Reviewed, UniProtKB/Swiss-Prot Q03164 (HRX_HUMAN)

Names and origin

Protein names

Recommended name:
    Histone-lysine N-methyltransferase HRX
    EC=2.1.1.43
Alternative name(s):
    Zinc finger protein HRX
    ALL-1
    Trithorax-like protein
    Lysine N-methyltransferase 2A
    CXXC-type zinc finger protein 7

Gene names

Name:	MLL
Synonyms:	ALL1, CXXC7, HRX, HTRX, KMT2A, TRX1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	3969 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Histone methyltransferase. Methylates 'Lys-4' of histone H3. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. Promotes PPP1R15A-induced apoptosis. Ref.14 Ref.29
Catalytic activity	S-adenosyl-L-methionine + histone L-lysine = S-adenosyl-L-homocysteine + histone N(6)-methyl-L-lysine. Ref.29
Subunit structure	Interacts with SBF1 and PPP1R15A. Component of the MLL complex, at least composed of MLL, ASH2L, RBBP5, DPY30, WDR5, MEN1, HCFC1 and HCFC2. Ref.14 Ref.13
Subcellular location	Nucleus.
Tissue specificity	Heart, lung, brain and T- and B-lymphocytes.
Involvement in disease	Chromosomal aberrations involving MLL are a cause of acute leukemias. Translocation t(1;11)(q21;q23) with MLLT11/AF1Q; translocation t(3;11)(p21;q23) with NCKIPSD/AF3p21; translocation t(3,11)(q25,q23) with GMPS; translocation t(4;11)(q21;q23) with AFF1/MLLT2/AF4; insertion ins(5;11)(q31;q13q23) with AFF4/AF5Q31; translocation t(5;11)(q12;q23) with AF5-alpha/CENPK; translocation t(6;11)(q27;q23) with MLLT4/AF6; translocation t(9;11)(p22;q23) with MLLT3/AF9; translocation t(10;11)(p11.2;q23) with ABI1; translocation t(10;11)(p12;q23) with MLLT10/AF10; t(11;15)(q23;q14) with CASC5 and ZFYVE19; translocation t(11;17)(q23;q21) with MLLT6/AF17; translocation t(11;19)(q23;p13.3) with ELL; translocation t(11;19)(q23;p13.3) with MLLT1/ENL; translocation t(11;19)(q23;p23) with GAS7; translocation t(X;11)(q13;q23) with FOXO4/AFX1. Translocation t(3;11)(q28;q23) with LPP. Translocation t(10;11)(q22;q23) with TET1. Translocation t(9;11)(q34;q23) with DAB2IP. Translocation t(4;11)(p12;q23) with FRYL. Fusion proteins MLL-MLLT1, MLL-MLLT3 and MLL-ELL interact with PPP1R15A and, on the contrary to unfused MLL, inhibit PPP1R15A-induced apoptosis. Ref.14 A chromosomal aberration involving MLL may be a cause of chronic neutrophilic leukemia. Translocation t(4;11)(q21;q23) with SEPT11. Ref.14
Sequence similarities	Belongs to the histone-lysine methyltransferase family. TRX/MLL subfamily. Contains 3 A.T hook DNA-binding domains. Contains 1 bromo domain. Contains 1 CXXC-type zinc finger. Contains 3 PHD-type zinc fingers. Contains 1 post-SET domain. Contains 1 SET domain.
Sequence caution	The sequence AAG26332.2 differs from that shown. Reason: Miscellaneous discrepancy. Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
Biological process	Apoptosis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Proto-oncogene
Domain	Bromodomain Repeat Zinc-finger
Ligand	DNA-binding Metal-binding S-adenosyl-L-methionine Zinc
Molecular function	Chromatin regulator Methyltransferase Transferase
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	apoptosis Inferred from electronic annotation. Source: UniProtKB-KW chromatin modification Inferred from electronic annotation. Source: UniProtKB-KW embryonic hemopoiesis Traceable author statement. Source: UniProtKB protein complex assembly Ref.24 Inferred from direct assay. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro transcription from RNA polymerase II promoter Traceable author statement. Source: ProtInc
Cellular component	histone methyltransferase complex Inferred from electronic annotation. Source: InterPro
Molecular function	RNA polymerase II transcription factor activity Traceable author statement. Source: ProtInc histone methyltransferase activity (H3-K4 specific) Inferred from electronic annotation. Source: InterPro protein homodimerization activity Inferred from direct assay. Source: UniProtKB transcription factor activity Non-traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		4	EBI-591370,EBI-591370
cyp33	Q9V3G3	1	EBI-591370,EBI-128445	From a different organism.
PPIE	Q9UNP9	1	EBI-591370,EBI-591818

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q03164-1)

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.

Isoform 14P-18B (identifier: Q03164-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1407-1444: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 3969

