P51825 (AFF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
AF4/FMR2 family member 1

Alternative name(s):
ALL1-fused gene from chromosome 4 protein
Short name=Protein AF-4
Protein FEL
Proto-oncogene AF4

Gene names

Name:	AFF1
Synonyms:	AF4, FEL, MLLT2, PBM1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1210 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Subcellular location	Nucleus Potential.
Involvement in disease	Note=A chromosomal aberration involving AFF1 is associated with acute leukemias. Translocation t(4;11)(q21;q23) with MLL/HRX. The result is a rogue activator protein.
Sequence similarities	Belongs to the AF4 family.
Sequence caution	The sequence AAA36642.1 differs from that shown. Reason: Frameshift at positions 897, 905 and 1178.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	sequence-specific DNA binding transcription factor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1210	1210	AF4/FMR2 family member 1		PRO_0000215910
Regions
	Compositional bias	483 – 492	10	Poly-Ser
	Compositional bias	835 – 843	9	Poly-Ser
	Compositional bias	866 – 869	4	Poly-Pro
	Compositional bias	871 – 874	4	Poly-Ser
Amino acid modifications
	Modified residue	199	1	Phosphoserine Ref.5
	Modified residue	206	1	Phosphoserine Ref.5 Ref.6 Ref.7 Ref.8
	Modified residue	212	1	Phosphoserine Ref.5 Ref.6 Ref.7
	Modified residue	216	1	Phosphoserine Ref.7
	Modified residue	220	1	Phosphothreonine Ref.6
	Modified residue	245	1	Phosphoserine Ref.7
	Modified residue	588	1	Phosphoserine Ref.4 Ref.5 Ref.7
	Modified residue	681	1	N6-acetyllysine Ref.9
	Modified residue	697	1	Phosphothreonine Ref.7
	Modified residue	750	1	Phosphoserine Ref.5 Ref.6 Ref.7 Ref.8
	Modified residue	755	1	Phosphothreonine Ref.5 Ref.6
	Modified residue	766	1	Phosphothreonine Ref.4
	Modified residue	1209	1	Phosphothreonine Ref.5 Ref.7
Natural variations
	Natural variant	209	1	P → A. Corresponds to variant rs3733378 [ dbSNP | Ensembl ].		VAR_020370
	Natural variant	1204	1	Q → K in a breast cancer sample; somatic mutation. Ref.10		VAR_036130
Experimental info
	Sequence conflict	46	1	K → R in AAA36642. Ref.2
	Sequence conflict	624	1	E → G in AAA36642. Ref.2
	Sequence conflict	899 – 905	7	SASSTKS → VPAVPRV in AAA36642. Ref.2
	Sequence conflict	928 – 929	2	EH → AD in AAA36642. Ref.2
	Sequence conflict	999	1	I → N in AAA36642. Ref.2
	Sequence conflict	1096	1	A → AR in AAA36642. Ref.2
	Sequence conflict	1140	1	N → I in AAA36642. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P51825 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: F0E334DF8FC2FF04	FASTA	1,210	131,422
	10 20 30 40 50 60 MAAQSSLYND DRNLLRIREK ERRNQEAHQE KEAFPEKIPL FGEPYKTAKG DELSSRIQNM 70 80 90 100 110 120 LGNYEEVKEF LSTKSHTHRL DASENRLGKP KYPLIPDKGS SIPSSSFHTS VHHQSIHTPA 130 140 150 160 170 180 SGPLSVGNIS HNPKMAQPRT EPMPSLHAKS CGPPDSQHLT QDRLGQEGFG SSHHKKGDRR 190 200 210 220 230 240 ADGDHCASVT DSAPERELSP LISLPSPVPP LSPIHSNQQT LPRTQGSSKV HGSSNNSKGY 250 260 270 280 290 300 CPAKSPKDLA VKVHDKETPQ DSLVAPAQPP SQTFPPPSLP SKSVAMQQKP TAYVRPMDGQ 310 320 330 340 350 360 DQAPSESPEL KPLPEDYRQQ TFEKTDLKVP AKAKLTKLKM PSQSVEQTYS NEVHCVEEIL 370 380 390 400 410 420 KEMTHSWPPP LTAIHTPSTA EPSKFPFPTK DSQHVSSVTQ NQKQYDTSSK THSNSQQGTS 430 440 450 460 470 480 SMLEDDLQLS DSEDSDSEQT PEKPPSSSAP PSAPQSLPEP VASAHSSSAE SESTSDSDSS 490 500 510 520 530 540 SDSESESSSS DSEENEPLET PAPEPEPPTT NKWQLDNWLT KVSQPAAPPE GPRSTEPPRR 550 560 570 580 590 600 HPESKGSSDS ATSQEHSESK DPPPKSSSKA PRAPPEAPHP GKRSCQKSPA QQEPPQRQTV 610 620 630 640 650 660 GTKQPKKPVK ASARAGSRTS LQGEREPGLL PYGSRDQTSK DKPKVKTKGR PRAAASNEPK 670 680 690 700 710 720 PAVPPSSEKK KHKSSLPAPS KALSGPEPAK DNVEDRTPEH FALVPLTESQ GPPHSGSGSR 730 740 750 760 770 780 TSGCRQAVVV QEDSRKDRLP LPLRDTKLLS PLRDTPPPQS LMVKITLDLL SRIPQPPGKG 790 800 810 820 830 840 SRQRKAEDKQ PPAGKKHSSE KRSSDSSSKL AKKRKGEAER DCDNKKIRLE KEIKSQSSSS 850 860 870 880 890 