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P51825

- AFF1_HUMAN

UniProt

P51825 - AFF1_HUMAN

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Protein
AF4/FMR2 family member 1
Gene
AFF1, AF4, FEL, MLLT2, PBM1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. sequence-specific DNA binding transcription factor activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. positive regulation of transcription, DNA-templated Source: Ensembl
Complete GO annotation...

Names & Taxonomyi

Protein namesi
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 namesi
Name:AFF1
Synonyms:AF4, FEL, MLLT2, PBM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:7135. AFF1.

Subcellular locationi

Nucleus Reviewed prediction

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving AFF1 is associated with acute leukemias. Translocation t(4;11)(q21;q23) with KMT2A/MLL1. The result is a rogue activator protein.

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

Orphaneti99860. Precursor B-cell acute lymphoblastic leukemia.
PharmGKBiPA30851.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12101210AF4/FMR2 family member 1
PRO_0000215910Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei206 – 2061Phosphoserine5 Publications
Modified residuei212 – 2121Phosphoserine3 Publications
Modified residuei220 – 2201Phosphothreonine1 Publication
Modified residuei588 – 5881Phosphoserine1 Publication
Modified residuei681 – 6811N6-acetyllysine1 Publication
Modified residuei697 – 6971Phosphothreonine2 Publications
Modified residuei750 – 7501Phosphoserine3 Publications
Modified residuei755 – 7551Phosphothreonine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP51825.
PaxDbiP51825.
PRIDEiP51825.

PTM databases

PhosphoSiteiP51825.

Expressioni

Gene expression databases

ArrayExpressiP51825.
BgeeiP51825.
CleanExiHS_AFF1.
GenevestigatoriP51825.

Interactioni

Subunit structurei

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).

Binary interactionsi

WithEntry#Exp.IntActNotes
tatP046083EBI-2610180,EBI-6164389From a different organism.

Protein-protein interaction databases

BioGridi110445. 28 interactions.
DIPiDIP-56407N.
IntActiP51825. 15 interactions.
MINTiMINT-1198004.
STRINGi9606.ENSP00000305689.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni768 – 7703

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LM0NMR-A738-779[»]
ProteinModelPortaliP51825.
SMRiP51825. Positions 10-71, 738-779.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi483 – 49210Poly-Ser
Compositional biasi835 – 8439Poly-Ser
Compositional biasi866 – 8694Poly-Pro
Compositional biasi871 – 8744Poly-Ser

Sequence similaritiesi

Belongs to the AF4 family.

Phylogenomic databases

eggNOGiNOG120323.
HOVERGENiHBG004189.
KOiK15184.
OMAiEPYKTAK.
OrthoDBiEOG767390.
PhylomeDBiP51825.
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: P51825-1) [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

