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Protein

Protein AF-10

Gene

MLLT10

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

Functioni

Probably involved in transcriptional regulation. In vitro or as fusion protein with KMT2A/MLL1 has transactivation activity. Binds to cruciform DNA.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei266 – 2661KMT2A/MLL1 fusion point (in acute myeloid leukemia patient B)
Sitei627 – 6271KMT2A/MLL1 fusion point (in acute myeloid leukemia patient C)
Sitei664 – 6641KMT2A/MLL1 fusion point (in acute myeloid leukemia patient A)

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri22 – 7453PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri68 – 8518C4-typeAdd
BLAST
Zinc fingeri134 – 19764PHD-type 2PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • transcription factor activity, sequence-specific DNA binding Source: ProtInc
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Protein AF-10
Alternative name(s):
ALL1-fused gene from chromosome 10 protein
Gene namesi
Name:MLLT10
Synonyms:AF10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:16063. MLLT10.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving MLLT10 is associated with acute leukemias. Translocation t(10;11)(p12;q23) with KMT2A/MLL1. The result is a rogue activator protein.

A chromosomal aberration involving MLLT10 is associated with diffuse histiocytic lymphomas. Translocation t(10;11)(p13;q14) with PICALM.

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

MalaCardsiMLLT10.
Orphaneti99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBiPA30849.

Polymorphism and mutation databases

BioMutaiMLLT10.
DMDMi527504034.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10681068Protein AF-10PRO_0000215935Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki280 – 280Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei436 – 4361PhosphoserineBy similarity
Modified residuei532 – 5321PhosphoserineBy similarity
Modified residuei684 – 6841PhosphoserineCombined sources
Modified residuei686 – 6861PhosphoserineCombined sources
Modified residuei689 – 6891PhosphoserineBy similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP55197.
PaxDbiP55197.
PRIDEiP55197.

PTM databases

iPTMnetiP55197.
PhosphoSiteiP55197.

Expressioni

Tissue specificityi

Expressed abundantly in testis.

Gene expression databases

BgeeiP55197.
CleanExiHS_MLLT10.
ExpressionAtlasiP55197. baseline and differential.
GenevisibleiP55197. HS.

Organism-specific databases

HPAiHPA005747.

Interactioni

Subunit structurei

Self-associates. Interacts with FSTL3 isoform 2; the interaction enhances MLLT10 in vitro transcriptional activity and self-association. Interacts with YEATS4. Interacts with SS18. Interacts with DOT1L; this interaction also occurs with the KMT2A/MLL1 fusion protein.4 Publications

Protein-protein interaction databases

BioGridi113723. 24 interactions.
DIPiDIP-37633N.
IntActiP55197. 14 interactions.
STRINGi9606.ENSP00000307411.

Structurei

Secondary structure

1
1068
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 294Combined sources
Beta strandi39 – 413Combined sources
Beta strandi50 – 523Combined sources
Helixi53 – 553Combined sources
Helixi69 – 724Combined sources
Beta strandi73 – 753Combined sources
Turni77 – 793Combined sources
Beta strandi83 – 864Combined sources
Beta strandi89 – 957Combined sources
Beta strandi98 – 1025Combined sources
Helixi103 – 1086Combined sources
Beta strandi113 – 1153Combined sources
Turni117 – 1204Combined sources
Beta strandi122 – 1243Combined sources
Helixi130 – 1323Combined sources
Helixi138 – 1425Combined sources
Helixi146 – 1483Combined sources
Beta strandi159 – 1613Combined sources
Helixi168 – 1747Combined sources
Beta strandi177 – 1815Combined sources
Beta strandi183 – 1864Combined sources
Beta strandi188 – 1925Combined sources
Helixi195 – 1995Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5DAGX-ray1.60A1-208[»]
5DAHX-ray2.61A/B1-208[»]
ProteinModelPortaliP55197.
SMRiP55197. Positions 25-78, 127-197.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni80 – 287208Self-associationAdd
BLAST
Regioni141 – 23393Interaction with FSTL3Add
BLAST
Regioni311 – 674364DNA-bindingAdd
BLAST
Regioni703 – 78482Transactivation domain; required for DOT1L-bindingAdd
BLAST
Regioni750 – 77829Leucine-zipperAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi229 – 24012Glu/Lys-richAdd
BLAST