3969

Histone-lysine N-methyltransferase HRX

PRO_0000124876

Regions

Domain

1703 – 1748

46

Bromo; divergent

Domain

3828 – 3949

122

SET

Domain

3953 – 3969

17

Post-SET

DNA binding

169 – 180

12

A.T hook 1

DNA binding

217 – 227

11

A.T hook 2

DNA binding

301 – 309

9

A.T hook 3

Zinc finger

1147 – 1195

49

CXXC-type

Zinc finger

1431 – 1482

52

PHD-type 1

Zinc finger

1479 – 1533

55

PHD-type 2

Zinc finger

1566 – 1627

62

PHD-type 3

Compositional bias

17 – 102

86

Ala/Gly/Ser-rich

Compositional bias

137 – 143

7

Poly-Gly

Compositional bias

561 – 564

4

Poly-Pro

Compositional bias

568 – 571

4

Poly-Pro

Sites

Site

1334 – 1335

2

Breakpoint for translocation to form MLL-ZFYVE19 oncogene

Site

1362 – 1363

2

Breakpoint for translocation to form MLL-AF3P21 and MLL-CASC5 oncogenes

Site

1362 – 1363

2

Breakpoint for translocation to form MLL-CENPK oncogene

Site

1362

1

Breakpoint for translocation to form MLL-FRYL fusion protein

Site

1406 – 1407

2

Breakpoint for translocation to form MLL-AFF4 fusion protein

Site

1444 – 1445

2

Breakpoint for translocation to form MLL-GAS7 oncogene

Site

1444 – 1445

2

Breakpoint for translocation to form MLL-LPP

Amino acid modifications

Modified residue

136

1

Phosphoserine Ref.36

Modified residue

153

1

Phosphoserine Ref.36

Modified residue

197

1

Phosphoserine Ref.36

Modified residue

202

1

Phosphoserine Ref.36

Modified residue

279

1

Phosphoserine Ref.32

Modified residue

337

1

Phosphothreonine Ref.28 Ref.34

Modified residue

506

1

Phosphothreonine Ref.36

Modified residue

518

1

Phosphoserine Ref.36 Ref.35

Modified residue

636

1

N6-acetyllysine Ref.37

Modified residue

680

1

Phosphoserine Ref.36

Modified residue

831

1

Phosphoserine Ref.36

Modified residue

840

1

Phosphothreonine Ref.36

Modified residue

926

1

Phosphoserine Ref.34

Modified residue

1056

1

Phosphoserine Ref.36

Modified residue

1130

1

N6-acetyllysine Ref.37

Modified residue

1235

1

N6-acetyllysine Ref.37

Modified residue

1241

1

Phosphoserine Ref.34

Modified residue

1837

1

Phosphoserine Ref.35 Ref.30

Modified residue

1839

1

Phosphothreonine Ref.36

Modified residue

1845

1

Phosphothreonine Ref.36 Ref.35

Modified residue

2098

1

Phosphoserine Ref.36

Modified residue

2147

1

Phosphothreonine Ref.36

Modified residue

2151

1

Phosphoserine Ref.36 Ref.26

Modified residue

2153

1

Phosphothreonine Ref.34

Modified residue

2525

1

Phosphothreonine Ref.36

Modified residue

2691

1

Phosphoserine Ref.34

Modified residue

2729

1

Phosphoserine Ref.34

Modified residue

2866

1

Phosphoserine Ref.26

Modified residue

2940

1

Phosphothreonine Ref.26

Modified residue

2955

1

Phosphoserine Ref.36 Ref.34

Modified residue

3036

1

Phosphoserine Ref.36 Ref.26

Modified residue

3372

1

Phosphothreonine Ref.36

Modified residue

3511

1

Phosphoserine Ref.36 Ref.26

Modified residue

3518

1

Phosphoserine Ref.36

Cross-link

216

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.33

Cross-link

220

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.33

Cross-link

221

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.33

Natural variations

Alternative sequence

1407 – 1444

38

Missing in isoform 14P-18B.

VSP_006666

Natural variant

30

1

A → G: dbSNP rs9332745. Ref.2

VAR_021317

Natural variant

53

1

A → V: dbSNP rs9332747. Ref.3

VAR_021318

Natural variant

502

1

E → K: dbSNP rs9332772. Ref.3

VAR_021319

Natural variant

1975

1

Q → P: dbSNP rs693598.

VAR_052652

Natural variant

2319

1

S → T: dbSNP rs9332837. Ref.3

VAR_021320

Natural variant

2354

1

P → R: dbSNP rs9332838. Ref.3

VAR_021321

Natural variant

2387

1

Q → R: dbSNP rs9332839. Ref.3

VAR_021322

Natural variant

3714

1

V → I: dbSNP rs9332859. Ref.3

VAR_021323

Natural variant

3773

1

S → A: dbSNP rs9332861. Ref.3

VAR_021324

Experimental info

Sequence conflict

144

1

E → ELTTQIPCSWRTKGHIHDKK TEPFRLLAWSWCLN Ref.2

Sequence conflict

317 – 379

63

GLLIN…LLQRA → VSSLILNWKSPRKSGKTRKE HLHLQKKIRQLSDKALEGLS QLGLFLLQKGQMQPLLSNSY RGQ Ref.1

Sequence conflict

556

1

Q → E Ref.2

Sequence conflict

556

1

Q → E Ref.5

Sequence conflict

1487

1

R → G Ref.7

Sequence conflict

1603

1

S → SGTE Ref.2

Sequence conflict

1603

1

S → SGTE Ref.5

Sequence conflict

1603

1

S → SGTE Ref.9

Sequence conflict

1616

1

S → C Ref.8

Sequence conflict

1937

1

Q → H Ref.6

Sequence conflict

2181

1

P → S Ref.6

Sequence conflict

3556

1

K → N Ref.5

Sequence conflict

3718

1

R → G Ref.2

Sequence conflict

3759

1

N → D Ref.2

Sequence conflict

3813

1

D → G Ref.2

Sequence conflict

3901

1

A → R Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

3969

Helix Strand Turn

Details...

