressed in fetal heart, lung, brain and to a lower extent liver. Ref.1
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15
Involvement in disease	Note=A chromosomal aberration involving AFF4 is found in acute lymphoblastic leukemia (ALL). Insertion ins(5;11)(q31;q13q23) that forms a MLL-AFF4 fusion protein.
Sequence similarities	Belongs to the AF4 family.
Sequence caution	The sequence AAI00288.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence BAD92784.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc
Cellular component	mitochondrion Inferred from direct assay. Source: HPA nucleolus Inferred from direct assay. Source: HPA
Molecular function	protein binding Inferred from physical interaction. Source: IntAct sequence-specific DNA binding transcription factor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CCNT1	O60563	5	EBI-395282,EBI-2479671
MLLT1	Q03111	8	EBI-395282,EBI-1384215
MLLT3	P42568	4	EBI-395282,EBI-716132

Alternative products

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

Isoform 1 (identifier: Q9UHB7-1)

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: Q9UHB7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     880-900: EKAPSSSSNCPPSAPTLDSSK → VKCWGPGAFENHSTCHVTFPG
     901-1163: Missing.

Isoform 3 (identifier: Q9UHB7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     351-353: ESQ → VSK
     354-1163: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1163	1163	AF4/FMR2 family member 4		PRO_0000239393
Regions
	Compositional bias	102 – 461	360	Ser-rich
	Compositional bias	836 – 899	64	Ser-rich
Sites
	Site	350 – 351	2	Breakpoint for insertion to form MLL-AFF4 fusion protein
Amino acid modifications
	Modified residue	31	1	Phosphoserine Ref.14
	Modified residue	32	1	Phosphoserine Ref.11 Ref.14
	Modified residue	79	1	N6-acetyllysine Ref.16
	Modified residue	124	1	Phosphoserine Ref.11
	Modified residue	178	1	Phosphoserine Ref.14
	Modified residue	210	1	Phosphoserine Ref.14
	Modified residue	212	1	Phosphoserine Ref.11
	Modified residue	222	1	Phosphoserine Ref.11
	Modified residue	387	1	Phosphoserine Ref.8 Ref.12
	Modified residue	388	1	Phosphoserine Ref.8 Ref.12
	Modified residue	389	1	Phosphoserine Ref.8 Ref.12
	Modified residue	392	1	Phosphoserine Ref.8 Ref.12
	Modified residue	487	1	Phosphoserine Ref.11 Ref.13
	Modified residue	491	1	Phosphoserine Ref.13
	Modified residue	499	1	Phosphoserine Ref.9
	Modified residue	514	1	Phosphoserine Ref.11
	Modified residue	528	1	Phosphothreonine Ref.11
	Modified residue	549	1	Phosphoserine Ref.8 Ref.11 Ref.14
	Modified residue	599	1	Phosphoserine Ref.11
	Modified residue	617	1	Phosphoserine Ref.14
	Modified residue	668	1	Phosphotyrosine Ref.14
	Modified residue	671	1	Phosphoserine Ref.14
	Modified residue	674	1	Phosphothreonine Ref.10
	Modified residue	694	1	Phosphoserine Ref.11 Ref.12 Ref.14
	Modified residue	703	1	Phosphoserine Ref.8 Ref.11 Ref.12 Ref.13 Ref.14
	Modified residue	706	1	Phosphoserine Ref.8 Ref.11 Ref.12 Ref.13 Ref.14
	Modified residue	712	1	Phosphotyrosine Ref.12
	Modified residue	814	1	Phosphoserine Ref.11 Ref.14
	Modified residue	836	1	Phosphoserine Ref.11 Ref.14
	Modified residue	1043	1	Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14
	Modified residue	1055	1	Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14
