O00255 (MEN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Menin

Gene names

Name:	MEN1
Synonyms:	SCG2

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	615 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential component of a MLL/SET1 histone methyltransferase (HMT) complex, a complex that specifically methylates 'Lys-4' of histone H3 (H3K4). Functions as a transcriptional regulator. Binds to the TERT promoter and represses telomerase expression. Plays a role in TGFB1-mediated inhibition of cell-proliferation, possibly regulating SMAD3 transcriptional activity. Represses JUND-mediated transcriptional activation on AP1 sites, as well as that mediated by NFKB subunit RELA. Positively regulates HOXC8 and HOXC6 gene expression. May be involved in normal hematopoiesis through the activation of HOXA9 expression By similarity. May be involved in DNA repair. Ref.6 Ref.7 Ref.8 Ref.9 Ref.11
Subunit structure	Component of the MLL-HCF complex, at least composed of MLL, MEN1, ASH2L, RBBP5, DPY30, WDR5, HCFC1 and HCFC2. Component of the menin-associated histone methyltransferase complex, at least composed of MLL4/WBP7, MEN1, ASH2L, RBBP5, DPY30 and WDR5. Interacts with POLR2B. Interacts with POLR2A phosphorylated at 'Ser-5', but not with the unphosphorylated, nor 'Ser-2' phosphorylated POLR2A forms. Interacts with FANCD2 and DBF4. Interacts with JUND. Interacts with SMAD3, but not with SMAD2, nor SMAD4. Directly interacts with NFKB1, NFKB2 and RELA. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13
Subcellular location	Nucleus. Note: Concentrated in nuclear body-like structures. Relocates to the nuclear matrix upon gamma irradiation. Ref.8
Tissue specificity	Ubiquitous.
Involvement in disease	Familial multiple endocrine neoplasia type I (MEN1) [MIM:131100]: Autosomal dominant disorder characterized by tumors of the parathyroid glands, gastro-intestinal endocrine tissue, the anterior pituitary and other tissues. Cutaneous lesions and nervous-tissue tumors can exist. Prognosis in MEN1 patients is related to hormonal hypersecretion by tumors, such as hypergastrinemia causing severe peptic ulcer disease (Zollinger-Ellison syndrome, ZES), primary hyperparathyroidism, and acute forms of hyperinsulinemia. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.1 Ref.3 Ref.5 Ref.11 Ref.17 Ref.18 Ref.20 Ref.21 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.38 Ref.39 Ref.40 Ref.41 Ref.43 Ref.44 Ref.46 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.54 Ref.55 Ref.56 Ref.57 Ref.58 Ref.60 Ref.61 Familial isolated hyperparathyroidism (FIHP) [MIM:145000]: Autosomal dominant disorder characterized by hypercalcemia, elevated parathyroid hormone (PTH) levels, and uniglandular or multiglandular parathyroid tumors. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Ref.23 Ref.38 Ref.45 Ref.47 Ref.53 Ref.54
Sequence caution	The sequence ABQ12624.1 differs from that shown. Reason: Frameshift at position 383. The frameshift is caused by a single nucleotide deletion which is found in a MEN1 kindred. The sequence ABQ12627.1 differs from that shown. Reason: Frameshift at position 97. The frameshift is caused by a single nucleotide deletion which is found in a MEN1 kindred.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Ligand	DNA-binding
Molecular function	Chromatin regulator Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Non-traceable author statement Ref.8. Source: UniProtKB MAPK cascade Inferred from direct assay PubMed 12226747. Source: UniProtKB brain development Inferred from electronic annotation. Source: Compara cell cycle arrest Inferred from electronic annotation. Source: Compara chromatin remodeling Inferred from electronic annotation. Source: Compara embryonic skeletal system morphogenesis Inferred from electronic annotation. Source: Compara hemopoiesis Inferred from electronic annotation. Source: Compara histone lysine methylation Inferred from direct assay Ref.11. Source: GOC leukocyte homeostasis Inferred from electronic annotation. Source: Compara maternal process involved in female pregnancy Inferred from electronic annotation. Source: Compara negative regulation of JNK cascade Inferred from direct assay PubMed 12226747. Source: UniProtKB negative regulation of cell proliferation Inferred from direct assay PubMed 15331604. Source: UniProtKB negative regulation of cyclin-dependent protein serine/threonine kinase activity Inferred from mutant phenotype PubMed 15640349. Source: UniProtKB negative regulation of organ growth Inferred from electronic annotation. Source: Compara negative regulation of osteoblast differentiation Inferred from genetic interaction PubMed 15563473. Source: MGI negative regulation of sequence-specific DNA binding transcription factor activity Inferred from direct assay Ref.6PubMed 12226747. Source: UniProtKB negative regulation of telomerase activity Inferred from mutant phenotype Ref.9. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.5. Source: UniProtKB osteoblast development Inferred from genetic interaction PubMed 15563473. Source: MGI osteoblast fate commitment Inferred from electronic annotation. Source: Compara palate development Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of cell division Inferred from electronic annotation. Source: Compara positive regulation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of histone methylation Inferred from electronic annotation. Source: Compara positive regulation of osteoblast differentiation Inferred from electronic annotation. Source: Compara positive regulation of protein binding Inferred from direct assay PubMed 20484083. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Traceable author statement. Source: Reactome positive regulation of transforming growth factor beta receptor signaling pathway Inferred from mutant phenotype Ref.7. Source: UniProtKB regulation of activin receptor signaling pathway Inferred from electronic annotation. Source: Compara response to UV Inferred from direct assay PubMed 16690369. Source: UniProtKB response to gamma radiation Inferred from direct assay Ref.8. Source: UniProtKB transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome transforming growth factor beta receptor signaling pathway Traceable author statement. Source: Reactome
Cellular_component	chromatin Inferred from direct assay Ref.8. Source: UniProtKB cleavage furrow Inferred from direct assay PubMed 14508515. Source: UniProtKB cytosol Inferred from direct assay PubMed 14508515. Source: UniProtKB histone methyltransferase complex Inferred from direct assay Ref.13. Source: MGI nuclear matrix Inferred from direct assay Ref.8. Source: UniProtKB
Molecular_function	Y-form DNA binding Inferred from direct assay PubMed 15331604. Source: UniProtKB chromatin binding Inferred from electronic annotation. Source: Compara double-stranded DNA binding Inferred from direct assay PubMed 15331604. Source: UniProtKB four-way junction DNA binding Inferred from direct assay PubMed 15331604. Source: UniProtKB protein binding, bridging Inferred from direct assay PubMed 20484083. Source: UniProtKB sequence-specific DNA binding Inferred from electronic annotation. Source: Compara transcription regulatory region DNA binding Inferred from direct assay PubMed 20484083. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FANCD2	Q9BXW9	4	EBI-592789,EBI-359343
MYH9	P35579	7	EBI-592789,EBI-350338
Nme1	Q05982	5	EBI-592789,EBI-1165329	From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O00255-1)

Also known as: Long;

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: O00255-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     149-153: Missing.