900 SSSHKESSKT KPSRPSSQSS KKEMLPPPPV SSSSQKPAKP ALKRSRREAD TCGQDPPKSA 910 920 930 940 950 960 SSTKSNHKDS SIPKQRRVEG KGSRSSSEHK GSSGDTANPF PVPSLPNGNS KPGKPQVKFD 970 980 990 1000 1010 1020 KQQADLHMRE AKKMKQKAEL MTDRVGKAFK YLEAVLSFIE CGIATESESQ SSKSAYSVYS 1030 1040 1050 1060 1070 1080 ETVDLIKFIM SLKSFSDATA PTQEKIFAVL CMRCQSILNM AMFRCKKDIA IKYSRTLNKH 1090 1100 1110 1120 1130 1140 FESSSKVAQA PSPCIASTGT PSPLSPMPSP ASSVGSQSSA GSVGSSGVAA TISTPVTIQN 1150 1160 1170 1180 1190 1200 MTSSYVTITS HVLTAFDLWE QAEALTRKNK EFFARLSTNV CTLALNSSLV DLVHYTRQGF 1210 QQLQELTKTP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genes on chromosomes 4, 9, and 19 involved in 11q23 abnormalities in acute leukemia share sequence homology and/or common motifs." Nakamura T., Alder H., Gu Y., Prasad R., Canaani O., Kamada N., Gale R.P., Lange B., Crist W.M., Nowell P.C., Croce C.M., Canaani E. Proc. Natl. Acad. Sci. U.S.A. 90:4631-4635(1993) [PubMed: 8506309] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"A serine/proline-rich protein is fused to HRX in t(4;11) acute leukemias." Morrissey J., Tkachuk D.C., Milatovich A., Francke U., Link M., Cleary M.L. Blood 81:1124-1131(1993) [PubMed: 8443374] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION WITH MLL/HRX.
[3]	"The t(4;11) chromosome translocation of human acute leukemias fuses the ALL-1 gene, related to Drosophila trithorax, to the AF-4 gene." Gu Y., Nakamura T., Alder H., Prasad R., Canaani O., Cimino G., Croce C.M., Canaani E. Cell 71:701-708(1992) [PubMed: 1423625] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH MLL/HRX.
[4]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588 AND THR-766, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-206; SER-212; SER-588; SER-750; THR-755 AND THR-1209, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-212; THR-220; SER-750 AND THR-755, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-212; SER-216; SER-245; SER-588; THR-697; SER-750 AND THR-1209, MASS SPECTROMETRY.
[8]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206 AND SER-750, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[9]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-681, MASS SPECTROMETRY.
[10]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-1204.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	L13773 mRNA. Translation: AAA58360.1. L25050 mRNA. Translation: AAA36642.1. Frameshift.
IPI	IPI00873029.
PIR	A58198. I39410.
RefSeq	NP_005926.1. NM_005935.2.
UniGene	Hs.480190.
3D structure databases
ProteinModelPortal	P51825.
ModBase	Search...
Protein-protein interaction databases
IntAct	P51825. 13 interactions.
MINT	MINT-1198004.
STRING	P51825.
PTM databases
PhosphoSite	P51825.
Polymorphism databases
DMDM	1703194.
Proteomic databases
PRIDE	P51825.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000307808; ENSP00000305689; ENSG00000172493.
GeneID	4299.
KEGG	hsa:4299.
UCSC	uc003hqj.2. human.
Organism-specific databases
CTD	4299.
GeneCards	GC04P087856.
H-InvDB	HIX0031433.
HGNC	HGNC:7135. AFF1.
MIM	159557. gene.
neXtProt	NX_P51825.
Orphanet	99860. Precursor B-cell acute lymphoblastic leukemia.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG07840.
HOVERGEN	HBG004189.
OrthoDB	EOG4M91QS.
Gene expression databases
ArrayExpress	P51825.
Bgee	P51825.
CleanEx	HS_AFF1.
Genevestigator	P51825.
GermOnline	ENSG00000172493. Homo sapiens.
Family and domain databases
InterPro	IPR007797. TF_AF4/FMR2. IPR015479. Transcrpt_fact_AF4. [Graphical view]
KO	K15184.
PANTHER	PTHR10528. AF-4. 1 hit. PTHR10528:SF6. Transcrpt_fact_AF4. 1 hit.
Pfam	PF05110. AF-4. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	16923.
SOURCE	Search...

Entry information

Entry name

AFF1_HUMAN

Accession

Primary (citable) accession number: P51825

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 94 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.