Beta strand

1151 – 1154

4

Beta strand

1156 – 1158

3

Turn

1159 – 1162

4

Beta strand

1168 – 1170

3

Helix

1171 – 1174

4

Helix

1177 – 1179

3

Beta strand

1183 – 1185

3

Turn

1190 – 1192

3

Beta strand

1197 – 1200

4

Turn

1204 – 1206

3

Helix

2847 – 2856

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2007. Version 5. Checksum: 1150F37EAB1430D3	FASTA	3,969	431,764
	10 20 30 40 50 60 MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPPVGGGG PGAPPSPPAV 70 80 90 100 110 120 AAAAAAAGSS GAGVPGGAAA ASAASSSSAS SSSSSSSSAS SGPALLRVGP GFDAALQVSA 130 140 150 160 170 180 AIGTNLRRFR AVFGESGGGG GSGEDEQFLG FGSDEEVRVR SPTRSPSVKT SPRKPRGRPR 190 200 210 220 230 240 SGSDRNSAIL SDPSVFSPLN KSETKSGDKI KKKDSKSIEK KRGRPPTFPG VKIKITHGKD 250 260 270 280 290 300 ISELPKGNKE DSLKKIKRTP SATFQQATKI KKLRAGKLSP LKSKFKTGKL QIGRKGVQIV 310 320 330 340 350 360 RRRGRPPSTE RIKTPSGLLI NSELEKPQKV RKDKEGTPPL TKEDKTVVRQ SPRRIKPVRI 370 380 390 400 410 420 IPSSKRTDAT IAKQLLQRAK KGAQKKIEKE AAQLQGRKVK TQVKNIRQFI MPVVSAISSR 430 440 450 460 470 480 IIKTPRRFIE DEDYDPPIKI ARLESTPNSR FSAPSCGSSE KSSAASQHSS QMSSDSSRSS 490 500 510 520 530 540 SPSVDTSTDS QASEEIQVLP EERSDTPEVH PPLPISQSPE NESNDRRSRR YSVSERSFGS 550 560 570 580 590 600 RTTKKLSTLQ SAPQQQTSSS PPPPLLTPPP PLQPASSISD HTPWLMPPTI PLASPFLPAS 610 620 630 640 650 660 TAPMQGKRKS ILREPTFRWT SLKHSRSEPQ YFSSAKYAKE GLIRKPIFDN FRPPPLTPED 670 680 690 700 710 720 VGFASGFSAS GTAASARLFS PLHSGTRFDM HKRSPLLRAP RFTPSEAHSR IFESVTLPSN 730 740 750 760 770 780 RTSAGTSSSG VSNRKRKRKV FSPIRSEPRS PSHSMRTRSG RLSSSELSPL TPPSSVSSSL 790 800 810 820 830 840 SISVSPLATS ALNPTFTFPS HSLTQSGESA EKNQRPRKQT SAPAEPFSSS SPTPLFPWFT 850 860 870 880 890 900 PGSQTERGRN KDKAPEELSK DRDADKSVEK DKSRERDRER EKENKRESRK EKRKKGSEIQ 910 920 930 940 950 960 SSSALYPVGR VSKEKVVGED VATSSSAKKA TGRKKSSSHD SGTDITSVTL GDTTAVKTKI 970 980 990 1000 1010 1020 LIKKGRGNLE KTNLDLGPTA PSLEKEKTLC LSTPSSSTVK HSTSSIGSML AQADKLPMTD 1030 1040 1050 1060 1070 1080 KRVASLLKKA KAQLCKIEKS KSLKQTDQPK AQGQESDSSE TSVRGPRIKH VCRRAAVALG 1090 1100 1110 1120 1130 1140 RKRAVFPDDM PTLSALPWEE REKILSSMGN DDKSSIAGSE DAEPLAPPIK PIKPVTRNKA 1150 1160 1170 1180 1190 1200 PQEPPVKKGR RSRRCGQCPG CQVPEDCGVC TNCLDKPKFG GRNIKKQCCK MRKCQNLQWM 1210 1220 1230 1240 1250 1260 PSKAYLQKQA KAVKKKEKKS KTSEKKDSKE SSVVKNVVDS SQKPTPSARE DPAPKKSSSE 1270 1280 1290 1300 1310 1320 PPPRKPVEEK SEEGNVSAPG PESKQATTPA SRKSSKQVSQ PALVIPPQPP TTGPPRKEVP 1330 1340 1350 1360 1370 1380 KTTPSEPKKK QPPPPESGPE QSKQKKVAPR PSIPVKQKPK EKEKPPPVNK QENAGTLNIL 1390 1400 1410 1420 1430 1440 STLSNGNSSK QKIPADGVHR IRVDFKEDCE AENVWEMGGL GILTSVPITP RVVCFLCASS 1450 1460 1470 1480 1490 1500 GHVEFVYCQV CCEPFHKFCL EENERPLEDQ LENWCCRRCK FCHVCGRQHQ ATKQLLECNK 1510 1520 1530 1540 1550 1560 CRNSYHPECL GPNYPTKPTK KKKVWICTKC VRCKSCGSTT PGKGWDAQWS HDFSLCHDCA 1570 1580 1590 1600 1610 1620 KLFAKGNFCP LCDKCYDDDD YESKMMQCGK CDRWVHSKCE NLSDEMYEIL SNLPESVAYT 1630 1640 1650 1660 1670 1680 CVNCTERHPA EWRLALEKEL QISLKQVLTA LLNSRTTSHL LRYRQAAKPP DLNPETEESI 1690 1700 1710 1720 1730 1740 PSRSSPEGPD PPVLTEVSKQ DDQQPLDLEG VKRKMDQGNY TSVLEFSDDI VKIIQAAINS 1750 1760 1770 1780 1790 1800 DGGQPEIKKA NSMVKSFFIR QMERVFPWFS VKKSRFWEPN KVSSNSGMLP NAVLPPSLDH 1810 1820 1830 1840 1850 1860 NYAQWQEREE NSHTEQPPLM