Sequence similaritiesi

Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri22 – 7453PHD-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri68 – 8518C4-typeAdd
BLAST
Zinc fingeri134 – 19764PHD-type 2PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0956. Eukaryota.
COG5141. LUCA.
GeneTreeiENSGT00740000114866.
HOGENOMiHOG000049087.
HOVERGENiHBG004186.
InParanoidiP55197.
OMAiKSPHLGN.
OrthoDBiEOG7K6PT9.
PhylomeDBiP55197.
TreeFamiTF316118.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
SMARTiSM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 4 (identifier: P55197-4) [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
MVSSDRPVSL EDEVSHSMKE MIGGCCVCSD ERGWAENPLV YCDGHGCSVA
60 70 80 90 100
VHQACYGIVQ VPTGPWFCRK CESQERAARV RCELCPHKDG ALKRTDNGGW
110 120 130 140 150
AHVVCALYIP EVQFANVSTM EPIVLQSVPH DRYNKTCYIC DEQGRESKAA
160 170 180 190 200
TGACMTCNKH GCRQAFHVTC AQFAGLLCEE EGNGADNVQY CGYCKYHFSK
210 220 230 240 250
LKKSKRGSNR SYDQSLSDSS SHSQDKHHEK EKKKYKEKDK HKQKHKKQPE
260 270 280 290 300
PSPALVPSLT VTTEKTYTST SNNSISGSLK RLEDTTARFT NANFQEVSAH
310 320 330 340 350
TSSGKDVSET RGSEGKGKKS SAHSSGQRGR KPGGGRNPGT TVSAASPFPQ
360 370 380 390 400
GSFSGTPGSV KSSSGSSVQS PQDFLSFTDS DLRNDSYSHS QQSSATKDVH
410 420 430 440 450
KGESGSQEGG VNSFSTLIGL PSTSAVTSQP KSFENSPGDL GNSSLPTAGY
460 470 480 490 500
KRAQTSGIEE ETVKEKKRKG NKQSKHGPGR PKGNKNQENV SHLSVSSASP
510 520 530 540 550
TSSVASAAGS ITSSSLQKSP TLLRNGSLQS LSVGSSPVGS EISMQYRHDG
560 570 580 590 600
ACPTTTFSEL LNAIHNGIYN SNDVAVSFPN VVSGSGSSTP VSSSHLPQQS
610 620 630 640 650
SGHLQQVGAL SPSAVSSAAP AVATTQANTL SGSSLSQAPS HMYGNRSNSS
660 670 680 690 700
MAALIAQSEN NQTDQDLGDN SRNLVGRGSS PRGSLSPRSP VSSLQIRYDQ
710 720 730 740 750
PGNSSLENLP PVAASIEQLL ERQWSEGQQF LLEQGTPSDI LGMLKSLHQL
760 770 780 790 800
QVENRRLEEQ IKNLTAKKER LQLLNAQLSV PFPTITANPS PSHQIHTFSA
810 820 830 840 850
QTAPTTDSLN SSKSPHIGNS FLPDNSLPVL NQDLTSSGQS TSSSSALSTP
860 870 880 890 900
PPAGQSPAQQ GSGVSGVQQV NGVTVGALAS GMQPVTSTIP AVSAVGGIIG
910 920 930 940 950
ALPGNQLAIN GIVGALNGVM QTPVTMSQNP TPLTHTTVPP NATHPMPATL
960 970 980 990 1000
TNSASGLGLL SDQQRQILIH QQQFQQLLNS QQLTPEQHQA FLYQLMQHHH
1010 1020 1030 1040 1050
QQHHQPELQQ LQIPGPTQIP INNLLAGTQA PPLHTATTNP FLTIHGDNAS
1060
QKVARLSDKT GPVAQEKS
Length:1,068
Mass (Da):113,320
Last modified:July 24, 2013 - v2
Checksum:i0C4D9B77F61BFEEE
GO
Isoform 1 (identifier: P55197-1) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     566-566: N → NDRGDSSTLTKQELKFI
     986-1011: EQHQAFLYQLMQHHHQQHHQPELQQL → VHRHPHFTQLPPTHFSPSMEIMQVRK
     1012-1068: Missing.

