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Q9UHB7

- AFF4_HUMAN

UniProt

Q9UHB7 - AFF4_HUMAN

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Protein

AF4/FMR2 family member 4

Gene

AFF4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei350 – 3512Breakpoint for insertion to form KMT2A/MLL1-AFF4 fusion protein

GO - Molecular functioni

  1. sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

  1. spermatid development Source: Ensembl
  2. transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
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 namesi
Name:AFF4
Synonyms:AF5Q31, MCEF
ORF Names:HSPC092
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:17869. AFF4.

Subcellular locationi

Nucleus 1 Publication
Note: Associates to transcriptionally active chromatin but not at snRNA genes.By similarity

GO - Cellular componenti

  1. mitochondrion Source: HPA
  2. nucleolus Source: HPA
  3. nucleus Source: HPA
  4. transcriptionally active chromatin Source: UniProtKB
  5. transcription elongation factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA142672641.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11631163AF4/FMR2 family member 4PRO_0000239393Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei387 – 3871Phosphoserine1 Publication
Modified residuei388 – 3881Phosphoserine1 Publication
Modified residuei389 – 3891Phosphoserine1 Publication
Modified residuei392 – 3921Phosphoserine1 Publication
Modified residuei549 – 5491Phosphoserine2 Publications
Modified residuei671 – 6711Phosphoserine2 Publications
Modified residuei674 – 6741Phosphothreonine1 Publication
Modified residuei694 – 6941Phosphoserine1 Publication
Modified residuei703 – 7031Phosphoserine2 Publications
Modified residuei706 – 7061Phosphoserine2 Publications
Modified residuei712 – 7121Phosphotyrosine1 Publication
Modified residuei814 – 8141Phosphoserine2 Publications
Modified residuei822 – 8221N6-acetyllysineBy similarity
Modified residuei836 – 8361Phosphoserine1 Publication
Modified residuei1043 – 10431Phosphoserine4 Publications
Modified residuei1055 – 10551Phosphoserine2 Publications
Modified residuei1058 – 10581Phosphoserine3 Publications
Modified residuei1062 – 10621Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UHB7.
PaxDbiQ9UHB7.
PeptideAtlasiQ9UHB7.
PRIDEiQ9UHB7.

PTM databases

PhosphoSiteiQ9UHB7.

Expressioni

Tissue specificityi

Ubiquitously expressed. Strongly expressed in heart, placenta, skeletal muscle, pancreas and to a lower extent in brain.2 Publications

Developmental stagei

Expressed in fetal heart, lung, brain and to a lower extent liver.1 Publication

Gene expression databases

BgeeiQ9UHB7.
CleanExiHS_AFF4.
ExpressionAtlasiQ9UHB7. baseline and differential.
GenevestigatoriQ9UHB7.

Organism-specific databases

HPAiHPA023690.

Interactioni

Subunit structurei

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, EAF2, CDK9, MLLT3/AF9, AFF (AFF1 or AFF4), the P-TEFb complex and ELL (ELL, ELL2 or ELL3). Interacts with ELL.By similarity5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCNT1O605635EBI-395282,EBI-2479671
MLLT1Q031118EBI-395282,EBI-1384215
MLLT3P425684EBI-395282,EBI-716132
tatP046084EBI-395282,EBI-6164389From a different organism.

Protein-protein interaction databases

BioGridi118016. 27 interactions.
IntActiQ9UHB7. 16 interactions.
MINTiMINT-1469196.
STRINGi9606.ENSP00000265343.

Structurei

Secondary structure

1
1163
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1813Combined sources
Helixi47 – 5610Combined sources
Helixi59 – 624Combined sources
Turni63 – 653Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4IMYX-ray2.94G/H/I2-73[»]
4OGRX-ray3.00C/G/L2-73[»]
4OR5X-ray2.90E/J32-69[»]
ProteinModelPortaliQ9UHB7.
SMRiQ9UHB7. Positions 4-69.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi102 – 461360Ser-richAdd
BLAST
Compositional biasi836 – 89964Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the AF4 family.Curated

Phylogenomic databases

eggNOGiNOG121636.
GeneTreeiENSGT00530000063217.
HOVERGENiHBG004189.
InParanoidiQ9UHB7.
KOiK15185.
OMAiKRYNPSS.
OrthoDBiEOG767390.
PhylomeDBiQ9UHB7.
TreeFamiTF326216.