Isoform 3 (identifier: O00255-3)

The sequence of this isoform differs from the canonical sequence as follows:
     149-153: Missing.
     189-223: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 615

615

Menin

PRO_0000096411

Regions

Region

219 – 395

177

Interaction with FANCD2

Amino acid modifications

Modified residue

599

1

Phosphothreonine Ref.15

Natural variations

Alternative sequence

149 – 153

5

Missing in isoform 2 and isoform 3.

VSP_004323

Alternative sequence

189 – 223

35

Missing in isoform 3.

VSP_015854

Natural variant

12

1

P → L in MEN1; no effect on histone methylation; almost no effect on JUND-binding. Ref.5 Ref.11

VAR_005425

Natural variant

22

1

L → R in MEN1; no effect on histone methylation; almost no effect on JUND-binding; no repression of JUND transactivation. Ref.1 Ref.5 Ref.11

VAR_005426

Natural variant

26

1

E → K in parathyroid adenoma and MEN1. Ref.19 Ref.24
Corresponds to variant rs28931612 [ dbSNP | Ensembl ].

VAR_005427

Natural variant

39

1

L → W in MEN1. Ref.38 Ref.43 Ref.50

VAR_005428

Natural variant

42

1

G → D in MEN1. Ref.20 Ref.50

VAR_005429

Natural variant

45

1

E → G in MEN1. Ref.33

VAR_005430

Natural variant

45

1

E → K in MEN1. Ref.44 Ref.58

VAR_039587

Natural variant

89 – 95

7

Missing in MEN1.

VAR_065152

Natural variant

98

1

R → L in MEN1. Ref.50

VAR_039588

Natural variant

110

1

G → E in MEN1. Ref.60

VAR_039589

Natural variant

119

1

Missing in MEN1. Ref.1 Ref.32 Ref.43 Ref.52

VAR_005431

Natural variant

135

1

K → I in MEN1. Ref.31

VAR_005434

Natural variant

139

1

H → D in MEN1; almost complete loss of histone methylation; strong decrease in JUND-binding; no repression of JUND transactivation. Ref.5 Ref.11 Ref.29 Ref.48

VAR_005432

Natural variant

139

1

H → P in MEN1. Ref.58

VAR_039590

Natural variant

139

1

H → R in MEN1. Ref.34

VAR_039591

Natural variant

139

1

H → Y in MEN1; familial and sporadic cases; almost no effect on JUND-binding; no repression of JUND transactivation. Ref.5

VAR_005433

Natural variant

144

1

F → V in MEN1. Ref.61

VAR_005436

Natural variant

147

1

I → F in MEN1. Ref.3

VAR_065153

Natural variant

157

1

L → W in parathyroid tumors; somatic. Ref.29

VAR_065154

Natural variant

158

1

D → V in MEN1 and FIHP. Ref.54

VAR_039592

Natural variant

159

1

S → I in MEN1. Ref.52

VAR_039593

Natural variant

160

1

S → F in MEN1. Ref.40

VAR_039594

Natural variant

161

1

G → D in MEN1 and parathyroid tumor. Ref.39 Ref.42 Ref.61

VAR_008017

Natural variant

165

1

A → P in MEN1; strong decrease in JUND-binding. Ref.5 Ref.20 Ref.50

VAR_005437

Natural variant

165

1

A → T in MEN1. Ref.50

VAR_039595

Natural variant

167

1

V → F in MEN1. Ref.50

VAR_039596

Natural variant

169

1

A → D in MEN1. Ref.20 Ref.50

VAR_005438

Natural variant

170

1

C → R in MEN1. Ref.50 Ref.56

VAR_039597

Natural variant

171 – 173

3

Missing in MEN1.

VAR_005439

Natural variant

173

1

L → P in MEN1. Ref.24

VAR_039598

Natural variant

176

1

R → Q. Ref.1 Ref.18 Ref.28 Ref.38 Ref.58 Ref.59
Corresponds to variant rs607969 [ dbSNP | Ensembl ].

VAR_005440

Natural variant

177

1

D → Y in MEN1. Ref.38 Ref.50

VAR_005441

Natural variant

181

1

A → P in MEN1; loss of JUND-binding. Ref.5

VAR_005442

Natural variant

184

1

E → D in MEN1. Ref.38 Ref.61

VAR_005443

Natural variant

184

1

E → K in MEN1. Ref.46 Ref.61

VAR_039599

Natural variant

184

1

E → Q in MEN1. Ref.43

VAR_039600

Natural variant

186

1

H → R in MEN1. Ref.61

VAR_039601

Natural variant

188

1

W → R in MEN1 and parathyroid tumor. Ref.36 Ref.42

VAR_039602

Natural variant

188

1

W → S in MEN1. Ref.18 Ref.20

VAR_005444

Natural variant

189

1

V → E in FIHP. Ref.23

VAR_005445

Natural variant

220

1

V → F Found in a parathyroid carcinoma sample; somatic mutation. Ref.62

VAR_064937

Natural variant

220

1

V → M in MEN1. Ref.44 Ref.61

VAR_039603

Natural variant

228

1

L → P in MEN1. Ref.43 Ref.50 Ref.56

VAR_005446

Natural variant

230

1

G → R in MEN1. Ref.36

VAR_039604

Natural variant

234

1

R → L in MEN1. Ref.41

VAR_039605

Natural variant

245

1

V → F in MEN1. Ref.50

VAR_039606

Natural variant

246

1

C → F in MEN1. Ref.56

VAR_039607

Natural variant

246

1

C → R in MEN1. Ref.39

VAR_008018

Natural variant

246

1

C → Y in MEN1. Ref.36

VAR_039608

Natural variant

247

1

A → V in MEN1; almost complete loss of histone methylation; loss of JUND-binding; no repression of JUND transactivation. Ref.5 Ref.11

VAR_005447

Natural variant

258

1

S → P in MEN1. Ref.36

VAR_039609

Natural variant

258

1

S → W in parathyroid tumor. Ref.42

VAR_039610

Natural variant

260

1

E → K in FIHP. Ref.22

VAR_005448

Natural variant

264

1

L → R in MEN1. Ref.61

VAR_039611

Natural variant

265

1

Q → P in FIHP. Ref.47

VAR_039612

Natural variant

266

1

Q → QLQ in MEN1.