Show »
Length:1,027
Mass (Da):109,026
Checksum:i7C7C0059DDD46589
GO
Isoform 2 (identifier: P55197-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     81-126: RCELCPHKDG...VSTMEPIVLQ → AESRSVAQAK...GMQFLLVSLI
     127-1068: Missing.

Note: No experimental confirmation available.
Show »
Length:126
Mass (Da):13,851
Checksum:iB8E45EC6C2BA9FA8
GO
Isoform 3 (identifier: P55197-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     81-179: RCELCPHKDG...CAQFAGLLCE → MVCNSCWLAS...VIWRFKKERW
     180-1068: Missing.

Note: No experimental confirmation available.
Show »
Length:179
Mass (Da):20,047
Checksum:iE522FE1E4B1ED346
GO

Sequence cautioni

The sequence BC129946 differs from that shown. Reason: Frameshift at position 235. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei81 – 17999RCELC…GLLCE → MVCNSCWLASSENVTPGYIE HHCACASPHPRCLVSNVPPV SGALMHCFWACLTTAAFFGP QSFTTCHMSFLVSRDILFYI YGFMPFISVVIWRFKKERW in isoform 3. 1 PublicationVSP_044552Add
BLAST
Alternative sequencei81 – 12646RCELC…PIVLQ → AESRSVAQAKVQWCDLSPLQ PLLPGFKRFSCLSLPNGMQF LLVSLI in isoform 2. 1 PublicationVSP_043044Add
BLAST
Alternative sequencei127 – 1068942Missing in isoform 2. 1 PublicationVSP_043045Add
BLAST
Alternative sequencei180 – 1068889Missing in isoform 3. 1 PublicationVSP_044553Add
BLAST
Alternative sequencei566 – 5661N → NDRGDSSTLTKQELKFI in isoform 1. 1 PublicationVSP_047517
Alternative sequencei986 – 101126EQHQA…ELQQL → VHRHPHFTQLPPTHFSPSME IMQVRK in isoform 1. 1 PublicationVSP_047518Add
BLAST
Alternative sequencei1012 – 106857Missing in isoform 1. 1 PublicationVSP_047519Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13948 mRNA. Translation: AAA79972.1.
AY598745 mRNA. Translation: AAT47519.1.
AL161799
, AL358780, AL359697, AL357372 Genomic DNA. Translation: CAI39663.1.
AL358780
, AL161799, AL357372, AL359697 Genomic DNA. Translation: CAI13979.1.
AL358780 Genomic DNA. Translation: CAI13982.1.
AL358780 Genomic DNA. Translation: CAI13983.1.
AL359697
, AL357372, AL358780, AL161799 Genomic DNA. Translation: CAH73410.1.
AL357372
, AL359697, AL358780, AL161799 Genomic DNA. Translation: CAI41348.1.
BC080577 mRNA. Translation: AAH80577.1.
BC094844 mRNA. No translation available.
BC129946 mRNA. No translation available.
CCDSiCCDS55706.1. [P55197-2]
CCDS55707.1. [P55197-3]
CCDS55708.1. [P55197-4]
CCDS7135.1. [P55197-1]
PIRiI38759.
RefSeqiNP_001182555.1. NM_001195626.1. [P55197-4]
NP_001182556.1. NM_001195627.1. [P55197-2]
NP_001182557.1. NM_001195628.1. [P55197-3]
NP_001182559.1. NM_001195630.1. [P55197-3]
NP_004632.1. NM_004641.3. [P55197-1]
XP_005252665.1. XM_005252608.2. [P55197-4]
UniGeneiHs.30385.

