CPLM-022927

Genbank Nucleotide ID

AF4/FMR2 family member 4

Protein Synonyms/Alias

ALL1-fused gene from chromosome 5q31 protein; Protein AF-5q31; Major CDK9 elongation factor-associated protein

AF5Q31; MCEF; HSPC092

Homo sapiens (Human)

Position	Peptide	Type	References
63	LGNYDEMKDFIGDRS	ubiquitination	[1]
79	PKLVAIPKPTVPPSA	acetylation	[2]
252	KSNSMLQKPTAYVRP	acetylation	[3, 4]
288	GNSMTELKPSSKAHL	ubiquitination	[1, 5, 6, 7, 8]
292	TELKPSSKAHLTKLK	ubiquitination	[6, 7]
297	SSKAHLTKLKIPSQP	ubiquitination	[6]
299	KAHLTKLKIPSQPLD	ubiquitination	[7]
344	PCKTEPSKFPFPTKE	ubiquitination	[1, 7, 9]
350	SKFPFPTKESQQSNF	ubiquitination	[6]
363	NFGTGEQKRYNPSKT	ubiquitination	[1, 7]
503	IPSSQGYKKEGREQG	acetylation	[4]
583	EEPRGGLKIESETPV	ubiquitination	[1, 6]
747	EKKNVPEKHTREAQK	acetylation	[8]
822	PAGPVPSKDPKTEHG	acetylation	[4]
964	EKNAQESKSPFPMYS	ubiquitination	[1]
996	PDATAADKRLTVLCL	ubiquitination	[1]

[1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[3] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
[4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[6] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[7] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[9] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]

Functional Description

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.

MOD_RES 387 387 Phosphoserine.
MOD_RES 388 388 Phosphoserine.
MOD_RES 389 389 Phosphoserine.
MOD_RES 392 392 Phosphoserine.
MOD_RES 549 549 Phosphoserine.
MOD_RES 671 671 Phosphoserine.
MOD_RES 674 674 Phosphothreonine.
MOD_RES 694 694 Phosphoserine.
MOD_RES 703 703 Phosphoserine.
MOD_RES 706 706 Phosphoserine.
MOD_RES 712 712 Phosphotyrosine.
MOD_RES 814 814 Phosphoserine.
MOD_RES 836 836 Phosphoserine.
MOD_RES 1043 1043 Phosphoserine.
MOD_RES 1055 1055 Phosphoserine.
MOD_RES 1058 1058 Phosphoserine.
MOD_RES 1062 1062 Phosphoserine.

3D-structure; Alternative splicing; Chromosomal rearrangement; Complete proteome; Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome; Transcription; Transcription regulation.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005739; C:mitochondrion; IDA:HPA.
GO:0005730; C:nucleolus; IDA:HPA.
GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
GO:0007286; P:spermatid development; IEA:Compara.
GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.

IPR007797; TF_AF4/FMR2.