O14770 (MEIS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Homeobox protein Meis2

Alternative name(s):
Meis1-related protein 1

Gene names

Name:	MEIS2
Synonyms:	MRG1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	477 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in transcriptional regulation. Binds to HOX or PBX proteins to form dimers, or to a DNA-bound dimer of PBX and HOX proteins and thought to have a role in stabilization of the homeoprotein-DNA complex. Isoform 3/Meis2B is required for the activity of a PDX1:PBX1b:MEIS2b complex in pancreatic acinar cells involved in the transcriptional activation of the ELA1 enhancer; the complex binds to the enhancer B element and cooperates with the transcription factor 1 complex (PTF1) bound to the enhancer A element; MEIS2 is not involved in complex DNA-binding. Probably in complex with PBX1, is involved in transcriptional regulation by KLF4. Isoform 3/Meis2B and isoform 4/Meis2D can bind to a EPHA8 promoter sequence containing the DNA motif 5'-CGGTCA-3'; in cooperation with a PBX protein (such as PBX2) is proposed to be involved in the transcriptional activation of EPHA8 in the developing midbrain. May be involved in regulation of myeloid differentiation. Can bind to the DNA sequence 5'-TGACAG-3'in the activator ACT sequence of the D(1A) dopamine receptor (DRD1) promoter and activate DRD1 transcription; isoform 5/Meis2E cannot activate DRD1 transcription. Ref.1 Ref.7 Ref.11
Subunit structure	Isoform 2/Meis2A interacts with TLX1. Isoform 3/Meis2B interacts with HOXA13 and PBX1 isoform PBX1b. Isoform 4/Meis2D interacts with SP1, SP3 and KLF4. Isoform 4/Meis2D and isoform 5/Meis2E interact with PBX1 isoform PBX1a; the interaction partially relieves MEIS2 autoinhibition. Isoform 3/Meis2B is part of a PDX1:PBX1b:MEIS2b complex; Meis2B is recruited by PBX1b and can be replaced by isoform 4/Meis2D in a small fraction of complexes. Can form trimeric complexes including HOXB8 and PBX2 or PBX3. Ref.9 Ref.10 Ref.11
Subcellular location	Nucleus By similarity.
Tissue specificity	Expressed in various tissues. Expressed at high level in the lymphoid organs of hematopoietic tissues. Also expressed in some regions of the brain, such as the putamen.
Developmental stage	Expressed in the proliferative zones of the fetal neocortex. Expressed at a very high level in the developing ganglionic eminence and at a more moderate level in the cortical plate. Ref.8
Sequence similarities	Belongs to the TALE/MEIS homeobox family. Contains 1 homeobox DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Homeobox
Ligand	DNA-binding
Molecular function	Activator Developmental protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	eye development Inferred from electronic annotation. Source: Compara negative regulation of myeloid cell differentiation Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc positive regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	sequence-specific DNA binding Inferred from direct assay PubMed 17178831PubMed 17178831. Source: MGI sequence-specific DNA binding transcription factor activity Non-traceable author statement Ref.1. Source: ProtInc transcription corepressor activity Traceable author statement Ref.1. Source: ProtInc transcription factor binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TLX1	P31314	4	EBI-6390216,EBI-2820655

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O14770-1)

Also known as: Meis2C;

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 2 (identifier: O14770-2)

Also known as: Meis2A;

The sequence of this isoform differs from the canonical sequence as follows:
     384-401: LQSMPGDYVSQGGPMGMS → PMSGMGMNMGMDGQWHYM
     402-477: Missing.

Isoform 3 (identifier: O14770-3)

Also known as: Meis2B;

The sequence of this isoform differs from the canonical sequence as follows:
     346-352: Missing.
     384-401: LQSMPGDYVSQGGPMGMS → PMSGMGMNMGMDGQWHYM
     402-477: Missing.

Isoform 4 (identifier: O14770-4)

Also known as: Meis2D;

The sequence of this isoform differs from the canonical sequence as follows:
     346-352: Missing.

Isoform 5 (identifier: O14770-5)

Also known as: Meis2E;

The sequence of this isoform differs from the canonical sequence as follows:
     301-302: HP → VY
     303-477: Missing.