Genome annotation databases

EnsembliENST00000307729; ENSP00000307411; ENSG00000078403. [P55197-4]
ENST00000377059; ENSP00000366258; ENSG00000078403. [P55197-4]
ENST00000377072; ENSP00000366272; ENSG00000078403. [P55197-1]
ENST00000377091; ENSP00000366295; ENSG00000078403. [P55197-2]
ENST00000377100; ENSP00000366304; ENSG00000078403. [P55197-3]
ENST00000621220; ENSP00000484335; ENSG00000078403. [P55197-2]
ENST00000631589; ENSP00000488569; ENSG00000078403. [P55197-4]
GeneIDi8028.
KEGGihsa:8028.
UCSCiuc001iqq.3. human. [P55197-4]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U13948 mRNA. Translation: AAA79972.1.
AY598745 mRNA. Translation: AAT47519.1.
AL161799
, AL358780, AL359697, AL357372 Genomic DNA. Translation: CAI39663.1.
AL358780
, AL161799, AL357372, AL359697 Genomic DNA. Translation: CAI13979.1.
AL358780 Genomic DNA. Translation: CAI13982.1.
AL358780 Genomic DNA. Translation: CAI13983.1.
AL359697
, AL357372, AL358780, AL161799 Genomic DNA. Translation: CAH73410.1.
AL357372
, AL359697, AL358780, AL161799 Genomic DNA. Translation: CAI41348.1.
BC080577 mRNA. Translation: AAH80577.1.
BC094844 mRNA. No translation available.
BC129946 mRNA. No translation available.
CCDSiCCDS55706.1. [P55197-2]
CCDS55707.1. [P55197-3]
CCDS55708.1. [P55197-4]
CCDS7135.1. [P55197-1]
PIRiI38759.
RefSeqiNP_001182555.1. NM_001195626.1. [P55197-4]
NP_001182556.1. NM_001195627.1. [P55197-2]
NP_001182557.1. NM_001195628.1. [P55197-3]
NP_001182559.1. NM_001195630.1. [P55197-3]
NP_004632.1. NM_004641.3. [P55197-1]
XP_005252665.1. XM_005252608.2. [P55197-4]
UniGeneiHs.30385.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5DAGX-ray1.60A1-208[»]
5DAHX-ray2.61A/B1-208[»]
ProteinModelPortaliP55197.
SMRiP55197. Positions 25-78, 127-197.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113723. 24 interactions.
DIPiDIP-37633N.
IntActiP55197. 14 interactions.
STRINGi9606.ENSP00000307411.

PTM databases

iPTMnetiP55197.
PhosphoSiteiP55197.

Polymorphism and mutation databases

BioMutaiMLLT10.
DMDMi527504034.

Proteomic databases

EPDiP55197.
PaxDbiP55197.
PRIDEiP55197.

Protocols and materials databases

DNASUi8028.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307729; ENSP00000307411; ENSG00000078403. [P55197-4]
ENST00000377059; ENSP00000366258; ENSG00000078403. [P55197-4]
ENST00000377072; ENSP00000366272; ENSG00000078403. [P55197-1]
ENST00000377091; ENSP00000366295; ENSG00000078403. [P55197-2]
ENST00000377100; ENSP00000366304; ENSG00000078403. [P55197-3]
ENST00000621220; ENSP00000484335; ENSG00000078403. [P55197-2]
ENST00000631589; ENSP00000488569; ENSG00000078403. [P55197-4]
GeneIDi8028.
KEGGihsa:8028.
UCSCiuc001iqq.3. human. [P55197-4]