	Modified residue	1058	1	Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14 Ref.15
	Modified residue	1062	1	Phosphoserine Ref.12 Ref.13
Natural variations
	Alternative sequence	351 – 353	3	ESQ → VSK in isoform 3.		VSP_019218
	Alternative sequence	354 – 1163	810	Missing in isoform 3.		VSP_019219
	Alternative sequence	880 – 900	21	EKAPS…LDSSK → VKCWGPGAFENHSTCHVTFP G in isoform 2.		VSP_019220
	Alternative sequence	901 – 1163	263	Missing in isoform 2.		VSP_019221
	Natural variant	136	1	T → P. Corresponds to variant rs34527550 [ dbSNP | Ensembl ].		VAR_053003
	Natural variant	757	1	S → T Found in a clear cell renal carcinoma case; somatic mutation. Ref.18		VAR_064693
Experimental info
	Sequence conflict	264	1	E → G in AAM00184. Ref.2
	Sequence conflict	359	1	T → I in AAM00184. Ref.2
	Sequence conflict	383	1	D → G in AAM00184. Ref.2
	Sequence conflict	445	1	E → G in AAM00184. Ref.2
	Sequence conflict	870	1	K → R in AAF28915. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 474E1906B8832AC1	FASTA	1,163	127,459
	10 20 30 40 50 60 MNREDRNVLR MKERERRNQE IQQGEDAFPP SSPLFAEPYK VTSKEDKLSS RIQSMLGNYD 70 80 90 100 110 120 EMKDFIGDRS IPKLVAIPKP TVPPSADEKS NPNFFEQRHG GSHQSSKWTP VGPAPSTSQS 130 140 150 160 170 180 QKRSSGLQSG HSSQRTSAGS SSGTNSSGQR HDRESYNNSG SSSRKKGQHG SEHSKSRSSS 190 200 210 220 230 240 PGKPQAVSSL NSSHSRSHGN DHHSKEHQRS KSPRDPDANW DSPSRVPFSS GQHSTQSFPP 250 260 270 280 290 300 SLMSKSNSML QKPTAYVRPM DGQESMEPKL SSEHYSSQSH GNSMTELKPS SKAHLTKLKI 310 320 330 340 350 360 PSQPLDASAS GDVSCVDEIL KEMTHSWPPP LTAIHTPCKT EPSKFPFPTK ESQQSNFGTG 370 380 390 400 410 420 EQKRYNPSKT SNGHQSKSML KDDLKLSSSE DSDGEQDCDK TMPRSTPGSN SEPSHHNSEG 430 440 450 460 470 480 ADNSRDDSSS HSGSESSSGS DSESESSSSD SEANEPSQSA SPEPEPPPTN KWQLDNWLNK 490 500 510 520 530 540 VNPHKVSPAS SVDSNIPSSQ GYKKEGREQG TGNSYTDTSG PKETSSATPG RDSKTIQKGS 550 560 570 580 590 600 ESGRGRQKSP AQSDSTTQRR TVGKKQPKKA EKAAAEEPRG GLKIESETPV DLASSMPSSR 610 620 630 640 650 660 HKAATKGSRK PNIKKESKSS PRPTAEKKKY KSTSKSSQKS REIIETDTSS SDSDESESLP 670 680 690 700 710 720 PSSQTPKYPE SNRTPVKPSS VEEEDSFFRQ RMFSPMEEKE LLSPLSEPDD RYPLIVKIDL 730 740 750 760 770 780 NLLTRIPGKP YKETEPPKGE KKNVPEKHTR EAQKQASEKV SNKGKRKHKN EDDNRASESK 790 800 810 820 830 840 KPKTEDKNSA GHKPSSNRES SKQSAAKEKD LLPSPAGPVP SKDPKTEHGS RKRTISQSSS 850 860 870 880 890 900 LKSSSNSNKE TSGSSKNSSS TSKQKKTEGK TSSSSKEVKE KAPSSSSNCP PSAPTLDSSK 910 920 930 940 950 960 PRRTKLVFDD RNYSADHYLQ EAKKLKHNAD ALSDRFEKAV YYLDAVVSFI ECGNALEKNA 970 980 990 1000 1010 1020 QESKSPFPMY SETVDLIKYT MKLKNYLAPD ATAADKRLTV LCLRCESLLY LRLFKLKKEN 1030 1040 1050 1060 1070 1080 ALKYSKTLTE HLKNSYNNSQ APSPGLGSKA VGMPSPVSPK LSPGNSGNYS SGASSASASG 1090 1100 1110 1120 1130 1140 SSVTIPQKIH QMAASYVQVT SNFLYATEIW DQAEQLSKEQ KEFFAELDKV MGPLIFNASI 1150 1160 MTDLVRYTRQ GLHWLRQDAK LIS
	Isoform 2 [UniParc]. Checksum: A7C5BAE4A45086AE	FASTA	900	98,205