MAAQSSLYND DRNLLRIREK ERRNQEAHQE KEAFPEKIPL FGEPYKTAKG     50
DELSSRIQNM LGNYEEVKEF LSTKSHTHRL DASENRLGKP KYPLIPDKGS 100
SIPSSSFHTS VHHQSIHTPA SGPLSVGNIS HNPKMAQPRT EPMPSLHAKS 150
CGPPDSQHLT QDRLGQEGFG SSHHKKGDRR ADGDHCASVT DSAPERELSP 200
LISLPSPVPP LSPIHSNQQT LPRTQGSSKV HGSSNNSKGY CPAKSPKDLA 250
VKVHDKETPQ DSLVAPAQPP SQTFPPPSLP SKSVAMQQKP TAYVRPMDGQ 300
DQAPSESPEL KPLPEDYRQQ TFEKTDLKVP AKAKLTKLKM PSQSVEQTYS 350
NEVHCVEEIL KEMTHSWPPP LTAIHTPSTA EPSKFPFPTK DSQHVSSVTQ 400
NQKQYDTSSK THSNSQQGTS SMLEDDLQLS DSEDSDSEQT PEKPPSSSAP 450
PSAPQSLPEP VASAHSSSAE SESTSDSDSS SDSESESSSS DSEENEPLET 500
PAPEPEPPTT NKWQLDNWLT KVSQPAAPPE GPRSTEPPRR HPESKGSSDS 550
ATSQEHSESK DPPPKSSSKA PRAPPEAPHP GKRSCQKSPA QQEPPQRQTV 600
GTKQPKKPVK ASARAGSRTS LQGEREPGLL PYGSRDQTSK DKPKVKTKGR 650
PRAAASNEPK PAVPPSSEKK KHKSSLPAPS KALSGPEPAK DNVEDRTPEH 700
FALVPLTESQ GPPHSGSGSR TSGCRQAVVV QEDSRKDRLP LPLRDTKLLS 750
PLRDTPPPQS LMVKITLDLL SRIPQPPGKG SRQRKAEDKQ PPAGKKHSSE 800
KRSSDSSSKL AKKRKGEAER DCDNKKIRLE KEIKSQSSSS SSSHKESSKT 850
KPSRPSSQSS KKEMLPPPPV SSSSQKPAKP ALKRSRREAD TCGQDPPKSA 900
SSTKSNHKDS SIPKQRRVEG KGSRSSSEHK GSSGDTANPF PVPSLPNGNS 950
KPGKPQVKFD KQQADLHMRE AKKMKQKAEL MTDRVGKAFK YLEAVLSFIE 1000
CGIATESESQ SSKSAYSVYS ETVDLIKFIM SLKSFSDATA PTQEKIFAVL 1050
CMRCQSILNM AMFRCKKDIA IKYSRTLNKH FESSSKVAQA PSPCIASTGT 1100
PSPLSPMPSP ASSVGSQSSA GSVGSSGVAA TISTPVTIQN MTSSYVTITS 1150
HVLTAFDLWE QAEALTRKNK EFFARLSTNV CTLALNSSLV DLVHYTRQGF 1200
QQLQELTKTP 1210
Length:1,210
Mass (Da):131,422
Last modified:October 1, 1996 - v1
Checksum:iF0E334DF8FC2FF04
GO
Isoform 2 (identifier: P51825-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MAAQS → MAFTERVNSSGN
     1096-1096: A → AR

Note: No experimental confirmation available.

Show »
Length:1,218
Mass (Da):132,384
Checksum:i8C9DCE41FF2EA841
GO
Isoform 3 (identifier: P51825-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1096-1096: A → AR

Show »
Length:1,211
Mass (Da):131,578
Checksum:iFD08BE7A2BE38BFC
GO

Sequence cautioni

The sequence AAA36642.1 differs from that shown. Reason: Frameshift at positions 897, 905 and 1178.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti209 – 2091P → A.
Corresponds to variant rs3733378 [ dbSNP | Ensembl ].
VAR_020370
Natural varianti1204 – 12041Q → K in a breast cancer sample; somatic mutation. 1 Publication
VAR_036130

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 55MAAQS → MAFTERVNSSGN in isoform 2.
VSP_046095
Alternative sequencei1096 – 10961A → AR in isoform 2 and isoform 3.
VSP_046096

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461K → R in AAA36642. 1 Publication
Sequence conflicti624 – 6241E → G in AAA36642. 1 Publication
Sequence conflicti762 – 7621M → V in BAG62103. 1 Publication
Sequence conflicti820 – 8201R → G in BAG62103. 1 Publication
Sequence conflicti899 – 9057SASSTKS → VPAVPRV in AAA36642. 1 Publication
Sequence conflicti928 – 9292EH → AD in AAA36642. 1 Publication
Sequence conflicti999 – 9991I → N in AAA36642. 1 Publication
Sequence conflicti1140 – 11401N → I in AAA36642. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L13773 mRNA. Translation: AAA58360.1.
L25050 mRNA. Translation: AAA36642.1. Frameshift.
AK300364 mRNA. Translation: BAG62103.1.
AC092658 Genomic DNA. No translation available.
AC093779 Genomic DNA. No translation available.
AC093827 Genomic DNA. No translation available.
CCDSiCCDS3616.1. [P51825-1]
CCDS54775.1. [P51825-2]
PIRiA58198.
I39410.
RefSeqiNP_001160165.1. NM_001166693.1. [P51825-2]
NP_005926.1. NM_005935.2. [P51825-1]
XP_005263064.1. XM_005263007.1. [P51825-2]
XP_005263065.1. XM_005263008.2. [P51825-2]
UniGeneiHs.480190.