VAR_039613

Natural variant

269

1

L → P in MEN1. Ref.38

VAR_005449

Natural variant

272

1

L → P in FIHP. Ref.38

VAR_005450

Natural variant

279

1

E → A in parathyroid tumor. Ref.42

VAR_039614

Natural variant

282

1

P → H in FIHP. Ref.53

VAR_039615

Natural variant

286

1

G → R in MEN1. Ref.50 Ref.56

VAR_039616

Natural variant

289

1

A → E in MEN1. Ref.20

VAR_005451

Natural variant

289

1

A → P in parathyroid tumor. Ref.42

VAR_039617

Natural variant

291

1

L → P in MEN1; almost no effect on JUND-binding. Ref.5

VAR_005452

Natural variant

310

1

G → D in FIHP. Ref.45

VAR_039618

Natural variant

314

1

A → P in MEN1; no effect on histone methylation; almost no effect on JUND-binding. Ref.5 Ref.11

VAR_005453

Natural variant

316

1

T → P in MEN1. Ref.50 Ref.56

VAR_039619

Natural variant

319

1

R → P in MEN1. Ref.50

VAR_005454

Natural variant

322

1

H → R in MEN1. Ref.43 Ref.50

VAR_039620

Natural variant

322

1

H → Y in MEN1. Ref.50 Ref.56

VAR_039621

Natural variant

325

1

P → L in MEN1. Ref.27

VAR_039622

Natural variant

325

1

P → R in MEN1. Ref.61

VAR_039623

Natural variant

330

1

A → P in MEN1. Ref.55

VAR_039624

Natural variant

342

1

A → D in MEN1. Ref.50
Corresponds to variant rs2071312 [ dbSNP | Ensembl ].

VAR_005455

Natural variant

342

1

A → P in MEN1. Ref.43

VAR_039625

Natural variant

346

1

W → R in MEN1. Ref.50

VAR_005456

Natural variant

347

1

A → P in MEN1. Ref.57

VAR_039626

Natural variant

349

1

T → R in MEN1; almost complete loss of histone methylation; almost no effect on JUND-binding. Ref.5 Ref.11 Ref.44

VAR_005457

Natural variant

353

1

I → N in MEN1. Ref.43

VAR_039627

Natural variant

358

1

Y → D in MEN1. Ref.41

VAR_039628

Natural variant

360

1

R → W in MEN1. Ref.61

VAR_039629

Natural variant

362

1

D → H in MEN1. Ref.50

VAR_039630

Natural variant

364

1

E → K in MEN1. Ref.31

VAR_005458

Natural variant

368

1

Missing in MEN1. Ref.1 Ref.52

VAR_005459

Natural variant

373

1

A → D in MEN1. Ref.50

VAR_005460

Natural variant

377

1

I → M in MEN1. Ref.50

VAR_039631

Natural variant

378

1

P → S in MEN1. Ref.41

VAR_039632

Natural variant

390

1

A → V in MEN1. Ref.43

VAR_039633

Natural variant

416

1

A → P in MEN1 and FIHP. Ref.54

VAR_039634

Natural variant

418

1

L → R in MEN1. Ref.3

VAR_065155

Natural variant

419

1

L → P in MEN1. Ref.3 Ref.49

VAR_039635

Natural variant

420

1

R → P in MEN1. Ref.41

VAR_039636

Natural variant

423 – 426

4

Missing in MEN1.

VAR_005463

Natural variant

423

1

D → H in MEN1. Ref.60

VAR_039637

Natural variant

423

1

D → N in MEN1. Ref.28 Ref.50 Ref.52 Ref.56

VAR_005461

Natural variant

423

1

Missing in MEN1.

VAR_005462

Natural variant

426

1

C → Y in MEN1. Ref.61

VAR_039638

Natural variant

428

1

W → S in MEN1. Ref.30

VAR_039639

Natural variant

432

1

S → R in MEN1. Ref.26

VAR_039640

Natural variant

441

1

W → C in MEN1. Ref.61

VAR_039641

Natural variant

441

1

W → R in MEN1; no effect on histone methylation; almost no effect on JUND-binding; modest repression of JUND transactivation. Ref.1 Ref.5 Ref.11 Ref.61

VAR_005464

Natural variant

449

1

L → P in MEN1. Ref.35

VAR_039642

Natural variant

452

1

F → S in MEN1; sporadic; with Zollinger-Ellison syndrome.

VAR_005465

Natural variant

476

1

W → C in MEN1. Ref.3

VAR_065156

Natural variant

532

1

R → C in MEN1. Ref.50

VAR_039643

Natural variant

545

1

P → S in MEN1. Ref.56

VAR_039644

Natural variant

546

1

T → A. Ref.1 Ref.3 Ref.4 Ref.27 Ref.28 Ref.36 Ref.38 Ref.58 Ref.63
Corresponds to variant rs2959656 [ dbSNP | Ensembl ].

VAR_005466

Natural variant

549

1

P → S in MEN1. Ref.43

VAR_039645

Natural variant

557

1

T → S in adrenal adenoma; somatic. Ref.37

VAR_039646

Natural variant

560

1

S → N in MEN1. Ref.50

VAR_005467

Natural variant

560

1

S → R in MEN1. Ref.50

VAR_039647

Secondary structure

1

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615

Helix Strand Turn

Details...

