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Protein

AF4/FMR2 family member 4

Gene

Aff4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

GO - Biological processi

  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • spermatid development Source: MGI
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
AF4/FMR2 family member 4
Gene namesi
Name:Aff4
Synonyms:Alf4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2136171. Aff4.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: MGI
  • transcriptionally active chromatin Source: UniProtKB
  • transcription elongation factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Mice are infertile with azoospermia. Spermatogenesis is arrested at the level of spermiogenesis.1 Publication

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11601160AF4/FMR2 family member 4PRO_0000239394Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei382 – 3821PhosphoserineBy similarity
Modified residuei383 – 3831PhosphoserineBy similarity
Modified residuei384 – 3841PhosphoserineBy similarity
Modified residuei387 – 3871PhosphoserineBy similarity
Modified residuei482 – 4821PhosphoserineCombined sources
Modified residuei485 – 4851PhosphoserineCombined sources
Modified residuei486 – 4861PhosphoserineCombined sources
Modified residuei544 – 5441PhosphoserineBy similarity
Modified residuei666 – 6661PhosphoserineBy similarity
Modified residuei669 – 6691PhosphothreonineBy similarity
Modified residuei689 – 6891PhosphoserineCombined sources
Modified residuei698 – 6981PhosphoserineCombined sources
Modified residuei701 – 7011PhosphoserineCombined sources
Modified residuei707 – 7071PhosphotyrosineBy similarity
Modified residuei809 – 8091PhosphoserineCombined sources
Modified residuei817 – 8171N6-acetyllysineCombined sources
Modified residuei831 – 8311PhosphoserineBy similarity
Modified residuei1040 – 10401PhosphoserineCombined sources
Modified residuei1052 – 10521PhosphoserineBy similarity
Modified residuei1055 – 10551PhosphoserineBy similarity
Modified residuei1059 – 10591PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9ESC8.
MaxQBiQ9ESC8.
PaxDbiQ9ESC8.
PRIDEiQ9ESC8.

PTM databases

iPTMnetiQ9ESC8.
PhosphoSiteiQ9ESC8.

Expressioni

Tissue specificityi

Highly expressed in testis by Sertoli cells, and at low levels in other tissues.1 Publication

Developmental stagei

Expressed throughout embryogenesis with maximum expression at 10.5 and 12.5 dpc.1 Publication

Gene expression databases

BgeeiQ9ESC8.
CleanExiMM_AFF4.
ExpressionAtlasiQ9ESC8. baseline and differential.
GenevisibleiQ9ESC8. MM.

Interactioni

Subunit structurei

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 ELL2; the interaction is direct and leads to stabilize ELL2 and prevent ELL2 ubiquitination and degradation (By similarity). Interacts with ELL3; the interaction is direct.By similarity1 Publication

Protein-protein interaction databases

BioGridi220280. 1 interaction.
IntActiQ9ESC8. 2 interactions.
MINTiMINT-4129260.
STRINGi10090.ENSMUSP00000051479.

Structurei

3D structure databases

ProteinModelPortaliQ9ESC8.
SMRiQ9ESC8. Positions 4-69.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi102 – 456355Ser-richAdd
BLAST
Compositional biasi784 – 896113Ser-richAdd
BLAST
Compositional biasi1032 – 107948Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the AF4 family.Curated