Isoform 6 (identifier: O14770-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-89: MAQRYDELPH...IYGHPLFPLL → M
     346-352: Missing.
     384-401: LQSMPGDYVSQGGPMGMS → PMSGMGMNMGMDGQWHYM
     402-477: Missing.

Isoform 7 (identifier: O14770-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: Missing.
     346-352: Missing.
     384-401: LQSMPGDYVSQGGPMGMS → PMSGMGMNMGMDGQWHYM
     402-477: Missing.

Note: No experimental confirmation available.

Isoform 8 (identifier: O14770-8)

The sequence of this isoform differs from the canonical sequence as follows:
     1-13: Missing.
     384-401: LQSMPGDYVSQGGPMGMS → PMSGMGMNMGMDGQWHYM
     402-477: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 477

477

Homeobox protein Meis2

PRO_0000049108

Regions

DNA binding

276 – 338

63

Homeobox; TALE-type

Region

71 – 191

121

Required for interaction with PBX1 By similarity

Region

340 – 477

138

Transcriptional activation domain

Compositional bias

195 – 244

50

Ser/Thr-rich

Compositional bias

246 – 273

28

Asp/Glu-rich (acidic)

Compositional bias

266 – 273

8

Poly-Asp

Amino acid modifications

Modified residue

198

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 89

89

MAQRY…LFPLL → M in isoform 6.

VSP_043219

Alternative sequence

1 – 13

13

Missing in isoform 7 and isoform 8.

VSP_043494

Alternative sequence

301 – 302

2

HP → VY in isoform 5.

VSP_002243

Alternative sequence

303 – 477

175

Missing in isoform 5.

VSP_002244

Alternative sequence

346 – 352

7

Missing in isoform 3, isoform 4, isoform 6 and isoform 7.

VSP_002242

Alternative sequence

384 – 401

18

LQSMP…PMGMS → PMSGMGMNMGMDGQWHYM in isoform 2, isoform 3, isoform 6, isoform 7 and isoform 8.

VSP_002245

Alternative sequence

402 – 477

76

Missing in isoform 2, isoform 3, isoform 6, isoform 7 and isoform 8.

VSP_002246

Experimental info

Mutagenesis

85

1

L → A: Impairs interaction with PBX1; when associated with A-88. Ref.9

Mutagenesis

88

1

L → A: Impairs interaction with PBX1; when associated with A-85. HELIX 285 297.

Mutagenesis

94 – 97

4

EKCE → NNGT: Impairs interaction with PBX1. Ref.9

Mutagenesis

151

1

I → A: Impairs interaction with PBX1; when associated with A-154. Ref.9

Mutagenesis

154

1

L → A: Impairs interaction with PBX1; when associated with A-151. Ref.9

Mutagenesis

158 – 159

2

LL → AA: Impairs interaction with PBX1; when associated with A-161.

Mutagenesis

161

1

L → A: Impairs interaction with PBX1; when associated with 158-A-A-159. Ref.9

Mutagenesis

332

1

R → M: Impairs DNA binding and PBX1-dependent trasncriptional activation. No effect on interaction with PBX1. Ref.9 Ref.11

Secondary structure

1

.

.

.

.

.

.

.

.

477

Helix Strand Turn

Details...