Organism-specific databases

CTDi8028.
GeneCardsiMLLT10.
HGNCiHGNC:16063. MLLT10.
HPAiHPA005747.
MalaCardsiMLLT10.
MIMi602409. gene.
neXtProtiNX_P55197.
Orphaneti99861. Precursor T-cell acute lymphoblastic leukemia.
PharmGKBiPA30849.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0956. Eukaryota.
COG5141. LUCA.
GeneTreeiENSGT00740000114866.
HOGENOMiHOG000049087.
HOVERGENiHBG004186.
InParanoidiP55197.
OMAiKSPHLGN.
OrthoDBiEOG7K6PT9.
PhylomeDBiP55197.
TreeFamiTF316118.

Miscellaneous databases

ChiTaRSiMLLT10. human.
GeneWikiiMLLT10.
GenomeRNAii8028.
PROiP55197.
SOURCEiSearch...

Gene expression databases

BgeeiP55197.
CleanExiHS_MLLT10.
ExpressionAtlasiP55197. baseline and differential.
GenevisibleiP55197. HS.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR019786. Zinc_finger_PHD-type_CS.
IPR011011. Znf_FYVE_PHD.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
SMARTiSM00249. PHD. 2 hits.
[Graphical view]
SUPFAMiSSF57903. SSF57903. 1 hit.
PROSITEiPS01359. ZF_PHD_1. 1 hit.
PS50016. ZF_PHD_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel class of zinc finger/leucine zipper genes identified from the molecular cloning of the t(10;11) translocation in acute leukemia."
    Chaplin T., Ayton P., Bernard O.A., Saha V., Della Valle V., Hillion J., Gregorini A., Lillington D., Berger R., Young B.D.
    Blood 85:1435-1441(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "hDOT1L links histone methylation to leukemogenesis."
    Okada Y., Feng Q., Lin Y., Jiang Q., Li Y., Coffield V.M., Su L., Xu G., Zhang Y.
    Cell 121:167-178(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), INTERACTION WITH DOT1L.
  3. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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 2; 3 AND 4).
    Tissue: Ovary and Prostate.
  5. "Biochemical analyses of the AF10 protein: the extended LAP/PHD-finger mediates oligomerisation."
    Linder B., Newman R., Jones L.K., Debernardi S., Young B.D., Freemont P., Verrijzer C.P., Saha V.
    J. Mol. Biol. 299:369-378(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SELF-ASSOCIATION, SUBCELLULAR LOCATION, DNA-BINDING.
  6. "The synovial sarcoma associated protein SYT interacts with the acute leukemia associated protein AF10."
    de Bruijn D.R., dos Santos N.R., Thijssen J., Balemans M., Debernardi S., Linder B., Young B.D., Geurts van Kessel A.
    Oncogene 20:3281-3289(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SS18.
  7. "The MLL fusion partner AF10 binds GAS41, a protein that interacts with the human SWI/SNF complex."
    Debernardi S., Bassini A., Jones L.K., Chaplin T., Linder B., de Bruijn D.R.H., Meese E., Young B.D.
    Blood 99:275-281(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH YEATS4.
  8. "The AF10 leucine zipper is required for leukemic transformation of myeloid progenitors by MLL-AF10."
    DiMartino J.F., Ayton P.M., Chen E.H., Naftzger C.C., Young B.D., Cleary M.L.
    Blood 99:3780-3785(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TRANSACTIVATION DOMAIN.
  9. "AF10-dependent transcription is enhanced by its interaction with FLRG."
    Forissier S., Razanajaona D., Ay A.S., Martel S., Bartholin L., Rimokh R.
    Biol. Cell 99:563-571(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SELF-ASSOCIATION, INTERACTION WITH FSTL3.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684 AND SER-686, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "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].
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAF10_HUMAN
AccessioniPrimary (citable) accession number: P55197
Secondary accession number(s): B1ANA8
, Q5JT37, Q5VX90, Q66K63
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 24, 2013
Last modified: June 8, 2016
This is version 143 of the entry and version 2 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 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.