Helix

5 – 8

4

Helix

16 – 27

12

Beta strand

29 – 31

3

Helix

34 – 49

16

Beta strand

63 – 67

5

Turn

70 – 72

3

Beta strand

74 – 79

6

Helix

83 – 100

18

Helix

103 – 105

3

Helix

109 – 111

3

Helix

115 – 127

13

Beta strand

137 – 139

3

Helix

143 – 148

6

Helix

159 – 172

14

Beta strand

179 – 182

4

Beta strand

187 – 192

6

Helix

193 – 195

3

Beta strand

197 – 199

3

Beta strand

205 – 207

3

Helix

209 – 211

3

Helix

217 – 221

5

Helix

225 – 230

6

Helix

237 – 246

10

Beta strand

251 – 253

3

Helix

259 – 275

17

Turn

276 – 280

5

Helix

282 – 294

13

Helix

303 – 317

15

Helix

324 – 335

12

Helix

339 – 353

15

Helix

360 – 362

3

Helix

363 – 374

12

Helix

376 – 389

14

Helix

408 – 410

3

Helix

412 – 429

18

Helix

439 – 450

12

Helix

454 – 457

4

Beta strand

461 – 463

3

Beta strand

555 – 557

3

Helix

561 – 566

6

Helix

567 – 569

3

Beta strand

572 – 574

3

Helix

577 – 585

9

Helix

603 – 612

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Long) [UniParc]. Last modified January 11, 2011. Version 4. Checksum: DDDF850EA5AB77B4	FASTA	615	68,023
	10 20 30 40 50 60 MGLKAAQKTL FPLRSIDDVV RLFAAELGRE EPDLVLLSLV LGFVEHFLAV NRVIPTNVPE 70 80 90 100 110 120 LTFQPSPAPD PPGGLTYFPV ADLSIIAALY ARFTAQIRGA VDLSLYPREG GVSSRELVKK 130 140 150 160 170 180 VSDVIWNSLS RSYFKDRAHI QSLFSFITGW SPVGTKLDSS GVAFAVVGAC QALGLRDVHL 190 200 210 220 230 240 ALSEDHAWVV FGPNGEQTAE VTWHGKGNED RRGQTVNAGV AERSWLYLKG SYMRCDRKME 250 260 270 280 290 300 VAFMVCAINP SIDLHTDSLE LLQLQQKLLW LLYDLGHLER YPMALGNLAD LEELEPTPGR 310 320 330 340 350 360 PDPLTLYHKG IASAKTYYRD EHIYPYMYLA GYHCRNRNVR EALQAWADTA TVIQDYNYCR 370 380 390 400 410 420 EDEEIYKEFF EVANDVIPNL LKEAASLLEA GEERPGEQSQ GTQSQGSALQ DPECFAHLLR 430 440 450 460 470 480 FYDGICKWEE GSPTPVLHVG WATFLVQSLG RFEGQVRQKV RIVSREAEAA EAEEPWGEEA 490 500 510 520 530 540 REGRRRGPRR ESKPEEPPPP KKPALDKGLG TGQGAVSGPP RKPPGTVAGT ARGPEGGSTA 550 560 570 580 590 600 QVPAPTASPP PEGPVLTFQS EKMKGMKELL VATKINSSAI KLQLTAQSQV QMKKQKVSTP 610 SDYTLSFLKR QRKGL
	Isoform 2 (Short) [UniParc]. Checksum: 9BF844C0302B43EF	FASTA	610	67,497
	10 20 30 40 50 60 MGLKAAQKTL FPLRSIDDVV RLFAAELGRE EPDLVLLSLV LGFVEHFLAV NRVIPTNVPE 70 80 90 100 110 120 LTFQPSPAPD PPGGLTYFPV ADLSIIAALY ARFTAQIRGA VDLSLYPREG GVSSRELVKK 130 140 150 160 170 180 VSDVIWNSLS RSYFKDRAHI QSLFSFITGT KLDSSGVAFA VVGACQALGL RDVHLALSED 190 200 210 220 230 240 HAWVVFGPNG EQTAEVTWHG KGNEDRRGQT VNAGVAERSW LYLKGSYMRC DRKMEVAFMV 250 260 270 280 290 300 CAINPSIDLH TDSLELLQLQ QKLLWLLYDL GHLERYPMAL GNLADLEELE PTPGRPDPLT 310 320 330 340 350 360 LYHKGIASAK TYYRDEHIYP YMYLAGYHCR NRNVREALQA WADTATVIQD YNYCREDEEI 370 380 390 400 410 420 YKEFFEVAND VIPNLLKEAA SLLEAGEERP GEQSQGTQSQ GSALQDPECF AHLLRFYDGI 430 440 450 460 470 480 CKWEEGSPTP VLHVGWATFL VQSLGRFEGQ VRQKVRIVSR EAEAAEAEEP WGEEAREGRR 490 500 510 520 530 540 RGPRRESKPE EPPPPKKPAL DKGLGTGQGA VSGPPRKPPG TVAGTARGPE GGSTAQVPAP 550 560 570 580 590 600 TASPPPEGPV LTFQSEKMKG MKELLVATKI NSSAIKLQLT AQSQVQMKKQ KVSTPSDYTL 610 SFLKRQRKGL
	Isoform 3 [UniParc]. Checksum: 3A06BE24447818A3	FASTA	575	63,748
	10 20 30 40 50 60 MGLKAAQKTL FPLRSIDDVV RLFAAELGRE EPDLVLLSLV LGFVEHFLAV NRVIPTNVPE 70 80 90 100 110 120 LTFQPSPAPD PPGGLTYFPV ADLSIIAALY ARFTAQIRGA VDLSLYPREG GVSSRELVKK 130 140 150 160 170 180 VSDVIWNSLS RSYFKDRAHI QSLFSFITGT KLDSSGVAFA VVGACQALGL RDVHLALSED 190 200 210 220 230 240 HAWSWLYLKG SYMRCDRKME VAFMVCAINP SIDLHTDSLE LLQLQQKLLW LLYDLGHLER 250 260 270 280 290 300 YPMALGNLAD LEELEPTPGR PDPLTLYHKG IASAKTYYRD EHIYPYMYLA GYHCRNRNVR 310 320 330 340 350 360 EALQAWADTA TVIQDYNYCR EDEEIYKEFF EVANDVIPNL LKEAASLLEA GEERPGEQSQ 370 380 390 400 410 420 GTQSQGSALQ DPECFAHLLR FYDGICKWEE GSPTPVLHVG WATFLVQSLG RFEGQVRQKV 430 440 450 460 470 480 RIVSREAEAA EAEEPWGEEA REGRRRGPRR ESKPEEPPPP KKPALDKGLG TGQGAVSGPP 490 500 510 520 530 540 RKPPGTVAGT ARGPEGGSTA QVPAPTASPP PEGPVLTFQS EKMKGMKELL VATKINSSAI 550 560 570 KLQLTAQSQV QMKKQKVSTP SDYTLSFLKR QRKGL

