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

General annotation (Comments)

Function	Key component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. In the SEC complex, AFF4 acts as a central scaffold that recruits other factors through direct interactions with ELL proteins (ELL, ELL2 or ELL3) and the P-TEFb complex. In case of infection by HIV-1 virus, the SEC complex is recruited by the viral Tat protein to stimulate viral gene expression. Ref.16 Ref.17 Ref.23
Subunit structure	Interacts with ELL3; the interaction is direct By similarity. Interacts with ELL2; the interaction is direct and leads to stabilize ELL2 and prevent ELL2 ubiquitination and degradation. Component of the super elongation complex (SEC), at least composed of EAF1, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Interacts with ELL. Ref.2 Ref.16 Ref.17 Ref.21
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
Involvement in disease	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	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	spermatid development Inferred from electronic annotation. Source: Compara transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc
Cellular_component	mitochondrion Inferred from direct assay. Source: HPA nucleolus Inferred from direct assay. Source: HPA
Molecular_function	sequence-specific DNA binding transcription factor activity Traceable author statement Ref.1. 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
tat	P04608	4	EBI-395282,EBI-6164389	From a different organism.

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

387

1

Phosphoserine Ref.13

Modified residue

388

1

Phosphoserine Ref.13

Modified residue

389

1

Phosphoserine Ref.13

Modified residue

392

1

Phosphoserine Ref.13

Modified residue

549

1

Phosphoserine Ref.12 Ref.14

Modified residue

671

1

Phosphoserine Ref.13 Ref.14

Modified residue

674

1

Phosphothreonine Ref.11

Modified residue

694

1

Phosphoserine Ref.13

Modified residue

703

1

Phosphoserine Ref.8 Ref.13

Modified residue

706

1

Phosphoserine Ref.8 Ref.13

Modified residue

712

1

Phosphotyrosine Ref.13

Modified residue

814

1

Phosphoserine Ref.12 Ref.18

Modified residue

836

1

Phosphoserine Ref.18

Modified residue

1043

1

Phosphoserine Ref.12 Ref.13 Ref.14 Ref.18

Modified residue

1055

1

Phosphoserine Ref.12 Ref.13

Modified residue

1058

1

Phosphoserine Ref.13 Ref.14 Ref.15

Modified residue

1062

1

Phosphoserine 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.24

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

Secondary structure

1

.

.

.

.

.

.

1163

Helix Strand Turn

Details...

Helix

47 – 55

9

Helix

59 – 62

4

Helix

63 – 65

3

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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 111-122, IDENTIFICATION IN P-TEFB 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703 AND SER-706, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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.
[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]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-674, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-549; SER-814; SER-1043 AND SER-1055, MASS SPECTROMETRY. 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-387; SER-388; SER-389; SER-392; SER-671; SER-694; SER-703; SER-706; TYR-712; SER-1043; SER-1055; SER-1058 AND SER-1062, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-549; SER-671; SER-1043 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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1058, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"HIV-1 Tat and host AFF4 recruit two transcription elongation factors into a bifunctional complex for coordinated activation of HIV-1 transcription." He N., Liu M., Hsu J., Xue Y., Chou S., Burlingame A., Krogan N.J., Alber T., Zhou Q. Mol. Cell 38:428-438(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE SEC COMPLEX.
[17]	"AFF4, a component of the ELL/P-TEFb elongation complex and a shared subunit of MLL chimeras, can link transcription elongation to leukemia." Lin C., Smith E.R., Takahashi H., Lai K.C., Martin-Brown S., Florens L., Washburn M.P., Conaway J.W., Conaway R.C., Shilatifard A. Mol. Cell 37:429-437(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE SEC COMPLEX.
[18]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-814; SER-836 AND SER-1043, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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].
[20]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"The ubiquitin ligase Siah1 controls ELL2 stability and formation of super elongation complexes to modulate gene transcription." Liu M., Hsu J., Chan C., Li Z., Zhou Q. Mol. Cell 46:325-334(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ELL2.
[22]	"The super elongation complex (SEC) family in transcriptional control." Luo Z., Lin C., Shilatifard A. Nat. Rev. Mol. Cell Biol. 13:543-547(2012) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON THE SUPER ELONGATION COMPLEX.
[23]	"HIV-1 Tat recruits transcription elongation factors dispersed along a flexible AFF4 scaffold." Chou S., Upton H., Bao K., Schulze-Gahmen U., Samelson A.J., He N., Nowak A., Lu H., Krogan N.J., Zhou Q., Alber T. Proc. Natl. Acad. Sci. U.S.A. 110:E123-E131(2013) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[24]	"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] [Europe PMC] [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

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4IMY	X-ray	2.94	G/H/I	2-73	[»]

ProteinModelPortal

Q9UHB7.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UHB7. 15 interactions.

MINT

MINT-1469196.

STRING

9606.ENSP00000265343.

PTM databases

PhosphoSite

Q9UHB7.

Polymorphism databases

DMDM

74720814.

Proteomic databases

PaxDb

Q9UHB7.

PeptideAtlas

Q9UHB7.

PRIDE

Q9UHB7.

Protocols and materials databases

DNASU

27125.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265343; ENSP00000265343; ENSG00000072364.
ENST00000378595; ENSP00000367858; ENSG00000072364.

GeneID

27125.

KEGG

hsa:27125.

UCSC

uc003kyd.3. human.
uc003kye.1. human.
uc003kyf.4. human.

Organism-specific databases

CTD

27125.

GeneCards

GC05M132211.

HGNC

HGNC:17869. AFF4.

HPA

HPA023690.

MIM

604417. gene.

neXtProt

NX_Q9UHB7.

PharmGKB

PA142672641.

GenAtlas

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Phylogenomic databases

eggNOG

NOG121636.

HOVERGEN

HBG004189.

InParanoid

Q9UHB7.

KO

K15185.

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]

PANTHER

PTHR10528. PTHR10528. 1 hit.

Pfam

PF05110. AF-4. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

AFF4. human.

GenomeRNAi

27125.

NextBio

49830.

SOURCE

Search...

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:	May 29, 2013
This is version 95 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.