Genome annotation databases

EnsembliENST00000307808; ENSP00000305689; ENSG00000172493. [P51825-1]
ENST00000395146; ENSP00000378578; ENSG00000172493. [P51825-2]
GeneIDi4299.
KEGGihsa:4299.
UCSCiuc003hqj.4. human. [P51825-1]

Polymorphism databases

DMDMi1703194.

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
L13773 mRNA. Translation: AAA58360.1 .
L25050 mRNA. Translation: AAA36642.1 . Frameshift.
AK300364 mRNA. Translation: BAG62103.1 .
AC092658 Genomic DNA. No translation available.
AC093779 Genomic DNA. No translation available.
AC093827 Genomic DNA. No translation available.
CCDSi CCDS3616.1. [P51825-1 ]
CCDS54775.1. [P51825-2 ]
PIRi A58198.
I39410.
RefSeqi NP_001160165.1. NM_001166693.1. [P51825-2 ]
NP_005926.1. NM_005935.2. [P51825-1 ]
XP_005263064.1. XM_005263007.1. [P51825-2 ]
XP_005263065.1. XM_005263008.2. [P51825-2 ]
UniGenei Hs.480190.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LM0 NMR - A 738-779 [» ]
ProteinModelPortali P51825.
SMRi P51825. Positions 10-71, 738-779.
ModBasei Search...

Protein-protein interaction databases

BioGridi 110445. 28 interactions.
DIPi DIP-56407N.
IntActi P51825. 15 interactions.
MINTi MINT-1198004.
STRINGi 9606.ENSP00000305689.

PTM databases

PhosphoSitei P51825.

Polymorphism databases

DMDMi 1703194.

Proteomic databases

MaxQBi P51825.
PaxDbi P51825.
PRIDEi P51825.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000307808 ; ENSP00000305689 ; ENSG00000172493 . [P51825-1 ]
ENST00000395146 ; ENSP00000378578 ; ENSG00000172493 . [P51825-2 ]
GeneIDi 4299.
KEGGi hsa:4299.
UCSCi uc003hqj.4. human. [P51825-1 ]

Organism-specific databases

CTDi 4299.
GeneCardsi GC04P087856.
HGNCi HGNC:7135. AFF1.
MIMi 159557. gene.
neXtProti NX_P51825.
Orphaneti 99860. Precursor B-cell acute lymphoblastic leukemia.
PharmGKBi PA30851.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG120323.
HOVERGENi HBG004189.
KOi K15184.
OMAi EPYKTAK.
OrthoDBi EOG767390.
PhylomeDBi P51825.
TreeFami TF326216.

Miscellaneous databases

ChiTaRSi AFF1. human.
GeneWikii AFF1.
GenomeRNAii 4299.
NextBioi 16923.
PROi P51825.
SOURCEi Search...

Gene expression databases

ArrayExpressi P51825.
Bgeei P51825.
CleanExi HS_AFF1.
Genevestigatori P51825.

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. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), CHROMOSOMAL TRANSLOCATION WITH KMT2A.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] [Europe PMC] [Abstract]
    Cited for: CHROMOSOMAL TRANSLOCATION WITH KMT2A.
  6. "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-206; SER-212 AND THR-697, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-212; THR-220; SER-750 AND THR-755, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-206; SER-212; SER-588 AND SER-750, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "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-206 AND SER-750, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-681, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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-206, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-697, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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.
  14. "Leukemia fusion target AF9 is an intrinsically disordered transcriptional regulator that recruits multiple partners via coupled folding and binding."
    Leach B.I., Kuntimaddi A., Schmidt C.R., Cierpicki T., Johnson S.A., Bushweller J.H.
    Structure 21:176-183(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 738-779 IN COMPLEX WITH MLLT3.
  15. Cited for: VARIANT [LARGE SCALE ANALYSIS] LYS-1204.

Entry informationi

Entry nameiAFF1_HUMAN
AccessioniPrimary (citable) accession number: P51825
Secondary accession number(s): B4DTU1, E9PBM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 117 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, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: 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

Dasty 3

Similar proteinsi