References

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[1]	"Positional cloning of the gene for multiple endocrine neoplasia-type 1." Chandrasekharappa S.C., Guru S.C., Manickam P., Olufemi S.-E., Collins F.S., Emmert-Buck M.R., Debelenko L.V., Zhuang Z., Lubensky I.A., Liotta L.A., Crabtree J.S., Wang Y., Roe B.A., Weisemann J., Boguski M.S., Agarwal S.K., Kester M.B., Kim Y.S. , Heppner C., Dong Q., Spiegel A.M., Burns A.L., Marx S.J. Science 276:404-407(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), VARIANTS MEN1 ARG-22; LYS-119 DEL; GLU-368 DEL AND ARG-441, VARIANTS GLN-176 AND ALA-546. Tissue: Leukocyte.
[2]	"Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y. Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Novel MEN1 germline mutations in Brazilian families with multiple endocrine neoplasia type 1." Toledo R.A., Lourenco D.M., Coutinho F.L., Quedas E., Mackowiack I., Machado M.C., Montenegro F., Cunha-Neto M.B., Liberman B., Pereira M.A., Correa P.H., Toledo S.P. Clin. Endocrinol. (Oxf.) 67:377-384(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), VARIANTS MEN1 89-LEU--ALA-95 DEL; PHE-147; ARG-418; PRO-419 AND CYS-476, VARIANT ALA-546.
[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] (ISOFORM 3), VARIANT ALA-546. Tissue: Placenta and Uterus.
[5]	"Menin interacts with the AP1 transcription factor JunD and represses JunD-activated transcription." Agarwal S.K., Guru S.C., Heppner C., Erdos M.R., Collins R.M., Park S.Y., Saggar S., Chandrasekharappa S.C., Collins F.S., Spiegel A.M., Marx S.J., Burns A.L. Cell 96:143-152(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH JUND, VARIANTS MEN1 LEU-12; ARG-22; ASP-139; TYR-139; PRO-165; PRO-181; VAL-247; PRO-291; PRO-314; ARG-349 AND ARG-441.
[6]	"The tumor suppressor protein menin interacts with NF-kappaB proteins and inhibits NF-kappaB-mediated transactivation." Heppner C., Bilimoria K.Y., Agarwal S.K., Kester M., Whitty L.J., Guru S.C., Chandrasekharappa S.C., Collins F.S., Spiegel A.M., Marx S.J., Burns A.L. Oncogene 20:4917-4925(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH NFKB1; NFKB2 AND RELA.
[7]	"Inactivation of menin, a Smad3-interacting protein, blocks transforming growth factor type beta signaling." Kaji H., Canaff L., Lebrun J.J., Goltzman D., Hendy G.N. Proc. Natl. Acad. Sci. U.S.A. 98:3837-3842(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH SMAD3.
[8]	"Menin associates with FANCD2, a protein involved in repair of DNA damage." Jin S., Mao H., Schnepp R.W., Sykes S.M., Silva A.C., D'Andrea A.D., Hua X. Cancer Res. 63:4204-4210(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FANCD2.
[9]	"Multiple tumor suppressor pathways negatively regulate telomerase." Lin S.Y., Elledge S.J. Cell 113:881-889(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TERT REPRESSION.
[10]	"Functional interaction between tumor suppressor menin and activator of S-phase kinase." Schnepp R.W., Hou Z., Wang H., Petersen C., Silva A., Masai H., Hua X. Cancer Res. 64:6791-6796(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DBF4.
[11]	"Menin associates with a trithorax family histone methyltransferase complex and with the hoxc8 locus." Hughes C.M., Rozenblatt-Rosen O., Milne T.A., Copeland T.D., Levine S.S., Lee J.C., Hayes D.N., Shanmugam K.S., Bhattacharjee A., Biondi C.A., Kay G.F., Hayward N.K., Hess J.L., Meyerson M. Mol. Cell 13:587-597(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN H3K4 METHYLATION, IDENTIFICATION IN THE MEN1-ASSOCIATED HISTONE METHYLTRANSFERASE COMPLEX, INTERACTION WITH POLR2A AND POLR2B, VARIANTS MEN1 LEU-12; ARG-22; ASP-139; VAL-247; PRO-314; ARG-349 AND ARG-441.
[12]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN THE MLL-HCF COMPLEX.
[13]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DPY30.
[14]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[15]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-599, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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.
[17]	"Germline mutations of the MEN1 gene in familial multiple endocrine neoplasia type 1 and related states." Agarwal S.K., Kester M.B., Debelenko L.V., Heppner C., Emmert-Buck M.R., Skarulis M.C., Doppman J.L., Kim Y.S., Lubensky I.A., Zhuang Z., Green J.S., Guru S.C., Manickam P., Olufemi S.E., Liotta L.A., Chandrasekharappa S.C., Collins F.S., Spiegel A.M., Burns A.L., Marx S.J. Hum. Mol. Genet. 6:1169-1175(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1.
[18]	"Identification of the multiple endocrine neoplasia type 1 (MEN1) gene." The European consortium on MEN1 Lemmens I., Van de Ven W.J.M., Kas K., Zhang C.X., Giraud S., Wautot V., Buisson N., De Witte K., Salandre J., Lenoir G., Pugeat M., Calender A., Parente F., Quincey D., Gaudray P., De Wit M.J., Lips C.J.M., Hoeppener J.W.M. , Khodaei S., Grant A.L., Weber G., Kytoelae S., Teh B.T., Farnebo F., Phelan C., Hayward N., Larsson C., Pannett A.A.J., Forbes S.A., Basset J.H.D., Thakker R.V. Hum. Mol. Genet. 6:1177-1183(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MEN1 SER-188, VARIANT GLN-176.
[19]	"Somatic mutation of the MEN1 gene in parathyroid tumours." Heppner C., Kester M.B., Agarwal S.K., Debelenko L.V., Emmert-Buck M.R., Guru S.C., Manickam P., Olufemi S.-E., Skarulis M.C., Doppman J.L., Alexander R.H., Kim Y.S., Saggar S.K., Lubensky I.A., Zhuang Z., Liotta L.A., Chandrasekharappa S.C., Collins F.S. , Spiegel A.M., Burns A.L., Marx S.J. Nat. Genet. 16:375-378(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PARATHYROID ADENOMA LYS-26.
[20]	"Characterization of mutations in patients with multiple endocrine neoplasia type 1." Bassett J.H.D., Forbes S.A., Pannett A.A.J., Lloyd S.E., Christie P.T., Wooding C., Harding B., Besser G.M., Edwards C.R., Monson J.P., Sampson J., Wass J.A.H., Wheeler M.H., Thakker R.V. Am. J. Hum. Genet. 62:232-244(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1 ASP-42; PRO-165; ASP-169; SER-188 AND GLU-289.
[21]	"Germ-line mutation analysis in patients with multiple endocrine neoplasia type 1 and related disorders." Giraud S., Zhang C.X., Serova-Sinilnikova O., Wautot V., Salandre J., Buisson N., Waterlot C., Bauters C., Porchet N., Aubert J.-P., Emy P., Cadiot G., Delemer B., Chabre O., Niccoli P., Leprat F., Duron F., Emperauger B. , Cougard P., Goudet P., Sarfati E., Riou J.-P., Guichard S., Rodier M., Meyrier A., Caron P., Vantyghem M.-C., Assayag M., Peix J.-L., Pugeat M., Rohmer V., Vallotton M., Lenoir G., Gaudray P., Proye C., Conte-Devolx B., Chanson P., Shugart Y.Y., Goldgar D., Murat A., Calender A. Am. J. Hum. Genet. 63:455-467(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1.
[22]	"A family with isolated hyperparathyroidism segregating a missense MEN1 mutation and showing loss of the wild-type alleles in the parathyroid tumors." Teh B.T., Esapa C.T., Houlston R., Grandell U., Farnebo F., Nordenskjoeld M., Pearce C.J., Carmichael D., Larsson C., Harris P.E. Am. J. Hum. Genet. 63:1544-1549(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FIHP LYS-260.
[23]	"Novel V184E MEN1 germline mutation in a Japanese kindred with familial hyperparathyroidism." Fujimori M., Shirahama S., Sakurai A., Hashizume K., Hama Y., Ito K., Shingu K., Kobayashi S., Amano J., Fukushima Y. Am. J. Med. Genet. 80:221-222(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FIHP GLU-189.