Phylogenomic databases

eggNOGiENOG410IGJB. Eukaryota.
ENOG410XRXU. LUCA.
GeneTreeiENSGT00530000063217.
HOGENOMiHOG000246991.
HOVERGENiHBG004189.
InParanoidiQ9ESC8.
KOiK15185.
OMAiKRYNPSS.
OrthoDBiEOG767390.
PhylomeDBiQ9ESC8.
TreeFamiTF326216.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9ESC8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNREDRNVLR MKERERRNQE IQQGEDAFPP SSPLFAEPYK VTSKEDKLSS
60 70 80 90 100
RIQSMLGNYD EMKDYIGDRS IPKLVAIPKP AVPTTTDEKA NPNFFEQRHG
110 120 130 140 150
GSHQSSKWTP VGPAPSTSQS QKRSSALQSG HSSQRSGAGG SGASSSGQRH
160 170 180 190 200
DRDSYSSSRK KGQHGSEHSK SRSSSPGKPQ AVSSLSSSHS RSHGNDHHSK
210 220 230 240 250
EHQRSKSPRD PDANWDSPSR GPFSSGQHSS QSFPPSLMSK SSSMLQKPTA
260 270 280 290 300
YVRPMDGQES VEPKLSSEHY SSQSHGNSMT ELKPSSKAHL TKLKIPSRPL
310 320 330 340 350
DASVSGDVSC VDEILKEMTH SWPPPLTAIH TPCKTEPSKF PFPTKESQQS
360 370 380 390 400
NFGPGEQKRY STAKTSNGHQ SKSMLKDDLK LSSSEDSDGE QDCDKTMPRS
410 420 430 440 450
TPGSNSEPSH HNSEGADNSR DDSSSHSGSE SSSGSDSESE SSSSDSEANE
460 470 480 490 500
PSQSASPEPE PPPTNKWQLD NWLNKVNPHK VSPASSVDSN IPSSQAYKKE
510 520 530 540 550
GREQGTASNY TDPGGTKETS SATPGRDSKT IQKGSESGRG RQKSPAQSDS
560 570 580 590 600
TTQRRTVGKK QPKKPEKSAA EEPRGGLKIE SETPVDMAAS MPSSRHKAAT
610 620 630 640 650
KGSRKPNIKK ESKSSPRPTA EKKKYKSASK PSQKSREIIE TDTSSSDSDG
660 670 680 690 700
SESLPPSSQT PKYPESNRTP VKPSSVEEED SFFRQRMFSP MEEKELLSPL
710 720 730 740 750
SEPDDRYPLI VKIDLNLLTR IPGKPYKETE PPKGEKKNVP EKHSREVQKQ
760 770 780 790 800
ASEKASNKGK RKHKNDDDTR ASESKKPKTE DKNSSGHKPS SSRESSKQSS
810 820 830 840 850
TKEKDLLPSP AGPILSKDSK TEHGSRKRTV SQSSSLKSSG TSSKENSGSS
860 870 880 890 900
SKSSSSSTAK QKKTEGKGPS SSKEAKEKAP NSSSNCPPST PTSESSKPRR
910 920 930 940 950
TKLAFDDRNY SADHYLQEAK KLKHNADALS DRFEKAVYYL DAVVSFIECG
960 970 980 990 1000
NALEKNAQES KSPFPMYSDT VELIKYTMKL KNYLAPDATA ADKRLTVLCL
1010 1020 1030 1040 1050
RCQSLLYLRL FKLKKENALK YSKTLTEHLK NSYSNSQAPS PGLGSKAVGM
1060 1070 1080 1090 1100
PSPVSPKLSP GNSGSYSSGG SSASASGSSV TIPQKIHQMA ASYVQVTSNF
1110 1120 1130 1140 1150
LYATEIWDQA EQLSKEQKEF FAELDKVMGP LIFNASIMTD LARYTRQGLH
1160
WLRQDAKLIS
Length:1,160
Mass (Da):126,639
Last modified:March 1, 2001 - v1
Checksum:i0C13253EAC9192B3
GO

Sequence cautioni

The sequence BAC28178.1 differs from that shown. Reason: Frameshift at position 921. Curated
The sequence BAC35763.1 differs from that shown. Reason: Frameshift at positions 573 and 577. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti932 – 9321R → S in BAC28178 (PubMed:16141072).Curated
Sequence conflicti980 – 9801L → Q in BAC28178 (PubMed:16141072).Curated
Sequence conflicti1088 – 10881Q → K in BAC28178 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF190449 mRNA. Translation: AAG17126.1.
AK033163 mRNA. Translation: BAC28178.1. Frameshift.
AK053034 mRNA. Translation: BAC35244.1.
AK054401 mRNA. Translation: BAC35763.1. Frameshift.
BC138999 mRNA. Translation: AAI39000.1.
CCDSiCCDS24676.1.
RefSeqiNP_291043.1. NM_033565.2.
XP_011247633.1. XM_011249331.1.
UniGeneiMm.395281.