Helix

285 – 297

13

Turn

298 – 300

3

Helix

306 – 316

11

Helix

320 – 335

16

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Meis2C) [UniParc]. Last modified February 21, 2001. Version 2. Checksum: 94EBD0801A312B24	FASTA	477	51,790
	10 20 30 40 50 60 MAQRYDELPH YGGMDGVGVP ASMYGDPHAP RPIPPVHHLN HGPPLHATQH YGAHAPHPNV 70 80 90 100 110 120 MPASMGSAVN DALKRDKDAI YGHPLFPLLA LVFEKCELAT CTPREPGVAG GDVCSSDSFN 130 140 150 160 170 180 EDIAVFAKQV RAEKPLFSSN PELDNLMIQA IQVLRFHLLE LEKVHELCDN FCHRYISCLK 190 200 210 220 230 240 GKMPIDLVID ERDGSSKSDH EELSGSSTNL ADHNPSSWRD HDDATSTHSA GTPGPSSGGH 250 260 270 280 290 300 ASQSGDNSSE QGDGLDNSVA SPGTGDDDDP DKDKKRQKKR GIFPKVATNI MRAWLFQHLT 310 320 330 340 350 360 HPYPSEEQKK QLAQDTGLTI LQVNNWFINA RRRIVQPMID QSNRAGFLLD PSVSQGAAYS 370 380 390 400 410 420 PEGQPMGSFV LDGQQHMGIR PAGLQSMPGD YVSQGGPMGM SMAQPSYTPP QMTPHPTQLR 430 440 450 460 470 HGPPMHSYLP SHPHHPAMMM HGGPPTHPGM TMSAQSPTML NSVDPNVGGQ VMDIHAQ
	Isoform 2 (Meis2A) [UniParc]. Checksum: 0682C0E92326516D	FASTA	401	43,791
	10 20 30 40 50 60 MAQRYDELPH YGGMDGVGVP ASMYGDPHAP RPIPPVHHLN HGPPLHATQH YGAHAPHPNV 70 80 90 100 110 120 MPASMGSAVN DALKRDKDAI YGHPLFPLLA LVFEKCELAT CTPREPGVAG GDVCSSDSFN 130 140 150 160 170 180 EDIAVFAKQV RAEKPLFSSN PELDNLMIQA IQVLRFHLLE LEKVHELCDN FCHRYISCLK 190 200 210 220 230 240 GKMPIDLVID ERDGSSKSDH EELSGSSTNL ADHNPSSWRD HDDATSTHSA GTPGPSSGGH 250 260 270 280 290 300 ASQSGDNSSE QGDGLDNSVA SPGTGDDDDP DKDKKRQKKR GIFPKVATNI MRAWLFQHLT 310 320 330 340 350 360 HPYPSEEQKK QLAQDTGLTI LQVNNWFINA RRRIVQPMID QSNRAGFLLD PSVSQGAAYS 370 380 390 400 PEGQPMGSFV LDGQQHMGIR PAGPMSGMGM NMGMDGQWHY M
	Isoform 3 (Meis2B) [UniParc]. Checksum: 6BCC0382F0C55296	FASTA	394	43,061
	10 20 30 40 50 60 MAQRYDELPH YGGMDGVGVP ASMYGDPHAP RPIPPVHHLN HGPPLHATQH YGAHAPHPNV 70 80 90 100 110 120 MPASMGSAVN DALKRDKDAI YGHPLFPLLA LVFEKCELAT CTPREPGVAG GDVCSSDSFN 130 140 150 160 170 180 EDIAVFAKQV RAEKPLFSSN PELDNLMIQA IQVLRFHLLE LEKVHELCDN FCHRYISCLK 190 200 210 220 230 240 GKMPIDLVID ERDGSSKSDH EELSGSSTNL ADHNPSSWRD HDDATSTHSA GTPGPSSGGH 250 260 270 280 290 300 ASQSGDNSSE QGDGLDNSVA SPGTGDDDDP DKDKKRQKKR GIFPKVATNI MRAWLFQHLT 310 320 330 340 350 360 HPYPSEEQKK QLAQDTGLTI LQVNNWFINA RRRIVQPMID QSNRAVSQGA AYSPEGQPMG 370 380 390 SFVLDGQQHM GIRPAGPMSG MGMNMGMDGQ WHYM
	Isoform 4 (Meis2D) [UniParc]. Checksum: C15C82B9F0098CB9	FASTA	470	51,060
	10 20 30 40 50 60 MAQRYDELPH YGGMDGVGVP ASMYGDPHAP RPIPPVHHLN HGPPLHATQH YGAHAPHPNV 70 80 90 100 110 120 MPASMGSAVN DALKRDKDAI YGHPLFPLLA LVFEKCELAT CTPREPGVAG GDVCSSDSFN 130 140 150 160 170 180 EDIAVFAKQV RAEKPLFSSN PELDNLMIQA IQVLRFHLLE LEKVHELCDN FCHRYISCLK 190 200 210 220 230 240 GKMPIDLVID ERDGSSKSDH EELSGSSTNL ADHNPSSWRD HDDATSTHSA GTPGPSSGGH 250 260 270 280 290 300 ASQSGDNSSE QGDGLDNSVA SPGTGDDDDP DKDKKRQKKR GIFPKVATNI MRAWLFQHLT 310 320 330 340 350 360 HPYPSEEQKK QLAQDTGLTI LQVNNWFINA RRRIVQPMID QSNRAVSQGA AYSPEGQPMG 370 380 390 400 410 420 SFVLDGQQHM GIRPAGLQSM PGDYVSQGGP MGMSMAQPSY TPPQMTPHPT QLRHGPPMHS 430 440 450 460 470 YLPSHPHHPA MMMHGGPPTH PGMTMSAQSP TMLNSVDPNV GGQVMDIHAQ