[24]	"MEN1 gene mutations in 12 MEN1 families and their associated tumors." Bartsch D., Kopp I., Bergenfelz A., Rieder H., Muench K., Jaeger K., Deiss Y., Schudy A., Barth P., Arnold R., Rothmund M., Simon B. Eur. J. Endocrinol. 139:416-420(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1 LYS-26 AND PRO-173.
[25]	"Analysis of recurrent germline mutations in the MEN1 gene encountered in apparently unrelated families." Agarwal S.K., Debelenko L.V., Kester M.B., Guru S.C., Manickam P., Olufemi S.-E., Skarulis M.C., Heppner C., Crabtree J.S., Lubensky I.A., Zhuang Z., Kim Y.S., Chandrasekharappa S.C., Collins F.S., Liotta L.A., Spiegel A.M., Burns A.L., Emmert-Buck M.R., Marx S.J. Hum. Mutat. 12:75-82(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1.
[26]	"Five novel mutations in the familial multiple endocrine neoplasia type 1 (MEN1) gene." Cote G.J., Lee J.E., Evans D.B., Huang E., Schultz P.N., Dang G.T., Qiu H., Shetelbine S., Sellin R.V., Gagel R.F. Hum. Mutat. 12:219-219(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MEN1 ARG-432.
[27]	"Absence of germ-line mutations of the multiple endocrine neoplasia type 1 (MEN1) gene in familial pituitary adenoma in contrast to MEN1 in Japanese." Tanaka C., Yoshimoto K., Yamada S., Nishioka H., Ii S., Moritani M., Yamaoka T., Itakura M. J. Clin. Endocrinol. Metab. 83:960-965(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MEN1 LEU-325, VARIANT ALA-546.
[28]	"Mutation analysis of the MEN1 gene in multiple endocrine neoplasia type 1, familial acromegaly and familial isolated hyperparathyroidism." Teh B.T., Kytoelae S., Farnebo F., Bergman L., Wong F.K., Weber G., Hayward N., Larsson C., Skogseid B., Beckers A., Phelan C., Edwards M., Epstein M., Alford F., Hurley D., Grimmond S., Silins G., Walters M. , Stewart C., Cardinal J., Khodaei S., Parente F., Tranebjaerg L., Jorde R., Menon J., Khir A., Tan T.T., Chan S.P., Zaini A., Khalid B.A.K., Sandelin K., Thompson N., Brandi M.-L., Warth M., Stock J., Leisti J., Cameron D., Shepherd J.J., Oeberg K., Nordenskjoeld M., Salmela P. J. Clin. Endocrinol. Metab. 83:2621-2626(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MEN1 ASN-423, VARIANTS GLN-176 AND ALA-546.
[29]	"Parathyroid MEN1 gene mutations in relation to clinical characteristics of nonfamilial primary hyperparathyroidism." Carling T., Correa P., Hessman O., Hedberg J., Skogseid B., Lindberg D., Rastad J., Westin G., Akerstrom G. J. Clin. Endocrinol. Metab. 83:2960-2963(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MEN1 ASP-139, VARIANT TRP-157.
[30]	"Menin mutations in MEN1 patients." Mayr B., Brabant G., von zur Muehlen A. J. Clin. Endocrinol. Metab. 83:3004-3005(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MEN1 SER-428.
[31]	"Somatic mutations of the MEN1 tumor suppressor gene detected in sporadic angiofibromas." Boeni R., Vortmeyer A.O., Pack S., Park W.-S., Burg G., Hofbauer G., Darling T., Liotta L., Zhuang Z. J. Invest. Dermatol. 111:539-540(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1 ILE-135 AND LYS-364.
[32]	"Novel MEN1 gene mutations in familial multiple endocrine neoplasia type 1." Sakurai A., Shirahama S., Fujimori M., Katai M., Itakura Y., Kobayashi S., Amano J., Fukushima Y., Hashizume K. J. Hum. Genet. 43:199-201(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1 LYS-119 DEL AND 171-GLN--LEU-173 DEL.
[33]	"Identification of five novel germline mutations of the MEN1 gene in Japanese multiple endocrine neoplasia type 1 (MEN1) families." Sato M., Matsubara S., Miyauchi A., Ohye H., Imachi H., Murao K., Takahara J. J. Med. Genet. 35:915-919(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MEN1 GLY-45.
[34]	"Molecular pathology of multiple endocrine neoplasia type I: two novel germline mutations and updated classification of mutations affecting MEN1 gene." Martin-Campos J.M., Catasus L., Chico A., Mayoral C., Lagarda E., Gallart L., Mato E., Rodriguez-Espinosa J., Matias-Guiu X., De Leiva A., Blanco-Vaca F. Diagn. Mol. Pathol. 8:195-204(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MEN1 ARG-139.
[35]	"A new mutation of the MEN1 gene in an Italian kindred with multiple endocrine neoplasia type 1." Cetani F., Pardi E., Cianferotti L., Vignali E., Picone A., Miccoli P., Pinchera A., Marcocci C. Eur. J. Endocrinol. 140:429-433(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MEN1 PRO-449.
[36]	"Germline MEN1 mutations in sixteen Japanese families with multiple endocrine neoplasia type 1 (MEN1)." Hai N., Aoki N., Matsuda A., Mori T., Kosugi S. Eur. J. Endocrinol. 141:475-480(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1 ARG-188; ARG-230; TYR-246 AND PRO-258, VARIANT ALA-546.
[37]	"MEN I gene mutations in sporadic adrenal adenomas." Schulte K.-M., Heinze M., Mengel M., Simon D., Scheuring S., Koehrer K., Roeher H.-D. Hum. Genet. 105:603-610(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ADRENAL ADENOMA SER-557.
[38]	"Mutation analysis of the MEN1 gene in Belgian patients with multiple endocrine neoplasia type 1 and related diseases." Poncin J., Abs R., Velkeniers B., Bonduelle M., Abramowicz M., Legros J.-J., Verloes A., Meurisse M., van Gaal L., Verellen C., Koulischer L., Beckers A. Hum. Mutat. 13:54-60(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1 TRP-39; TYR-177; ASP-184 AND PRO-269, VARIANT FIHP PRO-272, VARIANTS GLN-176 AND ALA-546.
[39]	"Germline mutations in the multiple endocrine neoplasia type 1 gene: evidence for frequent splicing defects." Mutch M.G., Dilley W.G., Sanjurjo F., Debenedetti M.K., Doherty G.M., Wells S.A. Jr., Goodfellow P.J., Lairmore T.C. Hum. Mutat. 13:175-185(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1 ASP-161 AND ARG-246.
[40]	"Germline mutations in the MEN1 gene: creation of a new splice acceptor site and insertion of 7 intron nucleotides into the mRNA." Engelbach M., Forst T., Hankeln T., Tratzky M., Heerdt S., Pfuetzner A., Kann P., Kunt T., Schneider S., Schmidt E.R., Beyer J. Int. J. Mol. Med. 4:483-485(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MEN1 PHE-160.
[41]	"Identification of MEN1 gene mutations in families with MEN 1 and related disorders." Bergman L., Teh B.T., Cardinal J., Palmer J., Walters M., Shepherd J., Cameron D., Hayward N. Br. J. Cancer 83:1009-1014(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1 LEU-234; ASP-358; SER-378 AND PRO-420.
[42]	"Screening of the MEN1 gene and discovery of germ-line and somatic mutations in apparently sporadic parathyroid tumors." Uchino S., Noguchi S., Sato M., Yamashita H., Yamashita H., Watanabe S., Murakami T., Toda M., Ohshima A., Futata T., Mizukoshi T., Koike E., Takatsu K., Terao K., Wakiya S., Nagatomo M., Adachi M. Cancer Res. 60:5553-5557(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PARATHYROID TUMOR ASP-161; ARG-188; TRP-258; ALA-279 AND PRO-289.
[43]	"Criteria for mutation analysis in MEN 1-suspected patients: MEN 1 case-finding." Roijers J.F.M., de Wit M.J., van der Luijt R.B., Ploos van Amstel H.K., Hoeppener J.W.M., Lips C.J.M. Eur. J. Clin. Invest. 30:487-492(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1 TRP-39; LYS-119 DEL; GLN-184; PRO-228; ARG-322; PRO-342; ASN-353; VAL-390 AND SER-549.