KKIIPAPKPK GPGEPDSPTP LHPPTPPILS TDRSREDSPE 1870 1880 1890 1900 1910 1920 LNPPPGIEDN RQCALCLTYG DDSANDAGRL LYIGQNEWTH VNCALWSAEV FEDDDGSLKN 1930 1940 1950 1960 1970 1980 VHMAVIRGKQ LRCEFCQKPG ATVGCCLTSC TSNYHFMCSR AKNCVFLDDK KVYCQRHRDL 1990 2000 2010 2020 2030 2040 IKGEVVPENG FEVFRRVFVD FEGISLRRKF LNGLEPENIH MMIGSMTIDC LGILNDLSDC 2050 2060 2070 2080 2090 2100 EDKLFPIGYQ CSRVYWSTTD ARKRCVYTCK IVECRPPVVE PDINSTVEHD ENRTIAHSPT 2110 2120 2130 2140 2150 2160 SFTESSSKES QNTAEIISPP SPDRPPHSQT SGSCYYHVIS KVPRIRTPSY SPTQRSPGCR 2170 2180 2190 2200 2210 2220 PLPSAGSPTP TTHEIVTVGD PLLSSGLRSI GSRRHSTSSL SPQRSKLRIM SPMRTGNTYS 2230 2240 2250 2260 2270 2280 RNNVSSVSTT GTATDLESSA KVVDHVLGPL NSSTSLGQNT STSSNLQRTV VTVGNKNSHL 2290 2300 2310 2320 2330 2340 DGSSSSEMKQ SSASDLVSKS SSLKGEKTKV LSSKSSEGSA HNVAYPGIPK LAPQVHNTTS 2350 2360 2370 2380 2390 2400 RELNVSKIGS FAEPSSVSFS SKEALSFPHL HLRGQRNDRD QHTDSTQSAN SSPDEDTEVK 2410 2420 2430 2440 2450 2460 TLKLSGMSNR SSIINEHMGS SSRDRRQKGK KSCKETFKEK HSSKSFLEPG QVTTGEEGNL 2470 2480 2490 2500 2510 2520 KPEFMDEVLT PEYMGQRPCN NVSSDKIGDK GLSMPGVPKA PPMQVEGSAK ELQAPRKRTV 2530 2540 2550 2560 2570 2580 KVTLTPLKME NESQSKNALK ESSPASPLQI ESTSPTEPIS ASENPGDGPV AQPSPNNTSC 2590 2600 2610 2620 2630 2640 QDSQSNNYQN LPVQDRNLML PDGPKPQEDG SFKRRYPRRS ARARSNMFFG LTPLYGVRSY 2650 2660 2670 2680 2690 2700 GEEDIPFYSS STGKKRGKRS AEGQVDGADD LSTSDEDDLY YYNFTRTVIS SGGEERLASH 2710 2720 2730 2740 2750 2760 NLFREEEQCD LPKISQLDGV DDGTESDTSV TATTRKSSQI PKRNGKENGT ENLKIDRPED 2770 2780 2790 2800 2810 2820 AGEKEHVTKS SVGHKNEPKM DNCHSVSRVK TQGQDSLEAQ LSSLESSRRV HTSTPSDKNL 2830 2840 2850 2860 2870 2880 LDTYNTELLK SDSDNNNSDD CGNILPSDIM DFVLKNTPSM QALGESPESS SSELLNLGEG 2890 2900 2910 2920 2930 2940 LGLDSNREKD MGLFEVFSQQ LPTTEPVDSS VSSSISAEEQ FELPLELPSD LSVLTTRSPT 2950 2960 2970 2980 2990 3000 VPSQNPSRLA VISDSGEKRV TITEKSVASS ESDPALLSPG VDPTPEGHMT PDHFIQGHMD 3010 3020 3030 3040 3050 3060 ADHISSPPCG SVEQGHGNNQ DLTRNSSTPG LQVPVSPTVP IQNQKYVPNS TDSPGPSQIS 3070 3080 3090 3100 3110 3120 NAAVQTTPPH LKPATEKLIV VNQNMQPLYV LQTLPNGVTQ KIQLTSSVSS TPSVMETNTS 3130 3140 3150 3160 3170 3180 VLGPMGGGLT LTTGLNPSLP TSQSLFPSAS KGLLPMSHHQ HLHSFPAATQ SSFPPNISNP 3190 3200 3210 3220 3230 3240 PSGLLIGVQP PPDPQLLVSE SSQRTDLSTT VATPSSGLKK RPISRLQTRK NKKLAPSSTP 3250 3260 3270 3280 3290 3300 SNIAPSDVVS NMTLINFTPS QLPNHPSLLD LGSLNTSSHR TVPNIIKRSK SSIMYFEPAP 3310 3320 3330 3340 3350 3360 LLPQSVGGTA ATAAGTSTIS QDTSHLTSGS VSGLASSSSV LNVVSMQTTT TPTSSASVPG 3370 3380 3390 3400 3410 3420 HVTLTNPRLL GTPDIGSISN LLIKASQQSL GIQDQPVALP PSSGMFPQLG TSQTPSTAAI 3430 3440 3450 3460 3470 3480 TAASSICVLP STQTTGITAA SPSGEADEHY QLQHVNQLLA SKTGIHSSQR DLDSASGPQV 3490 3500 3510 3520 3530 3540 SNFTQTVDAP NSMGLEQNKA LSSAVQASPT SPGGSPSSPS SGQRSASPSV PGPTKPKPKT 3550 3560 3570 3580 3590 3600 KRFQLPLDKG NGKKHKVSHL RTSSSEAHIP DQETTSLTSG TGTPGAEAEQ QDTASVEQSS 3610 3620 3630 3640 3650 3660 QKECGQPAGQ VAVLPEVQVT QNPANEQESA EPKTVEEEES NFSSPLMLWL QQEQKRKESI 3670 3680 3690 3700 3710 3720 TEKKPKKGLV FEISSDDGFQ ICAESIEDAW KSLTDKVQEA RSNARLKQLS FAGVNGLRML 3730 3740 3750 3760 3770 3780 GILHDAVVFL IEQLSGAKHC RNYKFRFHKP EEANEPPLNP HGSARAEVHL RKSAFDMFNF 3790 3800 3810 3820 3830 3840 LASKHRQPPE YNPNDEEEEE VQLKSARRAT SMDLPMPMRF RHLKKTSKEA VGVYRSPIHG 3850 3860 3870 3880 3890 3900 RGLFCKRNID AGEMVIEYAG NVIRSIQTDK REKYYDSKGI GCYMFRIDDS EVVDATMHGN 3910 3920 3930 3940 3950 3960 AARFINHSCE PNCYSRVINI DGQKHIVIFA MRKIYRGEEL TYDYKFPIED ASNKLPCNCG AKKCRKFLN