	Isoform 5 (Meis2E) [UniParc]. Checksum: 059D4D332A95FE5F	FASTA	302	32,837
	10 20 30 40 50 60 MAQRYDELPH YGGMDGVGVP ASMYGDPHAP RPIPPVHHLN HGPPLHATQH YGAHAPHPNV 70 80 90 100 110 120 MPASMGSAVN DALKRDKDAI YGHPLFPLLA LVFEKCELAT CTPREPGVAG GDVCSSDSFN 130 140 150 160 170 180 EDIAVFAKQV RAEKPLFSSN PELDNLMIQA IQVLRFHLLE LEKVHELCDN FCHRYISCLK 190 200 210 220 230 240 GKMPIDLVID ERDGSSKSDH EELSGSSTNL ADHNPSSWRD HDDATSTHSA GTPGPSSGGH 250 260 270 280 290 300 ASQSGDNSSE QGDGLDNSVA SPGTGDDDDP DKDKKRQKKR GIFPKVATNI MRAWLFQHLT VY
	Isoform 6 [UniParc]. Checksum: 4DF1350FB0F28AF1	FASTA	306	33,598
	10 20 30 40 50 60 MALVFEKCEL ATCTPREPGV AGGDVCSSDS FNEDIAVFAK QVRAEKPLFS SNPELDNLMI 70 80 90 100 110 120 QAIQVLRFHL LELEKVHELC DNFCHRYISC LKGKMPIDLV IDERDGSSKS DHEELSGSST 130 140 150 160 170 180 NLADHNPSSW RDHDDATSTH SAGTPGPSSG GHASQSGDNS SEQGDGLDNS VASPGTGDDD 190 200 210 220 230 240 DPDKDKKRQK KRGIFPKVAT NIMRAWLFQH LTHPYPSEEQ KKQLAQDTGL TILQVNNWFI 250 260 270 280 290 300 NARRRIVQPM IDQSNRAVSQ GAAYSPEGQP MGSFVLDGQQ HMGIRPAGPM SGMGMNMGMD GQWHYM
	Isoform 7 [UniParc]. Checksum: 4F6D947B1EDA0528	FASTA	381	41,542
	10 20 30 40 50 60 MDGVGVPASM YGDPHAPRPI PPVHHLNHGP PLHATQHYGA HAPHPNVMPA SMGSAVNDAL 70 80 90 100 110 120 KRDKDAIYGH PLFPLLALVF EKCELATCTP REPGVAGGDV CSSDSFNEDI AVFAKQVRAE 130 140 150 160 170 180 KPLFSSNPEL DNLMIQAIQV LRFHLLELEK VHELCDNFCH RYISCLKGKM PIDLVIDERD 190 200 210 220 230 240 GSSKSDHEEL SGSSTNLADH NPSSWRDHDD ATSTHSAGTP GPSSGGHASQ SGDNSSEQGD 250 260 270 280 290 300 GLDNSVASPG TGDDDDPDKD KKRQKKRGIF PKVATNIMRA WLFQHLTHPY PSEEQKKQLA 310 320 330 340 350 360 QDTGLTILQV NNWFINARRR IVQPMIDQSN RAVSQGAAYS PEGQPMGSFV LDGQQHMGIR 370 380 PAGPMSGMGM NMGMDGQWHY M
	Isoform 8 [UniParc]. Checksum: E9F5455311C5BC69	FASTA	388	42,272
	10 20 30 40 50 60 MDGVGVPASM YGDPHAPRPI PPVHHLNHGP PLHATQHYGA HAPHPNVMPA SMGSAVNDAL 70 80 90 100 110 120 KRDKDAIYGH PLFPLLALVF EKCELATCTP REPGVAGGDV CSSDSFNEDI AVFAKQVRAE 130 140 150 160 170 180 KPLFSSNPEL DNLMIQAIQV LRFHLLELEK VHELCDNFCH RYISCLKGKM PIDLVIDERD 190 200 210 220 230 240 GSSKSDHEEL SGSSTNLADH NPSSWRDHDD ATSTHSAGTP GPSSGGHASQ SGDNSSEQGD 250 260 270 280 290 300 GLDNSVASPG TGDDDDPDKD KKRQKKRGIF PKVATNIMRA WLFQHLTHPY PSEEQKKQLA 310 320 330 340 350 360 QDTGLTILQV NNWFINARRR IVQPMIDQSN RAGFLLDPSV SQGAAYSPEG QPMGSFVLDG 370 380 QQHMGIRPAG PMSGMGMNMG MDGQWHYM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Three-amino acid extension loop homeodomain proteins Meis2 and TGIF differentially regulate transcription." Yang Y., Hwang C.K., D'Souza U.M., Lee S.-H., Junn E., Mouradian M.M. J. Biol. Chem. 275:20734-20741(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), FUNCTION. Tissue: Brain.