Genome annotation databases

EnsembliENSMUST00000060945; ENSMUSP00000051479; ENSMUSG00000049470.
GeneIDi93736.
KEGGimmu:93736.
UCSCiuc007ivu.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF190449 mRNA. Translation: AAG17126.1.
AK033163 mRNA. Translation: BAC28178.1. Frameshift.
AK053034 mRNA. Translation: BAC35244.1.
AK054401 mRNA. Translation: BAC35763.1. Frameshift.
BC138999 mRNA. Translation: AAI39000.1.
CCDSiCCDS24676.1.
RefSeqiNP_291043.1. NM_033565.2.
XP_011247633.1. XM_011249331.1.
UniGeneiMm.395281.

3D structure databases

ProteinModelPortaliQ9ESC8.
SMRiQ9ESC8. Positions 4-69.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi220280. 1 interaction.
IntActiQ9ESC8. 2 interactions.
MINTiMINT-4129260.
STRINGi10090.ENSMUSP00000051479.

PTM databases

iPTMnetiQ9ESC8.
PhosphoSiteiQ9ESC8.

Proteomic databases

EPDiQ9ESC8.
MaxQBiQ9ESC8.
PaxDbiQ9ESC8.
PRIDEiQ9ESC8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000060945; ENSMUSP00000051479; ENSMUSG00000049470.
GeneIDi93736.
KEGGimmu:93736.
UCSCiuc007ivu.2. mouse.

Organism-specific databases

CTDi27125.
MGIiMGI:2136171. Aff4.

Phylogenomic databases

eggNOGiENOG410IGJB. Eukaryota.
ENOG410XRXU. LUCA.
GeneTreeiENSGT00530000063217.
HOGENOMiHOG000246991.
HOVERGENiHBG004189.
InParanoidiQ9ESC8.
KOiK15185.
OMAiKRYNPSS.
OrthoDBiEOG767390.
PhylomeDBiQ9ESC8.
TreeFamiTF326216.

Miscellaneous databases

ChiTaRSiAff4. mouse.
PROiQ9ESC8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ESC8.
CleanExiMM_AFF4.
ExpressionAtlasiQ9ESC8. baseline and differential.
GenevisibleiQ9ESC8. MM.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Identification of 40 genes on a 1-Mb contig around the IL-4 cytokine family gene cluster on mouse chromosome 11."
    Wenderfer S.E., Slack J.P., McCluskey T.S., Monaco J.J.
    Genomics 63:354-373(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: NIH Black Swiss.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Head, Ovary and Testis.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Infertility with defective spermiogenesis in mice lacking AF5q31, the target of chromosomal translocation in human infant leukemia."
    Urano A., Endoh M., Wada T., Morikawa Y., Itoh M., Kataoka Y., Taki T., Akazawa H., Nakajima H., Komuro I., Yoshida N., Hayashi Y., Handa H., Kitamura T., Nosaka T.
    Mol. Cell. Biol. 25:6834-6845(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482; SER-485; SER-486; SER-689; SER-698; SER-701; SER-809 AND SER-1040, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Pancreas and Testis.
  6. Cited for: SUBCELLULAR LOCATION.
  7. "The RNA Pol II elongation factor Ell3 marks enhancers in ES cells and primes future gene activation."
    Lin C., Garruss A.S., Luo Z., Guo F., Shilatifard A.
    Cell 152:144-156(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ELL3.
  8. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiAFF4_MOUSE
AccessioniPrimary (citable) accession number: Q9ESC8
Secondary accession number(s): B2RST9
, Q8C6K4, Q8C6W3, Q8CCH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: March 1, 2001
Last modified: June 8, 2016
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.