	Isoform 14P-18B. Checksum: B8E736C88E83D50B	FASTA	3,931	427,733
	10 20 30 40 50 60 MAHSCRWRFP ARPGTTGGGG GGGRRGLGGA PRQRVPALLL PPGPPVGGGG PGAPPSPPAV 70 80 90 100 110 120 AAAAAAAGSS GAGVPGGAAA ASAASSSSAS SSSSSSSSAS SGPALLRVGP GFDAALQVSA 130 140 150 160 170 180 AIGTNLRRFR AVFGESGGGG GSGEDEQFLG FGSDEEVRVR SPTRSPSVKT SPRKPRGRPR 190 200 210 220 230 240 SGSDRNSAIL SDPSVFSPLN KSETKSGDKI KKKDSKSIEK KRGRPPTFPG VKIKITHGKD 250 260 270 280 290 300 ISELPKGNKE DSLKKIKRTP SATFQQATKI KKLRAGKLSP LKSKFKTGKL QIGRKGVQIV 310 320 330 340 350 360 RRRGRPPSTE RIKTPSGLLI NSELEKPQKV RKDKEGTPPL TKEDKTVVRQ SPRRIKPVRI 370 380 390 400 410 420 IPSSKRTDAT IAKQLLQRAK KGAQKKIEKE AAQLQGRKVK TQVKNIRQFI MPVVSAISSR 430 440 450 460 470 480 IIKTPRRFIE DEDYDPPIKI ARLESTPNSR FSAPSCGSSE KSSAASQHSS QMSSDSSRSS 490 500 510 520 530 540 SPSVDTSTDS QASEEIQVLP EERSDTPEVH PPLPISQSPE NESNDRRSRR YSVSERSFGS 550 560 570 580 590 600 RTTKKLSTLQ SAPQQQTSSS PPPPLLTPPP PLQPASSISD HTPWLMPPTI PLASPFLPAS 610 620 630 640 650 660 TAPMQGKRKS ILREPTFRWT SLKHSRSEPQ YFSSAKYAKE GLIRKPIFDN FRPPPLTPED 670 680 690 700 710 720 VGFASGFSAS GTAASARLFS PLHSGTRFDM HKRSPLLRAP RFTPSEAHSR IFESVTLPSN 730 740 750 760 770 780 RTSAGTSSSG VSNRKRKRKV FSPIRSEPRS PSHSMRTRSG RLSSSELSPL TPPSSVSSSL 790 800 810 820 830 840 SISVSPLATS ALNPTFTFPS HSLTQSGESA EKNQRPRKQT SAPAEPFSSS SPTPLFPWFT 850 860 870 880 890 900 PGSQTERGRN KDKAPEELSK DRDADKSVEK DKSRERDRER EKENKRESRK EKRKKGSEIQ 910 920 930 940 950 960 SSSALYPVGR VSKEKVVGED VATSSSAKKA TGRKKSSSHD SGTDITSVTL GDTTAVKTKI 970 980 990 1000 1010 1020 LIKKGRGNLE KTNLDLGPTA PSLEKEKTLC LSTPSSSTVK HSTSSIGSML AQADKLPMTD 1030 1040 1050 1060 1070 1080 KRVASLLKKA KAQLCKIEKS KSLKQTDQPK AQGQESDSSE TSVRGPRIKH VCRRAAVALG 1090 1100 1110 1120 1130 1140 RKRAVFPDDM PTLSALPWEE REKILSSMGN DDKSSIAGSE DAEPLAPPIK PIKPVTRNKA 1150 1160 1170 1180 1190 1200 PQEPPVKKGR RSRRCGQCPG CQVPEDCGVC TNCLDKPKFG GRNIKKQCCK MRKCQNLQWM 1210 1220 1230 1240 1250 1260 PSKAYLQKQA KAVKKKEKKS KTSEKKDSKE SSVVKNVVDS SQKPTPSARE DPAPKKSSSE 1270 1280 1290 1300 1310 1320 PPPRKPVEEK SEEGNVSAPG PESKQATTPA SRKSSKQVSQ PALVIPPQPP TTGPPRKEVP 1330 1340 1350 1360 1370 1380 KTTPSEPKKK QPPPPESGPE QSKQKKVAPR PSIPVKQKPK EKEKPPPVNK QENAGTLNIL 1390 1400 1410 1420 1430 1440 STLSNGNSSK QKIPADGVHR IRVDFKFVYC QVCCEPFHKF CLEENERPLE DQLENWCCRR 1450 1460 1470 1480 1490 1500 CKFCHVCGRQ HQATKQLLEC NKCRNSYHPE CLGPNYPTKP TKKKKVWICT KCVRCKSCGS 1510 1520 1530 1540 1550 1560 TTPGKGWDAQ WSHDFSLCHD CAKLFAKGNF CPLCDKCYDD DDYESKMMQC GKCDRWVHSK 1570 1580 1590 1600 1610 1620 CENLSDEMYE ILSNLPESVA YTCVNCTERH PAEWRLALEK ELQISLKQVL TALLNSRTTS 1630 1640 1650 1660 1670 1680 HLLRYRQAAK PPDLNPETEE SIPSRSSPEG PDPPVLTEVS KQDDQQPLDL EGVKRKMDQG 1690 1700 1710 1720 1730 1740 NYTSVLEFSD DIVKIIQAAI NSDGGQPEIK KANSMVKSFF IRQMERVFPW FSVKKSRFWE 1750 1760 1770 1780 1790 1800 PNKVSSNSGM LPNAVLPPSL DHNYAQWQER EENSHTEQPP LMKKIIPAPK PKGPGEPDSP 1810 1820 1830 1840 1850 1860 TPLHPPTPPI LSTDRSREDS PELNPPPGIE DNRQCALCLT YGDDSANDAG RLLYIGQNEW 1870 1880 1890 1900 1910 1920 THVNCALWSA EVFEDDDGSL KNVHMAVIRG KQLRCEFCQK PGATVGCCLT SCTSNYHFMC 