[2]	"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] (ISOFORMS 6 AND 8). Tissue: Tongue.
[3]	"Analysis of the DNA sequence and duplication history of human chromosome 15." Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C. Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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 4 AND 7). Tissue: Muscle and Testis.
[6]	"Chromosomal mapping to 15q14 and expression analysis of the human MEIS2 homeobox gene." Smith J.E. Jr., Afonja O., Yee H.T., Inghirami G., Takeshita K. Mamm. Genome 8:951-952(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 271-477 (ISOFORM 3).
[7]	"DNA binding and transcriptional activation by a PDX1.PBX1b.MEIS2b trimer and cooperation with a pancreas-specific basic helix-loop-helix complex." Liu Y., MacDonald R.J., Swift G.H. J. Biol. Chem. 276:17985-17993(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Spatiotemporal distribution of PAX6 and MEIS2 expression and total cell numbers in the ganglionic eminence in the early developing human forebrain." Larsen K.B., Lutterodt M.C., Laursen H., Graem N., Pakkenberg B., Mollgard K., Moller M. Dev. Neurosci. 32:149-162(2010) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[9]	"An autoinhibitory effect of the homothorax domain of Meis2." Hyman-Walsh C., Bjerke G.A., Wotton D. FEBS J. 277:2584-2597(2010) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN, INTERACTION WITH PBX1, MUTAGENESIS OF LEU-85; LEU-88; 94-GLU--GLU-97; ILE-151; LEU-154; 158-LEU-LEU-159; LEU-161 AND ARG-332.
[10]	"MEIS proteins as partners of the TLX1/HOX11 oncoprotein." Milech N., Gottardo N.G., Ford J., D'Souza D., Greene W.K., Kees U.R., Watt P.M. Leuk. Res. 34:358-363(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TLX1.
[11]	"Cooperative transcriptional activation by Klf4, Meis2, and Pbx1." Bjerke G.A., Hyman-Walsh C., Wotton D. Mol. Cell. Biol. 31:3723-3733(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SP1; SP3 AND KLF4, MUTAGENESIS OF ARG-332.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF178948 mRNA. Translation: AAF81638.1.
AF179896 mRNA. Translation: AAF81639.1.
AF179897 mRNA. Translation: AAF81640.1.
AF179898 mRNA. Translation: AAF81641.1.
AF179899 mRNA. Translation: AAF81642.1.
AK056038 mRNA. Translation: BAG51610.1.
AK056620 mRNA. Translation: BAG51768.1.
AC018563 Genomic DNA. No translation available.
AC069483 Genomic DNA. No translation available.
AC078909 Genomic DNA. No translation available.
CH471125 Genomic DNA. Translation: EAW92353.1.
CH471125 Genomic DNA. Translation: EAW92354.1.
CH471125 Genomic DNA. Translation: EAW92356.1.
BC001516 mRNA. Translation: AAH01516.1.
BC001844 mRNA. Translation: AAH01844.3.
BC007202 mRNA. Translation: AAH07202.1.
BC050431 mRNA. Translation: AAH50431.1.
AF017418 mRNA. Translation: AAB70270.1.