Family and domain databases

InterProiIPR007797. TF_AF4/FMR2.
[Graphical view]
PANTHERiPTHR10528. PTHR10528. 1 hit.
PfamiPF05110. AF-4. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UHB7-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MNREDRNVLR MKERERRNQE IQQGEDAFPP SSPLFAEPYK VTSKEDKLSS
60 70 80 90 100
RIQSMLGNYD EMKDFIGDRS IPKLVAIPKP TVPPSADEKS NPNFFEQRHG
110 120 130 140 150
GSHQSSKWTP VGPAPSTSQS QKRSSGLQSG HSSQRTSAGS SSGTNSSGQR
160 170 180 190 200
HDRESYNNSG SSSRKKGQHG SEHSKSRSSS PGKPQAVSSL NSSHSRSHGN
210 220 230 240 250
DHHSKEHQRS KSPRDPDANW DSPSRVPFSS GQHSTQSFPP SLMSKSNSML
260 270 280 290 300
QKPTAYVRPM DGQESMEPKL SSEHYSSQSH GNSMTELKPS SKAHLTKLKI
310 320 330 340 350
PSQPLDASAS GDVSCVDEIL KEMTHSWPPP LTAIHTPCKT EPSKFPFPTK
360 370 380 390 400
ESQQSNFGTG EQKRYNPSKT SNGHQSKSML KDDLKLSSSE DSDGEQDCDK
410 420 430 440 450
TMPRSTPGSN SEPSHHNSEG ADNSRDDSSS HSGSESSSGS DSESESSSSD
460 470 480 490 500
SEANEPSQSA SPEPEPPPTN KWQLDNWLNK VNPHKVSPAS SVDSNIPSSQ
510 520 530 540 550
GYKKEGREQG TGNSYTDTSG PKETSSATPG RDSKTIQKGS ESGRGRQKSP
560 570 580 590 600
AQSDSTTQRR TVGKKQPKKA EKAAAEEPRG GLKIESETPV DLASSMPSSR
610 620 630 640 650
HKAATKGSRK PNIKKESKSS PRPTAEKKKY KSTSKSSQKS REIIETDTSS
660 670 680 690 700
SDSDESESLP PSSQTPKYPE SNRTPVKPSS VEEEDSFFRQ RMFSPMEEKE
710 720 730 740 750
LLSPLSEPDD RYPLIVKIDL NLLTRIPGKP YKETEPPKGE KKNVPEKHTR
760 770 780 790 800
EAQKQASEKV SNKGKRKHKN EDDNRASESK KPKTEDKNSA GHKPSSNRES
810 820 830 840 850
SKQSAAKEKD LLPSPAGPVP SKDPKTEHGS RKRTISQSSS LKSSSNSNKE
860 870 880 890 900
TSGSSKNSSS TSKQKKTEGK TSSSSKEVKE KAPSSSSNCP PSAPTLDSSK
910 920 930 940 950
PRRTKLVFDD RNYSADHYLQ EAKKLKHNAD ALSDRFEKAV YYLDAVVSFI
960 970 980 990 1000
ECGNALEKNA QESKSPFPMY SETVDLIKYT MKLKNYLAPD ATAADKRLTV
1010 1020 1030 1040 1050
LCLRCESLLY LRLFKLKKEN ALKYSKTLTE HLKNSYNNSQ APSPGLGSKA
1060 1070 1080 1090 1100
VGMPSPVSPK LSPGNSGNYS SGASSASASG SSVTIPQKIH QMAASYVQVT
1110 1120 1130 1140 1150
SNFLYATEIW DQAEQLSKEQ KEFFAELDKV MGPLIFNASI MTDLVRYTRQ
1160
GLHWLRQDAK LIS
Length:1,163
Mass (Da):127,459
Last modified:May 1, 2000 - v1
Checksum:i474E1906B8832AC1
GO
Isoform 2 (identifier: Q9UHB7-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:900
Mass (Da):98,205
Checksum:iA7C5BAE4A45086AE
GO
Isoform 3 (identifier: Q9UHB7-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:353
Mass (Da):38,823
Checksum:iF7811E19E60C9A92
GO

Sequence cautioni

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti264 – 2641E → G in AAM00184. (PubMed:12065898)Curated
Sequence conflicti359 – 3591T → I in AAM00184. (PubMed:12065898)Curated
Sequence conflicti383 – 3831D → G in AAM00184. (PubMed:12065898)Curated
Sequence conflicti445 – 4451E → G in AAM00184. (PubMed:12065898)Curated
Sequence conflicti870 – 8701K → R in AAF28915. (PubMed:11042152)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti136 – 1361T → P.
Corresponds to variant rs34527550 [ dbSNP | Ensembl ].
VAR_053003
Natural varianti757 – 7571S → T Found in a clear cell renal carcinoma case; somatic mutation. 1 Publication
VAR_064693