1930 1940 1950 1960 1970 1980 SRAKNCVFLD DKKVYCQRHR DLIKGEVVPE NGFEVFRRVF VDFEGISLRR KFLNGLEPEN 1990 2000 2010 2020 2030 2040 IHMMIGSMTI DCLGILNDLS DCEDKLFPIG YQCSRVYWST TDARKRCVYT CKIVECRPPV 2050 2060 2070 2080 2090 2100 VEPDINSTVE HDENRTIAHS PTSFTESSSK ESQNTAEIIS PPSPDRPPHS QTSGSCYYHV 2110 2120 2130 2140 2150 2160 ISKVPRIRTP SYSPTQRSPG CRPLPSAGSP TPTTHEIVTV GDPLLSSGLR SIGSRRHSTS 2170 2180 2190 2200 2210 2220 SLSPQRSKLR IMSPMRTGNT YSRNNVSSVS TTGTATDLES SAKVVDHVLG PLNSSTSLGQ 2230 2240 2250 2260 2270 2280 NTSTSSNLQR TVVTVGNKNS HLDGSSSSEM KQSSASDLVS KSSSLKGEKT KVLSSKSSEG 2290 2300 2310 2320 2330 2340 SAHNVAYPGI PKLAPQVHNT TSRELNVSKI GSFAEPSSVS FSSKEALSFP HLHLRGQRND 2350 2360 2370 2380 2390 2400 RDQHTDSTQS ANSSPDEDTE VKTLKLSGMS NRSSIINEHM GSSSRDRRQK GKKSCKETFK 2410 2420 2430 2440 2450 2460 EKHSSKSFLE PGQVTTGEEG NLKPEFMDEV LTPEYMGQRP CNNVSSDKIG DKGLSMPGVP 2470 2480 2490 2500 2510 2520 KAPPMQVEGS AKELQAPRKR TVKVTLTPLK MENESQSKNA LKESSPASPL QIESTSPTEP 2530 2540 2550 2560 2570 2580 ISASENPGDG PVAQPSPNNT SCQDSQSNNY QNLPVQDRNL MLPDGPKPQE DGSFKRRYPR 2590 2600 2610 2620 2630 2640 RSARARSNMF FGLTPLYGVR SYGEEDIPFY SSSTGKKRGK RSAEGQVDGA DDLSTSDEDD 2650 2660 2670 2680 2690 2700 LYYYNFTRTV ISSGGEERLA SHNLFREEEQ CDLPKISQLD GVDDGTESDT SVTATTRKSS 2710 2720 2730 2740 2750 2760 QIPKRNGKEN GTENLKIDRP EDAGEKEHVT KSSVGHKNEP KMDNCHSVSR VKTQGQDSLE 2770 2780 2790 2800 2810 2820 AQLSSLESSR RVHTSTPSDK NLLDTYNTEL LKSDSDNNNS DDCGNILPSD IMDFVLKNTP 2830 2840 2850 2860 2870 2880 SMQALGESPE SSSSELLNLG EGLGLDSNRE KDMGLFEVFS QQLPTTEPVD SSVSSSISAE 2890 2900 2910 2920 2930 2940 EQFELPLELP SDLSVLTTRS PTVPSQNPSR LAVISDSGEK RVTITEKSVA SSESDPALLS 2950 2960 2970 2980 2990 3000 PGVDPTPEGH MTPDHFIQGH MDADHISSPP CGSVEQGHGN NQDLTRNSST PGLQVPVSPT 3010 3020 3030 3040 3050 3060 VPIQNQKYVP NSTDSPGPSQ ISNAAVQTTP PHLKPATEKL IVVNQNMQPL YVLQTLPNGV 3070 3080 3090 3100 3110 3120 TQKIQLTSSV SSTPSVMETN TSVLGPMGGG LTLTTGLNPS LPTSQSLFPS ASKGLLPMSH 3130 3140 3150 3160 3170 3180 HQHLHSFPAA TQSSFPPNIS NPPSGLLIGV QPPPDPQLLV SESSQRTDLS TTVATPSSGL 3190 3200 3210 3220 3230 3240 KKRPISRLQT RKNKKLAPSS TPSNIAPSDV VSNMTLINFT PSQLPNHPSL LDLGSLNTSS 3250 3260 3270 3280 3290 3300 HRTVPNIIKR SKSSIMYFEP APLLPQSVGG TAATAAGTST ISQDTSHLTS GSVSGLASSS 3310 3320 3330 3340 3350 3360 SVLNVVSMQT TTTPTSSASV PGHVTLTNPR LLGTPDIGSI SNLLIKASQQ SLGIQDQPVA 3370 3380 3390 3400 3410 3420 LPPSSGMFPQ LGTSQTPSTA AITAASSICV LPSTQTTGIT AASPSGEADE HYQLQHVNQL 3430 3440 3450 3460 3470 3480 LASKTGIHSS QRDLDSASGP QVSNFTQTVD APNSMGLEQN KALSSAVQAS PTSPGGSPSS 3490 3500 3510 3520 3530 3540 PSSGQRSASP SVPGPTKPKP KTKRFQLPLD KGNGKKHKVS HLRTSSSEAH IPDQETTSLT 3550 3560 3570 3580 3590 3600 SGTGTPGAEA EQQDTASVEQ SSQKECGQPA GQVAVLPEVQ VTQNPANEQE SAEPKTVEEE 3610 3620 3630 3640 3650 3660 ESNFSSPLML WLQQEQKRKE SITEKKPKKG LVFEISSDDG FQICAESIED AWKSLTDKVQ 3670 3680 3690 3700 3710 3720 EARSNARLKQ LSFAGVNGLR MLGILHDAVV FLIEQLSGAK HCRNYKFRFH KPEEANEPPL 3730 3740 3750 3760 3770 3780 NPHGSARAEV HLRKSAFDMF NFLASKHRQP PEYNPNDEEE EEVQLKSARR ATSMDLPMPM 3790 3800 3810 3820 3830 3840 RFRHLKKTSK EAVGVYRSPI HGRGLFCKRN IDAGEMVIEY AGNVIRSIQT DKREKYYDSK 3850 3860 3870 3880 3890 3900 GIGCYMFRID DSEVVDATMH GNAARFINHS CEPNCYSRVI NIDGQKHIVI FAMRKIYRGE 3910 3920 3930 ELTYDYKFPI EDASNKLPCN CGAKKCRKFL N