	10 20 30 40 50 60 MNREDRNVLR MKERERRNQE IQQGEDAFPP SSPLFAEPYK VTSKEDKLSS RIQSMLGNYD 70 80 90 100 110 120 EMKDFIGDRS IPKLVAIPKP TVPPSADEKS NPNFFEQRHG GSHQSSKWTP VGPAPSTSQS 130 140 150 160 170 180 QKRSSGLQSG HSSQRTSAGS SSGTNSSGQR HDRESYNNSG SSSRKKGQHG SEHSKSRSSS 190 200 210 220 230 240 PGKPQAVSSL NSSHSRSHGN DHHSKEHQRS KSPRDPDANW DSPSRVPFSS GQHSTQSFPP 250 260 270 280 290 300 SLMSKSNSML QKPTAYVRPM DGQESMEPKL SSEHYSSQSH GNSMTELKPS SKAHLTKLKI 310 320 330 340 350 360 PSQPLDASAS GDVSCVDEIL KEMTHSWPPP LTAIHTPCKT EPSKFPFPTK ESQQSNFGTG 370 380 390 400 410 420 EQKRYNPSKT SNGHQSKSML KDDLKLSSSE DSDGEQDCDK TMPRSTPGSN SEPSHHNSEG 430 440 450 460 470 480 ADNSRDDSSS HSGSESSSGS DSESESSSSD SEANEPSQSA SPEPEPPPTN KWQLDNWLNK 490 500 510 520 530 540 VNPHKVSPAS SVDSNIPSSQ GYKKEGREQG TGNSYTDTSG PKETSSATPG RDSKTIQKGS 550 560 570 580 590 600 ESGRGRQKSP AQSDSTTQRR TVGKKQPKKA EKAAAEEPRG GLKIESETPV DLASSMPSSR 610 620 630 640 650 660 HKAATKGSRK PNIKKESKSS PRPTAEKKKY KSTSKSSQKS REIIETDTSS SDSDESESLP 670 680 690 700 710 720 PSSQTPKYPE SNRTPVKPSS VEEEDSFFRQ RMFSPMEEKE LLSPLSEPDD RYPLIVKIDL 730 740 750 760 770 780 NLLTRIPGKP YKETEPPKGE KKNVPEKHTR EAQKQASEKV SNKGKRKHKN EDDNRASESK 790 800 810 820 830 840 KPKTEDKNSA GHKPSSNRES SKQSAAKEKD LLPSPAGPVP SKDPKTEHGS RKRTISQSSS 850 860 870 880 890 900 LKSSSNSNKE TSGSSKNSSS TSKQKKTEGK TSSSSKEVKV KCWGPGAFEN HSTCHVTFPG
	Isoform 3 [UniParc]. Checksum: F7811E19E60C9A92	FASTA	353	38,823
	10 20 30 40 50 60 MNREDRNVLR MKERERRNQE IQQGEDAFPP SSPLFAEPYK VTSKEDKLSS RIQSMLGNYD 70 80 90 100 110 120 EMKDFIGDRS IPKLVAIPKP TVPPSADEKS NPNFFEQRHG GSHQSSKWTP VGPAPSTSQS 130 140 150 160 170 180 QKRSSGLQSG HSSQRTSAGS SSGTNSSGQR HDRESYNNSG SSSRKKGQHG SEHSKSRSSS 190 200 210 220 230 240 PGKPQAVSSL NSSHSRSHGN DHHSKEHQRS KSPRDPDANW DSPSRVPFSS GQHSTQSFPP 250 260 270 280 290 300 SLMSKSNSML QKPTAYVRPM DGQESMEPKL SSEHYSSQSH GNSMTELKPS SKAHLTKLKI 310 320 330 340 350 PSQPLDASAS GDVSCVDEIL KEMTHSWPPP LTAIHTPCKT EPSKFPFPTK VSK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"AF5q31, a newly identified AF4-related gene, is fused to MLL in infant acute lymphoblastic leukemia with ins(5;11)(q31;q13q23)." Taki T., Kano H., Taniwaki M., Sako M., Yanagisawa M., Hayashi Y. Proc. Natl. Acad. Sci. U.S.A. 96:14535-14540(1999) [PubMed: 10588740] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION WITH MLL, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Tissue: Placenta.
[2]	"MCEF, the newest member of the AF4 family of transcription factors involved in leukemia, is a positive transcription elongation factor-b-associated protein." Estable M.C., Naghavi M.H., Kato H., Xiao H., Qin J., Vahlne A., Roeder R.G. J. Biomed. Sci. 9:234-245(2002) [PubMed: 12065898] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 111-122, IDENTIFICATION IN PTEF-B COMPLEX, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Tissue: Fetal brain.
[3]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[4]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed: 15372022] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-363 (ISOFORMS 1/2). Tissue: Blood, Brain and Skin.
[7]	"Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells." Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X. , Gu J., Chen S.-J., Chen Z. Genome Res. 10:1546-1560(2000) [PubMed: 11042152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 788-1163 (ISOFORM 2). Tissue: Umbilical cord blood.