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei351 – 3533ESQ → VSK in isoform 3. 1 PublicationVSP_019218
Alternative sequencei354 – 1163810Missing in isoform 3. 1 PublicationVSP_019219Add
BLAST
Alternative sequencei880 – 90021EKAPS…LDSSK → VKCWGPGAFENHSTCHVTFP G in isoform 2. 2 PublicationsVSP_019220Add
BLAST
Alternative sequencei901 – 1163263Missing in isoform 2. 2 PublicationsVSP_019221Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4164.1. [Q9UHB7-1]
RefSeqiNP_055238.1. NM_014423.3. [Q9UHB7-1]
XP_005272020.1. XM_005271963.2. [Q9UHB7-1]
UniGeneiHs.519313.
Hs.664840.

Genome annotation databases

EnsembliENST00000265343; ENSP00000265343; ENSG00000072364. [Q9UHB7-1]
ENST00000378595; ENSP00000367858; ENSG00000072364. [Q9UHB7-2]
GeneIDi27125.
KEGGihsa:27125.
UCSCiuc003kyd.3. human. [Q9UHB7-1]
uc003kye.1. human. [Q9UHB7-2]
uc003kyf.4. human. [Q9UHB7-3]

Polymorphism databases

DMDMi74720814.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS4164.1. [Q9UHB7-1 ]
RefSeqi NP_055238.1. NM_014423.3. [Q9UHB7-1 ]
XP_005272020.1. XM_005271963.2. [Q9UHB7-1 ]
UniGenei Hs.519313.
Hs.664840.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4IMY X-ray 2.94 G/H/I 2-73 [» ]
4OGR X-ray 3.00 C/G/L 2-73 [» ]
4OR5 X-ray 2.90 E/J 32-69 [» ]
ProteinModelPortali Q9UHB7.
SMRi Q9UHB7. Positions 4-69.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 118016. 27 interactions.
IntActi Q9UHB7. 16 interactions.
MINTi MINT-1469196.
STRINGi 9606.ENSP00000265343.

PTM databases

PhosphoSitei Q9UHB7.

Polymorphism databases

DMDMi 74720814.

Proteomic databases

MaxQBi Q9UHB7.
PaxDbi Q9UHB7.
PeptideAtlasi Q9UHB7.
PRIDEi Q9UHB7.

Protocols and materials databases

DNASUi 27125.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265343 ; ENSP00000265343 ; ENSG00000072364 . [Q9UHB7-1 ]
ENST00000378595 ; ENSP00000367858 ; ENSG00000072364 . [Q9UHB7-2 ]
GeneIDi 27125.
KEGGi hsa:27125.
UCSCi uc003kyd.3. human. [Q9UHB7-1 ]
uc003kye.1. human. [Q9UHB7-2 ]
uc003kyf.4. human. [Q9UHB7-3 ]

Organism-specific databases

CTDi 27125.
GeneCardsi GC05M132211.
HGNCi HGNC:17869. AFF4.
HPAi HPA023690.
MIMi 604417. gene.
neXtProti NX_Q9UHB7.
PharmGKBi PA142672641.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG121636.
GeneTreei ENSGT00530000063217.
HOVERGENi HBG004189.
InParanoidi Q9UHB7.
KOi K15185.
OMAi KRYNPSS.
OrthoDBi EOG767390.
PhylomeDBi Q9UHB7.
TreeFami TF326216.

Miscellaneous databases

ChiTaRSi AFF4. human.
GenomeRNAii 27125.
NextBioi 49830.
PROi Q9UHB7.
SOURCEi Search...

Gene expression databases

Bgeei Q9UHB7.
CleanExi HS_AFF4.
ExpressionAtlasi Q9UHB7. baseline and differential.
Genevestigatori Q9UHB7.

Family and domain databases

InterProi IPR007797. TF_AF4/FMR2.
[Graphical view ]
PANTHERi PTHR10528. PTHR10528. 1 hit.
Pfami PF05110. AF-4. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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, 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. 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: IDENTIFICATION IN THE SEC COMPLEX.
  22. "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].
  23. "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.
  24. "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.
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "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.
  27. Cited for: VARIANT THR-757.

Entry informationi

Entry nameiAFF4_HUMAN
AccessioniPrimary (citable) accession number: Q9UHB7
Secondary accession number(s): B2RP19
, B7WPD2, Q498B2, Q59FB3, Q6P592, Q8TDR1, Q9P0E4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: May 1, 2000
Last modified: October 29, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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