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukemias." Tkachuk D.C., Kohler S., Cleary M.L. Cell 71:691-700(1992) [PubMed: 1423624] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Exon/intron structure of the human ALL-1 (MLL) gene involved in translocations to chromosomal region 11q23 and acute leukaemias." Nilson I., Loechner K., Siegler G., Greil J., Beck J.D., Fey G.H., Marschalek R. Br. J. Haematol. 93:966-972(1996) [PubMed: 8703835] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-30.
[3]	NIEHS SNPs program Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-53; LYS-502; THR-2319; ARG-2354; ARG-2387; ILE-3714 AND ALA-3773.
[4]	"Two distinct portions of LTG19/ENL at 19p13 are involved in t(11;19) leukemia." Yamamoto K., Seto M., Komatsu H., Iida S., Akao Y., Kojima S., Kodera Y., Nakazawa S., Ariyoshi Y., Takahashi T., Ueda R. Oncogene 8:2617-2625(1993) [PubMed: 8378076] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1909.
[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: 1423625] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 63-3969, CHROMOSOMAL TRANSLOCATION WITH AFF1/MLLT2.
[6]	"A trithorax-like gene is interrupted by chromosome 11q23 translocations in acute leukaemias." Djabali M., Selleri L., Parry P., Bower M., Young B.D., Evans G.A. Nat. Genet. 2:113-118(1992) [PubMed: 1303259] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1317-2328. Tissue: Brain.
[7]	"Sequence analysis of the breakpoint cluster region in the ALL-1 gene involved in acute leukemia." Gu Y., Alder H., Nakamura T., Schichman S.A., Prasad R., Canaani O., Saito H., Croce C.M., Canaani E. Cancer Res. 54:2327-2330(1994) [PubMed: 8162575] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1251-1538.
[8]	"The human MLL gene: nucleotide sequence, homology to the Drosophila trx zinc-finger domain, and alternative splicing." Mbangkollo D., Burnett R., McCabe N., Thirman M., Gill H., Yu H., Rowley J.D., Diaz M.O. DNA Cell Biol. 14:475-483(1995) [PubMed: 7598802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1251-1654 (ISOFORM 14P-18B).
[9]	"Molecular analysis of the chromosomal breakpoint and fusion transcripts in the acute lymphoblastic SEM cell line with chromosomal translocation t(4;11)." Marschalek R., Greil J., Lochner K., Nilson I., Siegler G., Zweckbronner I., Beck J.D., Fey G.H. Br. J. Haematol. 90:308-320(1995) [PubMed: 7794749] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1212-1603.
[10]	"A method for identifying genes within yeast artificial chromosomes: application to isolation of MLL fusion cDNAs from acute leukaemia translocations." Forster A., Rabbitts T.H. Oncogene 8:3157-3160(1993) [PubMed: 8414518] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1421-1540.
[11]	"Fusion of the MLL gene with two different genes, AF-6 and AF-5alpha, by a complex translocation involving chromosomes 5, 6, 8 and 11 in infant leukemia." Taki T., Hayashi Y., Taniwaki M., Seto M., Ueda R., Hanada R., Suzukawa K., Yokota J., Morishita K. Oncogene 13:2121-2130(1996) [PubMed: 8950979] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH CENPK.
[12]	"ABI-1, a human homolog to mouse Abl-interactor 1, fuses the MLL gene in acute myeloid leukemia with t(10;11)(p11.2;q23)." Taki T., Shibuya N., Taniwaki M., Hanada R., Morishita K., Bessho F., Yanagisawa M., Hayashi Y. Blood 92:1125-1130(1998) [PubMed: 9694699] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH ABI1.
[13]	"Association of SET domain and myotubularin-related proteins modulates growth control." Cui X., De Vivo I., Slany R., Miyamoto A., Firestein R., Cleary M.L. Nat. Genet. 18:331-337(1998) [PubMed: 9537414] [Abstract] Cited for: INTERACTION WITH SBF1.
[14]	"Leukemic HRX fusion proteins inhibit GADD34-induced apoptosis and associate with the GADD34 and hSNF5/INI1 proteins." Adler H.T., Chinery R., Wu D.Y., Kussick S.J., Payne J.M., Fornace A.J. Jr., Tkachuk D.C. Mol. Cell. Biol. 19:7050-7060(1999) [PubMed: 10490642] [Abstract] Cited for: INTERACTION WITH PPP1R15A, DISEASE, FUNCTION.
[15]	"AF5q31, a newly identified AF4-related gene, is fused to MLL in infant acute lymphoblastic leukemia with ins(5;11)(q31;q13q23)." Taki T., Kano H., Taniwaki M., Sako M., Yanagisawa M., Hayashi Y. Proc. Natl. Acad. Sci. U.S.A. 96:14535-14540(1999) [PubMed: 10588740] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH AFF4. Tissue: Placenta.
[16]	"t(3;11) translocation in treatment-related acute myeloid leukemia fuses MLL with the GMPS (guanosine 5-prime monophosphate synthetase) gene." Pegram L.D., Megonigal M.D., Lange B.J., Nowell P.C., Rowley J.D., Rappaport E.F., Felix C.A. Blood 96:4360-4362(2000) [PubMed: 11110714] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH GMPS.
[17]	"Detection of leukemia-associated MLL-GAS7 translocation early during chemotherapy with DNA topoisomerase II inhibitors." Megonigal M.D., Cheung N.-K.V., Rappaport E.F., Nowell P.C., Wilson R.B., Jones D.H., Addya K., Leonard D.G.B., Kushner B.H., Williams T.M., Lange B.J., Felix C.A. Proc. Natl. Acad. Sci. U.S.A. 97:2814-2819(2000) [PubMed: 10706619] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH GAS7.
[18]	"Novel SH3 protein encoded by the AF3p21 gene is fused to the mixed lineage leukemia protein in a therapy-related leukemia with t(3;11)(p21;q23)." Sano K., Hayakawa A., Piao J.-H., Kosaka Y., Nakamura H. Blood 95:1066-1068(2000) [PubMed: 10648423] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH NCKIPSD/AF3P21.
[19]	"Human LPP gene is fused to MLL in a secondary acute leukemia with a t(3;11) (q28;q23)." Daheron L., Veinstein A., Brizard F., Drabkin H., Lacotte L., Guilhot F., Larsen C.J., Brizard A., Roche J. Genes Chromosomes Cancer 31:382-389(2001) [PubMed: 11433529] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH LPP.
[20]	"A t(11;15) fuses MLL to two different genes, AF15q14 and a novel gene MPFYVE on chromosome 15." Chinwalla V., Chien A., Odero M., Neilly M.B., Zeleznik-Le N.J., Rowley J.D. Oncogene 22:1400-1410(2003) [PubMed: 12618766] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH ZFYVE19 AND CASC5.
[21]	"LCX, leukemia-associated protein with a CXXC domain, is fused to MLL in acute myeloid leukemia with trilineage dysplasia having t(10;11)(q22;q23)." Ono R., Taki T., Taketani T., Taniwaki M., Kobayashi H., Hayashi Y. Cancer Res. 62:4075-4080(2002) [PubMed: 12124344] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH TET1.
[22]	"Characterization of the MLL partner gene AF15q14 involved in t(11;15)(q23;q14)." Kuefer M.U., Chinwalla V., Zeleznik-Le N.J., Behm F.G., Naeve C.W., Rakestraw K.M., Mukatira S.T., Raimondi S.C., Morris S.W. Oncogene 22:1418-1424(2003) [PubMed: 12618768] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH CASC5.
[23]	"Identification of a novel RAS GTPase-activating protein (RASGAP) gene at 9q34 as an MLL fusion partner in a patient with de novo acute myeloid leukemia." von Bergh A.R.M., Wijers P.M., Groot A.J., van Zelderen-Bhola S., Falkenburg J.H.F., Kluin P.M., Schuuring E. Genes Chromosomes Cancer 39:324-334(2004) [PubMed: 14978793] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH DAB2IP.
[24]	"Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression." Yokoyama A., Wang Z., Wysocka J., Sanyal M., Aufiero D.J., Kitabayashi I., Herr W., Cleary M.L. Mol. Cell. Biol. 24:5639-5649(2004) [PubMed: 15199122] [Abstract] Cited for: IDENTIFICATION IN THE MLL COMPLEX.
[25]	"FLJ10849, a septin family gene, fuses MLL in a novel leukemia cell line CNLBC1 derived from chronic neutrophilic leukemia in transformation with t(4;11)(q21;q23)." Kojima K., Sakai I., Hasegawa A., Niiya H., Azuma T., Matsuo Y., Fujii N., Tanimoto M., Fujita S. Leukemia 18:998-1005(2004) [PubMed: 14999297] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH SEPT11.
[26]	"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-2151; SER-2866; THR-2940; SER-3036 AND SER-3511, MASS SPECTROMETRY. Tissue: Epithelium.
[27]	"AF4p12, a human homologue to the furry gene of Drosophila, as a novel MLL fusion partner." Hayette S., Cornillet-Lefebvre P., Tigaud I., Struski S., Forissier S., Berchet A., Doll D., Gillot L., Brahim W., Delabesse E., Magaud J.-P., Rimokh R. Cancer Res. 65:6521-6525(2005) [PubMed: 16061630] [Abstract] Cited for: CHROMOSOMAL TRANSLOCATION WITH FRYL.
[28]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-337, MASS SPECTROMETRY. Tissue: Epithelium.
[29]	"ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation." Nakamura T., Mori T., Tada S., Krajewski W., Rozovskaia T., Wassell R., Dubois G., Mazo A., Croce C.M., Canaani E. Mol. Cell 10:1119-1128(2002) [PubMed: 12453419] [Abstract] Cited for: FUNCTION, ENZYME ACTIVITY.
[30]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1837, MASS SPECTROMETRY. Tissue: Epithelium.
[31]	"PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4 methyltransferase complex." Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T., Dressler G.R., Copeland T.D., Kalkum M., Ge K. J. Biol. Chem. 282:20395-20406(2007) [PubMed: 17500065] [Abstract] Cited for: IDENTIFICATION IN THE MLL COMPLEX.
[32]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279, MASS SPECTROMETRY. Tissue: Epithelium.
[33]	"The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells." Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., Haines D.S., Figeys D. J. Proteome Res. 6:298-305(2007) [PubMed: 17203973] [Abstract] Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-216; LYS-220 AND LYS-221, MASS SPECTROMETRY. Tissue: Lung adenocarcinoma.
[34]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-337; SER-926; SER-1241; THR-2153; SER-2691; SER-2729 AND SER-2955, MASS SPECTROMETRY.
[35]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518; SER-1837 AND THR-1845, MASS SPECTROMETRY.
[36]	"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-136; SER-153; SER-197; SER-202; THR-506; SER-518; SER-680; SER-831; THR-840; SER-1056; THR-1839; THR-1845; SER-2098; THR-2147; SER-2151; THR-2525; SER-2955; SER-3036; THR-3372; SER-3511 AND SER-3518, MASS SPECTROMETRY.
[37]	"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-636; LYS-1130 AND LYS-1235, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