IPI

IPI00023696.
IPI00171219.
IPI00221237.
IPI00221238.
IPI00746958.

RefSeq

NP_001207411.1. NM_001220482.1.
NP_002390.1. NM_002399.3.
NP_733774.1. NM_170674.4.
NP_733775.1. NM_170675.4.
NP_733776.1. NM_170676.4.
NP_733777.1. NM_170677.4.
NP_758526.1. NM_172315.2.
NP_758527.1. NM_172316.2.

UniGene

Hs.510989.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3K2A	X-ray	1.95	A/B	281-345	[»]

ProteinModelPortal

O14770.

ModBase

Search...

Protein-protein interaction databases

IntAct

O14770. 3 interactions.

STRING

9606.ENSP00000326296.

PTM databases

PhosphoSite

O14770.

Proteomic databases

PaxDb

O14770.

PRIDE

O14770.

Protocols and materials databases

DNASU

4212.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000314177; ENSP00000326296; ENSG00000134138.
ENST00000338564; ENSP00000341400; ENSG00000134138.
ENST00000340545; ENSP00000339549; ENSG00000134138.
ENST00000382766; ENSP00000372216; ENSG00000134138.
ENST00000397620; ENSP00000380745; ENSG00000134138.
ENST00000397624; ENSP00000380749; ENSG00000134138.
ENST00000424352; ENSP00000404185; ENSG00000134138.
ENST00000444725; ENSP00000391887; ENSG00000134138.
ENST00000559085; ENSP00000453390; ENSG00000134138.
ENST00000559561; ENSP00000453497; ENSG00000134138.
ENST00000561208; ENSP00000453793; ENSG00000134138.

GeneID

4212.

KEGG

hsa:4212.

UCSC

uc001zjo.3. human.
uc001zjp.3. human.
uc001zjr.3. human.
uc001zjs.3. human.

Organism-specific databases

CTD

4212.

GeneCards

GC15M037183.

HGNC

HGNC:7001. MEIS2.

HPA

CAB004999.
HPA003256.

MIM

601740. gene.

neXtProt

NX_O14770.

PharmGKB

PA30741.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG302919.

HOGENOM

HOG000253923.

HOVERGEN

HBG055193.

InParanoid

O14770.

KO

K16670.

OMA

LHASQHY.

OrthoDB

EOG4XPQFW.

PhylomeDB

O14770.

Gene expression databases

ArrayExpress

O14770.

Bgee

O14770.

CleanEx

HS_MEIS2.

Genevestigator

O14770.

GermOnline

ENSG00000134138. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.60. 1 hit.

InterPro

IPR008422. Homeobox_KN_domain.
IPR001356. Homeodomain.
IPR009057. Homeodomain-like.
[Graphical view]

Pfam

PF05920. Homeobox_KN. 1 hit.
[Graphical view]

SMART

SM00389. HOX. 1 hit.
[Graphical view]

SUPFAM

SSF46689. Homeodomain_like. 1 hit.

PROSITE

PS00027. HOMEOBOX_1. False negative.
PS50071. HOMEOBOX_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

MEIS2. human.

EvolutionaryTrace

O14770.

GenomeRNAi

4212.

NextBio

16594.

SOURCE

Search...

Entry information

Entry name

MEIS2_HUMAN

Accession

Primary (citable) accession number: O14770
Secondary accession number(s): A6NJI5 , A8MWD5, B3KP98, B3KPQ6, Q96DI2, Q96KI4, Q96KI5, Q9NRS1, Q9NRS2, Q9NRS3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	February 21, 2001
Last modified:	May 1, 2013
This is version 119 of the entry and version 2 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.