[44]	"MEN1 gene mutation analysis in Italian patients with multiple endocrine neoplasia type 1." Morelli A., Falchetti A., Martineti V., Becherini L., Mark M., Friedman E., Brandi M.L. Eur. J. Endocrinol. 142:131-137(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1 LYS-45; MET-220 AND ARG-349.
[45]	"A novel mutation of the MEN1 gene in a Japanese kindred with familial isolated primary hyperparathyroidism." Honda M., Tsukada T., Tanaka H., Maruyama K., Yamaguchi K., Obara T., Yamaji T., Ishibashi M. Eur. J. Endocrinol. 142:138-143(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FIHP ASP-310.
[46]	"A novel mutation E179K of the MEN1 gene predisposes for multiple endocrine neoplasia-type 1 (MEN1)." Weinhaeusel A., Vierhapper H., Schlegl R., Wagner T., Muhr D., Scheuba C., Niederle B., Haas O.A. Hum. Mutat. 16:533-533(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MEN1 LYS-184.
[47]	"Familial isolated hyperparathyroidism as a variant of multiple endocrine neoplasia type 1 in a large Danish pedigree." Kassem M., Kruse T.A., Wong F.K., Larsson C., Teh B.T. J. Clin. Endocrinol. Metab. 85:165-167(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FIHP PRO-265.
[48]	"Pituitary macroadenoma in a 5-year-old: an early expression of multiple endocrine neoplasia type 1." Stratakis C.A., Schussheim D.H., Freedman S.M., Keil M.F., Pack S.D., Agarwal S.K., Skarulis M.C., Weil R.J., Lubensky I.A., Zhuang Z., Oldfield E.H., Marx S.J. J. Clin. Endocrinol. Metab. 85:4776-4780(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MEN1 ASP-139.
[49]	"Identification of three novel menin mutations (c.741delGTCA, c.1348T>C, c.1785delA) in unrelated Italian families affected with multiple endocrine neoplasia type 1: additional information for mutational screening." Asteria C., Faglia G., Roncoroni R., Borretta G., Ribotto P., Beck-Peccoz P. Hum. Mutat. 17:237-237(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MEN1 PRO-419.
[50]	"Germline mutation profile of MEN1 in multiple endocrine neoplasia type 1: search for correlation between phenotype and the functional domains of the MEN1 protein." Wautot V., Vercherat C., Lespinasse J., Chambe B., Lenoir G.M., Zhang C.X., Porchet N., Cordier M., Beroud C., Calender A. Hum. Mutat. 20:35-47(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1 TRP-39; ASP-42; LEU-98; PRO-165; THR-165; PHE-167; ASP-169; ARG-170; TYR-177; PRO-228; PHE-245; ARG-286; PRO-316; PRO-319; TYR-322; ARG-322; ASP-342; ARG-346; HIS-362; ASP-373; MET-377; ASN-423; CYS-532; ASN-560 AND ARG-560.
[51]	"A novel six-nucleotide insertion in exon 4 of the MEN1 gene, 878insCTGCAG, in three patients with familial insulinoma and primary hyperparathyroidism." Okamoto H., Tamada A., Hai N., Doi M., Uchimura I., Hirata Y., Kosugi S. Jpn. J. Clin. Oncol. 32:368-370(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MEN1 LEU-GLN-266 INS.
[52]	"Frequent occurrence of an intron 4 mutation in multiple endocrine neoplasia type 1." Turner J.J.O., Leotlela P.D., Pannett A.A.J., Forbes S.A., Bassett J.H.D., Harding B., Christie P.T., Bowen-Jones D., Ellard S., Hattersley A., Jackson C.E., Pope R., Quarrell O.W., Trembath R., Thakker R.V. J. Clin. Endocrinol. Metab. 87:2688-2693(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1 LYS-119 DEL; ILE-159; GLU-368 DEL AND ASN-423.
[53]	"Genetic screening for MEN1 mutations in families presenting with familial primary hyperparathyroidism." Perrier N.D., Villablanca A., Larsson C., Wong M., Ituarte P., Teh B.T., Clark O.H. World J. Surg. 26:907-913(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FIHP HIS-282.
[54]	"Multiple endocrine neoplasia type 1 (MEN1) germline mutations in familial isolated primary hyperparathyroidism." Pannett A.A.J., Kennedy A.M., Turner J.J.O., Forbes S.A., Cavaco B.M., Bassett J.H.D., Cianferotti L., Harding B., Shine B., Flinter F., Maidment C.G.H., Trembath R., Thakker R.V. Clin. Endocrinol. (Oxf.) 58:639-646(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1 AND FIHP VAL-158 AND PRO-416.
[55]	"Germline mutations of the MEN1 gene in Korean families with multiple endocrine neoplasia type 1 (MEN1) or MEN1-related disorders." Park J.-H., Kim I.-J., Kang H.C., Lee S.-H., Shin Y., Kim K.-H., Lim S.-B., Kang S.-B., Lee K.U., Kim S.Y., Lee M.-S., Lee M.-K., Park J.-H., Moon S.-D., Park J.-G. Clin. Genet. 64:48-53(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MEN1 PRO-330.
[56]	"Efficient mutation detection in MEN1 gene using a combination of single-strand conformation polymorphism (MDGA) and heteroduplex analysis." Groupe d'etude des neoplasies endocriniennes multiples Crepin M., Escande F., Pigny P., Buisine M.-P., Calender A., Porchet N., Odou M.-F. Electrophoresis 24:26-33(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1 ARG-170; PRO-228; PHE-246; ARG-286; PRO-316; TYR-322; ASN-423 AND SER-545.
[57]	"A novel missense mutation of the MEN1 gene in a multiple endocrine neoplasia type 1 patient associated with carcinoid syndrome." Ukita C., Yamaguchi M., Tanaka T., Shigeta H., Nishikawa M. Intern. Med. 42:1112-1116(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MEN1 PRO-347.
[58]	"Mutational and gross deletion study of the MEN1 gene and correlation with clinical features in Spanish patients." Cebrian A., Ruiz-Llorente S., Cascon A., Pollan M., Diez J.J., Pico A., Telleria D., Benitez J., Robledo M. J. Med. Genet. 40:E72-E72(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1 LYS-45 AND PRO-139, VARIANTS GLN-176 AND ALA-546.
[59]	"Unusual presentation of multiple endocrine neoplasia type 1 in a young woman with a novel mutation of the MEN1 gene." Balogh K., Patocs A., Majnik J., Varga F., Illyes G., Hunyady L., Racz K. J. Hum. Genet. 49:380-386(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GLN-176.
[60]	"Novel mutations in the MEN1 gene in subjects with multiple endocrine neoplasia-1." Jap T.-S., Chiu C.-Y., Won J.G.-S., Wu Y.-C., Chen H.-S. Clin. Endocrinol. (Oxf.) 62:336-342(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1 GLU-110 AND HIS-423.
[61]	"Clinical testing for multiple endocrine neoplasia type 1 in a DNA diagnostic laboratory." Klein R.D., Salih S., Bessoni J., Bale A.E. Genet. Med. 7:131-138(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS MEN1 VAL-144; ASP-161; ASP-184; LYS-184; ARG-186; MET-220; ARG-264; ARG-325; TRP-360; TYR-426; CYS-441 AND ARG-441.
[62]	"Identification of MEN1 and HRPT2 somatic mutations in paraffin-embedded (sporadic) parathyroid carcinomas." Haven C.J., van Puijenbroek M., Tan M.H., Teh B.T., Fleuren G.J., van Wezel T., Morreau H. Clin. Endocrinol. (Oxf.) 67:370-376(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PHE-220, ASSOCIATION WITH PARATHYROID CARCINOMA.
[63]	"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: VARIANT [LARGE SCALE ANALYSIS] ALA-546, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U93236 mRNA. Translation: AAC51228.1.
U93237 Genomic DNA. Translation: AAC51229.1.
U93237 Genomic DNA. Translation: AAC51230.1.
AP001462 Genomic DNA. No translation available.
EF443091 Genomic DNA. Translation: ABQ12621.1.
EF443092 Genomic DNA. Translation: ABQ12622.1.
EF443093 Genomic DNA. Translation: ABQ12623.1.
EF443094 Genomic DNA. Translation: ABQ12624.1. Frameshift.
EF443095 Genomic DNA. Translation: ABQ12625.1.
EF443096 Genomic DNA. Translation: ABQ12626.1.
EF443097 Genomic DNA. Translation: ABQ12627.1. Frameshift.
BC002544 mRNA. Translation: AAH02544.1.
BC002664 mRNA. Translation: AAH02664.2.