L04284 mRNA. Translation: AAA58669.1.
Z69744 , Z69745, Z69746, Z69747, Z69748, Z69749, Z69750, Z69751, Z69752, Z69753, Z69754, Z69755, Z69756, Z69757, Z69758, Z69759, Z69760, Z69761, Z69762, Z69763, Z69764, Z69765, Z69766, Z69767, Z69768, Z69769, Z69770, Z69772, Z69773, Z69774, Z69775, Z69776, Z69777, Z69778, Z69779, Z69780 Genomic DNA. Translation: CAA93625.1.
AY373585 Genomic DNA. Translation: AAQ63624.1.
D14540 mRNA. Translation: BAA03407.1.
L04731 mRNA. No translation available.
L01986 mRNA. Translation: AAA92511.1.
U04737 Unassigned DNA. Translation: AAA18644.1.
S78570 mRNA. Translation: AAB34770.1.
X83604 Genomic DNA. Translation: CAA58584.1.
S66432 mRNA. Translation: AAB28545.1.
AF231998 mRNA. Translation: AAG26332.2. Sequence problems.

IPI

IPI00009286.
IPI00218500.

PIR

A44265.
I52578.
I53035.

RefSeq

NP_005924.2.

UniGene

Hs.258855

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AGH	NMR	-	C	2842-2869	[»]
2J2S	NMR	-	A	1146-1214	[»]
2JYI	NMR	-	A	1147-1203	[»]
2W5Y	X-ray	2.00	A	3785-3969	[»]
2W5Z	X-ray	2.20	A	3785-3969	[»]
3EG6	X-ray	1.72	C	3762-3773	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q03164. 13 interactions.

STRING

Q03164.

PTM databases

PhosphoSite

Q03164.

Proteomic databases

PRIDE

Q03164.

Genome annotation databases

Ensembl

ENST00000328469; ENSP00000333556; ENSG00000118058; Homo sapiens. [Genome view]
ENST00000354520; ENSP00000346516; ENSG00000118058; Homo sapiens. [Genome view]
ENST00000359313; ENSP00000352262; ENSG00000118058; Homo sapiens. [Genome view]
ENST00000389506; ENSP00000374157; ENSG00000118058; Homo sapiens. [Genome view]
ENST00000389507; ENSP00000374158; ENSG00000118058; Homo sapiens. [Genome view]
ENST00000392873; ENSP00000376612; ENSG00000118058; Homo sapiens. [Genome view]
ENST00000420751; ENSP00000402519; ENSG00000118058; Homo sapiens. [Genome view]

GeneID

4297.

KEGG

hsa:4297.

UCSC

uc001pta.1. human.

Organism-specific databases

CTD

4297.

GeneCards

GC11P117812.

HGNC

HGNC:7132. MLL.

HPA

CAB017794.
CAB024270.

MIM

159555. gene+phenotype.

Orphanet

86851. Leukemia of ambiguous lineage, acute.
513. Leukemia, lymphoblastic, acute.

PharmGKB

PA241.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q03164.

OMA

ISNAAVQ.

Gene expression databases

ArrayExpress

Q03164.

Bgee

Q03164.

CleanEx

HS_MLL.

Genevestigator

Q03164.

GermOnline

ENSG00000118058. Homo sapiens.

Family and domain databases

InterPro

IPR017956. AT_hook_DNA-bd_motif.
IPR001487. Bromodomain.
IPR003889. FYrich_C.
IPR018516. FYrich_C_sg.
IPR003888. FYrich_N.
IPR018518. FYrich_N_sg.
IPR016569. MeTrfase_trithorax.
IPR003616. Post-SET_Zn_bd.
IPR001214. SET.
IPR019786. Zinc_finger_PHD-type_CS.
IPR002857. Znf_CXXC.
IPR001965. Znf_PHD.
IPR019787. Znf_PHD-finger.
[Graphical view]

Pfam

PF02178. AT_hook. 1 hit.
PF05965. FYRC. 1 hit.
PF05964. FYRN. 1 hit.
PF00628. PHD. 3 hits.
PF00856. SET. 1 hit.
PF02008. zf-CXXC. 1 hit.
[Graphical view]

PIRSF

PIRSF010354. Methyltransferase_trithorax. 1 hit.

SMART

SM00384. AT_hook. 3 hits.
SM00297. BROMO. 1 hit.
SM00542. FYRC. 1 hit.
SM00541. FYRN. 1 hit.
SM00249. PHD. 4 hits.
SM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]

PROSITE

PS50014. BROMODOMAIN_2. 1 hit.
PS50868. POST_SET. 1 hit.
PS50280. SET. 1 hit.
PS51058. ZF_CXXC. 1 hit.
PS01359. ZF_PHD_1. 3 hits.
PS50016. ZF_PHD_2. 3 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

16915.

SOURCE

Search...

Entry information

Entry name

HRX_HUMAN

Accession

Primary (citable) accession number: Q03164
Secondary accession number(s): Q13743 , Q13744, Q14845, Q16364, Q6UBD1, Q9UMA3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	May 1, 2007
Last modified:	November 3, 2009
This is version 128 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.