[8]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387; SER-388; SER-389; SER-392; SER-549; SER-703 AND SER-706, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-674, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-124; SER-212; SER-222; SER-487; SER-514; THR-528; SER-549; SER-599; SER-694; SER-703; SER-706; SER-814; SER-836; SER-1043; SER-1055 AND SER-1058, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-387; SER-388; SER-389; SER-392; SER-694; SER-703; SER-706; TYR-712; SER-1043; SER-1055; SER-1058 AND SER-1062, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-487; SER-491; SER-703; SER-706; SER-1043; SER-1055; SER-1058 AND SER-1062, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[14]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-32; SER-178; SER-210; SER-549; SER-617; TYR-668; SER-671; SER-694; SER-703; SER-706; SER-814; SER-836; SER-1043; SER-1055 AND SER-1058, MASS SPECTROMETRY.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1058, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79, MASS SPECTROMETRY.
[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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]	"Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma." Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M. , Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A. Nature 469:539-542(2011) [PubMed: 21248752] [Abstract] Cited for: VARIANT THR-757.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF197927 mRNA. Translation: AAF18981.1. AF213987 mRNA. Translation: AAM00184.2. AB209547 mRNA. Translation: BAD92784.1. Different initiation. AC004500 Genomic DNA. No translation available. CH471062 Genomic DNA. Translation: EAW62305.1. BC063007 mRNA. Translation: AAH63007.1. BC100287 mRNA. Translation: AAI00288.1. Sequence problems. BC137226 mRNA. Translation: AAI37227.1. AF161355 mRNA. Translation: AAF28915.1.
IPI	IPI00004344. IPI00383219. IPI00658213.
RefSeq	NP_055238.1. NM_014423.3.
UniGene	Hs.519313. Hs.664840.
3D structure databases
ProteinModelPortal	Q9UHB7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UHB7. 14 interactions.
MINT	MINT-1469196.
STRING	Q9UHB7.
PTM databases
PhosphoSite	Q9UHB7.
Polymorphism databases
DMDM	74720814.
Proteomic databases
PeptideAtlas	Q9UHB7.
PRIDE	Q9UHB7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000265343; ENSP00000265343; ENSG00000072364. ENST00000378595; ENSP00000367858; ENSG00000072364.
GeneID	27125.
KEGG	hsa:27125.
UCSC	uc003kyd.1. human. uc003kye.1. human. uc003kyf.2. human.
Organism-specific databases
CTD	27125.
GeneCards	GC05M132211.
H-InvDB	HIX0005164.
HGNC	HGNC:17869. AFF4.
HPA	HPA023690.
MIM	604417. gene.
neXtProt	NX_Q9UHB7.
PharmGKB	PA142672641.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18665.
GeneTree	ENSGT00530000063217.
HOGENOM	HBG715005.
HOVERGEN	HBG004189.
InParanoid	Q9UHB7.
OMA	TEHLKNS.
OrthoDB	EOG4CC40N.
PhylomeDB	Q9UHB7.
Gene expression databases
ArrayExpress	Q9UHB7.
Bgee	Q9UHB7.
CleanEx	HS_AFF4.
Genevestigator	Q9UHB7.
GermOnline	ENSG00000072364. Homo sapiens.
Family and domain databases
InterPro	IPR007797. TF_AF4/FMR2. [Graphical view]
KO	K15185.
PANTHER	PTHR10528. AF-4. 1 hit.
Pfam	PF05110. AF-4. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	49830.
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Entry information

Entry name

AFF4_HUMAN

Accession

Primary (citable) accession number: Q9UHB7
Secondary accession number(s): B2RP19 , B7WPD2, Q498B2, Q59FB3, Q6P592, Q8TDR1, Q9P0E4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 13, 2006
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 80 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.