IPI

IPI00182106.
IPI00328838.
IPI00651636.

RefSeq

NP_000235.2. NM_000244.3.
NP_570711.1. NM_130799.2.
NP_570712.1. NM_130800.2.
NP_570713.1. NM_130801.2.
NP_570714.1. NM_130802.2.
NP_570715.1. NM_130803.2.
NP_570716.1. NM_130804.2.

UniGene

Hs.423348.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3U84	X-ray	2.50	A/B	2-615	[»]
3U85	X-ray	3.00	A	2-615	[»]
3U86	X-ray	2.84	A	2-615	[»]
3U88	X-ray	3.00	A/B	2-615	[»]
4GPQ	X-ray	1.46	A	1-598	[»]
4GQ3	X-ray	1.56	A	1-598	[»]
4GQ4	X-ray	1.27	A	1-598	[»]
4GQ6	X-ray	1.55	A	1-598	[»]
4I80	X-ray	3.10	A	2-615	[»]

ProteinModelPortal

O00255.

SMR

O00255. Positions 2-613.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24236N.

IntAct

O00255. 8 interactions.

STRING

9606.ENSP00000337088.

PTM databases

PhosphoSite

O00255.

Proteomic databases

PaxDb

O00255.

PRIDE

O00255.

Protocols and materials databases

DNASU

4221.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000312049; ENSP00000308975; ENSG00000133895.
ENST00000315422; ENSP00000323747; ENSG00000133895.
ENST00000337652; ENSP00000337088; ENSG00000133895.
ENST00000377313; ENSP00000366530; ENSG00000133895.
ENST00000377321; ENSP00000366538; ENSG00000133895.
ENST00000377326; ENSP00000366543; ENSG00000133895.
ENST00000394374; ENSP00000377899; ENSG00000133895.
ENST00000394376; ENSP00000377901; ENSG00000133895.
ENST00000443283; ENSP00000396940; ENSG00000133895.

GeneID

4221.

KEGG

hsa:4221.

UCSC

uc001obj.3. human.
uc001obl.3. human.
uc001obm.3. human.

Organism-specific databases

CTD

4221.

GeneCards

GC11M064570.

HGNC

HGNC:7010. MEN1.

HPA

HPA030342.

MIM

131100. phenotype.
145000. phenotype.
613733. gene.

neXtProt

NX_O00255.

Orphanet

99879. Familial isolated hyperparathyroidism.
99877. Familial parathyroid adenoma.
652. Multiple endocrine neoplasia type 1.
913. Zollinger-Ellison syndrome.

PharmGKB

PA30746.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG67412.

HOVERGEN

HBG000208.

InParanoid

O00255.

KO

K14970.

OMA

NNEHIYP.

OrthoDB

EOG4HT8RX.

PhylomeDB

O00255.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

O00255.

Bgee

O00255.

CleanEx

HS_MEN1.
HS_SCG2.

Genevestigator

O00255.

GermOnline

ENSG00000133895. Homo sapiens.

Family and domain databases

InterPro

IPR007747. Menin.
[Graphical view]

PANTHER

PTHR12693. PTHR12693. 1 hit.

Pfam

PF05053. Menin. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1615381.

ChiTaRS

MEN1. human.

GenomeRNAi

4221.

NextBio

16643.

SOURCE

Search...

Entry information

Entry name

MEN1_HUMAN

Accession

Primary (citable) accession number: O00255
Secondary accession number(s): A5HBC6 , A5HBC7, A5HBC8, A5HBC9, A5HBD0, A5HBD1, A5HBD2, O00632, Q9BUF0, Q9BUK2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 129 of the entry and version 4 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.