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Q9UHB7 (AFF4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1163 AA.
Sequence statusComplete.
Protein existenceEvidence 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.17 Ref.18 Ref.25

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.17 Ref.18 Ref.22

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 KMT2A/MLL1-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.

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11631163AF4/FMR2 family member 4
PRO_0000239393

Regions

Compositional bias102 – 461360Ser-rich
Compositional bias836 – 89964Ser-rich

Sites

Site350 – 3512Breakpoint for insertion to form KMT2A/MLL1-AFF4 fusion protein

Amino acid modifications

Modified residue3871Phosphoserine Ref.13
Modified residue3881Phosphoserine Ref.13
Modified residue3891Phosphoserine Ref.13
Modified residue3921Phosphoserine Ref.13
Modified residue5491Phosphoserine Ref.12 Ref.15
Modified residue6711Phosphoserine Ref.13 Ref.15
Modified residue6741Phosphothreonine Ref.11
Modified residue6941Phosphoserine Ref.13
Modified residue7031Phosphoserine Ref.8 Ref.13
Modified residue7061Phosphoserine Ref.8 Ref.13
Modified residue7121Phosphotyrosine Ref.13
Modified residue8141Phosphoserine Ref.12 Ref.19
Modified residue8221N6-acetyllysine By similarity
Modified residue8361Phosphoserine Ref.19
Modified residue10431Phosphoserine Ref.12 Ref.13 Ref.15 Ref.19
Modified residue10551Phosphoserine Ref.12 Ref.13
Modified residue10581Phosphoserine Ref.13 Ref.15 Ref.16
Modified residue10621Phosphoserine Ref.13

Natural variations

Alternative sequence351 – 3533ESQ → VSK in isoform 3.
VSP_019218
Alternative sequence354 – 1163810Missing in isoform 3.
VSP_019219
Alternative sequence880 – 90021EKAPS…LDSSK → VKCWGPGAFENHSTCHVTFP G in isoform 2.
VSP_019220
Alternative sequence901 – 1163263Missing in isoform 2.
VSP_019221
Natural variant1361T → P.
Corresponds to variant rs34527550 [ dbSNP | Ensembl ].
VAR_053003
Natural variant7571S → T Found in a clear cell renal carcinoma case; somatic mutation. Ref.26
VAR_064693

Experimental info

Sequence conflict2641E → G in AAM00184. Ref.2
Sequence conflict3591T → I in AAM00184. Ref.2
Sequence conflict3831D → G in AAM00184. Ref.2
Sequence conflict4451E → G in AAM00184. Ref.2
Sequence conflict8701K → R in AAF28915. Ref.7

Secondary structure

...... 1163
Helix Strand Turn

Details...

Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: 474E1906B8832AC1

FASTA1,163127,459
        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 

« Hide

Isoform 2 [UniParc].

Checksum: A7C5BAE4A45086AE
Show »

FASTA90098,205
Isoform 3 [UniParc].

Checksum: F7811E19E60C9A92
Show »

FASTA35338,823

References

« Hide '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 KMT2A/MLL1, 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, 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-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, 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]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1058, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[17]"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.
[18]"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.
[19]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[20]"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].
[21]"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].
[22]"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.
[23]"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.
[24]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"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.
[26]"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. expand/collapse author list , 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.

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.
CCDSCCDS4164.1. [Q9UHB7-1]
RefSeqNP_055238.1. NM_014423.3. [Q9UHB7-1]
XP_005272020.1. XM_005271963.2. [Q9UHB7-1]
UniGeneHs.519313.
Hs.664840.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4IMYX-ray2.94G/H/I2-73[»]
4OGRX-ray3.00C/G/L2-73[»]
4OR5X-ray2.90E/J32-69[»]
ProteinModelPortalQ9UHB7.
SMRQ9UHB7. Positions 3-67.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118016. 22 interactions.
IntActQ9UHB7. 16 interactions.
MINTMINT-1469196.
STRING9606.ENSP00000265343.

PTM databases

PhosphoSiteQ9UHB7.

Polymorphism databases

DMDM74720814.

Proteomic databases

MaxQBQ9UHB7.
PaxDbQ9UHB7.
PeptideAtlasQ9UHB7.
PRIDEQ9UHB7.

Protocols and materials databases

DNASU27125.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265343; ENSP00000265343; ENSG00000072364. [Q9UHB7-1]
ENST00000378595; ENSP00000367858; ENSG00000072364. [Q9UHB7-2]
GeneID27125.
KEGGhsa:27125.
UCSCuc003kyd.3. human. [Q9UHB7-1]
uc003kye.1. human. [Q9UHB7-2]
uc003kyf.4. human. [Q9UHB7-3]

Organism-specific databases

CTD27125.
GeneCardsGC05M132211.
HGNCHGNC:17869. AFF4.
HPAHPA023690.
MIM604417. gene.
neXtProtNX_Q9UHB7.
PharmGKBPA142672641.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG121636.
HOVERGENHBG004189.
InParanoidQ9UHB7.
KOK15185.
OMAKRYNPSS.
OrthoDBEOG767390.
PhylomeDBQ9UHB7.
TreeFamTF326216.

Gene expression databases

ArrayExpressQ9UHB7.
BgeeQ9UHB7.
CleanExHS_AFF4.
GenevestigatorQ9UHB7.

Family and domain databases

InterProIPR007797. TF_AF4/FMR2.
[Graphical view]
PANTHERPTHR10528. PTHR10528. 1 hit.
PfamPF05110. AF-4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSAFF4. human.
GenomeRNAi27125.
NextBio49830.
PROQ9UHB7.
SOURCESearch...

Entry information

Entry nameAFF4_HUMAN
AccessionPrimary (citable) accession number: Q9UHB7
Secondary accession number(s): B2RP19 expand/collapse secondary AC list , B7WPD2, Q498B2, Q59FB3, Q6P592, Q8TDR1, Q9P0E4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 107 of the entry and version 1 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 5

Human chromosome 5: entries, gene names and cross-references to MIM